Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
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O13535 | YH11B_YEAST | MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENLHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQKLTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQQSNDLNIESDHDFQSDIELHPEQLRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISDIESTGSGGMHRLDVPLLAPMSQSNTHESSHASKSKDFRHSDSYSDNETNHTNVPISSTGGTNNKTVPQTSEQETEKRIIHRSPSIDTSSSESNSLHHVVPIKTSDTCPKENTEESIIADLPLPDLPPEPPTELSDSFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIQAYHKEVNQLLMMKTWDTDRYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDPGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSHLVQELNKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH | 2.7.7.49; 2.7.7.7; 3.1.26.4; 3.4.23.- | null | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; proteolysis [GO:0006508]; retrotransposition [GO:0032197] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; retrotransposon nucleocapsid [GO:0000943] | aspartic-type endopeptidase activity [GO:0004190]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; RNA binding [GO:0003723]; RNA nuclease activity [GO:0004540]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523] | PF00665;PF07727;PF01021; | 3.30.420.10; | null | PTM: Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; | null | null | null | null | FUNCTION: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity). {ECO:0000250}.; FUNCTION: The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP. {ECO:0000250}.; FUNCTION: Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity). {ECO:0000250}.; FUNCTION: Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity). {ECO:0000250}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
O13547 | CCW14_YEAST | MRATTLLSSVVSLALLSKEVLATPPACLLACVAQVGKSSSTCDSLNQVTCYCEHENSAVKKCLDSICPNNDADAAYSAFKSSCSEQNASLGDSSSSASSSASSSSKASSSTKASSSSASSSTKASSSSASSSTKASSSSAAPSSSKASSTESSSSSSSSTKAPSSEESSSTYVSSSKQASSTSEAHSSSAASSTVSQETVSSALPTSTAVISTFSEGSGNVLEAGKSVFIAAVAAMLI | null | null | fungal-type cell wall organization [GO:0031505] | cell periphery [GO:0071944]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; mitochondrion [GO:0005739]; side of membrane [GO:0098552] | structural constituent of cell wall [GO:0005199] | PF05730; | null | CCW14 family | PTM: Extensively O-glycosylated.; PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer. | SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Lipid-anchor, GPI-anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP). | null | null | null | null | null | FUNCTION: Component of the inner layer of the cell wall. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
O13563 | RPN13_YEAST | MSMSSTVIKFRAGVCEYNEDSRLCTPIPVQGEIEIKPNEEEELGFWDFEWRPTEKPVGRELDPISLILIPGETMWVPIKSSKSGRIFALVFSSNERYFFWLQEKNSGNLPLNELSAKDKEIYNKMIGVLNNSSESDEEESNDEKQKAQDVDVSMQD | null | null | proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; ubiquitin-dependent protein catabolic process [GO:0006511] | nucleus [GO:0005634]; proteasome complex [GO:0000502]; proteasome regulatory particle, lid subcomplex [GO:0008541]; proteasome storage granule [GO:0034515] | endopeptidase activator activity [GO:0061133]; proteasome binding [GO:0070628]; ubiquitin binding [GO:0043130] | PF04683; | 2.30.29.70; | RPN13 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. | null | null | null | null | null | FUNCTION: Component of the 19S cap proteasome complex which acts as a regulatory subunit of the 26S proteasome, involved in the ATP-dependent degradation of ubiquitinated proteins. {ECO:0000269|PubMed:11029046, ECO:0000269|PubMed:7957966}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
O13601 | RSP1_SCHPO | MARTAFHDEFVDYYTILGAESTSSYVEIRQQYLKLVLRYHPDRNPGREAEVLPQFQLIQKAHEVLKDPKLRELFDQRRLLEAGRPDGVLRFRPKKSGPKNDISTKVASKVSVTMATKFAEKKKKQDRENVDSKDNNITNFSLHRSFSASGKMEKNNSFKEVSTSKSYISSGYLHPKTSPIFKKNGYATENVVDPISSSPRFKGPNYNKFNAKLYLESLREKRRTYTPLSEISNGLNSNGVENSSITKSSPRSSSSSNNERFKDTSEESIIFTSPNTPEHPSVYQTDITPEIKLEHSDNNSPSKPEIPFRHPTSKPLPPKPLSRSKSSSLSRNQTRSQLNDLSAENDSTSNSTEYDDQLQSILRSLAIEGDDDEVAKVLPKPPSVPTIQAPIPPEAPRNLTNASVDSYLNSFEMYQRRWSSYSIIYTQYAFQWQIFKNKCFQLDLMNTPGQSRLIDNWKEGSQAIQLFYAYEQMHLRALEELQSLKESLFASFGI | null | null | chaperone cofactor-dependent protein refolding [GO:0051085]; cytoplasmic microtubule organization [GO:0031122]; equatorial microtubule organizing center disassembly [GO:0031025]; interphase microtubule organizing center assembly [GO:0031024]; mitochondrion organization [GO:0007005]; negative regulation of apoptotic process [GO:0043066]; protein refolding [GO:0042026] | cell division site [GO:0032153]; cytoplasm [GO:0005737]; cytoplasmic microtubule plus-end [GO:1904511]; equatorial microtubule organizing center [GO:0000923]; interphase microtubule organizing center [GO:0031021]; mitochondrion [GO:0005739]; mitotic spindle pole body [GO:0044732]; nucleus [GO:0005634]; spindle pole body [GO:0005816] | Hsp70 protein binding [GO:0030544]; protein kinase binding [GO:0019901]; unfolded protein binding [GO:0051082] | PF00226; | 1.10.287.110; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15068790}. Nucleus {ECO:0000269|PubMed:15068790}. Note=Associates with the microtubule bundles. | null | null | null | null | null | FUNCTION: Has a role in the proper organization of the interphase microtubule cytoskeleton. Required for equatorial microtubule organizing center (eMTOC) disassembly into satellites, contributing to the dynamic redistribution of MTOC components for organization of interphase microtubules. {ECO:0000269|PubMed:15068790}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13648 | ANM3_SCHPO | MLVKPMACYFEIWTRKVTTIEDFSLAIANRFKQMGSHSDSEVDWDNEEEVWEDEVHEFCCLFCDSTFTCLKDLWSHCKEAHNFDFYQVKQQNNLDFYACIKLVNYIRSQVKEGKTPDLDKLSDILRSDEYMISVLPDDSVLFSLGDELDSDFEDDNTLEIEVENPADVSKDAEIKKLKLQNQLLISQLEEIRKDKMNELTSQTTDQLSVTPKKADNDSYYFESYAGNDIHFLMLNDSVRTEGYRDFVYHNKHIFAGKTVLDVGCGTGILSMFCAKAGAKKVYAVDNSDIIQMAISNAFENGLADQITFIRGKIEDISLPVGKVDIIISEWMGYALTFESMIDSVLVARDRFLAPSGIMAPSETRLVLTATTNTELLEEPIDFWSDVYGFKMNGMKDASYKGVSVQVVPQTYVNAKPVVFARFNMHTCKVQDVSFTSPFSLIIDNEGPLCAFTLWFDTYFTTKRTQPIPEAIDEACGFTTGPQGTPTHWKQCVLLLRNRPFLQKGTRVEGTISFSKNKKNNRDLDISVHWNVNGKADSQSYVLN | 2.1.1.- | null | methylation [GO:0032259]; ribosome biogenesis [GO:0042254] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | metal ion binding [GO:0046872]; protein-arginine N-methyltransferase activity [GO:0016274]; protein-arginine omega-N asymmetric methyltransferase activity [GO:0035242]; ribosome binding [GO:0043022] | PF21137;PF06325; | 2.70.160.11;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Protein arginine N-methyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15175657}. | null | null | null | null | null | FUNCTION: Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in ribosomal protein rps2. {ECO:0000269|PubMed:15175657, ECO:0000269|PubMed:16478994}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13666 | ERG3B_SCHPO | MDVVLQYADKYVFDTFYGKIAESFDSSSSFANTAVNSTTLGLAEKVNFAITSGLLDRNNVWRQFTSLFLITWIMGTLSYFLSASFAYYVYFDREEARRHPKFLKNQEHLELMVALKNLPGMAILTAPWFLAEIRGYGYVYDKLDEYGYFYLFFSIALFLLFSDFLIYWIHRALHHRWLYAPLHKLHHKWIVPTPYSSHAFHYLDGYSQSLPYHMFPFFFPLNKYVYLLLFGSVNYWTVLIHDGKYFSNNAVVNGAAHHAAHHMYFNYNYGQFFTLFDRLCSSYRQPDQELFDAELRNEKLQEQRIRFMETVQYTVEGKDDRTYASKKDN | 1.14.19.20 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:P53045}; | ergosterol biosynthetic process [GO:0006696]; sphingolipid biosynthetic process [GO:0030148]; sterol biosynthetic process [GO:0016126] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020] | C-4 methylsterol oxidase activity [GO:0000254]; C-5 sterol desaturase activity [GO:0000248]; delta7-sterol 5(6)-desaturase activity [GO:0050046]; iron ion binding [GO:0005506]; sphingolipid delta-4 desaturase activity [GO:0042284]; sphingosine hydroxylase activity [GO:0000170] | PF04116; | null | Sterol desaturase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=episterol + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = 5-dehydroepisterol + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46560, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:23929, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:52972; EC=1.14.19.20; Evidence={ECO:0000250|UniProtKB:P32353}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46561; Evidence={ECO:0000250|UniProtKB:P32353}; | null | PATHWAY: Steroid metabolism; ergosterol biosynthesis. {ECO:0000269|PubMed:18310029}. | null | null | FUNCTION: C-5 sterol desaturase; part of the third module of ergosterol biosynthesis pathway that includes by the late steps of the pathway (PubMed:18310029). Erg31 and erg32 catalyze the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. The lanosterol 14-alpha-demethylase erg11/cyp1 catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol. In the next steps, a complex process involving various demethylation, reduction and desaturation reactions catalyzed by the C-14 reductase erg24 and the C-4 demethylation complex erg25-erg26-erg27 leads to the production of zymosterol. Erg28 likely functions in the C-4 demethylation complex reaction by tethering erg26 and Erg27 to the endoplasmic reticulum or to facilitate interaction between these proteins. Then, the sterol 24-C-methyltransferase erg6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase erg2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturases erg31 and erg32 then catalyze the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase erg4 to produce ergosterol (Probable) (PubMed:18310029). In the genus Schizosaccharomyces, a second route exists between lanosterol and fecosterol, via the methylation of lanosterol to eburicol by erg6, followed by C14-demethylation by erg11/cyp1 and C4-demethylation by the demethylation complex erg25-erg26-erg27 (Probable) (PubMed:8586261). {ECO:0000250|UniProtKB:P32353, ECO:0000269|PubMed:18310029, ECO:0000305|PubMed:18310029, ECO:0000305|PubMed:8586261}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13684 | PCS1_SCHPO | MRKNNMQTSKDSELKEQAKGKSSKLIHKLPKQRTRISQGQMHSTQDFVNNEDQDAYSVRENENELHINNSGMSELNKKLQLPNVELSTLSHTQEQEFNELNKLIRKINELQEFYLLEDLAKPVTNAGADADDTIVKDLKKELENEKKANHSLKNELLKTREQIKNYSKINILIKELFGLEVADCIEDEDGYRFNCKNTGRRGTLEYQLLLDDQNFTFTPRLNVQTDEELMKHLPDYLLEEIIFTKEQGKLFSARLMKALQD | null | null | attachment of mitotic spindle microtubules to kinetochore [GO:0051315]; cell division [GO:0051301]; meiotic sister chromatid segregation [GO:0045144]; mitotic chromosome centromere condensation [GO:1990893]; mitotic sister chromatid segregation [GO:0000070] | chromosome, centromeric core domain [GO:0034506]; chromosome, centromeric region [GO:0000775]; cytosol [GO:0005829]; kinetochore [GO:0000776]; mitotic spindle [GO:0072686]; monopolin complex [GO:0033551]; nucleolus [GO:0005730]; nucleus [GO:0005634] | microtubule site clamp [GO:1990644] | PF12539; | 3.90.1150.80; | null | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12689592}. Chromosome, centromere {ECO:0000269|PubMed:12689592}. Note=Nucleolar during G2 (PubMed:12689592). Localizes to the centromeres throughout most stages of vegetative growth and meiotic development apart from the horse tail stage of prophase I (PubMed:12689592). Localizes to the central core of the centromere (PubMed:17627824). | null | null | null | null | null | FUNCTION: The monopolin-like pcs1/mde4 complex is essential for accurate chromosome segregation during mitosis and meiosis II. May clamp together microtubule binding sites on the same kinetochore, preventing merotelic attachment of microtubules. In contrast to its S.cerevisiae ortholog CSM1, is not required ofr mono-orientation during meiosis I. {ECO:0000269|PubMed:12689592, ECO:0000269|PubMed:17627824}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13685 | UBC13_SCHPO | MALPKRIIKEIETLTRDPPPGIVAAPTEDNLRYFKITMEGPQQSAYEGGKFHLELFLPDEYPMMPPNVRFLTKIYHPNVDKLGRICLSTLKKDWSPALQIRTVLLSIQALMGAPNPDDPLDNDVAKIWKENEPQAIANAREWTKKYAV | 2.3.2.23 | null | cytoplasm to vacuole targeting by the NVT pathway [GO:0120113]; postreplication repair [GO:0006301]; protein K63-linked ubiquitination [GO:0070534]; UV-damage excision repair [GO:0070914] | cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin protein ligase activity [GO:0061630] | PF00179; | 3.10.110.10; | Ubiquitin-conjugating enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388}. | null | null | FUNCTION: Has a role in the DNA error-free postreplication repair (PRR) pathway. The ubc13/spm2 heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. {ECO:0000269|PubMed:12531016}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13688 | NSE6_SCHPO | MNASNNISKFPDLDNSSKLIDHILDSDDSEELDELPDISSLVPSARAQSRKQYLKNDSSNSSTYRWNIDLLSSTATIDDSVAKRRKLAVQNLLQYDSTQTFQTGDEIDELIGKSVGSNVLNVLRSNPIYDDDLRYEYCSNSKARVPDWNTLKAECLKDNDLEFNEGIIPTTFGDLLSAKLVPLDIALSICSLQFFRSLGDTTCSEWIANLEKIFYSYKSSSNNLNQIVRFIFETTADMIGIDLAKRQVPIQLERTSASENLKSNLKIKVINFLKCCGTLYRFSDDTVRFEMIQDACRILIDNQVGSFCKWQFSQFMELPISLNPDFLISNIHKVSESPRVWVTILSSLSRSCQKFRKKIAFTLFVGKQSKNDDSDFSSLCQRLDEISASCNNDYTTLLYQIRTFGYAVDEKHFKTNERLECLLEKLRKIDLTISGSTDHLLLSRCEVKDCIHRLFMVLYYLNTNSAPELERIIESDLPNNNKQKDRYFKDKTSNLSMKENKSFSAKKVKKGKKKNKRQAYKR | null | null | DNA damage response [GO:0006974]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724] | nucleus [GO:0005634]; Smc5-Smc6 complex [GO:0030915] | chromatin-protein adaptor activity [GO:0140463] | PF08691; | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16478984, ECO:0000269|PubMed:16823372}. Chromosome {ECO:0000269|PubMed:16478984}. | null | null | null | null | null | FUNCTION: Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. May prevent formation of excessive Holliday junctions or assist in their resolution. {ECO:0000269|PubMed:16478984}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13692 | GAS5_SCHPO | MNFLHFLTTSLLLLGGSRLALADSASSAIKIKGNAFFNSDTNERFYVRGVDYQPGGSSTLVDPLADTSICKRDLPYLQGLNINTIRVYQVDNSANHDECMSALQDAGIYVILDLATSSNSISRLDAASSYNAVFLQGIFATIDAFKNYTNVLGFFAGNEVANTAENSATTTWVKAALRDAKEYISKNSDRDIPVGYSAADVAEIRVQCADFFACGNSSVRADFYGMNMYEWCGADSSFTISGYDQRMEEFANYSIPLFLSEYGCNDVTKESDGTPDRPFDEVDAIFSSEMSSVFSGGLVYQYSEEGNNYGLVVIDGDNVTISKNYETLKEKYASAANYTGDGDYSSSPATLTCPADDSYFTSFPLPTMPSEAKGFIESGAGQPLGFNAPSNQEFSANATALVSPGPHSVSTTINTNIVQATISQSSTSGSSSGSSSASTTASSSSVSSGSSISSGSSSMSTSYTSASGSSAHSSGSSSGSSSATSSASTFNLSRFYVFAGILAISGLVFA | null | null | cell wall (1->3)-beta-D-glucan metabolic process [GO:0034407]; fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process [GO:0071970]; fungal-type cell wall organization [GO:0031505] | cell surface [GO:0009986]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | 1,3-beta-glucanosyltransferase activity [GO:0042124] | PF03198; | 3.20.20.80; | Glycosyl hydrolase 72 family | PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer. | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:17230583}. Membrane {ECO:0000269|PubMed:17230583}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17230583}. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP). | null | null | null | null | null | FUNCTION: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. {ECO:0000250}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13710 | SMC5_SCHPO | MDGLRPSKRRKSNPLYSDYALGSIVRIKLVNFVTYDYCELFPGPYLNLIIGPNGTGKSTIVSAICIGLGWPPKLLGRAKEAREFIKYGKNTATIEIEMKYRDDETVTITRQISQDKSSSFSINREACATSSITSLMDTFNVQLNNLCHFLPQDRVAEFAQLDPYSRLMETERAIDHEGLLPAHEKLIDLRKREREILQNKNQGQSTLNSLKDRQQALEKEVNIFKEREKIKSYIEMLGLAKMLVIYREKTNVFNQLRADKKKLKKDLKDLVEEFQPILDKGEELRSDLKLKDDTFNDYSSASMELNTSNLRARASFSNFMENEKKLYEKVNTNRTLLRNANLTLNEAQQSVKSLTERQGPRPSDNGVQDLQEKMQEVNAEKLQHENEKLESSHELGSIRTLKAQKLIDLDNIKRELSYYNDATKRKLDFMSSAPGWEDAYQTYQLLKEYESAFEAPAYGPIYMNLKCKEKGFAALIEGFFRTDTFRTFIMSNYNDYLKLMDLITSKTKYTPTIREFSSERKKKIEDFEPPCSREKLQSFGFDGYVIDFLEGPEVVLVALCHMLKIHQIPIAKRELPPASVNALNNFRLANGDPVLKTYLAGSSIHLVFRSAYGDREITRRTDPLPSRSIYFSENVEMDLVKRKEEQLNAQLSQLENLQNEERKLQEKVNEHESLLSRTNDILSTLRKERDEKLIPIHEWQQLQERIEHQTLLLRQREKVPEQFAAEIEKNEDIRKENFEALMNSVLKVKENSIKATNNFEKMLGSRLNVIEAKYKLEKHEMDANQVNARLTEVQDRLKDITDKLASAREDAMSLYGSVVDSLQTQSSDRQTAITELNEEFATSSEVDNKISIEETKLKFMNVNSYVMEQYDARKKEIEELESKMSDFDQSVEELQDEMNSIKEDWVSKLEENVQCISDRFSKGMSGMGYAGEVRLGKSDDYDKWYIDILVQFREEEGLQKLTGQRQSGGERSVSTIMYLLSLQGLAIAPFRIVDEINQGMDPRNERVVHRHIVNSVCDNAVSQYFLVTPKLLPDLTYHRNLKVLCICNGAWLPATFRTSLSTYFEKLKKSALISSS | null | null | double-strand break repair via homologous recombination [GO:0000724]; meiotic cell cycle [GO:0051321] | cytoplasm [GO:0005737]; division septum [GO:0000935]; nucleus [GO:0005634]; Smc5-Smc6 complex [GO:0030915]; spindle pole body [GO:0005816] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; single-stranded DNA binding [GO:0003697] | PF02463; | 3.40.50.300; | SMC family, SMC5 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}. Barrier septum {ECO:0000269|PubMed:16823372}. Chromosome {ECO:0000269|PubMed:16823372}. | null | null | null | null | null | FUNCTION: Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Plays a critical role in meiosis. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13712 | MUG61_SCHPO | MEVPSYFDPDYDPSSLRVVDLRNILTEYQIYYPSTAKKAQLITLFSKLRRAKNGLISMTELQQKNVPPSSRSPRRRVAGVTNNVTARISSKRKINMVDEANDTEISKTSQFEDNVMGMLQDENVQVLNTNTITISEESEFHASKIAKIDSRNEEITHIPFETQTELNAAVVNLDNSMESSFSIVQNLTNKDSSVDTATYDFSAEVGNIVTPASKFLDYDQSYLVNASVSGDPTPVKVLNTTSPKSENPLNQSSFLSFLGENLKPKFTSRSSSVYASPIKSSLNSLECNPSNLLSVRKNFQQSSDSYLKSNKSFDQLNNLVGLSTGNSENFTPENNSFSWTHPKKNSSSPLPQSQSSSIFVEHLNQLYEANASIHRPVNPAFSTNFGLEASNTSTPEKKKFDSQKPDDDSVNEISSDLGLSTTGIDRVEENISLTKDRQPKRPYFSLGSFISLIFSFTKVVNSLWLVLLVVPLLGFVGFWHQEVQRVGFCGVPAEPYPSSLYYLQPGVLRSSIESAYSFAHSLGIEASCQPCPENAECGFNRQLFCKEGLKASFPLLADFGLKPYPRCIPNTVKVNKVEEMVQAFMSIIGKWYYKAPKEFATFESAKNLNGKSFVDNFKDRYYMYKQDIDNVVGLKDFKVYLKTTLNRLYNSKLTRKVLYYLFSPLFTLELWKLRVRGALSKFPTNCLRSVYSHTVSLMKYLTSAVISCWRIYLLIGILAAITGTVVWRIRVYAKKHVVKHGVSVCVSHCIAKLQKTKLKSLTDFSVNPRVEVVQLRSDCFVSGVADDKGLFELVHLPLSIQLEIWEKVVSVLEGMVSVKVWDSERLAKNRAWEWIGVFSDDIAL | null | null | attachment of telomeric heterochromatin to nuclear envelope [GO:0140698]; chromosome segregation [GO:0007059]; meiotic cell cycle [GO:0051321]; nuclear membrane organization [GO:0071763] | chromosome, centromeric core domain [GO:0034506]; chromosome, subtelomeric region [GO:0099115]; endoplasmic reticulum membrane [GO:0005789]; heterochromatin [GO:0000792]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]; nuclear membrane [GO:0031965]; nuclear periphery [GO:0034399] | ATP binding [GO:0005524]; chromatin binding [GO:0003682]; heterochromatin-nuclear membrane anchor activity [GO:0062239] | PF12949;PF09402; | null | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Required for correct meiotic chromosome segregation. {ECO:0000269|PubMed:16303567}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13716 | AGN1_SCHPO | MKLVLFLVLLFSALINLTNADKMVVAHFIVGNTYPYTVSNWEEDIQDAIAVGIDGFALNMGSDAWQVERIEDAYDAAASVSSDFKLFISFDMSIISADADFIEGVVRRFADKPNQLYYDGKVFVSTFAGETDTFGYSDVSTGWDSAVKEPLASAGYPIYFVPSWTSLGQGALEESVADGFLSWNAWPTTDADMNDNDDIGYQNLANSLGKLYVAPVSPWFYTHLSYKNWAYKSDWLIIDRWNEMLSVQPDMIEVLTWNDYGESHYIGNIQGALPAGSEGYVDGFDHTAWRYLMSPYISAYKLGLSEPYINFESLFYWYRPTPKSATATADSLSYPSGGDYMEDEIFVLVYLLQSAEVTVTCGSTTQTFSGVPGVNQFTIPMETNASPSFTVARQGGTLASGTGPEIVDSLSIYNFNAYTGVLYF | 3.2.1.59 | null | cell cycle [GO:0007049]; cell septum edging catabolic process [GO:0030995]; fungal-type cell wall disassembly involved in conjugation with cellular fusion [GO:1904541] | extracellular region [GO:0005576]; mating projection actin fusion focus [GO:1990819]; mating projection tip [GO:0043332] | glucan endo-1,3-alpha-glucosidase activity [GO:0051118] | PF03659; | 3.20.20.80; | Glycosyl hydrolase 71 family | PTM: Not glycosylated. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15194814}. Secreted, cell wall {ECO:0000269|PubMed:15194814}. Note=Associates with the cell wall. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->3)-alpha-D-glucosidic linkages in isolichenin, pseudonigeran and nigeran.; EC=3.2.1.59; | null | null | null | null | FUNCTION: Has a role in cell separation where it is required for the degradation of the cell wall material surrounding the septum (the septum edging) which must be hydrolyzed before full separation of the daughter cells can occur. Hydrolyzes 1,3-alpha-glucan predominantly into pentasaccharides. {ECO:0000269|PubMed:15194814}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13728 | AIN1_SCHPO | MQANQWQSVQNRTFTKWFNTKLSSRDLPSVFDLRKDLSDGILLIQLLEIIGDENLGRYNRNPRMRVHRLENVNKALEYIKSKGMPLTNIGPADIVDGNLKLILGLIWTLILRFTIADINEEGLTAKEGLLLWCQRKTANYHPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIEVEDVCDVDRPDERSIMTYVAEYFHAFSTLDKVETAARRVERFTEVLMSTHDMKIDYESRMKRLLGSIARMQEYWHTVQFENNYTDVKSHSNNFAKFKATEKREWVKEKIDLESLLGTIQTNLKTYQLRKYEPPAGLKIVDLERQWKDFLSEEANQSKLINTHMREIKESMRIAFADRANSFSKMLSTISNEITNLQGDWRDQLDHVEFLQEHLGPLEVELASVKVLYDNCFQAGIEENDYTMFSYEDLEHEFGITANIIANKIKYLENELLEREKRTLSKQELDGITKVFRHFEKKKSNMLNEVEFYAALASLGLVYDTEEGTALFHRAANSEEGVTYERFTEIVMEELEDRDSARQVLYAFCDVADGKSYVTSDDLLRSQVRPNIVKFLECNMNKHSEGLDYLTWIKQLLAEDKEIV | null | null | actin crosslink formation [GO:0051764]; actin cytoskeleton organization [GO:0030036]; actin filament bundle assembly [GO:0051017]; actomyosin contractile ring assembly actin filament bundle convergence [GO:0071520] | actin filament bundle [GO:0032432]; actomyosin contractile ring [GO:0005826]; cell projection [GO:0042995]; cortical actin cytoskeleton [GO:0030864]; mitotic actomyosin contractile ring [GO:0110085]; plasma membrane [GO:0005886] | actin filament binding [GO:0051015]; actin lateral binding [GO:0003786]; protein-macromolecule adaptor activity [GO:0030674] | PF00307;PF08726; | 1.20.58.60;1.10.418.10;1.10.238.10; | Alpha-actinin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11294907}. Note=Localizes to the medial ring in an F-actin-dependent manner. | null | null | null | null | null | FUNCTION: Binds to actin and is involved in actin-ring formation and organization. Plays a role in cytokinesis and is involved in septation. {ECO:0000269|PubMed:11294907}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13734 | SGO2_SCHPO | MSKASLSPNVEDLKKKQIRQYKEIIRISKAQSIRIKELQLENERLLSENIDLRTTAINLEEQLETVQNENEENKTKLAALLNRFHEETDNFLSKLSLCQQEIQDTFKPVEANLAYDVDTDSEDLDEESVVKDTEEIIEQAQHDVSLRNLSGIEDENIIDDGETAINEQKKREANVFSDTQSAPQLKSGKALPADFENPYNLSNSKPVNNNNEDRVEAVTSENKSIDSAPQEKNHEYEIVSPKSLSNKINNQAAAQRRTEEDNANGVAQEENEGSQEAHFHSRIQSDTVIQSTPTKRKWDVDIQNKQINLASAATNVTGYVSETDSRPNRANSLDSAVLLVQSSNKSNRNGHHISDPNLNSSISLKFAPEDTAHNSLTSQENVGPQVTTTSLSNMTVAESPRTDTPREINGLVDSSVTNGNEKFSVEIMNDSNKIGLNPKSFTDEEREILTLFRNPPMRLSSEPPSSNGFSIAHPNNSPLRPPSLQGILNAEDRPYEIEPSRSSFATNDTGSYNNLELLSSVTNLKSPNENDRVTKTQSRRETKVKRRRKARIQETSEESTVVNEPNEKPDGRSRRERKKVNYALPGLRTKLRRNFDLPSDHVKAKKTRRAPKNSENDSATKTETANITSEAPTTSEVTLENSETLNL | null | null | cell division [GO:0051301]; homologous chromosome segregation [GO:0045143]; meiotic sister chromatid cohesion [GO:0051177]; mitotic sister chromatid biorientation [GO:1990758]; negative regulation of mitotic DNA replication initiation [GO:1903467] | chromosome, centromeric region [GO:0000775]; chromosome, subtelomeric region [GO:0099115]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; meiotic spindle [GO:0072687]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721] | chromatin-protein adaptor activity [GO:0140463] | PF07557;PF07558; | null | Shugoshin family | null | SUBCELLULAR LOCATION: Chromosome, centromere {ECO:0000269|PubMed:14730319, ECO:0000269|PubMed:14972679}. Note=Localizes to the centromere. Bub1 is required for centromeric localization (PubMed:14730319). At the onset of anaphase I, Sgo1 decreases markedly (PubMed:14730319). {ECO:0000269|PubMed:14730319}. | null | null | null | null | null | FUNCTION: Involved in chromosome cohesion during mitosis and meiosis by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms. Required for faithful mitotic chromosome segregation and proper kinetochore orientation during meiosis I. In contrast to sgo1, it is dispensable for centromeric protection of rec8 during meiosis I as well as protection of rad21 during mitosis. Required to sense the lack of tension at centromeres during mitosis. {ECO:0000269|PubMed:14730319, ECO:0000269|PubMed:14972679, ECO:0000269|PubMed:16229998}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13736 | SLA1_SCHPO | MANLPIIGIYKVLYSYEPQEINPGEEIPENEREISIVEDEIVCLLEKGEDDWYLVKRNVNSNDDDEEIGIVPSNYITEAEPSTKMKALYDYTQQSVDEISFQADQTLDCYGDTDSDWILVGFNNNFGLAPRNYVEGMDASSAPASQEPSASGVNAPTVSAPNSMVSPPPSFQPPSAAAPATSLPSDYNPPPPPPPPPAVEDQAADANEPDDYYSSGRAVSPEIPPTYTPKQADPLPAPPPPPPPTLPPQSTNTSQLPMPSRNVNNLGSQVNIPPPPATPSQPPRPPTNASTRSTGTSSSMAHSYDSPPSPSSPSDAYGDPNQHLKLRTDSHDDSRAYDSSSSMGNPAYEKWEVREVVGKKKKRTGILAINNKSIVLTFTKTMDAAQVWPVTDLVNYSSERKHVFIEFNSDSGITSLHLHASSNTNADNIIRALGDVAGSARAAGLREIAAASGSPMPKLPSDSALHRLNAASDAAGVNGGRTGDYEMSTVYGDRSARAEDHKPKDSSAGQKMGTVLYDFIAEAADELTVKANMRVVIVNDTASSDWWKCSVDGKEGVVPSNFIKPDTEGDAKSPPSSSKSGQGSSLSRRASKHESKHKRDSKHEARPESKHESHRESKSAEKDKKDKKDKKEDSKRSRSHSVSKPDSSKLRTWTDRTGAFKVEAEFLGYSDDKIHLHKTNGVKISVPSAKMSYKDLDYVELMTGKKVYSRTERKKDTQKQSHDHGHSHSKSHDREKEKEKKKDREHRKHRETEEEDEGPPPQPARPESTRPALAPPSSSHSNDKYDVIQERPKISYDWFDFFLRCGVDFTVCNRYTHNFNNEHLDEACIPSLNPDTLRTLGLKEGDIIRVMNHVNELNGVSTKPASAITPETKSTVNQIMSGGEALAAPVAVPAPIPAPVAEPAPPAAPAKEVVEKAPSPPATRPKSTTPQKFDDDAWANKPVTEPPVRASSVTVEPARVTESMNKMNISEEAKKPEAPSRPRTAPIPEPEEQKKAPVEKKDAEKSVQAPIPAQPTGNITIQNAYFTAPQPMAADPFQSPLYVQPTGFQPPPSALPIQPTGYMQPIPVQATGYQPLMVQPTGLQPHMTGVMPQVTGVMPQMTGVVPQMTGVMPQMTGVQVQKTGAMPQQPVNYGYQVAGMQPQATGIISQPTGIRAQATGIMTQPTGLHTQATGMMQPTGMQPQATGIMPQATGMMQPTGMQPQVTGIMPQSMPMQPQMTGVQVQKTGMVAQPMLSQYTGYQQNYTPTAMPAADGYGMQPSMNDTQAYYNMNAQTPVNYGFAGGQDTSFGYEQQQMYSPMQQQQQQYYGTEMQPDMGYQQPMMSNYYDPMQMQQQTPYGYNQTGMEGYSEYGYAQPAGNMANPMSYDPVSNASLYMPSDYNQQTQPANYYDSSFGGAQGANEAGKKASIYQATPDNPFGF | null | null | actin cortical patch assembly [GO:0000147]; endocytosis [GO:0006897]; regulation of actin filament polymerization [GO:0030833] | actin cortical patch [GO:0030479]; cell division site [GO:0032153]; cell tip [GO:0051286]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; nuclear pore [GO:0005643]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037] | actin binding [GO:0003779]; identical protein binding [GO:0042802]; protein-macromolecule adaptor activity [GO:0030674]; ubiquitin binding [GO:0043130] | PF08226;PF00018;PF03983; | 2.30.29.30;2.30.30.40;2.30.30.700;1.10.150.50; | SLA1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, actin patch {ECO:0000269|PubMed:16823372}. Note=Cytoplasmic and cortical actin patches. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization (By similarity). {ECO:0000250}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13759 | CSX1_SCHPO | MSIDCLYRRSSLFDTSFVPLHSSIPATSKMSASNSDVNAPISPVVDEGKSELVSPTLERLVAPFNCSPSSTPLQDVAGVGSKMSDTLWMGDLEPWMDATFIQQLWASLNEPVNVKVMRSKASSSETLISYCFVQFSSSAAAERALMKYNNTMIPGAHCTFKLNWATGGGIQHNNFVSRDPEFSIFVGDLLPTTEDSDLFMTFRSIYPSCTSAKIIVDPVTGLSRKYGFVRFSSEKEQQHALMHMQGYLCQGRPLRISVASPKSRASIAADSALGIVPTSTSNRQPNQDLCSMDPLNTTVFVGGLASNLSEKDLQVCFQPFGRILNIKIPFGKGCGFVQYSEKSAAEKAINTMQGALVGTSHIRLAWGHNTLPVSALSQSQSQVSDEGFDRTLSANQIFGMNQSVIGANSGSSNSSGSSLKSAPVSPRTAAAQSLLPNSVVSSINGMNSVNFSTISPPPLSRSASISPTLSGSGSGLTPLSSHFPSAATGLVGGQVYPQSSVLQSSKINGSAKVQPSVKLPEWLQPFSGNNHNSFATQDLLTRVSSLKLVDDEQPASLNGSAFQARASRPWNLGRERQSSLIDLRHELEQNENGLEKSGFGLNLRGRLPPRSYSTFNCTGQYLQPSLRLSRDS | null | null | 3'-UTR-mediated mRNA stabilization [GO:0070935]; cellular response to oxidative stress [GO:0034599]; mRNA splice site recognition [GO:0006376]; positive regulation of gene expression [GO:0010628]; regulation of mRNA stability involved in response to oxidative stress [GO:2000815] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; ribonucleoprotein complex [GO:1990904] | mRNA binding [GO:0003729]; RNA binding [GO:0003723] | PF00076; | 3.30.70.330; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14633985, ECO:0000269|PubMed:16823372}. | null | null | null | null | null | FUNCTION: Regulates global gene expression after oxidative stress. Interacts and stabilizes atf1 and pcr1 mRNAs after oxidative stress, thus controlling their turnover. {ECO:0000269|PubMed:14633985}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13766 | MDE10_SCHPO | MRLVLLFSCVLAVSSYAEIILAHSDENLLSRTKNNLSKWNENRLYDYGSKSTMSLPVSSLFPALQTLWIGVVADCSYVTHFTSRMEAKKHIFQEFEGVSTLYEDSFNINVQIHSLILPSAHDCSANVVDRPEISMSPRISIEEKLEIFSKWKYESPGNNVFEAISPHERESFPSEPQVSVLFTSSVKRSPHGVSWFATICSETHIENEWHVGPLSVVSAYPNDRLVVAHEIGHILGLIHDCNKKSCGDHSEACCPLSSSLCDAQELYIMNPSNSYTYANLRFSDCSILQLHSLVEKKYVSLSCLSKPSEKSVLRLGTCGNGIVEDGEECDCGEDCENNPCCDGKTCKLTKGSLCDDQQDACCYQCHFKNAGTLCRQSTNPCDKPEFCTGISSKCPVDENWDDGRICQDSLGMGSCASGVCTSASRQCKKLTNFSSLSCHSDSCKVSCQNEDGTCFISAKDYIDGTRCRGGLCYNGVCVPIEGSSASWSKQPSLFCASGTMLISLAVIAWFFW | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | ascospore wall assembly [GO:0030476]; membrane protein ectodomain proteolysis [GO:0006509]; proteolysis [GO:0006508] | ascospore wall [GO:0005619]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270] | PF00200;PF13688; | 3.40.390.10;4.10.70.10; | null | PTM: Glycosylated. {ECO:0000269|PubMed:14871934}. | SUBCELLULAR LOCATION: Endoplasmic reticulum. Spore wall. Note=Endoplasmic reticulum during meiosis. Located at the spore rim at the end of meiosis. | null | null | null | null | null | FUNCTION: Has a role in the development of the spore envelope. {ECO:0000269|PubMed:14871934, ECO:0000269|PubMed:16303567}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13768 | ERCC3_SCHPO | MSLKRKNNAREGTPDEDLEEYSDYSDVDNYGEEDDDSYKPAPRIRINNNKTKAQTTTNSNEARQSGISAMFGQNDFSNLLGLKLDHTARPLWINPIDGRIILEAFSPLAEQAIDFLVTISEPVSRPAFIHEYRITAYSLYAAVSVGLKTEDIIAVLDRLSKTPIPPSIVDFIRACTVSYGKVKLVLKKNRYFIESGDASVLRLLLRDPVIGPLRIDYSTQSSKQKSSKPSNEDNVEDKKDITNDSSKETAEKSSSDELFSAVVGLQEEEDDEDAVHLFEIKHSSVETIKKRCAEIDYPLLEEYDFRNDNINPDLPIDLKPSTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKTLVGITAACTIKKSVIVLCTSSVSVMQWRQQFLQWSNIKPDHIAVFTADHKERFHSEAGVVVSTYSMVANTRNRSYDSQKMMDFLTGREWGFILLDEVHVVPAAMFRRVVTTIAAHTKLGLTATLVREDDKIDDLNFLIGPKMYEANWMDLAQKGHIAKVQCAEVWCAMTTEFYNEYLRENSRKRMLLYIMNPKKFQACQFLIDYHEKRGDKIIVFSDNVYALRAYAIKLGKYFIYGGTPQQERMRILENFQYNELVNTIFLSKVGDTSIDLPEATCLIQISSHYGSRRQEAQRLGRILRAKRRNDEGFNAFFYSLVSKDTQEMYYSSKRQAFLIDQGYAFKVITNLKGMENLPNLAYASKAERLELLQEVLLQNEEAADLDDGEDTSFGSRSLSRAPAKAKRSSGSLSTLAGADNMAYVEYNKSANKQLKKDSKEHHALFRKHLYTKRR | 5.6.2.4 | null | transcription initiation at RNA polymerase II promoter [GO:0006367]; transcription-coupled nucleotide-excision repair [GO:0006283] | nucleotide-excision repair factor 3 complex [GO:0000112]; nucleus [GO:0005634]; transcription factor TFIIH core complex [GO:0000439]; transcription factor TFIIH holo complex [GO:0005675]; transcription preinitiation complex [GO:0097550] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; RNA polymerase II general transcription initiation factor activity [GO:0016251] | PF16203;PF13625;PF04851; | 3.40.50.300; | Helicase family, RAD25/XPB subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889}. | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000305|PubMed:15937491}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4; Evidence={ECO:0000305|PubMed:15937491}; | null | null | null | null | FUNCTION: Probable ATP-dependent 3'-5' DNA helicase/translocase (Probable) (PubMed:15937491). Binds dsDNA rather than ssDNA, unzipping it in a translocase rather than classical helicase activity (By similarity). Component of the general transcription and DNA repair factor IIH (TFIIH) core complex. When complexed to CDK-activating kinase (CAK), involved in RNA transcription by RNA polymerase II. Also involved in transcription-coupled nucleotide excision repair (NER) of damaged DNA. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment (By similarity). The ATPase activity of XPB/ptr8, but not its helicase activity, is required for DNA opening (PubMed:15937491). In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of XPB/ptr8 is required for promoter escape but not for promoter opening (PubMed:15937491). Plays a role in mRNA export (PubMed:15937491, PubMed:17212653). {ECO:0000250|UniProtKB:Q00578, ECO:0000269|PubMed:15937491, ECO:0000269|PubMed:17212653, ECO:0000305|PubMed:15937491}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13788 | SSR1_SCHPO | MSNVTENKHDLHENGVPDSAQPMELDVSKKEDTEPEVRDEAKEFLLSQLPQVEVPEWAQWFDFSKVHEIEKKQNPEFFDGKNTSKTPEVYKEYRDFMISTFRLNSKVYLTFTACRRNLAGDVCAVLRVHRFLEQWGLINYNVNPDTRPSKIGPPSTSHFQILADTPRGLVPLLPPPSSSIPRSKAVTIEDPSIVRTNIYDPSLDDVLKGKGSTPNQKPSLSNLHENNIDQSDSPQHCYCCGNKFNESYYQSQTAQKYNVCISCYQQNRFPSPTTIADYKEVAIQNKIEDDDTWTAQELVLLSEGVEMYSDDWAKVASHVNTKSVEECILKFLNLPSSDKALFKMDKVHTNPVVDSLQGKNPILSVVSFLAKMVPPSSFTQKSSAKEEESDKVKGESVYPKPESESYDVEMNGKSLEDSDSLSELYLTNEEKKMASIIKDSVNVQIKLIESKLSHFDYLDQHIRLKSQELDAFAQATYREKLYMKRECQNARKKIEQQLQSKDTAANGLPVQSSAETSVIPASSMSPS | null | null | chromatin remodeling [GO:0006338]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription initiation-coupled chromatin remodeling [GO:0045815] | chromatin [GO:0000785]; cytosol [GO:0005829]; nBAF complex [GO:0071565]; npBAF complex [GO:0071564]; nucleus [GO:0005634]; RSC-type complex [GO:0016586]; SWI/SNF complex [GO:0016514] | DNA binding [GO:0003677]; histone binding [GO:0042393]; nucleosomal DNA binding [GO:0031492]; zinc ion binding [GO:0008270] | PF00249;PF04433;PF16495; | 1.10.10.60;1.10.10.10; | SMARCC family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:16823372}. | null | null | null | null | null | FUNCTION: Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. Controls particularly membrane and organelle development genes. Part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. {ECO:0000269|PubMed:18622392}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13790 | CUL1_SCHPO | MTTLNTNDKDLPIVKKYDSLNGTWDFLKTGVSQIFERLDEGMTITKYMELYTAIHNYCADASKTITVDNFNDQTANVLGEALYNNLVLYLEEYLARLRKECISQTNHEEQLAAYAKYWTRFTTSARFINHLFGYLNRYWVKLKNRFTETLVYDIYTLCLVSWHHHVFSHIRDSLLQNLLYMFTKKRLYEPTDMKYVEVCVDSITSLSFDKTDMTKPNLSSYKTFFETNFIENTKNFYAKESSEYLASHSITDYLKKAEIRLAEEEELVRLYLHESTLKPLLEATEDVLIAQHEEVLHNDFARMLDQNCSEDIIRMYRLMSRTPNGLQPLRQTFEEFVKRSGFAAVAKIVPQVGGEADVDPKEYMEMLLSTYKASKELVNTAFHGDTDFTKSLDTAFRELVNRNVVCQRSSSRSPELLAKYADSILRKSNKNVDIDDVEDCLSSIIIIFRYVEDKDVFQNFYTKLLAKRLVNGTSNSQDAESSMLSKLKEVCGFEYTSKLQRMFQDISLSQEITEAFWQLPQSRAGNIDFSALVLGTSFWPLSPNNVNFHLPEELVPLYEGFQNYYYSCHNGRKLSWLFHLSKGEIKARINPQTNVTYVFQVSTYQMGVLLLYNHRDSYTYEELAKITGLSTDFLTGILNIFLKAKVLLLGDNDKLGDPNSTYKINENFRMKKIRVQLNLPIRSEQKQESLETHKTIEEDRKLLLQSAIVRIMKARRTLKHVVLVKETIDQIKSRFTPKVSDIKQCIDMLIEKEYLERQGRDEYIYLA | null | null | cell cycle [GO:0007049]; cell division [GO:0051301]; protein ubiquitination [GO:0016567]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146] | cytosol [GO:0005829]; nuclear SCF ubiquitin ligase complex [GO:0043224]; SCF ubiquitin ligase complex [GO:0019005] | inositol hexakisphosphate binding [GO:0000822]; protein-macromolecule adaptor activity [GO:0030674]; ubiquitin protein ligase binding [GO:0031625] | PF00888;PF10557; | 1.20.1310.10;1.10.10.10; | Cullin family | PTM: Neddylated; enhancing the ubiquitin-ligase activity. {ECO:0000250|UniProtKB:P47050}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(pop1-pop2) is required for the maintenance of ploidy and directs ubiquitination of cig2. {ECO:0000269|PubMed:9990507}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13795 | POF8_SCHPO | MFVPRQLNVRKIKAFTGKENNSIADGNNNKLKDEHYKHNEASKEPSHSISGGLMLNQQDRQLIEPLNPDFLSAVDSILEIYFHRERQKEKVHLAFLIQQDDFWKGIRPNPTQNNLKYALSYVTNALFHFDNSSHMVIRNENIVLPLDIPLYDRIIYVEPVPATLSNKSLLLAGKLRKYLKEFLPYVDAIGTPEGYAFVILYKKVDQSALSKLPVPPGWVLLTRKEWTNREEKYFENQLHLVKASSSDVSNSSNSFPENRYPKLTKVEKQMTKSVSKTSQTDKDEDNLDFTKNLLTRIKNLHPLTNKSTIHSLLSYVFSRQTQNIACEPMYIDYRKDETEAIIRWKTPLHAETCINAFRTQERKQNSHDDIRAHRKKGSSRPFLIAELITGEEEKNYWRMLKK | null | null | nuclear RNA surveillance [GO:0071027]; snRNA processing [GO:0016180]; telomerase catalytic core complex assembly [GO:1904868]; telomerase RNA stabilization [GO:0090669]; telomere maintenance via telomerase [GO:0007004] | chromosome, telomeric repeat region [GO:0140445]; cytosol [GO:0005829]; nucleus [GO:0005634]; sno(s)RNA-containing ribonucleoprotein complex [GO:0005732]; telomerase holoenzyme complex [GO:0005697] | chromatin binding [GO:0003682]; telomerase RNA binding [GO:0070034] | PF19977; | 3.30.70.330; | LARP7 family | null | SUBCELLULAR LOCATION: Chromosome, telomere {ECO:0000269|PubMed:29422503}. Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}. | null | null | null | null | null | FUNCTION: RNA-binding protein required for assembly of the holoenzyme telomerase ribonucleoprotein (RNP) complex (PubMed:29422501, PubMed:29422503, PubMed:29422664). Specifically binds telomerase RNA ter1 and promotes assembly of ter1 with catalytic subunit trt1 (PubMed:29422501, PubMed:29422503). Telomerase is a ribonucleoprotein enzyme essential that copies new telomeric repeats onto chromosome ends and functions to maintain cell division (PubMed:29422501, PubMed:29422503, PubMed:29422664). {ECO:0000269|PubMed:29422501, ECO:0000269|PubMed:29422503, ECO:0000269|PubMed:29422664}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13799 | YE02_SCHPO | MSENSTDSKNFQFSEGSRESSNDELKVLLRDTETKEDEKSSFSNSEEESIIENLSDSSVNKEYAKNSLKLSDAVSESKYLNPLLKDKRHDRSFALHKVVVPDDYDYIPLNKHIPSDPPAKTYPFELDPFQSTAIKCVERMESVLVSAHTSAGKTVIAEYAIAQALKNRQRVIYTSPIKSLSNQKYRELLSEFGDVGLMTGDVSINPSASCLIMTTEILRAMLYKNSEIMHEIAWVIFDEVHYMRDKDRGVVWEETLILLPDAIRFIFLSATLPNALQFARWISEIHKQPCHVVYTDYRPTPLQHFIYPQGADGIYMLVDEKNKFKTENFKKVLEVLDHSTRQENYSKSSKKVKKSSSLERIINMVLSNRYDPIIVFCFSKKECEINAHQFGKLDLNDTENKELVTEIFDSAINQLSEEDRGLRQFEEMRSLLLRGIGIHHSGLLPILKELVEILFQEGLVRILFATETFSIGLNMPARTVLFTKAQKFSGNNFRWLTSGEYMQMSGRAGRRGIDTKGLSIVILDQSIDEQAARCLMNGQADVLNSAFHLSYGMILNLMRIEEISPEDILKKSFYQFQNMESLPLIKEELMQLKNEETSINIPNETAVKEFHDLKLQLEKYGEEIQKVMTHPDNCLPYLQSGRLIQIKLGGIIFPWGVLVNVIKREFDPNTREQVAPHETYVLDVLLPISSNSMSNHKVNPSILVPPRPNETPLYEIVSVLLTAVCNISSIRIYMPRELNSNESKLRAYRRVNEVIEEFKEIPYLDPLEHMHIESSTLSLSLRKLEILEPKLFDSPYYKDSKHRAEYHEFRKKLNLRAQIKDISTKITNTEAIIQLRELKIRQRVLRRLGFCTLENVIDIKGRVACEITSGDELLLVELIFQGFFNQMPPEEIAAALSCFVYEDKSEVSTLNLKEPFKKMYLTIIEAAKRIATVSLESKLQFNESDYLHQFKPDIMEPVSLWINGASFQEICIVSKLYEGSIVRTFRRLDELLKQLEHAAIVLGNNELKEKSVLTEQKLHRDIIFSASLYL | 3.6.4.- | null | maturation of 5.8S rRNA [GO:0000460]; nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts [GO:0033621]; RNA catabolic process [GO:0006401]; siRNA-independent facultative heterochromatin formation [GO:1902794]; sno(s)RNA processing [GO:0043144] | heterochromatin island [GO:1990342]; MTREC complex [GO:1990477]; nuclear body [GO:0016604]; nucleolus [GO:0005730]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724] | PF00270;PF08148;PF21408;PF13234; | 1.10.3380.30;1.20.1500.20;2.40.30.300;3.40.50.300; | Helicase family, SKI2 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. | null | null | null | null | null | null | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13801 | DRI1_SCHPO | MSKLPSPTMPLPESVGDLVVLHFETNLDDHGISIGRAPCEIHEICWVILDGKTLEKQHCESCSIREDSSRHGICGSASSLTEAIFTLDNSIQERLNFQGKPFTFVVMNGRELRVLLPKEARDQGITLPSYMRHPRLFDLSSEYAKWQIRMGAVPPYTITLSHIFGKLDVDSLPPITESKAIELSPSDAPYITKGLTQCWRLANATTLLLRKAEKDSRGHSLPSVLTQPINCQADARSFYAERSKIVHVAGLTNDVTQLELESWFTNHGVHPVALWTLKTPEPYKSTGTGFVLFASHEDAADALAFNGYCLGDRMLEIIPSSTKVLDKASDILIPFPSSKNRPRPGDWNCPMCGFSNFQRRTSCFRCSFPGPTHVSAATGSNTFSPDFPYGNSYGNGSSHFIANYGGSVHHSNENTMQSDLQHQNGNNAVNHHHSSRSFGGNVPFRAGDWKCGSEGCGYHNFAKNVCCLRCGASRATAAVVADHASGPVNGSYSHNSYSHIPPVMSTSPPNHSVYPYSQLSINSVTANHGQNFGGQNGGNVSRFDDHGRFKEVSRPSVTTDQGDWLCECGFTNFRRRSNCLRCNAPHYSNMQIPASLPSDFNAYV | null | null | cellular response to temperature stimulus [GO:0071502]; chromatin organization [GO:0006325]; regulation of heterochromatin formation [GO:0031445]; regulatory ncRNA-mediated gene silencing [GO:0031047] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein aggregate center [GO:0140453] | metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; RNA binding [GO:0003723] | PF00076;PF00641; | 3.30.70.330;3.30.420.10;4.10.1060.10; | null | null | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:33693625}. Nucleus {ECO:0000269|PubMed:33693625}. | null | null | null | null | null | FUNCTION: Mediates heterochromatin assembly by promoting RNAi-mediated heterochromatin silencing and histone deacetylation (PubMed:33693625). Binds pericetromeric transcripts and recruits the RNA-induced transcriptional silencing (RITS) complex to heterochromatin (PubMed:33693625). Recruits sir2 to chromatin to promote deacetylation of 'Lys-9' of histone H3 (PubMed:33693625). {ECO:0000269|PubMed:33693625}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13807 | DDB1_SCHPO | MTYVTYLHKPSSIRNAVFCKFVNASSWNVIVAKVNCLEVYSYENNRLCLITSANIFAKIVNVKAFKPVSSPTDHIIVATDSFRYFTLFWDANDNTVSNGIKIQDCSERSLRESQSGPLLLVDPFQRVICLHVYQGLLTIIPIFKSKKRFMTSHNNPSLHDNFSVRIQELNVVDIAMLYNSSRPSLAVLYKDSKSIVHLSTYKINVREQEIDEDDVVCHDIEEGKLIPSENGGVFVFGEMYVYYISKDIQVSKLLLTYPITAFSPSISNDPETGLDSSIYIVADESGMLYKFKALFTDETVSMELEKLGESSIASCLIALPDNHLFVGSHFNNSVLLQLPSITKNNHKLEILQNFVNIAPISDFIIDDDQTGSSIITCSGAYKDGTLRIIRNSINIENVALIEMEGIKDFFSVSFRANYDNYIFLSLICETRAIIVSPEGVFSANHDLSCEESTIFVSTIYGNSQILQITTKEIRLFDGKKLHSWISPMSITCGSSFADNVCVAVAGGLILFFEGITEVGRYQCDTEVSSLCFTEENVVYVGLWSADIIMLTYCQDGISLTHSLKLTDIPRSIVYSQKYGDDGGTLYVSTNNGYVLMFNFQNGQVIEHSLRRNQLGVAPIILKHFDSKEKNAIFALGEKPQLMYYESDKLVITPLSCTEMLNISSYVNPSLGVNMLYCTNSYISLAKMSEIRSLNVQTVSVKGFPRRICSNSLFYFVLCMQLEESIGTQEQRLLSFLRVYEKNTLSEIAHHKFNEYEMVESIILMNDDKRVVVGTGFNFPDQDAPDSGRLMVFEMTSDNNIEMQAEHKVQGSVNTLVLYKHLIVAGINASVCIFEYEHGTMHVRNSIRTPTYTIDISVNQDEIIAADLMKSITVLQFIDDQLIEVARDYHPLWATSVEILSERKYFVTEADGNAVILLRDNVSPQLSDRKKLRWYKKFYLGELINKTRHCTFIEPQDKSLVTPQLLCATVDGSLMIVGDAGMSNTPLLLQLQDNIRKVIPSFGGLSHKEWKEYRGENETSPSDLIDGSLIESILGLREPILNEIVNGGHEGTKLDISVQDLKSIIENLEKLHP | null | null | cell cycle [GO:0007049]; DNA repair [GO:0006281]; double-strand break repair via homologous recombination [GO:0000724]; nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts [GO:0033621]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]; transcription-coupled nucleotide-excision repair [GO:0006283] | Cul4-RING E3 ubiquitin ligase complex [GO:0080008]; cytosol [GO:0005829]; Ddb1-Ckn1 complex [GO:0070912]; Ddb1-Wdr21 complex [GO:0070913]; nucleolus [GO:0005730]; nucleus [GO:0005634]; site of double-strand break [GO:0035861] | DNA binding [GO:0003677] | PF03178;PF10433; | 1.10.150.910;2.130.10.10; | DDB1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12181326}. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Component of an E3 ubiquitin-protein ligase that includes cul4 (By similarity). Required for ubiquitination and the subsequent degradation of the DNA replication licensing factor cdt1 and of the ribonucleotide reductase inhibitor spd1. Also required for transcription-coupled nucleotide excision repair. {ECO:0000250, ECO:0000269|PubMed:12857752, ECO:0000269|PubMed:14701809, ECO:0000269|PubMed:15805471, ECO:0000269|PubMed:16252005, ECO:0000269|PubMed:16407242, ECO:0000269|PubMed:17039252, ECO:0000269|PubMed:18794354}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13816 | SCC3_SCHPO | MSESVTTGSDDDGGDRESSPVMLSQSFDPMSSSSNSSSEENSDDDYEKTISSKKRHPRPNSKGVNVKRSRRNAIVEEDPQEEIFNNLFAFLLDQKVDTMDIAVSWFADYAKDNQSALANLINFILKCCGCNRAINVFDVQDQDSASATLSQIQLSVERTSTRDYPLNSKNLKFRNFRKRLTGLLSNFVSQLSIRNYLYNSTVFEDIMSWVVAMSSSTMRPIRHTATVFCLNIMTFLCEKSKELLNEHAIATKQLEKEEKRSRVNRNRINELNNSLGEIVKQQDTLTTYLNDYFDSVFVHRYRDVEPKIRVDCLQELGVWINTVPSIFFSGSYLRYLGWMLSDINTTVRLTVVKVLRKFFETDSFIGGLRHFSSRFKERILEMSCVDADIGVRVASIRLCNAMRTCGFLENSEILKVLKLILDINPRVQREAVLFLCKVVDESVNEKIDLWGEEDYILKAFSQTSLTTFSVHWIKFSQMCKLLEEVRLSYQSSFDYDTLLRIFQKNGNFITPITQALLNACEIDSIYQSWEDISNFVLFDNYTSTLKDPIDSILSFCKLNDFQESILLQLLSASIQTVCNNNFITPKTVHNKQAAETTNDQNKDKDLLYLNLLPYINSITERNSASPTLLHDSLRLLFSMDLTEMTDPQLSRHFELLINNLKKFFLTNNDLQIIQGCTILFLRLDSIPALKEDLKLLVTDICDQTVTEFLKNFGSFNIQDAVITKDEFVIFEACLTRIEGCTSLKDFSDYPEFDIIYERLVSLLSRVPNSYEDTLKFSAINTLQSLLFWFFLRKDNPADEEKKKDDETKVFNCLINIMNNDSSKILQLQAARTFLETVIMKEGVKASHYNDDNRVSEEHNFLKPQFLDALLKILEGWLYTYAKVGQFPFKRLTQASSPHTQISLDKNPLNRRLLEHVCCDLTSKLLIVVSLSNTITPEFSQQFCELRGHYGPKLSAIVDEFLN | null | null | cell division [GO:0051301]; chromatin looping [GO:0140588]; chromosome segregation [GO:0007059]; mitotic sister chromatid cohesion [GO:0007064]; sister chromatid cohesion [GO:0007062] | chromatin [GO:0000785]; chromosome, subtelomeric region [GO:0099115]; cohesin complex [GO:0008278]; condensed nuclear chromosome [GO:0000794]; mating-type region heterochromatin [GO:0031934]; mitotic cohesin complex [GO:0030892]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721] | chromatin binding [GO:0003682]; DNA binding [GO:0003677] | PF21581;PF08514; | 1.25.10.10; | SCC3 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750, ECO:0000269|PubMed:11069892}. Chromosome, centromere {ECO:0000269|PubMed:11069892}. Note=Associates with chromatin. Cohesin complex mainly associates with broad centromere region. Also associates with mating-type heterochromatic region. | null | null | null | null | null | FUNCTION: Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the rad21 subunit of the cohesin complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. {ECO:0000269|PubMed:11069892}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13820 | ERG5_SCHPO | MEMNQTETLIPAARNVIRVLGYEIEYSKWTICFALLAVCIAYDQISYQMQKGHIPGPRFKIPFMGSFLDSMKPTFEKYNAKWQTGPLSCVSVFHKFVVIASERDLARKILNSPSYVQPCVVDAGKKILKHTNWVFLDGRDHIEYRKGLNGLFTTRALASYLPAQEAVYNKYFKEFLAHSKDDYAQYMIPFRDINVATSCRTFCGYYISDDAIKHIADEYWKITAAMELVNFPIVLPFTKVWYGIQSRKVVMRYFMKAAAESRKNMEAGNAPACMMEEWIHEMIETRKYKSENKEGAEKPSVLIREFSDEEISLTFLSFLFASQDATSSAMTWLFQLLADHPDVLQKVREEQLRIRKGDIDVPLSLDLMEKMTYTRAVVKECLRLRPPVLMVPYRVKKAFPITPDYTVPKDAMVIPTLYGALHDSKVYPEPETFNPDRWAPNGLAEQSPKNWMVFGNGPHVCLGQRYAVNHLIACIGKASIMLDWKHKRTPDSDTQMIFATTFPQDMCYLKFSPFDASTVDWKNSKEAFSNEAVSAATVETESA | 1.14.19.41 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | ergosterol biosynthetic process [GO:0006696]; sterol metabolic process [GO:0016125] | endoplasmic reticulum [GO:0005783] | C-22 sterol desaturase activity [GO:0000249]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity [GO:0016491] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | null | CATALYTIC ACTIVITY: Reaction=5-dehydroepisterol + H(+) + NADPH + O2 = ergosta-5,7,22,24(28)-tetraen-3beta-ol + 2 H2O + NADP(+); Xref=Rhea:RHEA:33467, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18249, ChEBI:CHEBI:52972, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.19.41; Evidence={ECO:0000305|PubMed:18310029}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33468; Evidence={ECO:0000305|PubMed:18310029}; | null | PATHWAY: Steroid metabolism; ergosterol biosynthesis. {ECO:0000269|PubMed:18310029}. | null | null | FUNCTION: C-22 sterol desaturase; part of the third module of ergosterol biosynthesis pathway that includes by the late steps of the pathway (PubMed:18310029). Erg5 converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. The lanosterol 14-alpha-demethylase erg11/cyp1 catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol. In the next steps, a complex process involving various demethylation, reduction and desaturation reactions catalyzed by the C-14 reductase erg24 and the C-4 demethylation complex erg25-erg26-erg27 leads to the production of zymosterol. Erg28 likely functions in the C-4 demethylation complex reaction by tethering erg26 and Erg27 to the endoplasmic reticulum or to facilitate interaction between these proteins. Then, the sterol 24-C-methyltransferase erg6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase erg2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturases erg31 and erg32 then catalyze the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase erg4 to produce ergosterol (Probable) (PubMed:18310029). In the genus Schizosaccharomyces, a second route exists between lanosterol and fecosterol, via the methylation of lanosterol to eburicol by erg6, followed by C14-demethylation by erg11/cyp1 and C4-demethylation by the demethylation complex erg25-erg26-erg27 (Probable) (PubMed:8586261). {ECO:0000250|UniProtKB:P54781, ECO:0000269|PubMed:18310029, ECO:0000305|PubMed:18310029, ECO:0000305|PubMed:8586261}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13821 | VPS27_SCHPO | MSRWWNSNSQFASDIEKATSETLPAGSEEISLYLEISDQIRSKSVDPKFAMRILKSRIDHSNPNVQIMALKLTDTCVKNGGSGFLLEIASREFMDNLVSILRSPAGIDEDVKMVILRYIQSWALAVPDTNSPLSYIIHVYQNLKDGDYEFPEPSQNITSKFLDTETPPDWTDSEVCLRCRTPFTFTNRKHHCRNCGGVFCNQCSSKTLSLPHLGINQPVRVCDSCYSLRTKPKGSKSRARNERKFHAKTRKTPSKPVTNNEDEDIKRAIELSLKEMPQSREPPSYERPSEANVVISQDQHLTEDEDEELKRAIAISLEEAQKSSQKDDNVTAPNNMNISYPSVPAHTVSTDIRSSPFSGRPSDNPSTLISTADADNITLYATLVQKLKKLPPGSIFTEYQLQELHENMGVMRTRMMRSLGETMSKYNGLIQALQKLQTCMRLNDALIEQRLSSTYAHHYIDSSMDSNRSIEPEPDVISTVRNSSTIPQASSSSVPKIVVDSSPVTENPPSHSDVMGQKDTISSYYSTDTDVSANVMGNRHDEVVFSDTASGEKNTKLNIDESTNYYNTDSIDKVGEPFDEISSGYDDLMNGNDKQGNDIPEVQEASLIEL | null | null | ascospore-type prospore assembly [GO:0031321]; cytoplasm to vacuole targeting by the NVT pathway [GO:0120113]; endocytosis [GO:0006897]; late endosome to vacuole transport [GO:0045324]; protein targeting to vacuole [GO:0006623]; protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043328] | cytosol [GO:0005829]; endosome membrane [GO:0010008]; ESCRT-0 complex [GO:0033565]; fungal-type vacuole membrane [GO:0000329]; nucleus [GO:0005634]; prospore membrane [GO:0005628] | metal ion binding [GO:0046872]; phosphatidylinositol-3-phosphate binding [GO:0032266]; ubiquitin binding [GO:0043130]; ubiquitin-like protein ligase activity [GO:0061659] | PF01363;PF02809;PF00790;PF21356; | 1.20.5.1940;1.25.40.90;6.10.140.100;3.30.40.10; | VPS27 family | null | SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:16823372}. | null | null | null | null | null | FUNCTION: Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane. {ECO:0000269|PubMed:17660439}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13826 | RFP1_SCHPO | MQFNGSNGIDESSVIDLTRSPSPPVETSISSTNIIDLDAIPDDSFPSSPVLSPRRRRMNRRRNERSRNFPSNHLSYLEDMIYLGPQVSTRRSSSRRDLMGMIARTFPEFSSVNSLSPSLFQLIVNRMRFDAIHPEWTNGSDDEYFSNHFEESYDDFTSSLENIKQSYKPPGPPKSGFTRSFNNDTLMVCPRCQEPLGTSKSKEKSALWATKCGHVYCGSCAKVLKTSKRSQSKCLVNDCGRYLNTKNAMWELFY | 2.3.2.27 | null | DNA repair [GO:0006281]; meiotic cell cycle [GO:0051321]; protein ubiquitination [GO:0016567]; stalled replication fork localization to nuclear periphery [GO:0120290]; ubiquitin-dependent protein catabolic process [GO:0006511] | chromatin [GO:0000785]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]; SUMO-targeted ubiquitin ligase complex [GO:0033768] | DNA binding [GO:0003677]; SUMO-ubiquitin ligase activity [GO:0140082]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF14634; | 3.30.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:17762864, ECO:0000269|PubMed:17762865}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Mediates ubiquitination and subsequent desumoylation/degradation of sumoylated proteins and proteins containing SUMO-like domains. Involved in maintaining genome stability where it acts in the cellular response to DNA damage. Has a role in meiosis. {ECO:0000269|PubMed:16303567, ECO:0000269|PubMed:17502373, ECO:0000269|PubMed:17762864, ECO:0000269|PubMed:17762865}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13828 | DCP2_SCHPO | MSFTNATFSQVLDDLSARFILNLPAEEQSSVERLCFQIEQAHWFYEDFIRAQNDQLPSLGLRVFSAKLFAHCPLLWKWSKVHEEAFDDFLRYKTRIPVRGAIMLDMSMQQCVLVKGWKASSGWGFPKGKIDKDESDVDCAIREVYEETGFDCSSRINPNEFIDMTIRGQNVRLYIIPGISLDTRFESRTRKEISKIEWHNLMDLPTFKKNKPQTMKNKFYMVIPFLAPLKKWIKKRNIANNTTKEKNISVDVDADASSQLLSLLKSSTAPSDLATPQPSTFPQPPVESHSSFDIKQKILHLLNEGNEPKSPIQLPPVSNLPLNPPIQSSNSRLSHDNNSFDPFAYLGLDPKNPSASFPRVVSQNNMLTNKPVLNNHFQQSMYSNLLKDQNSVQHLFAASDMPSPMELPSPSTVYHQVFYPPTSTSVSSYGLGKTPQPAYGSSSPYVNGHQTQQISSLPPFQSQTQFLARNSDNSGQSYNSEGDSNSKRLLSMLSQQDTTPSSSTLSKEANVQLANLFLTPNSLETKKFSDNSQGEEISDNLHGESCNNPNANSVHSAQLLQALLHPSATETKEETPKKTSDSLSLLTLLKSGLPTPANDLQNKSQNNERKASSQVKELEVKNYSKSTDLLKKTLRIPRNDEPLEAANQFDLLKVSPQQKSEVPPKRNELSQSKLKNRKKKENSETNKNHVDMSPGFVKILKRSPLADQKKEDTQESDFKGSDDHFLSYLQSVVSSNSNGLH | 3.-.-.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; | deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; methylguanosine-cap decapping [GO:0110156]; mRNA processing [GO:0006397]; nuclear-transcribed mRNA catabolic process, exonucleolytic, 5'-3' [GO:0034428]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; nucleus [GO:0005634]; P-body [GO:0000932]; RNA decapping complex [GO:0098745] | 5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity [GO:0140932]; 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity [GO:0140933]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; mRNA 5'-diphosphatase activity [GO:0034353]; mRNA cap binding [GO:0098808]; single-stranded RNA binding [GO:0003727] | PF05026;PF00293; | 1.10.10.1050;3.90.79.10; | Nudix hydrolase family, DCP2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:23319050}. Note=Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay. {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:23319050}. | null | null | null | null | null | FUNCTION: Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body. {ECO:0000269|PubMed:15671491}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13833 | CID1_SCHPO | MNISSAQFIPGVHTVEEIEAEIHKNLHISKSCSYQKVPNSHKEFTKFCYEVYNEIKISDKEFKEKRAALDTLRLCLKRISPDAELVAFGSLESGLALKNSDMDLCVLMDSRVQSDTIALQFYEELIAEGFEGKFLQRARIPIIKLTSDTKNGFGASFQCDIGFNNRLAIHNTLLLSSYTKLDARLKPMVLLVKHWAKRKQINSPYFGTLSSYGYVLMVLYYLIHVIKPPVFPNLLLSPLKQEKIVDGFDVGFDDKLEDIPPSQNYSSLGSLLHGFFRFYAYKFEPREKVVTFRRPDGYLTKQEKGWTSATEHTGSADQIIKDRYILAIEDPFEISHNVGRTVSSSGLYRIRGEFMAASRLLNSRSYPIPYDSLFEEAPIPPRRQKKTDEQSNKKLLNETDGDNSE | 2.7.7.19; 2.7.7.52 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17353264, ECO:0000269|PubMed:22885303}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17353264}; | mRNA polyadenylation [GO:0006378]; polyuridylation-dependent decapping of nuclear-transcribed mRNA [GO:0036450]; RNA 3' uridylation [GO:0071076] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; poly(A) RNA polymerase activity [GO:1990817]; RNA binding [GO:0003723]; RNA uridylyltransferase activity [GO:0050265]; UTP binding [GO:0002134] | PF01909;PF03828; | 1.10.1410.10;3.30.460.10; | DNA polymerase type-B-like family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12218190}. | CATALYTIC ACTIVITY: Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide; Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395, ChEBI:CHEBI:173116; EC=2.7.7.52; Evidence={ECO:0000269|PubMed:17353264, ECO:0000269|PubMed:17449726, ECO:0000269|PubMed:19430462, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0000269|PubMed:25712096}; CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; Evidence={ECO:0000269|PubMed:12218190, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12 uM for UTP {ECO:0000269|PubMed:22885303}; KM=312 uM for ATP {ECO:0000269|PubMed:22885303}; Note=Mutation of His-336 to Asn decreases the Km for ATP to 65 uM and increases the Km for UTP to 45 uM. {ECO:0000269|PubMed:22885303}; | null | null | null | FUNCTION: Cytoplasmic uridylyltransferase that mediates the terminal uridylation of mRNAs with short poly(A) tails such as such as act1, hcn1 and urg1 mRNAs, hence facilitating global mRNA decay (PubMed:17353264, PubMed:17449726, PubMed:19430462, PubMed:22751018, PubMed:22885303). Uridylates the 3' ends of actin mRNAs upon S-phase arrest (PubMed:17353264). Has also a weak poly(A) polymerase (PAP) activity (PubMed:22751018, PubMed:22885303). Residue His-336 is responsible for the specificity for UTP (PubMed:22751018, PubMed:22885303). Involved in cell cycle arrest where in association with crb2/rhp9 and chk1 it inhibits unscheduled mitosis (PubMed:10757807). {ECO:0000269|PubMed:10757807, ECO:0000269|PubMed:17353264, ECO:0000269|PubMed:17449726, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13836 | DXO_SCHPO | MLREFSFYDVPPAHVPPVSEPLEIACYSLSRDRELLLDDSKLSYYYPPPLFSDLNTGFPNRFHPPKSDPDPISIVKDVLMTKGIQMNSSFLTWRGLITKIMCAPLDPRNHWETYLVMDPTSGIIMMEERTRSETSYANQDRMCYWGYKFEAISTLPEIWDACSRDQIEQRDNQDVVPDEQYCSIVKINIGKSKLILAGEVDCIWDKKPCSAKESDVHSDDGTIEEDASNAENPNLHYVELKTSKKYPLENYGMRKKLLKYWAQSFLLGIGRIIIGFRDDNGILIEMKELFTHQIPKMLRPYFKPNDWTPNRLLVVLEHALEWIKQTVKQHPPSTEFTLSYTGGSKLVLRQII | 3.6.1.- | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:19194460}; Note=Divalent metal cation. {ECO:0000269|PubMed:19194460}; | cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000448]; mRNA processing [GO:0006397]; NAD-cap decapping [GO:0110155]; nuclear-transcribed mRNA catabolic process [GO:0000956]; nucleic acid metabolic process [GO:0090304] | cytosol [GO:0005829]; Las1 complex [GO:0090730]; nucleus [GO:0005634] | 5'-hydroxyl dinucleotide hydrolase activity [GO:0140432]; GDP binding [GO:0019003]; metal ion binding [GO:0046872]; mRNA 5'-diphosphatase activity [GO:0034353]; phosphodiesterase decapping endonuclease activity [GO:1990174]; RNA binding [GO:0003723]; RNA NAD-cap (NAD-forming) hydrolase activity [GO:0110152] | PF08652; | null | DXO/Dom3Z family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53063}. | CATALYTIC ACTIVITY: Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + H(+) + NAD(+); Xref=Rhea:RHEA:60880, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:15698, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:138282, ChEBI:CHEBI:144029; Evidence={ECO:0000269|PubMed:28283058}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60881; Evidence={ECO:0000269|PubMed:28283058}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside-ribonucleotide in mRNA + H2O = a (N(7)-methyl 5'-triphosphoguanosine)-nucleoside + a 5'-end phospho-ribonucleoside in mRNA + H(+); Xref=Rhea:RHEA:66928, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17313, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:138282, ChEBI:CHEBI:172876, ChEBI:CHEBI:172877; Evidence={ECO:0000250|UniProtKB:P53063}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66929; Evidence={ECO:0000250|UniProtKB:P53063}; CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + diphosphate + H(+); Xref=Rhea:RHEA:78683, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:138282, ChEBI:CHEBI:167618; Evidence={ECO:0000269|PubMed:19194460}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78684; Evidence={ECO:0000269|PubMed:19194460}; | null | null | null | null | FUNCTION: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (PubMed:28283058). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs (By similarity). In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs and mediates their subsequent degradation (PubMed:28283058). Specifically degrades pre-mRNAs with a defective m7G cap and is part of a pre-mRNA capping quality control (PubMed:28283058). Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1) (PubMed:28283058). Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates (PubMed:19194460). Stimulates exoribonuclease activity of dhp1, allowing it to degrade RNAs with stable secondary structure more effectively (PubMed:19194460). {ECO:0000250|UniProtKB:O70348, ECO:0000250|UniProtKB:Q06349, ECO:0000269|PubMed:19194460, ECO:0000269|PubMed:28283058}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13837 | GABAT_SCHPO | MSSTATVTESTHFFPNEPQGPSIKTETIPGPKGKAAAEEMSKYHDISAVKFPVDYEKSIGNYLVDLDGNVLLDVYSQIATIPIGYNNPTLLKAAKSDEVATILMNRPALGNYPPKEWARVAYEGAIKYAPKGQKYVYFQMSGSDANEIAYKLAMLHHFNNKPRPTGDYTAEENESCLNNAAPGSPEVAVLSFRHSFHGRLFGSLSTTRSKPVHKLGMPAFPWPQADFPALKYPLEEHVEENAKEEQRCIDQVEQILTNHHCPVVACIIEPIQSEGGDNHASPDFFHKLQATLKKHDVKFIVDEVQTGVGSTGTLWAHEQWNLPYPPDMVTFSKKFQAAGIFYHDLALRPHAYQHFNTWMGDPFRAVQSRYILQEIQDKDLLNNVKSVGDFLYAGLEELARKHPGKINNLRGKGKGTFIAWDCESPAARDKFCADMRINGVNIGGCGVAAIRLRPMLVFQKHHAQILLKKIDELI | 2.6.1.19 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P17649}; | gamma-aminobutyric acid catabolic process [GO:0009450]; glutamate decarboxylation to succinate [GO:0006540] | cytosol [GO:0005829]; mitochondrion [GO:0005739] | 4-aminobutyrate transaminase activity [GO:0003867]; 4-aminobutyrate:2-oxoglutarate transaminase activity [GO:0034386]; pyridoxal phosphate binding [GO:0030170] | PF00202; | 3.90.1150.10;3.40.640.10; | Class-III pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinate semialdehyde; Xref=Rhea:RHEA:23352, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57706, ChEBI:CHEBI:59888; EC=2.6.1.19; Evidence={ECO:0000269|PubMed:17355287}; | null | null | null | null | FUNCTION: Required for the degradation of gamma-aminobutyric acid (GABA), which is important for utilization of GABA as nitrogen source. Deaminates GABA to succinate-semialdehyde, which in turn is converted to succinate by the succinate semialdehyde dehydrogenase. Cannot transaminate beta-alanine (BAL). {ECO:0000269|PubMed:17355287}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13838 | NUP40_SCHPO | MSFGGSGSITNRSTLKPLSVDDLRSPSPQKEYRGFRTSVSNIPQEKKFVPSHLSHFGSSQQRRFAPEVSSPLAEPYESSSSFRLSLSSPPSSKFGGPSFGTPKPFLHTNRLGTGSLIEDAPPTQSIYDFSSSRQINALNVGQSSSPFSPVSEKVYDPSFTMSGAPQDSNTSVIVFGFPPELTNQVIAEFSRFGTIISENSLTASSAGFTPSKGPISGNWLQLTYAEPSSAAKAVLSNGMLINDSFMVGCIYSPAEAKEHVPKTLRNSNKDLEMTDASSSETSMSIPVHADAHFQSQSGLGKKVIVQHKNDIFKSSQKHQPRNWLFHYLFGFGSTEPIDEEEKSKTASDNTSLQTSLFGKIVQVVLHTLFGF | null | null | mRNA transport [GO:0051028]; NLS-bearing protein import into nucleus [GO:0006607]; nuclear pore organization [GO:0006999]; ribosomal subunit export from nucleus [GO:0000054] | nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]; nuclear pore central transport channel [GO:0044613]; nuclear pore nuclear basket [GO:0044615] | nucleic acid binding [GO:0003676]; phospholipid binding [GO:0005543]; structural constituent of nuclear pore [GO:0017056] | PF05172; | 3.30.70.330; | null | null | SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Biased towards cytoplasmic side. | null | null | null | null | null | FUNCTION: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). {ECO:0000269|PubMed:15116432}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13839 | FIN1_SCHPO | MEKYKILECIGHGSFGRIYKVQRLKDGALLAQKEIHFGNITRQEKQYIADEVNILRNLKHPNIVQYCGEELNRSAQVINLYMEYCGHGDLANLIQRYKEEKKRFTEQEVLKFFTQLLLALYRCHYGENAPACDSQWPREIFHPKQSVLHRDIKPANIFLDENNSVKLGDFGLSKLLDNTRVFTQSYVGTPYYMSPEIIRSSPYSAKSDVWALGCVIFEICMLTHPFEGRSYLELQRNICQGNLSCWDHHYSDDVFLLIRHCLEVNSDLRPTTYQLLRSPILSDIRSKLESERVVLEQSDLLHKKHQMLIQLENDLQFREQRLSARESELENVIASRLAQREEILRRELEKQLRDMDARYQRHMQTVVNSMQKMRVTSPVDHNEQPESSTAEMFVDCTIEASQSPLLHIPKLGISKPLQTLSCPGFTLTTQQPILKRPTLRKELSSRALHTTATLMKYRANASSLRTTPIDKDGQITSLQQKNGTSNQVADCMNKLLHTSLDGKKLSPSELCNKFSDGEGLPNRKVSKLSVESDETAVSASSGESVPTDSTLTDTKSKSVFVHPPSPQSLYVEKLEKLNIRSDEVSKPSKASKTLHGYALPSLASPYDVHAEEKIARENEMDGNFKTMKINQHPDEYVLRTPKKIQLLEGQKRSPVKQLGRLGYNKLRRSAMDNAGLELRKAASTSNYTSLQSRTLPGSWRDDEEEIPRPFLRKMLDARMMRA | 2.7.11.1 | null | cell division [GO:0051301]; chromosome segregation [GO:0007059]; negative regulation of septation initiation signaling [GO:0031030]; nuclear envelope organization [GO:0006998]; phosphorylation [GO:0016310]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitotic spindle [GO:0072686]; mitotic spindle pole body [GO:0044732]; nuclear envelope [GO:0005635]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, NIMA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:11927555}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; | null | null | null | null | FUNCTION: Promotes chromosome condensation and nuclear envelope dynamics during mitosis. Activity appears at metaphase-anaphase transition. {ECO:0000269|PubMed:11927555}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13842 | CDA1_SCHPO | MYETRDLTGNAGKPVDTNPWPNNSKIAVSFVVNYEEGGERSLLYEDEGFETFLTEAGLMPFPNRPVRERSIESCFEYGSRCGFWRILNLFKKHKVPFTCWAIGQAVEKNPVVVGAMEEAGCEVGSHSHRWINYEGVPPETEYEHIKKSVQAIQKASPSNSAPRSWYTGRASLNTRKLVCQVYKDLGLPQPFDSDEYNDDYPYWVADPLASKPGAEDDKGLLIVPYTLEVNDMKYAVAPGFCNSDDFYTYARDAFDVLYEEGLEGAPKMMTIGLHCRLTGRPGRFRGLQKLMEHITSKEGVWVATREQIAQAWSAKHPYKA | 3.-.-.- | null | ascospore wall assembly [GO:0030476]; ascospore wall chitin catabolic process [GO:0034232] | ascospore-type prospore [GO:0042764]; chitosan layer of spore wall [GO:0005631]; cytosol [GO:0005829]; nucleus [GO:0005634] | chitin binding [GO:0008061]; chitin deacetylase activity [GO:0004099]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF01522; | 3.20.20.370; | Polysaccharide deacetylase family | null | SUBCELLULAR LOCATION: Prospore {ECO:0000305|PubMed:15862318}. | null | null | null | null | null | FUNCTION: May deacetylate chitin (Probable). Required for spore formation (PubMed:15862318). {ECO:0000269|PubMed:15862318, ECO:0000305|PubMed:15862318}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13848 | I3ACR_SCHPO | MLIAAMGPKIPVPAYGVGTALFKKEKGEINRTIVDSVKNALAAGFIHIDCAEVYGNEEEVGVALKEANVPRSKLFITSKVMHNVDNIPEALNESLRKLGTDYLDLYLLHSPIPFYEKKIPISEGWKAMETALGTGLVHSVGVSNFRIPDLEELLKTSTITPRVNQIEFHPQVYKAAKPLVEFCQSKGIIVEGYGPLSPLVRDAQGPVAEFTKSLESKYHVSDTQILLKWAYSKGVIPITTTSKIERMKECLNFDSFTLDKADIDELGTLGVQHHKRTFMKHMDE | 1.1.1.190; 1.1.1.191 | null | null | cytosol [GO:0005829]; nucleus [GO:0005634] | alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; alpha-keto amide reductase activity [GO:0051268]; alpha-keto ester reductase activity [GO:0051269]; indole-3-acetaldehyde reductase (NADH) activity [GO:0047018]; indole-3-acetaldehyde reductase (NADPH) activity [GO:0047019]; oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor [GO:0016652] | PF00248; | 3.20.20.100; | Aldo/keto reductase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. | CATALYTIC ACTIVITY: Reaction=indole-3-ethanol + NAD(+) = H(+) + indole-3-acetaldehyde + NADH; Xref=Rhea:RHEA:14873, ChEBI:CHEBI:15378, ChEBI:CHEBI:17890, ChEBI:CHEBI:18086, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.190; Evidence={ECO:0000269|PubMed:16813561}; CATALYTIC ACTIVITY: Reaction=indole-3-ethanol + NADP(+) = H(+) + indole-3-acetaldehyde + NADPH; Xref=Rhea:RHEA:17037, ChEBI:CHEBI:15378, ChEBI:CHEBI:17890, ChEBI:CHEBI:18086, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.191; Evidence={ECO:0000269|PubMed:16813561}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=34 uM for NADP {ECO:0000269|PubMed:16813561}; KM=53.3 uM for NAD {ECO:0000269|PubMed:16813561}; | null | null | null | null | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13849 | CBPY_SCHPO | MLMKQTFLYFLLTCVVSAQFNGYVPPEQNGGDIVVPKDFYEKFGEDFIREQEESSAPLMNPVPERDEAEAPHHPKGHHEFNDDFEDDTALEHPGFKDKLDSFLQPARDFLHTVSDRLDNIFDDDEDEHVREKRPHDSADEDAPRRKHGKCKGKGKHHKGKHAKGKGKKSHPKPEDDSVFFDDERPKHHEFDDEDREFPAHHEPGEHMPPPPMHHKPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPFKHHELEEHEGPEHHRGPEDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHQGPKEKHNERPEQNMQSSHELLVIEAFADLINSVPVEEIAEEFSRFLDTLGIEYYGNIPVHIQENAPKDSSIPPLFEFDDDLELSDLTPEQFAYLEMLKAEGIDPMTAFRDQSHPAKPSNAQPADSSRPYAVFSQEENGEHVNLKAFPDHTLRVKDSKPESLGIDTVKQYTGYLDVEDDRHLFFWFFESRNDPENDPVVLWLNGGPGCSSLTGLFMELGPSSINIETLKPEYNPHSWNSNASVIFLDQPINTGFSNGDDSVLDTVTAGKDVYAFLNLFFAKFPQYAHLDFHIAGESYAGHYIPQFAKEIMEHNQGANFFVASGYEMEKQYINLKSVLIGNGLTDPLVQYYFYGKMACESPYGPIMSQEECDRITGAYDTCAKLITGCYQTGFTPVCIGASLYCNNAMIGPFTKTGLNIYDIREECRDQEHLCYPETGAIESYLNQEFVQEALGVEYDYKGCNTEVNIGFLFKGDWMRKTFRDDVTAILEAGLPVLIYAGDADYICNYMGNEAWTDALEWAGQREFYEAELKPWSPNGKEAGRGKSFKNFGYLRLYEAGHMVPFNQPEASLEMLNSWIDGSLFA | 3.4.16.5 | null | protein catabolic process in the vacuole [GO:0007039]; zymogen activation [GO:0031638] | fungal-type vacuole [GO:0000324] | serine-type carboxypeptidase activity [GO:0004185] | PF00450; | 1.10.287.410;3.40.50.1820; | Peptidase S10 family | null | SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:9209031}. Note=Lysosome-like vacuoles. | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal amino acid with broad specificity.; EC=3.4.16.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10074}; | null | null | null | null | FUNCTION: Involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13853 | ITS3_SCHPO | MKIDSNGIVNPHSITNEIPSYDEKQAVDLNGNAFAPNGTFQKKDLISHKNDFERTMRHDVLHTNPKIEVRSETHIYEPNDSLFKENQDFPSNPTAHSPSSSSNDSVITATGVPDGILRDSPIVSALEPPSSNSSSSPQLQNLKHQLSSPQPSRAPIDRSSSNPVTSSQQPPNDRSTLSSSQKAKRPLKRSYSEKNSSNAEPSGSRSGDRGTNVSTSGSLLDGIPPDIGSASWAEAVKQKRVNMRRRREELDDECVLVGTRVSEGHENYVTAYNMLTGIRVGVSRCQAKMDRELTPADFTARHKFTFDITGNELTPSAKYDFKFKDYAPWVFRHLRQLFHLDAADYLVSLTSKYILSELDSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLREILYDYYEHVKNNPNTLISQFYGLHRVKLPFGRKIHFVVMNNLFPPHRDIHQTFDLKGSTLGRELDENQPCQSPMCTMKDTNWIRRNMHLQFGPLKRQIFLTQVKADIDMLSSLGIMDYSLLVGIHDLSRGNRDKIRNSILSVYDPNVSQHRVPSINGNESHSNVHVIRQVVNSTGPVSLDQSCNLLPTDQFVERRNFMFYSDDGGFQATDENNEPGNFIFYIGIIDLLTKYSYVKRVEHLWKGINHSDSVISAVPPAEYASRFYKFVESSIKPTLLVLKPFPLKPQDGQRVNKQQSVNAGNVRTNNKHGSLNNNTAPSSRNAKSTSAHKSPKTEHRFPFPCRNVTTNTSSS | 2.7.1.68 | null | cell division [GO:0051301]; dynein-driven meiotic oscillatory nuclear movement [GO:0030989]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphorylation [GO:0016310] | cell division site [GO:0032153]; division septum [GO:0000935]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | 1-phosphatidylinositol-3-phosphate 4-kinase activity [GO:0052811]; 1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; 1-phosphatidylinositol-5-phosphate 4-kinase activity [GO:0016309]; ATP binding [GO:0005524]; phospholipid binding [GO:0005543] | PF01504; | 3.30.810.10;3.30.800.10; | null | PTM: Phosphorylated by casein kinase I. Phosphorylation inactivates the enzyme. {ECO:0000269|PubMed:9873063}. | SUBCELLULAR LOCATION: Nucleus. Membrane; Peripheral membrane protein. Note=The active form of the enzyme is membrane-associated and concentrates at the septum in dividing cells. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68; | null | null | null | null | FUNCTION: Involved, together with the calcineurin ppb1, in cytokinesis. {ECO:0000269|PubMed:10950958}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13877 | RPAB5_SCHPO | MIIPIRCFSCGKVIGDKWDTYLTLLQEDNTEGEALDKLGLQRYCCRRMILTHVDLIEKLLCYNPLSKQKNL | null | null | transcription by RNA polymerase I [GO:0006360]; transcription by RNA polymerase II [GO:0006366]; transcription by RNA polymerase III [GO:0006383]; transcription elongation by RNA polymerase I [GO:0006362]; transcription initiation at RNA polymerase II promoter [GO:0006367]; tRNA transcription by RNA polymerase III [GO:0042797] | cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]; RNA polymerase I complex [GO:0005736]; RNA polymerase II, core complex [GO:0005665]; RNA polymerase II, holoenzyme [GO:0016591]; RNA polymerase III complex [GO:0005666] | DNA binding [GO:0003677]; RNA polymerase I activity [GO:0001054]; RNA polymerase II activity [GO:0001055]; RNA polymerase III activity [GO:0001056]; zinc ion binding [GO:0008270] | PF01194; | 1.10.10.60; | Archaeal Rpo10/eukaryotic RPB10 RNA polymerase subunit family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, RBP10 is part of the core element with the central large cleft (By similarity). {ECO:0000250}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13881 | CLR2_SCHPO | MPAITCVWSDGRSDTWPNVNGHSRTRSVPSLKPLPHQDSKNLLYRQICGRLLAQHVFGGAGSTQPILNQLCKRLSTGNPNNTNASTVVTAPEKNVVSARHVRPNPKSSKDTLEKQPKYSSQIYLTDSFENYYLASLPTNYQLYQRDSNRENGNGKREFWLYGHPSGRPFRSVNDFLHHLYWLISDLTRNESTCCCVLCSGNMTRVRKNLQKENERMFHECKDDTYTWPSSYRLGEVVWIDINNELIPAIIVARNLINYESNQMDAVKLISDTFVEPYQYHCKQLGNSRYYFDMAAADIEPWSRHPLDLQKQEHLVAHSICQTWNLFGIFQPLEGIDMEEPKFHDENYSIPLTVLPTFGGESNSLDDHFYGIFRGAEKLWINDLCVISTSSLPSVLQKTSFMYISDIYVNEDDIVCFQGSLWTQIDKNALDYNDSADNIDEHKDDLKELPRRLQMVSKLSNTYFRCLHDKSVEYVCPFADVLGRWYEPWFVKGDLNYTSEVKERTSSRLSAVGSENWVDDDFYEYLLSEIDMVSAVVM | null | null | chromatin organization [GO:0006325]; heterochromatin formation [GO:0031507]; silent mating-type cassette heterochromatin formation [GO:0030466] | CENP-A containing chromatin [GO:0061638]; chromosome, subtelomeric region [GO:0099115]; mating-type region heterochromatin [GO:0031934]; pericentric heterochromatin [GO:0005721]; rDNA heterochromatin [GO:0033553]; SHREC complex [GO:0070824] | null | PF10383;PF16761; | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17289569}. Chromosome, centromere {ECO:0000269|PubMed:17289569}. Chromosome, telomere {ECO:0000269|PubMed:17289569}. Note=Associates with major heterochromatin, centromeres, sub-telomeres, rDNA and the mat locus. | null | null | null | null | null | FUNCTION: Required for deacetylation in the mating-type region and the centromere. Acts upstream of the histone deacetylases to promote transcriptional silencing. Required for proper positioning of nucleosomes at heterochromatic loci and for transcriptional gene silencing (TGS) function of the Snf2/Hdac-containing repressor complex (SHREC). {ECO:0000269|PubMed:15317867, ECO:0000269|PubMed:17289569}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13889 | E2AK1_SCHPO | MLGTSTKCSKRDCNYAKENISRIMPTIGLGYKQNFEKKTADTQSSCKLLLVALLESFCKHSDQTPEQSKQMFLYVAHSLQNSGIIDFEFSEELEPIRNAYADSLHNLLSKAFRSTLPMSSTKDSKKSRYSSPDGVLAKTASFLSVLSDGGYEDDVMNVKPSVNVLSNRLNHLPVEALESCFPQTTLESSTFADFCEHKDGTGNLSFSNFDSFPTVQRSRYASDFEELELLGKGGYGSVYKARNKFDGVEYALKKIPLRLRSFSTSSNIFRESRTLARLNHPNVIRFFSSWVELLPSSEKQIEEEPLASADETLSQSADIDNFMFDMDTGLLQHTYPSSVQILFQEDSVADDLTPCYSTKNSTCNLTDLFKKEADQDYAESHDCSSTTSQVDTLGKLAPTKSASEMLLMDSFLSEREEDECSNIPSFDQQPLCLYIQMALCEETLEKHINRRNKHIHGVMSKGLRNCYILLFARILEGVLYLHDAMHLVHRDLKPRNIFLSSGVHSEPCSVCLPNFSDEDNVEVSNAYEPVNQRTLCVVPKIGDFGLVLSQSDNLEEGTNSSAESSFVGTSTYAAPELFSKHMRSVMNNNSSTDIYALGILFFELLYPFNTRMERASAIANLKKGIFPHDFLDSMPEEASLIRSMLSSSNKRPTAAQLLTSNLFHDLVVNELHVYQALLEDAEKRNNNLKAELNILRVLNPNYDC | 2.7.11.1 | null | negative regulation of cytoplasmic translational initiation in response to stress [GO:1990625]; signaling [GO:0023052] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, GCN2 subfamily | PTM: Autophosphorylated. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; | null | null | null | null | FUNCTION: Mediates down-regulation of protein synthesis in response to stress conditions by the phosphorylation of the alpha subunit of eIF-2 (tif211) on 'Ser-52'. Protein synthesis is inhibited at the level of initiation. Activity is inhibited in the presence of heme. {ECO:0000269|PubMed:12242291}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13892 | EDC4L_SCHPO | MNEQDLLNSLRRDLNLPNLGKSHDGSEAVESTFPEKKESSLSAQQPHVDDQRSSLLSLLNAGLNASNQSPSNSGPKYYASHSSSTDALLQAFRDGAKPSGTASGADVKRSDSESTEATSNERPFNPVSAANLERLLMSSTGPQTPINGELKSNDSQDTAFQSSRNMPSDTSVASPDYSHSQSSSPIANYQESGNSEEPHKAEEQQQLSIYQLDNPGSGNYVWETVISPDKFETSTFAKCERNDIAIINRELDAQDNQLIHTNEDFIAYAVHREPIIRVIEISTGKSFLLHNNSPNKFVSVAWGNDSVIKNRLMAIDTTGQVLIFAVDIATSTSEIIFQLSGAQSLSDPIKSRFHWYPKSSTRFAVALSKHIIFFDLDLLNNISFPIPRSINAIQQLPCFLIDTGISAKEYDFSYDGTVFATVDKDALIKIYTVPTTFPSTPDKRPVPSEVSPIAIFTTRMERGPSKNYEKPINLRFISTPGTNNSRYLVIVYVMNQLITLFDLYSKRNIQTFRFNNRPTAATTTSFSQFSVDNERSTLLVGNPPSNSIYFFLFAKDETVSEQAPIYNSTYELILASLNTSEPVPADAKFSVIVAKKFEKAACISFTACKILESEDKYCIVVSNTDGYEYYSIPTSILDKTGKTVRSLESVQNYDADIGGTIDLTERHSTASPSTVNSGFSTPRSQATGFSKKKKDKGERFETKDKSSSVLSPSSYSASTFDAIPMDSIVSNILASLEKSVHKNYESLRSQLLEYKAANEKHTEAILSVVSSTLTENTGKILESVVEKSMQVALKEEIANSVRNALKNNLEKIESFLENSIAELQNSVREDFDKQTSSLAQLRYSIQNVAHAQKESEVKYNELNEQVKTLEGYVETVLEKFNDLKIENKVPETAPDVVPSSYPPAAESNVSVSSDTSTKDVEKQEPSSAEQPAQGIAESLRRLKEYVKAGSVKECVAEWCNMPSVAGFDVLSEISYDRMLENCSNLLLLTFIYHISLLDSVDDDRLSKRMEYISRICLNIDVNDPKVETVVHPVLTLTREALLRQSEFFSPIFKRRLVVLLRALDGKISEISVASSN | null | null | deadenylation-independent decapping of nuclear-transcribed mRNA [GO:0031087]; P-body assembly [GO:0033962] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; P-body [GO:0000932] | molecular adaptor activity [GO:0060090]; molecular condensate scaffold activity [GO:0140693] | null | 2.130.10.10; | WD repeat EDC4 family | null | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:23319050}. Note=Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay. {ECO:0000269|PubMed:23319050}. | null | null | null | null | null | FUNCTION: Involved in P-body formation. Acts as a functional homolog of human EDC4, which plays a role in mRNA decapping in the process of mRNA degradation. Enhances the decapping activity of dcp2 (PubMed:23319050). Together with edc3, acts as a scaffolding protein sufficient for the phase transition of the components of the 5' to 3' mRNA degradation machinery to form P-bodies. Intermolecular interactions between the edc3 Sm domain and at least 10 helical leucine-rich motifs in dcp2 and pdc1 build the core of the interaction network of this spontaneous clustering process (PubMed:24862735). {ECO:0000269|PubMed:23319050, ECO:0000269|PubMed:24862735}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13898 | PMT1_SCHPO | MDKQSTFQDPKEKHRIQRDVKLSRPRKRFSFLDYVVVIFLTVVAFCVRAQRLMNPAKVVFEELRYYNYAVDYVNNKLLMDVYPPLGKLLFSLVAALTGNKYELNTLDEPGQQYPFTDVAYSMRLFTCLLGSLLVPLMYGTVYFPTKSKTAASLAALFVIFDNGLITMSRYIMIEIPALYFMSLTAFYWSVYEAQQKRPFSLRWHTSLLSTGVALGLALSTKLSAMFTFGWLLILAAFHLWNLLGDLSVPMYRIVKHLFSYIFYLIGVPITVYLAVFAVHSHIAYKASVADAFLPPEHRHALAGNRFDDQFADVAYGSLVTIRNAIPEHGYLHSSELLYPEGTEQQIISLVDEPNQNALWIIEHEHSQDNNRSNIELLKDGSVVRLRHVMTGRALHSHEHKPIVSNNDWQLEASAYGGFGFEGDANDLFRIQILEKKSKHATSNGTVETLNTKFRLIHVFANCELMSSHRRFPDWGDYQREVTCCRNCVERSTTWFIESNYHDGLPSDSRKITYRKPGFLESFVEHNKLMWLKDRKMGDGHVYESSALTWPLLLGPLRFFYEQHLQVFFMGNPFVWYSVISLVAFFVIVQIFCLARWNLGYNDFGPSAFHYNYNIGKFVVAWLLHWAPYILETDRVFLYHYLPALYFGIAALGVSWSFLGNAVFGNRTAYKALSVIIMALMFLVYRLYSPFTYMTTLTKSSCRALELKGSWNFHCNTYLDNLSDYKFSSDAGETYFEKAAPHPFVYSEDTAKKSEGDTPLNKNLNDYYPSWDQRVEAGYKLAAQQKAEQEAREAAEKAASEAAERSSSEAAASSSSESVAAASVEAERLAMEADEFNGASETVDGASVEAERSAMEAAALNNAAESTEVVGSSPESVASEQEENVAESAQARVE | 2.4.1.109 | null | cell wall mannoprotein biosynthetic process [GO:0000032]; chain elongation of O-linked mannose residue [GO:0044845]; protein O-linked mannosylation [GO:0035269] | endomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nuclear membrane [GO:0031965] | dolichyl-phosphate-mannose-protein mannosyltransferase activity [GO:0004169] | PF02815;PF02366;PF16192; | 2.80.10.50; | Glycosyltransferase 39 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15809069}; Multi-pass membrane protein {ECO:0000269|PubMed:15809069}. Nucleus membrane {ECO:0000269|PubMed:15809069}; Multi-pass membrane protein {ECO:0000269|PubMed:15809069}. | CATALYTIC ACTIVITY: Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+); Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:137321; EC=2.4.1.109; CATALYTIC ACTIVITY: Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] = 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate + H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:137323; EC=2.4.1.109; | null | PATHWAY: Protein modification; protein glycosylation. | null | null | FUNCTION: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. Required for normal cell growth and septum formation. Shown to actively O-mannosylate wsc1. {ECO:0000269|PubMed:15809069, ECO:0000269|PubMed:15948957}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13899 | CRLS1_SCHPO | MLHTINYRSWHLAARQLGRSTFRKFTTESSTKSPIADVCFAFDSIDGVLIRGGRGLKEGTKTLKFLQKNNIPFILLTNGGGMHESVRAQRLSKTLSVSLTEDDFCQSHTPFRALADKYKHVLVLGGKDNSVRETAEKYGFKSVINELDVIAKLGTPFWPFTSFNEEDIKDAKDFDVTRPIEAVFTYVDPVRLGLDLQLVMELGQSKNGVLGTVSKTANEGPDIYFSNADLIWPNEYPLPRLGQGAFAICCESVFKELTGKDLRNTKYGKPHKLTYDYAKNILMKKHKTLGITNPPKEIFMVGDNPESDIRGANNYGWTSILVRTGIFQGDNSPKYSAKHVSDNVWEGVRWALSKHVPAAKLNKSMGEVRGFHTSSRVLNTVTKSNNSKPIQRPLRENIFTLPNLLTFSRLLSAPLIAYLYIYDYTKAAACFFLYAGFTDLVDGYIARKFDLGSIAGTVLDPLADKTLMTCLTICLAVRETMPLTLASLIIGRDVLLVSAVSYLRYKSLPAPKTFRRFFDFAIPTTELKPTRISKWNTALQLLLLGLLITEPILPFDASFAKSPLFYIVGCTTIASGASYCISRNTFRNIGKSKLQ | 2.7.8.41; 3.-.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q07560}; | cardiolipin biosynthetic process [GO:0032049]; mitochondrial membrane organization [GO:0007006]; phospholipid homeostasis [GO:0055091] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | cardiolipin synthase (CMP-forming) [GO:0043337]; cardiolipin synthase activity [GO:0008808]; hydrolase activity [GO:0016787] | PF01066;PF13344;PF13242; | 1.20.120.1760;3.40.50.1000; | HAD-like hydrolase superfamily; CDP-alcohol phosphatidyltransferase class-I family | PTM: [Isoform 1]: Proteolytically cleaved, presumably during its import into the mitochondrion by mitochondrial processing peptidase. {ECO:0000269|PubMed:29958934}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.; SUBCELLULAR LOCATION: [Cardiolipin synthase (CMP-forming)]: Mitochondrion inner membrane {ECO:0000305|PubMed:29958934}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Mitochondrial hydrolase]: Mitochondrion {ECO:0000269|PubMed:29958934}. | CATALYTIC ACTIVITY: [Mitochondrial hydrolase]: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a CDP-1,2-diacyl-sn-glycerol = a cardiolipin + CMP + H(+); Xref=Rhea:RHEA:32931, ChEBI:CHEBI:15378, ChEBI:CHEBI:58332, ChEBI:CHEBI:60377, ChEBI:CHEBI:62237, ChEBI:CHEBI:64716; EC=2.7.8.41; Evidence={ECO:0000305|PubMed:29958934}; | null | null | null | null | FUNCTION: [Cardiolipin synthase (CMP-forming)]: Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG) (PubMed:29958934). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions (PubMed:29958934). {ECO:0000269|PubMed:29958934}.; FUNCTION: [Mitochondrial hydrolase]: Activity is dispensable for viability. {ECO:0000269|PubMed:29958934}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13902 | DAK1_SCHPO | MDKHFINDPEVLVLDGLKSLADMNKTLTVHEEGKFIYFHDYNKKNVSVISGGGAGHEPTHSSFVGKGMLTAAVSGSIFASPSSKQIYTGIKQVESEAGTLVICKNYTGDILHFGMALEKQRTAGKKAELIAVADDVSVGRKKSGKVGRRGLSGTVLVHKIAGAAAARGLPLEAVTTIAKAAIDNLVSIGASLAHVHVPGHEPIAKEDEMKHDEMELGMGIHNEPGCKRISPIPSIDDLIAQMLKQMLDQSDKDRAYVKIEGDDEVVLLMNNLGGLSMLEFSAISHKVKEALAKEYKINPVRIFAGPFTTSLNGLGFGITLLRTTDRVKVEGEEYSLVDLIDQPVEAIGWPLCQPSDLKSKNKIGNVSIEEGQKDVKSPVTVDKEKVRQAIVNSMENLIKAEPKITKFDTMAGDGDCGTTLKRGAEGVLKFVKSDKFSDDPIRIVRDIADVIEDNMDGTSGALYAIFFHGFAKGMKDTLEKSKDISSKTWAAGLKVALDTLFKYTPARPGDSTMCDALVPFVETFVKTNDLNAAVEEARKGADATADMQAKLGRAVYVGDDVKVPDAGALGVVAIVEGFTK | 2.7.1.28; 2.7.1.29 | null | glycerol catabolic process [GO:0019563]; glycerol metabolic process [GO:0006071]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; glycerone kinase activity [GO:0004371]; triokinase activity [GO:0050354] | PF02733;PF02734; | 1.25.40.340; | Dihydroxyacetone kinase (DAK) family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + dihydroxyacetone = ADP + dihydroxyacetone phosphate + H(+); Xref=Rhea:RHEA:15773, ChEBI:CHEBI:15378, ChEBI:CHEBI:16016, ChEBI:CHEBI:30616, ChEBI:CHEBI:57642, ChEBI:CHEBI:456216; EC=2.7.1.29; Evidence={ECO:0000269|PubMed:10091325}; CATALYTIC ACTIVITY: Reaction=ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate + H(+); Xref=Rhea:RHEA:13941, ChEBI:CHEBI:15378, ChEBI:CHEBI:17378, ChEBI:CHEBI:30616, ChEBI:CHEBI:59776, ChEBI:CHEBI:456216; EC=2.7.1.28; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.01 mM for dihydroxyacetone {ECO:0000269|PubMed:10091325}; KM=0.63 mM for ATP {ECO:0000269|PubMed:10091325}; Vmax=29.4 mmol/min/mg enzyme {ECO:0000269|PubMed:10091325}; | PATHWAY: Polyol metabolism; glycerol fermentation; glycerone phosphate from glycerol (oxidative route): step 2/2. {ECO:0000305|PubMed:10091325}. | null | null | FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde. {ECO:0000250, ECO:0000269|PubMed:10091325}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13911 | PNK1_SCHPO | MSSKKRKSPPQESLTSYFEKSSKSSKKYGSQNKDSDSSSTCLQQKIEIQWSITDSLYIAKYGKLKKTKKFIAFDLDGTLIKTKSGRVFSKDAADWTWWHPSVVPKLKALYQDNYSLVIFSNQNGIPRKPSAGHTFQMKIRAIFESLDLPIVLYAAILKDKFRKPLTGMWNSFLKDVNRSIDLSFIKYVGDAAGRPGDHNSTDLKFAENIGIKFETPEQFFLGHSFVPPNFESFHPKNYLVRNSSSHPYHFKKSEHQEIVVLVGFPSSGKSTLAESQIVTQGYERVNQDILKTKSKCIKAAIEALKKEKSVVIDNTNPTIESRKMWIDIAQEFEIPIRCIHLQSSEELARHNNVFRYIHHNQKQLPEIAFNSFKSRFQMPTVEEGFTNVEEVPFKCLKDYEDTWNYWYE | 2.7.1.78; 3.1.3.32 | null | base-excision repair [GO:0006284]; DNA repair [GO:0006281]; phosphorylation [GO:0016310]; single strand break repair [GO:0000012] | nucleolus [GO:0005730]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity [GO:0046404]; double-stranded DNA binding [GO:0003690]; polynucleotide 3'-phosphatase activity [GO:0046403] | PF13671;PF08645; | 3.40.50.1000;3.40.50.300; | DNA 3' phosphatase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11729194, ECO:0000269|PubMed:16823372}. | CATALYTIC ACTIVITY: Reaction=a 3'end (2'-deoxyribonucleotide 3'-phosphate)-DNA + H2O = a 3'-end 2'-deoxyribonucleotide-DNA + phosphate; Xref=Rhea:RHEA:14113, Rhea:RHEA-COMP:13863, Rhea:RHEA-COMP:13864, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:138147, ChEBI:CHEBI:138148; EC=3.1.3.32; Evidence={ECO:0000269|PubMed:11729194}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14114; Evidence={ECO:0000305|PubMed:11729194}; CATALYTIC ACTIVITY: Reaction=a 5'-end dephospho-2'-deoxyribonucleoside-DNA + ATP = a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + ADP + H(+); Xref=Rhea:RHEA:15669, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:13184, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:136412, ChEBI:CHEBI:136416, ChEBI:CHEBI:456216; EC=2.7.1.78; Evidence={ECO:0000269|PubMed:11729194}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15670; Evidence={ECO:0000305|PubMed:11729194}; | null | null | null | null | FUNCTION: Catalyzes the phosphorylation of DNA at 5'-hydroxyl termini and can dephosphorylate its 3'-phosphate termini. Has a role in the repair of breaks in single-stranded DNA. {ECO:0000269|PubMed:11729194}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13917 | HPRT_SCHPO | MDPVRLYYSYNDIHKMCAQQAEKILETFRPDVIIAIGGGGFIPARILRTFLKKKGSKNIPIQAIGLSLYEELVSDSPEEVPGLEVKRTQWLDFSTLGMVDLVGKNILIVDEVDDTRTTLHYALRELQRDVAEQAKKLNREGEKTTFGIFVVHNKVKPKNAQLDKEILDKYYFTGCNTPDCWIMYPWEAQDIEEHDSHVAKMGDLKP | 2.4.2.8 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein. {ECO:0000250}; | GMP salvage [GO:0032263]; hypoxanthine metabolic process [GO:0046100]; IMP salvage [GO:0032264]; purine ribonucleoside salvage [GO:0006166]; XMP salvage [GO:0032265] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634] | guanine phosphoribosyltransferase activity [GO:0052657]; hypoxanthine phosphoribosyltransferase activity [GO:0004422]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; pentosyltransferase activity [GO:0016763]; xanthine phosphoribosyltransferase activity [GO:0000310] | PF00156; | 3.40.50.2020; | Purine/pyrimidine phosphoribosyltransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. | CATALYTIC ACTIVITY: Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053; EC=2.4.2.8; Evidence={ECO:0000250|UniProtKB:Q04178}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975; Evidence={ECO:0000250|UniProtKB:Q04178}; CATALYTIC ACTIVITY: Reaction=diphosphate + GMP = 5-phospho-alpha-D-ribose 1-diphosphate + guanine; Xref=Rhea:RHEA:25424, ChEBI:CHEBI:16235, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58115; EC=2.4.2.8; Evidence={ECO:0000250|UniProtKB:Q04178}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426; Evidence={ECO:0000250|UniProtKB:Q04178}; | null | null | null | null | FUNCTION: Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway (By similarity). {ECO:0000250}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13918 | ZHF1_SCHPO | MFDLARQTRIILLLGIDVTFFFIEIITGYAIDSLALIADSFHMLNDIVSLLVALWATRLAHSTSHEPKYTYGWQRAEILGALSNGVFLIALCMFIFMEAIERFIEPPSVSNPTLMFFVGSLGLLSNFVGIFLFHDHGHDHPHTHTAQNYDFPEEDDIESVLPSTIVHRCNTSQQEVSHTHTQVADSATESSPLLSYTGNHNGAGTSKPVNNHGSIEQDAPKQTKKRNLNMHGVFLHVLGDALGNIGVISAALFIKYTDYSWRFLFDPCISILLTFIILFSAIPLCKSAALILLQVAPQSIKLDDVSNLINHLDGVESVHELHIWQLSDVKLIATVHVCVTLPDDKGESYTKLTTDIRNVLQSFGIYDVTIQPEFANHPLLCDQGSSS | null | null | cellular detoxification of cadmium ion [GO:0098849]; detoxification of zinc ion [GO:0010312]; intracellular cobalt ion homeostasis [GO:0006877]; intracellular zinc ion homeostasis [GO:0006882]; zinc ion import into endoplasmic reticulum [GO:0140209]; zinc ion import into organelle [GO:0062111]; zinc ion transmembrane transport [GO:0071577] | endoplasmic reticulum membrane [GO:0005789]; fungal-type vacuole membrane [GO:0000329]; nuclear membrane [GO:0031965] | zinc ion sequestering activity [GO:0140486]; zinc ion transmembrane transporter activity [GO:0005385] | PF01545; | 1.20.1510.10; | Cation diffusion facilitator (CDF) transporter (TC 2.A.4) family, SLC30A subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11886869}; Multi-pass membrane protein {ECO:0000269|PubMed:11886869}. Nucleus membrane {ECO:0000269|PubMed:11886869}; Multi-pass membrane protein {ECO:0000269|PubMed:11886869}. | null | null | null | null | null | FUNCTION: Involved in zinc homeostasis, where it plays a role in its accumulation in the endoplasmic reticulum/nucleus. Also has a role in the sequestration of cadmium into the endoplasmic reticulum. {ECO:0000269|PubMed:11886869}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13919 | PST2_SCHPO | MEQTLAILKNDNSTLVAEMQNQLVHDFSPNGTALPELDIKAFVQKLGQRLCHRPYVYSAFMDVVKALHNEIVDFPGFIERISVILRDYPDLLEYLNIFLPSSYKYLLSNSGANFTLQFTTPSGPVSTPSTYVATYNDLPCTYHRAIGFVSRVRRALLSNPEQFFKLQDSLRKFKNSECSLSELQTIVTSLLAEHPSLAHEFHNFLPSSIFFGSKPPLGSFPLRGIQSSQFTLSNISDLLSQSRPDNLSPFSHLSNESSDFFKNVKNVLTDVETYHEFLKLLNLYVQGIIDRNILVSRGFGFLKSNSGLWRSFLSLTSLSPEEFLSVYNSACSDFPECGPSYRLLPVEERNISCSGRDDFAWGILNDDWVSHPTWASEESGFIVQRKTPYEEAMTKLEEERYEFDRHIEATSWTIKSLKKIQNRINELPEEERETYTLEEGLGLPSKSIYKKTIKLVYTSEHAEEMFKALERMPCLTLPLVISRLEEKNEEWKSVKRSLQPGWRSIEFKNYDKSLDSQCVYFKARDKKNVSSKFLLAEADILRSQAKLHFPLRSRSAFEFSFVYDNEIVLFDTCYMVCTYIVCNSPSGLKKVEHFFKNILPLHFGLEKDKFSIFLDQVFRGPDYDVNAPNIVGNKPVRRKRSNSITQLTEFVKQPKINGQRESRSAAAARKKEESGNKSQSNSQNSLSDESGNVTPVSKKQLSQPAAAIKASLKYPSHPDSLLEHQDHAGDTENEMHDDVDKEQFGYSSMYVFFRLFNLLYERLYELQRLEDQVSIIQQRIIPNPVSQKQKIWRDRWNDLSDVPDEKTHYENTYVMILRLIYGIVDQSAFEDYLRFYYGNKAYKIYTIDKLVWSAAKQVHHIVSDGKYKFVTSLVEQNSSASPKKNYDDFLYRLEIEKLLNPDEILFRFCWINKFKSFGIKIMKRANLIVDQSLDTQRRVWKKYVQNYRIQKLTEEISYKNYRCPFLCRNIEKERTVEQLVSRLQTKLLRSAELVSGLQAKLCLDSFKLLYLPRTEDSYIDASYLRLRDTDFLDCQNKRKQRWRNRWESLLKSVRGTSDNTAEVNFDADINALFIP | null | null | negative regulation of transcription by RNA polymerase II [GO:0000122]; transcription initiation-coupled chromatin remodeling [GO:0045815] | chromatin [GO:0000785]; nucleus [GO:0005634]; Rpd3S complex [GO:0032221]; Sin3-type complex [GO:0070822] | transcription corepressor activity [GO:0003714] | PF02671;PF08295;PF16879; | 1.20.1160.11; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810, ECO:0000269|PubMed:12773392}. | null | null | null | null | null | FUNCTION: Has a role in chromatin assembly and chromosome segregation. Involved in the deacetylation of histones. {ECO:0000269|PubMed:12773392}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13924 | HASP_SCHPO | MESRSKVKTYGKNRRYINKDIEIWASLDERPCALKPRNIENFNNQERSDLEHIHSKPKKDSLLSWNILLKKGSYKENELLAKRNQNLVPTVIIPASPRDNASKSVVSKKEVVNLSSSVALSGKPANNSKLDPLHRLLQIVAQEDALPFSQFVKSQTFEIQKIGEASYSEVYQASNADDVPVVWKVIPFGEDGQAQYADVLNEVQISQWIKVDGFANLHQVVVVKGTYPSLLLEEWDRYLMQNGSENDRPDSYSSTQLYCVLCLDHSGTDLEHFELRSWRECWSVFYETLKILSLVETRYEFEHRDLHWGNILIRKADRSEEEVSFLLNEISLDDIESVDFPGSQDKADDFDNILQVTLIDFTLARASYSQGIISYNEFNDPDLFNGVDDYQFDIYRLMSRVTKGRWAQFFPITNVLWLHYLIHQLLHKKNLSSPLTETETLMRSRLKQIFRLIDPVKTMQFQQAEDSIRSKSTVTSATSLLNWVRQKY | 2.7.11.1 | null | attachment of meiotic spindle microtubules to meiosis II kinetochore [GO:0051456]; intracellular signal transduction [GO:0035556]; mitotic cell cycle [GO:0000278]; mitotic sister chromatid biorientation [GO:1990758]; phosphorylation [GO:0016310] | chromosome, subtelomeric region [GO:0099115]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mating-type region heterochromatin [GO:0031934]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721] | ATP binding [GO:0005524]; histone H3T3 kinase activity [GO:0072354]; protein serine kinase activity [GO:0106310] | PF12330; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, Haspin subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. Chromosome. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; | null | null | null | null | FUNCTION: Serine/threonine haspin-like protein kinase involved in cell cycle regulation. Acts in chromosomal passenger complex (CPC) targeting to centromeres by phosphorylating histone H3 at 'Thr3' (H3T3ph). {ECO:0000269|PubMed:20929775}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13928 | RHO3_SCHPO | MSSCFGSKKKPIYRKIVILGDGAAGKTSLLNVFTKGYFPQVYEPTIFENYIHDIFVDGNSIELSLWDTAGQEEYDQLRSLSYSDTHVIMICFAVDSRDSLENVITKWLPEVSSNCPGVKLVLVALKCDLRGADEEQVDHSKIIDYEEGLAAAKKINAVRYLECSAKLNRGVNEAFTEAARVALAAQPRGTKDGADESHGTGCIIA | null | null | actin cytoskeleton organization [GO:0030036]; actin filament organization [GO:0007015]; cell cycle [GO:0007049]; cell division [GO:0051301]; establishment or maintenance of cell polarity [GO:0007163]; microtubule cytoskeleton organization [GO:0000226]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell shape [GO:0008360]; regulation of exocytosis [GO:0017157]; regulation of septum digestion after cytokinesis [GO:0010590]; signal transduction [GO:0007165]; small GTPase-mediated signal transduction [GO:0007264] | cell division site [GO:0032153]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rho family | PTM: Palmitoylated by the erf2-erf4 complex. {ECO:0000269|PubMed:23843742}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12415007, ECO:0000269|PubMed:12930742}; Lipid-anchor {ECO:0000269|PubMed:12415007, ECO:0000269|PubMed:12930742, ECO:0000269|PubMed:23843742}. Note=Found at the cell periphery and the growing tips of interphase cells. Localized to the division site during cell division. | null | null | null | null | null | FUNCTION: Involved in controlling cell shape and septation (PubMed:12415007). Regulates cell separation by modulating the function of the exocyst complex (PubMed:12930742). Involved in post-Golgi vesicle transport (PubMed:12930742). Involved in driving sexual development in a palmitoylation-dependent manner (PubMed:23843742). {ECO:0000269|PubMed:12415007, ECO:0000269|PubMed:12930742, ECO:0000269|PubMed:23843742}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13935 | TRM4B_SCHPO | MGKRNKKVTQGKRAYNDKSEIVLENKQFEGYYKKQNLFRGKPNDEFDSFMEYMRKPLPTTFRICGYRHHAFELKNHFEKYYVPSLKNVVHEGQTIPPPTVLPWYPDGLAYIVDAQKDVIRKSPPLKRLQRFLVSENEAGNINRQEAVSMLPPLFLDVEPHHVILDMCAAPGSKTAQLIEAVYKKANIKDAAHDSKNLKSVEGLVIANDADPKRAQMLVHQINRLNSPNILVVNHDASTMPNIYVKGSSPSDGLNVIEEKKILKFDRILADVPCSGDGTFRKNLSLWREWSANSAFSLHPLQLRILIRGLQLLKVGGCLVYSTCSINPIENEAVVTAALKATGGAVSLVDVSKKLPLLKRDPGLLSWKVLDDSLNEFQSPAENTNDKIELTESMWPLPEEEMSKLHIERCARLYPHMQNTGGFFVAVLQKTDPINSRSFDPKKYTASMEILPPENKRQRTEKGVDEASNSTLTKSGNSYFDEEPFVYINPDDTSIKTIVDFYGIDPSFPRDQFFVRNQSGIPVRSIYFACSLFKEIIEANTNRVKFVHGGVRFFVKQEISQLLKDFSLKANKDICNFRIHSNGVNIISPFLNEKHFYDAGLKDLKILVKNEYPHVEQFSESGMLKKEFEKMPLGCNILRVDAQTKDGALMDMLILQPIWRSPTSCNLMLARKEKQNLSLELFGMDV | 2.1.1.- | null | tRNA methylation [GO:0030488]; tRNA wobble base cytosine methylation [GO:0002127] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | mRNA (cytidine-5-)-methyltransferase activity [GO:0062152]; tRNA (cytidine-5-)-methyltransferase activity [GO:0016428]; tRNA binding [GO:0000049] | PF01189; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, RsmB/NOP family, TRM4 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. | CATALYTIC ACTIVITY: Reaction=cytidine(49) in tRNA precursor + S-adenosyl-L-methionine = 5-methylcytidine(49) in tRNA precursor + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54140, Rhea:RHEA-COMP:13804, Rhea:RHEA-COMP:13805, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000305|PubMed:23074192, ECO:0000305|PubMed:30646830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54141; Evidence={ECO:0000269|PubMed:23074192, ECO:0000305|PubMed:30646830}; CATALYTIC ACTIVITY: Reaction=cytidine(50) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(50) in tRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:61488, Rhea:RHEA-COMP:15838, Rhea:RHEA-COMP:15839, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000305|PubMed:30646830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61489; Evidence={ECO:0000305|PubMed:30646830}; CATALYTIC ACTIVITY: Reaction=cytidine(60) in tRNA(Asp) + S-adenosyl-L-methionine = 5-methylcytidine(60) in tRNA(Asp) + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51160, Rhea:RHEA-COMP:12902, Rhea:RHEA-COMP:12905, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000305|PubMed:23074192}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51161; Evidence={ECO:0000269|PubMed:23074192}; CATALYTIC ACTIVITY: Reaction=cytidine(61) in tRNA(Asp) + S-adenosyl-L-methionine = 5-methylcytidine(61) in tRNA(Asp) + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51164, Rhea:RHEA-COMP:12903, Rhea:RHEA-COMP:12906, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000305|PubMed:23074192}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51165; Evidence={ECO:0000269|PubMed:23074192}; CATALYTIC ACTIVITY: Reaction=cytidine(62) in tRNA(Asp) + S-adenosyl-L-methionine = 5-methylcytidine(62) in tRNA(Asp) + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51172, Rhea:RHEA-COMP:12904, Rhea:RHEA-COMP:12907, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000305|PubMed:23074192}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51173; Evidence={ECO:0000269|PubMed:23074192}; | null | null | null | null | FUNCTION: tRNA cytosine C(5)-methyltransferase that methylates cytosine to 5-methylcytosine (m5C) in tRNAs at position 49 and 50 (PubMed:30646830). Trm4a and trm4b methylate different sets of tRNAs (PubMed:30646830). Also methylates cytosine to m5C at positions (60, 61 and 62) in tRNA(Asp) (PubMed:23074192). {ECO:0000269|PubMed:23074192, ECO:0000269|PubMed:30646830}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13936 | SPT5_SCHPO | MDTNSPKSIDKDANSTEVDAAEQDAASVKINSTRASPNGSDLLNDDSEAAKITTNEKQSSPVDSHNESPNDTTINKGEDGNENEVDNVNNNDKKEDEDNVEENEEEADANEEEEEDEEDDEEDEEDEDESGGGRRKRARHDRRNQFLDIEAEVDEDEEELEDEEDEIGREDGFIEEEVGADYVGDDRRHRELDRQRQELQSVDAERLAEEYREKYGRSQTVVGDTSNVPQRLLLPSVNDPNIWAVRCKIGKEKDIVFTIMRKAMDLQYTSSPLEIISAFQRDSLVGYIYVEARKQSHVLDALNGVLNVYTNNMILVPIKEMPDLLKVQKQVVELLPGAYVRIRRGKYAGDLAQVDNLSENGLTARVRIVPRIDYSDGLKRKNSATRPQARLFNESEAFKSNPSKFSKRGPRLFLFNNEEFEDGFLVKDIRISSLITEGVNPTLDEVSKFNPNNEDLDLSSLALSVKGGHAEFQPGDHVEVYVGEQTGVSGVVENVRGSVITMVSSDGLRLDVPSRGLRKRFRHGDYVKVIAGKYKDDTGMVVRISKDEVTFLSDTLMTELTVFSRDLGEASSAQAVNSAYELHDLVQLDVNTVACIFSVDRDTYKVIDQNGGVRTVLASQITMRHSNRRGVATDRNGAEIRIGDKVKEVGGEGKQGTILHIYRAFVFLHNRDIAENNGVFSARSRNVATIAAKGARISADLTKMNPALSNGPALPPVANLKRTIGRDKAIGATVRIRRGPMKGLLGVIKDTTDANARVELHTGNKMVTIPKENLLYTTKTGELISYTEFIERSRGIRPGSISTADGPNVPNWAQGARTPAVANGSRTPAWNTGSRTPAWNSGSKTPAWNSGSRTPAWNSGNKTPAWNAGSRTPAWNSGNKTPAWNVGNKTPAWNSGAKTPAWNAGNKTPSWNNGTKTPAWNANQTPMVANGTNTSWGQTPAYGGFSETNWDTEDNSKPYTAPTPGAWAAPTPGGWDDEEGDSPKYVPPSP | null | null | mRNA processing [GO:0006397]; regulation of DNA-templated transcription elongation [GO:0032784]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription elongation by RNA polymerase II [GO:0006368]; transcription elongation-coupled chromatin remodeling [GO:0140673] | chromatin [GO:0000785]; DSIF complex [GO:0032044]; nucleus [GO:0005634] | mRNA binding [GO:0003729]; transcription elongation factor activity [GO:0003711] | PF12815;PF00467;PF03439;PF11942; | 2.30.30.30;3.30.70.940; | SPT5 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}. | null | null | null | null | null | FUNCTION: The spt4-spt5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene (By similarity). {ECO:0000250, ECO:0000269|PubMed:11893740}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13953 | EAF3_SCHPO | MAVSYKVNERVLCFHGPLLYEAKIVDTEMKGDVTTYLIHYKGWKNSWDEWVEQDRILQWTEENLKTQKELKNAAISTRQKPTSKKSASSTSKHDSTGVKTSGKRSRESSTVTVDGDSHELPSRIKTQKSESPIPQQVKRDGTTDAKNEETTKPENNEKDDFEEEPPLPKHKISVPDVLKLWLVDDWENITKNQQLIAIPRNPTVRAAIAAFRESKISHLNNEIDVDVFEQAMAGLVIYFNKCLGNMLLYRFERQQYLEIRQQYPDTEMCDLYGVEHLIRLFVSLPELIDRTNMDSQSIECLLNYIEEFLKYLVLHKDEYFIKEYQNAPPNYRSLVGV | null | null | DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA repair-dependent chromatin remodeling [GO:0140861]; regulation of DNA-templated transcription [GO:0006355]; transcription initiation-coupled chromatin remodeling [GO:0045815] | NuA4 histone acetyltransferase complex [GO:0035267]; nucleus [GO:0005634]; Rpd3S complex [GO:0032221] | null | PF05712;PF11717; | 2.30.30.140;1.10.274.30; | MRG family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00972, ECO:0000269|PubMed:12773392}. | null | null | null | null | null | FUNCTION: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair (By similarity). Also involved in deacetylation of histones, chromatin assembly and chromosome segregation. May act as a transcriptional oscillator, directing histone deacetylases to specific chromosomal domains. {ECO:0000250, ECO:0000269|PubMed:12773392}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13958 | SSN3_SCHPO | MKDGYKIIGFISSGTYGKVYKAVSSNSNDKRLFAIKKFKAESKQVSSNAQQTGVSQSAIREMMLCREIQHENIVSLVQVLLKDGTISMVFEYAEHDLLQIIHFHSRSRTRQIPPSILKSILWQIINGVAYLHENWIMHRDLKPANIMITATGKVKIGDLGLGRLIRDPILPFYSSDRVVVTIWYRAPELLLGAHDYTPAIDVWAIGCIYGEMLALSPLFKGDEIKMEDKKVVPFQSTQMLRIMELLGTPTEERWPGLKNYPEYYQLSSFEVRYWNNLLPQWYQTVKNRDPQGLDLLMKMLQYDPKSRITAKQALEHVFFTSDKLWTTSPFLNQPIHYPERRISEDDSEVSSKRVLSTSLRSESKRFKGN | 2.7.11.22; 2.7.11.23 | null | phosphorylation [GO:0016310]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261] | euchromatin [GO:0000791]; mediator complex [GO:0016592]; nucleus [GO:0005634] | ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353]; transcription coactivator activity [GO:0003713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23; | null | null | null | null | FUNCTION: Catalytic component of the Cdk8 module/Srb8-11 module which is a regulatory module of the Mediator complex that regulates basal RNA polymerase II transcription. The Cdk8 module may sterically hinder the interaction between Mediator and RNA polymerase II leading to transcriptional repression of a subset of genes regulated by Mediator. {ECO:0000269|PubMed:14534314}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13959 | RBX1_SCHPO | MEDEMQIDKKEVEIEQKPPRFEIKKWNAVALWQWDIVVDNCAICRNHIMDLCIECQANTDSAAAQECTVAWGTCNHAFHFHCISRWLNTRNVCPLDNREWEFQRYGH | null | null | heterochromatin formation [GO:0031507]; protein ubiquitination [GO:0016567]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; ubiquitin-dependent protein catabolic process [GO:0006511] | CLRC complex [GO:0043494]; cullin-RING ubiquitin ligase complex [GO:0031461]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear SCF ubiquitin ligase complex [GO:0043224]; nucleus [GO:0005634] | cullin family protein binding [GO:0097602]; histone H3K14 ubiquitin ligase activity [GO:0140851]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF12678; | 3.30.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Component of E3 ubiquitin ligase SCF complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Seems to recruit the E2 ubiquitination enzyme, like UBC3/CDC34, to the complex and brings it into close proximity to the substrate. Component of the rik1-associated E3 ubiquitin ligase complex that shows ubiquitin ligase activity and is required for histone H3K9 methylation. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci. {ECO:0000269|PubMed:12167173}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13961 | NDC1_SCHPO | MVMLRTSFPSGSRTKAVRYHTLLRPILQQRFLRACFALLCLCCITSYWFSSGPFISLSFWFLSLVRGFVCFFFMFPYFVMLKSRMSTQKVTKQSLGAQLFYDFSPKSFFLVYLTFAVSVSCLCLFYIKGHASSIRLQWIASPNAYELPSLNERFVYMTYFSHILILALTVEHLYLQRDSPSRPVINVSFFNYIFQNLGWLIRFSFRKSIICCLFTPFSYAILRSYIWRFAALLTSCCRRIAYTKTPPKWPLSLRLLLHSFWMAFIVCLTFQIALLIFRVFLYSGPMIRGKLLSARSNDPNGTLVDGMKTKKKPLTECIATEELWFIAKRDPQRIKSIFQDIDRSVSIWQELYSITESRCKELATSLKILQSTGDFSAATSKKSGLTKKTNIPYSPNSNHEEINSIPLRNKNIFVPPSQGHSPLLEKIKKQGSLPSTTPVNEGGISDIIPKSLYDQVIRFISTFYKAPVFGIFRKTLRRQNEALLPNPWLFCVTVNSLTQLVLKSLKYDTYGVVARDISSILAVYCDTFDVLVSYKRSLVKNHSNSTNLDDDFKNLNSAANALHCGIIDITEKFQDFFTQLNLSPRIERRCWVLFREYKSNS | null | null | mitotic spindle pole body duplication [GO:1903087]; mitotic spindle pole body insertion into the nuclear envelope [GO:0140480]; mitotic spindle pole body localization [GO:1990608]; mRNA transport [GO:0051028]; nuclear pore organization [GO:0006999]; protein transport [GO:0015031]; spindle pole body localization [GO:0070631] | cytoplasm [GO:0005737]; mitotic nuclear bridge midzone [GO:0140512]; mitotic nuclear bridge midzone membrane domain [GO:0140599]; mitotic spindle pole body [GO:0044732]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nuclear pore transmembrane ring [GO:0070762]; spindle pole body [GO:0005816] | spindle pole body-nuclear membrane anchor activity [GO:0106166] | PF09531; | null | NDC1 family | null | SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus membrane; Multi-pass membrane protein. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Central core structure of the nuclear pore complex. | null | null | null | null | null | FUNCTION: Component of the nuclear pore complex (NPC) and the spindle pole body (SPB), which plays a key role in de novo assembly and insertion of both structures in the nuclear envelope. Involved in the formation of the bipolar mitotic spindle. Anchors the spindle pole body in the nuclear envelope. {ECO:0000269|PubMed:9763447}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13978 | AT101_SCHPO | MTNTVTIELKIGYKYAAEVVKAVLGVILFHRQFSTVPARTIDVLDITVPTLVGAELNEQLATKAAEFIDTIRNEAGANGQMILLLYERSPKKSWFGKGNTIPWEQWILHTTILEEGDSYQESSLSLEAAVEQIVQAVNLRSLSYLPPVAMDSGNYPYEIVTPTSTEGWGSLLKRMIIENVSGGD | null | null | autophagosome assembly [GO:0000045]; macroautophagy [GO:0016236]; meiotic cell cycle [GO:0051321]; protein transport [GO:0015031]; sporulation resulting in formation of a cellular spore [GO:0030435] | Atg1/ULK1 kinase complex [GO:1990316]; cytosol [GO:0005829]; nucleus [GO:0005634]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045] | protein kinase binding [GO:0019901] | PF07855; | null | ATG101 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Preautophagosomal structure membrane {ECO:0000269|PubMed:23950735}; Peripheral membrane protein {ECO:0000269|PubMed:23950735}. | null | null | null | null | null | FUNCTION: Autophagy factor required for autophagosome formation (PubMed:23950735). Component of the atg1 kinase complex in which it stabilizes atg13 (PubMed:26030876, PubMed:28976798). Is also responsible for recruiting downstream factors to the autophagosome-formation site (PubMed:26030876). Has a role in meiosis and sporulation (PubMed:16303567). {ECO:0000269|PubMed:16303567, ECO:0000269|PubMed:23950735, ECO:0000269|PubMed:26030876, ECO:0000269|PubMed:28976798}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13983 | HRQ1_SCHPO | MSQTPIKKEESNDQDDKFEFKKYINEGKLPLKADNPKKKPQLGTIQANQPIPSIFDNLFNLFKVINTTYTFLYLRNSLTITFPLLNSSVKQSLKKELTIGDLSQLREICPQIIELNYKSLASLALEINKNVYTDLNPELYTGSTVSQSSEYVLVIELLETQERSSKRRRREGPTMKANIQRQKLDFNNLKKAIELRNQKFLQGIKEYIKKCQLTELDPTQQLLTQSRKNQPVPPDSPSIPNDSIENCNLNTKACSIEELLNEIASESSYEGQIVQEALHTYPAVEAQYGALSRPLSQELINALYTSRNIEKTYKHQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDNQSTAFFVFPTKSLAQDQKKSLIDILSYMPTLKNIRVDTFDGDTPLESRESIIRSANIIFTNPDMLHQTILPNANRWYYFFKNLKLFVLDEAHVYNGIFGVHVAFVLRRMRRIAEYFGNSQYRFVSCSATIEDPLQHMKKIFGVDNIKLINYTSSPSGSKKFVMWNPPYVDPKHPDDGKKSAISEASKLLIKFAEKRVRTIVFCRVRKTCESLMRLVRQELKTKQKGDLLSKIQSYRAGYTVQERRKIESEMFNGKLYGIIATNALELGIDIGSLDAVITIGFPYSLSNLRQQFGRAGRRNKSSLAVYIVETFPVDQFYLKHPILIHTQPNAELTLDLTNEVLLASHLQCAAYELPINIRSDEKFFGNQIQDICEANLEMVEESYRPHPKYLPFPASQVRIRSVSEDMFTLVDVTNDKNVILELLEPFRVALTAYEGAVYVYQGKTFIIRLLNINKRIITAHQVDVEWSTLQRDFTDVDPVRSLMKKTMHGSTNIYFGAVKATLHVFGYFKVNKQKDILDVVDITDHPVEIDSRGFWIDVPWHIIEVLSLKKINGAASIHAAQHALLSLMPIFISNSGNDIRTECKAGEKEYKEAKSERRRPSRLIFYDNCGDSSGAGLCNKAYEHTDELITMAIERIESCDCKVREGCPGCITSSKFEGGVCSGEVLDKVGALILLKMLLCQHVNLDIYADGPEIDSYHALRTLIPSC | 3.6.4.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q05549}; | interstrand cross-link repair [GO:0036297]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair involved in interstrand cross-link repair [GO:1901255]; UV-damage excision repair [GO:0070914] | nucleus [GO:0005634]; site of double-strand break [GO:0035861] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; bubble DNA binding [GO:0000405] | PF08839;PF00270;PF00271;PF09369; | 3.40.50.300; | Helicase family, HRQ1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22064477}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000269|PubMed:22064477}; | null | null | null | null | FUNCTION: Helicase with 3'-5' helicase activity involved in genome stability (PubMed:22064477). Functions in the nucleotide excision repair (NER) pathway and plays a critical role in DNA interstrand cross-link repair (PubMed:22064477). Unwinds relatively long duplex DNA up to 120-bp and requires a long 3'-tail of at least 70 nucleotides for efficient unwinding of duplex DNA (By similarity). Shows both processive helicase and DNA strand annealing activities (By similarity). Affects telomere length by a non-catalytic mechanism, probably through inhibiting telomerase by competing with it for ssDNA binding (By similarity). {ECO:0000250|UniProtKB:Q05549, ECO:0000269|PubMed:22064477}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13988 | POT1_SCHPO | MGEDVIDSLQLNELLNAGEYKIGELTFQSIRSSQELQKKNTIVNLFGIVKDFTPSRQSLHGTKDWVTTVYLWDPTCDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITLRSYRDRTQGLSKDQFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLNKIWDEQTNKHKNGELLSTSSARQNQTGLSYPSVSFSLLSQITPHQRCSFYAQVIKTWYSDKNFTLYVTDYTENELFFPMSPYTSSSRWRGPFGRFSIRCILWDEHDFYCRNYIKEGDYVVMKNVRTKIDHLGYLECILHGDSAKRYNMSIEKVDSEEPELNEIKSRKRLYVQNCQNGIEAVIEKLSQSQQSENPFIAHELKQTSVNEITAHVINEPASLKLTTISTILHAPLQNLLKPRKHRLRVQVVDFWPKSLTQFAVLSQPPSSYVWMFALLVRDVSNVTLPVIFFDSDAAELINSSKIQPCNLADHPQMTLQLKERLFLIWGNLEERIQHHISKGESPTLAAEDVETPWFDIYVKEYIPVIGNTKDHQSLTFLQKRWRGFGTKIV | null | null | regulation of telomere maintenance via telomerase [GO:0032210]; telomere capping [GO:0016233]; telomere maintenance [GO:0000723] | chromosome, telomeric repeat region [GO:0140445]; cytosol [GO:0005829]; nuclear telomere cap complex [GO:0000783]; nucleus [GO:0005634]; shelterin complex [GO:0070187]; telomere cap complex [GO:0000782] | G-rich strand telomeric DNA binding [GO:0098505]; single-stranded telomeric DNA binding [GO:0043047]; telomerase inhibitor activity [GO:0010521] | PF02765;PF16686; | 2.40.50.140; | Telombin family | null | SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. | null | null | null | null | null | FUNCTION: Single-stranded telomeric DNA-binding protein that is required to protect the 3'-end telomeric overhang. It binds the consensus sequence 5'-GGTTAC-3'. Regulates telomerase and telomere length. {ECO:0000269|PubMed:11349150, ECO:0000269|PubMed:12463756, ECO:0000269|PubMed:18535244}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13995 | DAP1_SCHPO | MASTQVVFIVTLFLYLLITRWRRKNEKSFIASEEPKQPEWRDYTPAELKEYNGSKNSLVFLAIKGTVYNVTMGSKFYGPQGPYSAFAGHDASRGLAKNSFDDEFIPDSDAEELDDCSDLNDEERQALNDWKAFFDQKYQAVGRLISPREARAAATISETEEKVAHN | null | null | ergosterol biosynthetic process [GO:0006696] | endomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | enzyme activator activity [GO:0008047]; metal ion binding [GO:0046872]; steroid binding [GO:0005496] | PF00173; | 3.10.120.10; | Cytochrome b5 family, MAPR subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Required for sterol biosynthesis. Functions as a positive regulator of cytochrome P450 enzymes erg5 and erg11. Function requires bound heme. {ECO:0000269|PubMed:17276356}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14003 | RFC3_SCHPO | MSIEKGKGRAMDIDLPLGSESTLPWVEKYRPANLEDVVSHKDIISTLEKFISSNRVPHMLFYGPPGTGKTSTILACARKIYGPNYRNQLMELNASDDRGIDAVREQIKNFASTRQIFASTFKMIILDEADAMTLAAQNALRRVIEKYTKNVRFCIICNYINKISPAIQSRCTRFRFQPLPPKEIEKTVDHVIQSEHCNIDPDAKMAVLRLSKGDMRKALNILQACHAAYDHIDVSAIYNCVGHPHPSDIDYFLKSIMNDEFVIAFNTISSIKQQKGLALQDILTCIFEALDELEIKPNAKIFILDQLATIEHRMSFGCSEKIQLSAMIASIKTGVDLAAKVN | null | null | DNA repair [GO:0006281]; DNA strand elongation involved in DNA replication [GO:0006271]; DNA-templated DNA replication [GO:0006261]; mitotic DNA replication leading strand elongation [GO:1903460]; UV-damage excision repair [GO:0070914] | chromatin [GO:0000785]; Ctf18 RFC-like complex [GO:0031390]; cytosol [GO:0005829]; DNA replication factor C complex [GO:0005663]; Elg1 RFC-like complex [GO:0031391]; nucleus [GO:0005634]; Rad17 RFC-like complex [GO:0031389] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA clamp loader activity [GO:0003689]; DNA clamp unloader activity [GO:0061860] | PF00004;PF08542; | 1.10.8.60;1.20.272.10;3.40.50.300; | Activator 1 small subunits family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. Subunit 3 binds ATP. Also involved in replication and DNA damage checkpoint controls, probably functioning as a checkpoint sensor. {ECO:0000269|PubMed:10588638, ECO:0000269|PubMed:16040599}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14008 | CAM2_SCHPO | MPASKEQTDEMKEAFVLYDIDKDGLIPTSHVGSVLRSLGINVTDAELAKLSNELGDAIDEKKFMSFVSNKLRETESEEEYIKAFRVFDKDNSGYIETAKFADYMKTLGEKLSDNEVQLMVQEADPTNSGSFDYYDFVQRIMAK | null | null | actin cytoskeleton organization [GO:0030036]; ascospore formation [GO:0030437]; ascospore-type prospore membrane formation [GO:0032120]; mitotic actomyosin contractile ring assembly [GO:1903475]; spindle pole body organization [GO:0051300] | cell cortex [GO:0005938]; cell cortex of cell tip [GO:0051285]; central plaque of spindle pole body [GO:0005823]; cortical cytoskeleton [GO:0030863]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mating projection actin fusion focus [GO:1990819]; mating projection tip [GO:0043332]; medial cortex [GO:0031097]; myosin I complex [GO:0045160]; myosin II complex [GO:0016460]; prospore membrane [GO:0005628] | calcium ion binding [GO:0005509]; enzyme regulator activity [GO:0030234]; myosin heavy chain binding [GO:0032036] | PF13499; | 1.10.238.10; | Calmodulin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:17202724}. Prospore membrane. Note=Accumulates at the cell poles in interphase cells and at the medial septation site in post-mitotic cells, colocalizing with myo1 and F-actin patches. During the mating process, a single dot is detected a the tip of the mating projection. During meiosis I, dots disperse into the cell periphery and the cytoplasm. At metaphase II, intense signals appear near meu14 rings which are formed at the leading edge of expanding forespore membranes. Localization is dependent upon myo1 with the exception of the localization to mating projections. {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:17202724}. | null | null | null | null | null | FUNCTION: Plays a role in meiosis and sporulation. {ECO:0000269|PubMed:12161753, ECO:0000269|PubMed:17202724, ECO:0000269|PubMed:21693583}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14011 | PRP19_SCHPO | MFCSISGETPKEPVISRVSGNVYEKRLIEQVIRETSKDPVTQQECTLEDLVPVKVPDFVRPRPPSATSLPALLSLFQEEWDSVALEQFELRRNLTETKQELSTALYSLDAALRVISRLTKERDEAREALAKFSDNIGTVSSKTIEVQEVEMGESDDQLKTSLRSTVEKTFQELSSKRKRTKLQPKWATDDAVSQLLQATPSTILENLETESTTSFFPSPENSSFVLCLHKDELLCLDIQSNSTLKIFEGSALACCWLTSSKIAVATADAISIFEFPVSSSGLQSVGEPTSSIPIDEKVNFLQAHPSGEYLLAASNEKCYIFSLKSQVYNITVAQHITSLAVHPDGNLFVAGLENGELRFFETSSGNELTKFGPHSSPVKTLQFGENGYWLVVTTNDDSDIFIWDLRKSELVQKIPLQTKVAAVSLDITSQLLVSSDGETLYVHIYVKSSKSWRCMSQTHVSSISNLVWLNELHQLLFSTSNGAILRLG | 2.3.2.27 | null | DNA repair [GO:0006281]; mRNA splicing, via spliceosome [GO:0000398]; protein K63-linked ubiquitination [GO:0070534] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; post-mRNA release spliceosomal complex [GO:0071014]; Prp19 complex [GO:0000974]; spliceosomal complex [GO:0005681]; U2-type catalytic step 1 spliceosome [GO:0071006] | ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF12894;PF08606; | 2.130.10.10;3.30.40.10; | WD repeat PRP19 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UMS4}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:P32523}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:P32523}. | null | null | FUNCTION: Probable ubiquitin-protein ligase involved in pre-mRNA splicing (By similarity). May also function in DNA repair (By similarity). {ECO:0000250|UniProtKB:P32523}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14019 | HAL4_SCHPO | MGEKDKLHEISSKFASLGLGSLKSTPKARETTEPPPPSSQQPPSTPNGKEAASPSALKQNVRPSLNSVQQTPASIDAVASSSNVSLQSQQPLSKPVVSSKPNQTTAMPPPSNNPSRHVSSTSNKPAAVSPNPAAHHAELPSGSVPPSASVSRANSTATTTPHKAGVVSNPAAANVHVLSVAASPNPSTPSNGPAPVSTTATPSRNPVTRLQRIFSQNSVSRQNSRTGRGAAVANTEETNSTGGSETGGAANSSSTSNPSSAKWSRFTVYDDASHTHQLRPARRQEKLGKMLKDFLAGNSKKREEERIAKEAADAQHQLSLVQSWINGYGQEKLADKKDPAKVSASFVEKYGRCQEVIGRGAFGVVRIAHKVDPQNSGSETLYAVKEFRRKPAESQKKYTKRLTSEFCISSSLRHPNVIHTLDLIQDGKGDYCEVMELCSGGDLYTLIMAAGRLEPMEADCFFKQLMRGVDYLHDMGVAHRDLKPENLLLTVSGSLKITDFGNGECFRMAWEKEAHMTCGLCGSAPYIAPEEYTESEFDPRAVDVWACGVIYMAMRTGRHLWRVAKKSEDEYYSRYLMDRKNESGYEPIEMLERSRCRNTLYNILHPNPTYRLTAKQIMKSEWVRSITLCEAGNAGL | 2.7.11.1 | null | intracellular monoatomic cation homeostasis [GO:0030003]; intracellular potassium ion homeostasis [GO:0030007]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310] | cytosol [GO:0005829] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; | null | null | null | null | FUNCTION: Promotes K(+) uptake, by the potassium transporter trk1-trk2, which leads to the subsequent cellular resistance to toxic cations such as Na(+), Li(+) and Ca(2+). {ECO:0000269|PubMed:15870269, ECO:0000269|PubMed:16164595}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14021 | PRW1_SCHPO | MAVSAVPHPSKQAQASEEGINQEKCINEEYKIWKKNSPFLYDLIITRALEWPCMSLQWYPEQQIFAEHGYTEQKMFLGVRADVGKYLLAVASIQLPYLNQTVPPTTMEGASAGDESSLRVNISNLYSHPESVCSAKLMPQDDSCVATVGNYHNDVLVFDKESFESYSSASESPLKPKYRLTKHTQPCTSVCWNFLSKGTLVSGSQDATLSCWDLNAYNESDSASVLKVHISSHEKQVSDVRFHYKHQDLLASVSYDQYLHVHDIRRPDASTKPARSVHAHSGPIHSVAFNPHNDFILATCSTDKTIALWDLRNLNQRLHTLEGHEDIVTKISFSPHEEPILASTSADRRTLVWDLSRIGEDQPAEEAQDGPPELLFMHGGHTSCTIDMDWCPNYNWTMATAAEDNILQIWTPSRSIWGNEQLEEDATAYLS | null | null | chromatin remodeling [GO:0006338]; regulation of DNA-templated transcription [GO:0006355]; transcription initiation-coupled chromatin remodeling [GO:0045815] | Clr6 histone deacetylase complex I'' [GO:1990483]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; Rpd3L complex [GO:0033698]; Rpd3L-Expanded complex [GO:0070210]; Rpd3S complex [GO:0032221] | H3-H4 histone complex chaperone activity [GO:0000510]; histone binding [GO:0042393]; nucleosome binding [GO:0031491] | PF12265;PF00400; | 2.130.10.10; | WD repeat HIR1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12773392}. | null | null | null | null | null | FUNCTION: Has a role in chromatin assembly and chromosome segregation. Involved in the deacetylation of histones. {ECO:0000269|PubMed:12773392}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14022 | CTA5_SCHPO | MDSIELKQLVPENDSEPGTPRQLLFQHYDISNEETIGIKPFKSIPAKVYILRVTEILTLGLLHLILTWLPEFRLKWIEAPCSNEDVEFVAISDPSGTSSIEKVSSICLKNDIQTSSFVLPSGKTRYFEYKKLRFYLEPLNLQWVLMPLETSAYSLVTSTPAYIQNGLDTFTIAKLRQVYGSNSLVSTKKSIVTILLNEVLHPFYLFQAVSVLIWLCDSFVFYSCCIVFISSYSIFLSVKESKESENRIHSIIGAPQPVTVIRNQVKQTVLADDLVIGDLLYFSNLDLKTCPVDGILFSSSCLLDESMVTGESVPARKFPLEDNSLDSWMIASCNIFSPHLIHAGTKFLKIDSTPSTPCLISVVRTGFRSNKGQLIRNLLYPNLRPSQLYLDSMSFLKTMAILSFVSIVFIAIYLNLYNASFGHVVLRSLDVLTILVPPALPATLSVGIANSIARLSRALIYTTSPESIHNAGCLSTFVFDKTGTLTENSVQLSCVYVKSGSNGLLKQVDADSLSLDSTKLNAHAYRVATCSQSLELVGNELVGDPLEVTLFTQFNGTFCATIRASNTPHPPLFSVSNSFDGPSQIFSIYKALEFDPVLRRMSVICSTSTERSLMLFTKGAPESILAISSQQSIPSNVQEVIHTLSSKGFRIIAFASKNLITPLQELIHLSRSTLESNVTFQGLFVLESPLRESSKDVISSLLRSKMEVSICSGDSLFTSVFVAKHCGALDSCNFIYTAELADSGDDCPQIHFEKIDLQTQNFQPIPDGFSLKDVILEKDSSLCMDGKLLQRLLTMLSFNEIKILLSKLRVLARMSPFDKATYVELCQKYGCKVGFCGDGANDCIALKQADVGVSLSDSEACAAASFVSKKKSIKDVFNVLLEGRCSLILSHRCFQYMVLCAIVQFSGVFFLYLKNYNFNDNQFLFMDLLIIFPLSAAMSYFDPAQNLTSNRPNSTLFGKGRVKDLGIQSVLIWLSHGLLTLILHELNWVELPEWQLEKSNTKNVLVTSIFLLSSLQYLGICIGINQSSEFLSPIWKKKTYVCLCTTIGLCNIYLCFANENHIISRCLQITRLPTLYRFIILFMGVISCCLTSILNM | 7.2.2.- | null | calcium ion transmembrane transport [GO:0070588]; intracellular calcium ion homeostasis [GO:0006874]; transmembrane transport [GO:0055085] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled monoatomic cation transmembrane transporter activity [GO:0019829]; metal ion binding [GO:0046872]; P-type transmembrane transporter activity [GO:0140358] | PF13246;PF00690;PF00122;PF12409; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type V subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:19168988}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; | null | null | null | null | FUNCTION: Plays a role in regulating calcium and manganese homeostasis responsible for cell cycle progression. {ECO:0000269|PubMed:19168988}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14023 | ELP3_SCHPO | MSTSSLAFLKAKACAEIVAELIASENQNKVINLNALKMRISKKHQLSESPRLTDIIAAIPPDAYLKESLMRKLRAKPVRTASGIAVVAVMCKPHRCPHIAMTGNVCVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYDPYEQARGRVEQLRSLGHTVDKVEYIIMGGTFMSLPESYRHTFIANLHNALSGATTEDLDEAVKFSEQSETKCVGITIETRPDYCLDQHLDEMLRYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCETFQLAKDTGYKVVTHMMPDLPNVGMERDIFQFQEYFENPAFRTDGLKLYPTLVIRGTGLYELWKTGRYKNYTPNALVDLIARILALVPPWTRIYRIQRDIPMPLVSSGVETGNLRELALNRMRDLGTKCRDIRAREVGMQEVHHKIHPEQVELLRRDYTANGGWETFLSYEDPKQDILIGLLRLRQCSDKTYRPEFTSQPTSLVRELHVYGSAVPVHSRDPKKFQHQGFGTLLLEEAERIAKYEHGSKKISVISGVGVRKYYQKLGYTLDGPYMSKWL | 2.3.1.311 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:Q02908}; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250|UniProtKB:Q02908}; | regulation of cytoplasmic translational fidelity [GO:0140018]; tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation [GO:0002926] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; elongator holoenzyme complex [GO:0033588]; nucleus [GO:0005634] | 4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; tRNA binding [GO:0000049]; tRNA uridine(34) acetyltransferase activity [GO:0106261] | PF04055;PF16199; | 3.40.630.30; | ELP3 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA + 2 H(+) + L-methionine; Xref=Rhea:RHEA:61020, Rhea:RHEA-COMP:10407, Rhea:RHEA-COMP:11727, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315, ChEBI:CHEBI:74882; EC=2.3.1.311; Evidence={ECO:0000250|UniProtKB:D5VRB9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61021; Evidence={ECO:0000250|UniProtKB:D5VRB9}; | null | PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000269|PubMed:22768388}. | null | null | FUNCTION: Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:22768388). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). {ECO:0000250|UniProtKB:D5VRB9, ECO:0000250|UniProtKB:Q02908, ECO:0000269|PubMed:22768388}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14031 | PGT1_SCHPO | MTARNSASIPTSIRKTSENEVSGDETPAGVGNLSTKTASKTSLTFRQSSSDESTSSYSGNHHNINIQHHPNRPFRTNSSSFSPNDYSISESPSKSKKDGVHVSAVQLDNETDSEVESEVEELERELEAIEDSVYPEVRAAVNPTDDVNLPVNTWRTWVLTTIFVIVFAAVNQFFSLRYPALSISFIVAQLILFPLGKLLNLLPNWKIGYGRFSFYLNSSPFNVKEHAAITIAVSLTSSTAYATNILSAQTSFYKQNLSWGYKILIVLTSQMLGYGFAGLTRRWIVYPAAMIWPQTLVSTVLFRTLHGNSGNDIGVLKNNRISANGWTISRYRFFAYVMIGSFVFYWFPGFIFKGLSYFTVLCWIWPKNRVVNQLFGYNSGLGILPLTFDWQQVVYNSNPLASPWWVICNTFGSVVLIFWIVVPILYYKGVWFSNYLPMLSSSTFDHTGVSYNSSRVLNSDYSFNHTKYESYSPLYMPMSYSMSTALNFAAVTAIFTHCALYNGKDIWQRLWKESGKDECIHRKLMRNYKEAPQWWYATLFIVVFGLTIFTVRYYDTQCPVWALIVALLIFIVNFIPQGVLEGITNQHVGLNIITELIGGYILPGKPLANLMIKLYGFIPMRQGLEFSRDLKLAQYMKIPPRILFFVQLFATILGGITQVAVQEWMNYHIPGICTTSQSNGFTCPNGRSIYNASLIWGAIGPAKMFSKGKPYYPLIFFFLIGAVAPFITWGLRKRFPKSWIGKLNAPVLFTGPGNIPPATGINYSSWAIVGFIFNYVIRKRAIHWWRKYNYVLAAAMDSGVAVAGVVIFLCVSYPGGKITWWGNTVYTKTYDWKSVPYRSLGPNETFGYTNW | null | null | glutathione import across plasma membrane [GO:0098709]; glutathione transmembrane transport [GO:0034775]; protein transport [GO:0015031] | endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]; plasma membrane of cell tip [GO:0031520] | glutathione transmembrane transporter activity [GO:0034634]; oligopeptide transmembrane transporter activity [GO:0035673] | PF03169; | null | Oligopeptide OPT transporter family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=63 uM for glutathione {ECO:0000269|PubMed:18662319}; | null | null | null | FUNCTION: High-affinity glutathione transporter which plays a role in scavenging glutathione from the extracellular environment for the maintenance of sulfur homeostasis. {ECO:0000269|PubMed:18662319}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14036 | SMD2_SCHPO | MADLVDKPRSELSEIELARLEEYEFSAGPLSVLQQAVKNHDQVLINCRNNKKLLARVKAFDRHSNMVLENVKEMWTEKKRTASGKKGKAINKDRFISKMFLRGDGVVLVVRIPSA | null | null | mRNA 5'-splice site recognition [GO:0000395]; spliceosomal snRNP assembly [GO:0000387] | catalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; nucleus [GO:0005634]; pICln-Sm protein complex [GO:0034715]; post-mRNA release spliceosomal complex [GO:0071014]; precatalytic spliceosome [GO:0071011]; Prp19 complex [GO:0000974]; spliceosomal complex [GO:0005681]; U1 snRNP [GO:0005685]; U2 snRNP [GO:0005686]; U2-type prespliceosome [GO:0071004]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U5 snRNP [GO:0005682] | RNA binding [GO:0003723] | PF01423; | 2.30.30.100; | SnRNP core protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62316}. | null | null | null | null | null | FUNCTION: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (By similarity). {ECO:0000250|UniProtKB:P62316}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14040 | DI3L2_SCHPO | MDLKPNIRRKEKRNLLKGEAALEKKGSIDRKTKNKAYPSTTHDPHQNDDSNIPGLGSGLLERIKDIVQRPTDTQLKGQDSNHKKASLTETKTEKAKVKPKAKKKNSKEKISKSSKQDEHKTDVHKESVSKLSKNLESRNNRDENSAKREKNNSHQVEADTNNATEMVSSNAKKSVYPLYYDSATVKKGLKSGTLFKGTLRILENHRSAFACMEDIPDFYVDGPIARNRAFHNDVVIVEPVMNNDSPTEKSNFLQNGVEKVKIKDHDDELGGAMEHLERLEIKSVASFKGDSRTRARVVAIEKRAEISKIVGILRAPGWSLKNVEYVSKKSSYAIFIPKDKRLPFITIHKNDLSDLSGENWIENILKHHDQLFSVEITRWSIYSRYPMGVLGEKLGNITDVEAYTNALLLENGISSSPFSDEVLNCLPPDDWIISHEEIKKRRDLRNELIITIDPETARDLDDAVSCRALDNGTYEVGVHIADVTHFVKPDSALDKEAASRATTVYLVQKAIPMLPPLLCERLCSLNPNVERLAFSVFWKLDSNGKEIGKRWFGKTVIKTCARLAYSEAQGVIEGKSWDDAVGKPIGGTHTPKDVETSILTLCEISRKLRKDRFAKGAVEINSTELKFQLDEYGMPNKCEVYEQTDANHLIEEFMLLANRSVAEHISKNFSNNSLLRRHASPKEKQINEFCHFLKSMNFDFDASSSAAFNASMVRLRSTFNEELVELFENMAVRSLNRAEYFCTGDFGEKTDWHHYALSFNHYTHFTSPIRRYPDIIVHRLLERSLKNTSPGIDKKNCSLVAAHCNEKKEKSTTVQEDSQQLFLSVYIAEYCKKHDKKSMPVQAFATRISGNSIDVYISEYGISNRVDLSSDDRIKSFIVAPDDSSVKITLFDDSQKTIALTDRFQVYLYSDYSRTFFSIRCSLVSLN | 3.1.13.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03045}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03045}; | mRNA catabolic process [GO:0006402]; nuclear-transcribed mRNA catabolic process, exonucleolytic [GO:0000291]; nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' [GO:0034427]; polyuridylation-dependent mRNA catabolic process [GO:1990074] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; P-body [GO:0000932] | 3'-5'-RNA exonuclease activity [GO:0000175]; metal ion binding [GO:0046872]; poly(U) RNA binding [GO:0008266] | PF17849;PF00773; | 2.40.50.690;2.40.50.700; | RNR ribonuclease family, DIS3L2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23503588}. Cytoplasm, P-body {ECO:0000269|PubMed:23503588}. | null | null | null | null | null | FUNCTION: 3'-5'-exoribonuclease that specifically recognizes RNAs polyuridylated at their 3' end and mediates their degradation. Component of an exosome-independent RNA degradation pathway that mediates degradation of cytoplasmic mRNAs that have been deadenylated and subsequently uridylated at their 3'. {ECO:0000255|HAMAP-Rule:MF_03045, ECO:0000269|PubMed:23503588}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14050 | MSY2_SCHPO | MNEHRREPHRRSGYQDDSAFTNTEKLVDELDHNVEPEQLLEKNRTDFKLMYVIVKFYRWFNNLSFITRWITIWFPLAGALVIPLAVGVSPYPNAKLGGVRIFWIFVWLEVAWGGFWVSRVIARLLPYILYPLMGILPFTMYKYTVILTALEMPLAIFFCSIVCVCTFSPIMIGKGNFTSTTVTTTTSATATPTASASSNAVESVFVTKTAASVPSWIKVITKILGAAVVTSIVLLLEKIFLHFIGFHYHEVQYQYRITDNKRNTAVLAKLLTAALDAPYHDSPRVRRQDYLLGLIDTRSMSESKGSGNGKLRKVKKISKNAKRIFSKTRNAISTAFTDMLGKHAKDLTPEQEFILETIRSKKKCLALARKIWYSLVPEGEDCFQKEDLIGLIPDDEINDIFHILDNDYSRTVTLDEMEQFTREISIEFRSISSSLRDVDLALGKLDRVGLGVVGIIAVLTFISFLDTSFATILAAFGTTLLSLSFVFSTSAQELMSSIIFLFSKHPFDISDVVIVNNIKYEVVSLSLLFTVFRTMGGSTVQAPNSLLNTLFIENLRRSQPQSETITIVSPFATDFKQLERLRDLLLTFVKENERDFRPIIDLNVSDFSTLDSLKFTVTYYYKSNWQNVSLQCVRRNKFMCALKNAIATTNLPAVADPVRGSPDYPFVIEQYNLERPEYSKTASRPQFSDISSTASSNSLSNKPGFAHSESRNYHTHDEDNSSDDNHKREDRGHLPAQYLRQSVATWQIPNLISAIEAYDSQNESSQENATYTVVESNGNANGDNTATNSQGATDNGQTTTNTTQNNVDNTQATTDNTQANTDNMQVAIDYSQNMDGQIQY | null | null | calcium ion transmembrane transport [GO:0070588]; cell volume homeostasis [GO:0006884]; intracellular calcium ion homeostasis [GO:0006874] | cortical endoplasmic reticulum [GO:0032541]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; mechanosensitive monoatomic ion channel activity [GO:0008381] | PF00924;PF21082; | 2.30.30.60; | MscS (TC 1.A.23) family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22910366}; Multi-pass membrane protein {ECO:0000305}. Note=Cortical endoplasmic reticulum. {ECO:0000269|PubMed:22910366}. | null | null | null | null | null | FUNCTION: Regulates intracellular calcium levels and cell volume for survival in response to hypo-osmotic shock (PubMed:22910366). Involved in maintaining vacuole integrity and protecting the nuclear envelope upon hypo-osmotic shock (PubMed:25041276). {ECO:0000269|PubMed:22910366, ECO:0000269|PubMed:25041276}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14063 | IMA1_SCHPO | MSASSRFIPEHRRQNYKGKGTFQADELRRRRETQQIEIRKQKREENLNKRRNLVDVQEPAEETIPLEQDKENDLELELQLPDLLKALYSDDIEAQIQATAKFRKALSKETNPPIQKVIDAGVVPRFVEFLSHENNLLKFEASWALTNVASGSSNQTHVVVEANAVPVFVSLLSSSEQDVREQAVWALGNIAGDSPMCRDHVLQCGVLEPLLNIIESNRRLSMLRNSTWTLSNMCRGKNPQPDWNSISQVIPVLSKLIYTLDEDVLVDALWAISYLSDGANEKIQAIIDAGIPRRLVELLMHPSAQVQTPALRSVGNIVTGDDVQTQVIINCGALSALLSLLSSPRDGVRKEACWTISNITAGNSSQIQYVIEANIIPPLIHLLTTADFKIQKEACWAISNATSGGARRPDQIRYLVEQGAIKPLCNLLACQDNKIIQVALDGIENILRVGELDRANNPDKINLYAVYVEDAGGMDLIHECQNSSNSEIYQKAYNIIEKFFGEEDEIEELEPETVGDTFTFGTTQEPAGDFQFSATNAEDMAM | null | null | NLS-bearing protein import into nucleus [GO:0006607]; protein import into nucleus [GO:0006606] | cytoplasm [GO:0005737]; nuclear envelope [GO:0005635]; nuclear periphery [GO:0034399]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139] | PF00514;PF16186;PF01749; | 1.20.5.690;1.25.10.10; | Importin alpha family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:15937127, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:9740803}. | null | null | null | null | null | FUNCTION: Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. Seems to act as a cytosolic receptor for both simple and bipartite NLS motifs. Has an essential role in mitotic chromosome condensation. Involved in nuclear protein import. Required for efficient nuclear import of both an SV40 nuclear localization signal-containing reporter protein and the pap1 component of the stress response MAP kinase pathway. Required for proper mitotic progression. {ECO:0000269|PubMed:15937127, ECO:0000269|PubMed:9740803}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14064 | BIR1_SCHPO | MKPITSSSKRRWNRFRREMCNYSKRLDTFQKKKWPRAKPTPETLATVGFYYNPISESNSEERLDNVTCYMCTKSFYDWEDDDDPLKEHITHSPSCPWAYILSSKNNPNQNPQAAALTKCREQTFVDKVWPYTNRPDYHCEPSVMAASGFVYNPTADAKDAAHCLYCDINLHDWEPDDDPYTEHKRRRADCVFFTWKDPNSLSPTKLSFLSTSNIDPEDLTEDNSILPVSPTRDSTKSHKTLNFSPSRKNNLNARPLTMSLYTNTSEEKDSQPTRAPQSPTKPVLLTAPRRKNKSPKKSKPAVFKPVKPIFSDEDEDDDDLTASQPFSKGICNDSMQVAKKNFTEEIPLKEDEKDNELEHLVSPATSVHTTVSDITGHQSVTDESDEQNNCMSTPPKIEIESKIEEEISVVSKSKEISSSVSSVGKEQNHTEKQVAIETPEQQKVEKEDEHLNLQGSFIEESTKQPISSKPSTSSPDMTDAATGGRVSSSSFRDKILQTNFSPRSTIDSFSNISKKRNSEEANDENDETNLKIPIPEKKRKFQEVLQSKNILVSSTEDSHEPVKVTEDSQTAIHVSKFEDLENKSMESEQSLQLLSESENDDKPLIDLIPLLAIKRKDNLVSGVLEKGKSTSTSKTKFDTSIVDFIEKPKTEISEVLPEEKRKAICDESQTVRVSIDRGVTKTRDVSSPVSDEKSENVNHEEANSGHTVMNVHSSLDPQPIVQPNELESGSYLKDLPDRNVGNSEKVTFQEDDINSPKLQSKNNQTVEAVNTETSDKLQEKEANHELENIEKIEEKLTEVDKVSLSDAFPDQEIKNSRTSVQNGTRSVSKNTPEKETKVDKIDNVSKKDVETSPGSCETSSAFAKTYAEKEVTSINLPSVRKPLDESYYDHSISPFDPLCQSSFLAPQTPVKSKHALPLVEANAPPWEPIDFSSLLESPVPNPVEPNKLSEKELDMTVEQWIKFMYAKCAKEFEEACEEKIEWLLEEGKRAEEYIQNL | null | null | cell division [GO:0051301]; mitotic sister chromatid biorientation [GO:1990758]; mitotic sister chromatid segregation [GO:0000070]; negative regulation of apoptotic process [GO:0043066]; positive regulation of protein ubiquitination [GO:0031398]; regulation of cell cycle [GO:0051726]; regulation of mitotic cytokinesis [GO:1902412]; signaling [GO:0023052] | chromatin [GO:0000785]; chromosome passenger complex [GO:0032133]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; meiotic spindle midzone [GO:1990385]; mitotic spindle [GO:0072686]; mitotic spindle midzone [GO:1990023]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721] | cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630] | PF00653; | null | null | PTM: Phosphorylated by ark1. {ECO:0000269|PubMed:11950927}. | SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere. Note=Interacts with the outer centromeric regions of the chromosomes during interphase. After chromatid separation moves to the middle of the spindle. | null | null | null | null | null | FUNCTION: Seems to act in the pleiotropic control of cell division. Has a role in chromosome segregation by recruiting condensin and ark1 kinase to appropriate sites as the cell progresses through mitosis. Ark1 activity depends upon bir1 function and phosphorylation. Ark1 with bir1 function is required for full-scale association with kinetochores and formation of a complex with mad3. {ECO:0000269|PubMed:10571085, ECO:0000269|PubMed:11554922, ECO:0000269|PubMed:16199877}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14072 | ATC4_SCHPO | MGSKALITSPDISSGQLYIKLPTFFHLYVWPFALFVYPYIGYVYQNKLYSEEVRYLTYIAVGTIHALFWLAGEWNTKVYCLMTCRKTDKVEQATHILVTPSKIGESSSVEPITKLVLPDSQTIQYSFSFQRKRFIYEPEKGCFANITFPMDEPSTIGTLKKSTGLTNIQSEIFLYRYGKNCFDIPIPTFGTLFKEHAVAPFFVFQIFCCVLWCLDDYWYFSLFSMFMIIALECSVVWQRQRTLTEFRTMSIKPYEIQVYRNKHWFPISTEDLLPNDVVSVLHNKEDSGLPCDLLLLSGSCVVNEAMLSGESTPLVKESIELRPEEAVIDVDELDKNAVLFGGTRVLQVTQSPFCKLKTPDNGVPAIVLRTGFETSQGSLVRTMVFSSEKVTANNRESLYFILFLLVFAIAASGYVWHVGSKTERSRYKLMLDCVMIITSVVPSELPMELSMAVNASLGALSKYYIYCTEPFRIPLSGHLDICCFDKTGTLTEEHMVVQGIAGVNRKDPYSLEKLSDASNDAILAIATAHTLVLLEQEGETPKVVGDPMEKATVENLGWSIEKKNFVSAPEGSVFYKGKVQIIRNFQFSSALKRQSSVSNVRVSGGSFKTFVSVKGAPEVIATMLREVPKDYEKIYKDYGRKGSRVLALGYKYFKNYIPENQVSDLSRESIESDLVFAGFLIFTSPLKEDARQTVQMLNNSSHRCMMITGDNPLTAVYVAEQVGIVEKPTLVLDIKHENEKILEWKSTDDTINLPMNPHKSLEASLYEKYDLCITGRALSQIINPDVIMSIFTHAWVYARVSPSQKEFMISTLKHNGYITLMCGDGTNDVGALKQAHVGVALLNASEEDMLEMQERARNQKLMGVYEKQIQLAKRFNLPTPPVPPALCHAFPPGPNNPHREKTQEGLNKVLEDLETKKASDVQLTEAEKAAERRANLANKMFDTLANASDDEAPKLKLGDASVAAPFTSKLAVVSSITNIVRQGRCTLVALVQMHKILALNCLITAYSLSVLHLDGIKFGDTQYTISGMLMSVCFYCVSRARPLETLSKERPQAGIFNTYIIGSVLGQFAIHIVTLIYITRVVYLYEDPLEKVDLEETFKPSLLNTAIYLLQLIQQVSTFAINYQGRPFREALSENKGMYYGLLGIAFVAIAGVTEFSPELNAKLQLVKMAYNFQIQLLATMVVDYAACWIIEELMKKYFRDNKPKEIVLRN | 7.4.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P39986}; | cell cycle [GO:0007049]; cell division [GO:0051301]; extraction of mislocalized protein from ER membrane [GO:0140569]; intracellular calcium ion homeostasis [GO:0006874]; protein transport [GO:0015031]; sporulation resulting in formation of a cellular spore [GO:0030435]; transmembrane transport [GO:0055085] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled monoatomic cation transmembrane transporter activity [GO:0019829]; membrane protein dislocase activity [GO:0140567]; metal ion binding [GO:0046872]; P-type ion transporter activity [GO:0015662] | PF00122; | 3.40.1110.10;2.70.150.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type V subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12058018, ECO:0000269|PubMed:16394583, ECO:0000269|PubMed:22132152}; Multi-pass membrane protein {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12058018}. | CATALYTIC ACTIVITY: Reaction=[protein]-with a C-terminal TM segment(out) + ATP + H2O = [protein]-with a C-terminal TM segment(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66168, Rhea:RHEA-COMP:16963, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90782, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P39986}; | null | null | null | null | FUNCTION: Endoplasmic reticulum translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum. Acts as a dislocase that mediates the ATP-dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane. Specifically binds mitochondrial tail-anchored transmembrane proteins: has an atypically large substrate-binding pocket that recognizes and binds moderately hydrophobic transmembranes with short hydrophilic lumenal domains (By similarity). Involved in controlling nuclear calcium ion levels. Required for cytokinesis and stabilizing microtubules (PubMed:12058018). Required for assembly of the forespore membrane (PubMed:16394583). Involved in calcium transport to the endoplasmic reticulum (PubMed:22132152). {ECO:0000250|UniProtKB:P39986, ECO:0000269|PubMed:12058018, ECO:0000269|PubMed:16394583, ECO:0000269|PubMed:22132152}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14079 | MDB1_SCHPO | MEIQFGNQRCRMVNSGGFLATDGSHLKEMETDDVLVEFLNIEHQLFIRNIRAIVKIADTTVLPSASDKKLLYYVFDETRVRINDTPVIFSKLEEDNANVNEGSKMGVMTVPNTPQKPNLQQQKFEAINANEDQIDYSSNLEQNYNSLIRQGSDQVIPLSRFASEKSALELEKELFSERIPESQSAAEPVLKVENSENDLDEKLVLDGQHVEGDHSSDTEEEVVSEDQKQLNKTDDESTFIESHQIYIQGETKSPSSVSQSLSGDPSLKPAEVFDRKQSAEINSPIEKDVNPQQNISDSSIKNNSIHSDEVNPEVRPDLTPSNENEESKRSAPEIALKEKESTSQDESNREAEEAPISTNYSFPSSSLEDQPDKNVQSSAVENKNKHTNLVTSSFNLTKPMKSFIRRNGLRVQESVTDETDFVILGSPPLRRTHKFLLATSLGIPLVSSQYLTDCIKSGKVLDFRSYKYKDEEAEAKWGFRLDDIHRRTCFNGKRLYITKAIRDSMVGDSIHGLYSILETSGAEIVGDIKRAQEKDTIILAQPDNDQEGRNMSATGLNVYKIELVALSILRDRIDFDEFLIDYDADSPTKVIGKRNVSKASRTGQGRKRSSRSSWNKPSAKEQRT | null | null | mitotic G2 DNA damage checkpoint signaling [GO:0007095] | cytoplasm [GO:0005737]; mitotic spindle midzone [GO:1990023]; nucleus [GO:0005634]; site of double-strand break [GO:0035861] | null | PF00533; | 3.40.50.10190; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:24806815, ECO:0000269|PubMed:26160178}. Chromosome {ECO:0000269|PubMed:24806815, ECO:0000269|PubMed:26160178}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:24806815, ECO:0000269|PubMed:26160178}. Note=Associated with chromatin. Relocalizes to discrete nuclear foci at DNA double strand breaks (DSBs) following DNA damage by the HO endonuclease and ionizing radiation (IR). Focus formation requires interaction with phosphorylated hta1 and hta2. During mitosis, localizes to spindles and concentrates at spindle midzones at late mitosis. Localization to spindle midzones requires ase1, but does not require phosphorylated hta1 nor hta2 (PubMed:24806815). Localizes to spindle midzones in anaphase (PubMed:26160178). {ECO:0000269|PubMed:24806815, ECO:0000269|PubMed:26160178}. | null | null | null | null | null | FUNCTION: Involved in DNA damage response (DDR) mediated through its interaction with phosphorylated H2A proteins hta1 and hta2 which mark the discrete foci of DNA damage. {ECO:0000269|PubMed:24806815}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14089 | IMB2_SCHPO | MGDNPWVLQEQVLVELSEVIKNSLSENSQTRNAALNLLEKAKDIPDLNNYLTCILINATELSVSIRSAAGLLLKNNVRVSSLESGSGLQSLDYTKSTVIRGLCDPEQLIRGISGNVITTIISRWGISTWPEVLPQLMEMLSSPASTTQEGAFSALTKICEDSAQELDRDFNGTRPLDFMIPRFIELARHENPKIRTDALFCLNQFVLIQSQSLYAHIDTFLETCYALATDVSPNVRKNVCQALVYLLDVRPDKIAPSLGSIVEYMLYSTQDSDQNVALEACEFWLAIAEQPDLCSALGPYLDKIVPMLLQGMVYSDMDLLLLGNDADDYDVEDREEDIRPQHAKGKSRITLNTQGPITQQGSSNADADELEDEDEDDDEFDEDDDAFMDWNLRKCSAAALDVLSSFWKQRLLEIILPHLKQSLTSEDWKVQEAGVLAVGAIAEGCMDGMVQYLPELYPYFLSLLDSKKPLVRTITCWTLGRYSKWASCLESEEDRQKYFVPLLQGLLRMVVDNNKKVQEAGCSAFAILEEQAGPSLVPYLEPILTNLAFAFQKYQRKNVLILYDAVQTLADYVGSALNDKRYIELLITPLLQKWSMIPDDDPNLFPLFECLSSVAVALRDGFAPFAAETYARTFRILRNTLYLITTAQNDPTVDVPDRDFLVTTLDLVSGIIQALGSQVSPLLAQADPPLGQIIGICAKDEVPEVRQSAYALLGDMCMYCFDQIRPYCDALLVDMLPQMQLPLLHVSASNNAIWSAGEMALQLGKDMQQWVKPLLERLICILKSKKSNTTVLENVAITIGRLGVYNPELVAPHLELFYQPWFEIIKTVGENEEKDSAFRGFCNILACNPQALSYLLPMFVLCVAEYENPSAELRDMFQKILQGSVELFNGKASWQASPEVLAQIQAQYGV | null | null | mRNA transport [GO:0051028]; protein import into nucleus [GO:0006606] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitotic spindle midzone [GO:1990023]; nuclear envelope [GO:0005635]; nuclear periphery [GO:0034399]; nucleus [GO:0005634] | GTP binding [GO:0005525]; nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139] | PF13513; | 1.25.10.10; | Importin beta family, Importin beta-2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}. | null | null | null | null | null | FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for arginine/glycine-rich nuclear localization signals (rg-NLS) and PY-NLS in cargo substrates. Its predominant cargo substrate seems to be mRNA-binding proteins. Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins. The complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo. The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. {ECO:0000250|UniProtKB:P38217}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14092 | HEM1_SCHPO | MERVVKLAAKHCPFVSKADPSALRRMAGAGLIRAGARCPVVRHALPVAAATGADVSRGFKSDSKQMAMEPSLDEIHLKAGVVNTGSRTCRHADAVKAAAEAATTTPVTKKHQMPKHYASDLNGVGPATTPRFDYDTFYREELDKKHRDKSYRYFNNINRLAKEYPLAHLADPNTRVEVWCSNDYLNMGGHKKIREAMHQCIETYGGGAGGTRNIAGHNQHAVRLEKSLADLHQKPAALVFGSCYVANDATLSTLGRKLPNCIFLSDEMNHASMINGIRNSRCEKIIFKHNDLVDLEAKLASLPLNRPKIIAFESVYSMSGNVAPISEICDLAKKYGAITFLDEVHAVGMYGPRGAGVAEETPGLLSRVDIITGTLAKSYGCVGGYIAASSTLVDMIRSLAPGFIFTTSLPPHVMVGALTAVEHLKVSNVEREQQRSAVRRVKQSLSEIGIPVLSNDTHIVPAMVGDAHLAKLASDSLLHDHNIYVQSINFPTVSVGTERLRITPTPAHNTEHYVQSLTNAMNDVWSKFNINRIDGWEKRGIDVGRLCKFPVLPFTTTH | 2.3.1.37 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P09950}; | heme biosynthetic process [GO:0006783]; hemoglobin biosynthetic process [GO:0042541]; protoporphyrinogen IX biosynthetic process [GO:0006782] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | 5-aminolevulinate synthase activity [GO:0003870]; pyridoxal phosphate binding [GO:0030170]; transaminase activity [GO:0008483] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-II pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:16823372}. | CATALYTIC ACTIVITY: Reaction=glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA; Xref=Rhea:RHEA:12921, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57305, ChEBI:CHEBI:356416; EC=2.3.1.37; Evidence={ECO:0000250|UniProtKB:P09950}; | null | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1. {ECO:0000250|UniProtKB:P09950}. | null | null | FUNCTION: Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis. {ECO:0000250|UniProtKB:P09950}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14098 | CTK1_SCHPO | MSYSKSTIYRRQGTEPNSHFRRTVEEKSQLSGTNEESLGGHTLSSNAFKNNSSSISPSSSAKDPREQRKRTFPLNDTHSSRARQHERPFRSRKSRRRKGKKAFSPRPGSPPSPSFYRSGSQKRARNLTTKDYFAKRSESSSSASVSPISPSANRNDSKRQASSFRRSPPSSVHMKPSAFNGRKVSRRPSSSPPPIPSIPHETTSSDTQKKSSVSSGFPENKHGKFHFHIPNERRSRFDQPPSKRMALTSTARESVPAPLPSPPSGPIYTYTYPKPAYEKIDQIGEGTYGKVYKAINTVTGDLVALKRIRLEQEKDGFPITTVREVKILQRLRHKNIVRLLEIMVEKSSVYMVFEYMDHDLTGVLLNSQLHFTPGNIKHLSKQIFEALAYLHHRGVLHRDIKGSNILLNNNGDLKFADFGLARFNTSSKSANYTNRVITLWFRPPELLLGETAYDTAVDIWSAGCIVMELFTGKPFFQGRDEISQLEVIYDMMGTPDVHSWPEVKNLPWYELLKPVEEKKSRFVETFKEILSPAAIDLCQKLLALNPFCRPSAHETLMHEYFTSESPPPEPAVILKNMQGSWHEWESKKRKSKR | 2.7.11.23 | null | mRNA processing [GO:0006397]; phosphorylation [GO:0016310]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968] | chromatin [GO:0000785]; CTDK-1 complex [GO:0070692]; cyclin/CDK positive transcription elongation factor complex [GO:0008024]; nuclear cyclin-dependent protein kinase holoenzyme complex [GO:0019908]; nucleolus [GO:0005730]; nucleus [GO:0005634] | ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353]; RNA polymerase II CTD heptapeptide repeat S2 kinase activity [GO:0140834] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15537703, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:17502918}. Note=Localized to nucleus during all cell cycle phases. {ECO:0000269|PubMed:15537703, ECO:0000269|PubMed:16823372}. | CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23; Evidence={ECO:0000250|UniProtKB:Q03957}; | null | null | null | null | FUNCTION: Catalytic subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. Involved in RNA polymerase II transcriptional elongation and pre-mRNA 3'-end processing (By similarity). Together with ctk2/lsc1, required for the regulation of cytokinesis by phosphorylating 'Ser-2' residues found in the heptad repeats of the CTD. Required for nuclear localization of ctk2/lsc1. Positively regulates the septation initiation network (SIN) and promotes successful completion of cytokinesis in response to perturbation of the actomyosin ring. Acts in parallel to clp1 to promote actomyosin ring stability upon cytokinesis checkpoint activation. {ECO:0000250, ECO:0000269|PubMed:15537703, ECO:0000269|PubMed:17502918}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14111 | PSD3_SCHPO | MPFTKSCRSANTLRKGIKNGKLILKIIVNDIDNVESCLSGDESNDSKKSSASFYMKLKYGSYRALADNILSTDENRKEDIAVFDVPLPNGLQIDTFTLCLYRKSKWKKQIVGEAYIGIQALLLSTNPDETCKYPVISPPSGRNKENQSPSHQICNLSLKWIIYDPEDADADSKTLAKAWLQQIKMNQTSIDPMSNISKSLKELEVDNVESDLEDSSFIAEPDSSIPPSESSVSISTDTGKETPPSKSKKSSNQPYVSIGEGNSDLLGFVFLEIISVSNLPPLKNVFRTGFDMDPFVITAFSKNIFRTKWLRHNLNPVYNEKFLFEVGAFESNYDLVFKVVDHDKMSLNDSIAVGSFNVQSIINSSAQVDPETGLYSFNIETSSPSQDTSSKAEDSPTVQKIADDFSSAVGKDLRTDIIEQIIPLTLCCKHDFSTPRDVKLSFKAMFFPIAALRQKFWRVMLAQYGDIEDGHIGKLGMYAVLDTLGSNIPNSMVDDIYTELSSKNHDDTSDSITVDEAVICLERLVDLVCHQDQQATQTPQSPSSNEESGPGTPTQTSDQYEDSEDSRNFPSKLYLVYLSNCPLCLKFKLSKVNQQKATVHLATCASHDWKRVDRLMMTSYVSLNQAQRRWFSKAFAKVVYGSSKVGSTSATTLVQNRQTGQIQEEKMNAYVRIGIRLLYRGIRNRRIEGSKVKKILRSLTLKQGMKYDSPISVKEIKPFIRFFDLNMNEVDMPVGGFKTFNEFFYRKLKPGSRPCAFPDNPDILVSPADSRIVAYECIEKATTYWIKGTEFTVERLLGYSNEAQRFVGGSICISRLAPQDYHRFHSPVNGCIGPITKIEGQYYTVNPMAIRSYLDVFGENVRVLIPIDSNEFGKVMLVAVGAMMVGSTVLTVDEGKIVQRSDELGYFKFGGSTVITLFEPNVTSFDEDLLRNSKTKIETLVKMGERIGQKIDPNKPTDAEDHSKSDS | 4.1.1.65 | COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP-Rule:MF_03209}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-Rule:MF_03209}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; | phosphatidylcholine biosynthetic process [GO:0006656]; phosphatidylethanolamine biosynthetic process [GO:0006646]; protein autoprocessing [GO:0016540] | cell division site [GO:0032153]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; fungal-type vacuole membrane [GO:0000329]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795] | metal ion binding [GO:0046872]; phosphatidylserine decarboxylase activity [GO:0004609]; phospholipid binding [GO:0005543] | PF00168;PF02666; | 2.60.40.150; | Phosphatidylserine decarboxylase family, PSD-B subfamily, Eukaryotic type II sub-subfamily | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase. {ECO:0000255|HAMAP-Rule:MF_03209}. | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_03209}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03209}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03209}. Endosome membrane {ECO:0000255|HAMAP-Rule:MF_03209}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03209}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03209}. Cytoplasm {ECO:0000269|PubMed:16823372}. Note=Localizes at the barrier septum. {ECO:0000269|PubMed:16823372}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262, ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP-Rule:MF_03209}; | null | PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2. {ECO:0000255|HAMAP-Rule:MF_03209}. | null | null | FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine (By similarity). Together with psd1 and psd2, responsible for the majority of phosphatidylethanolamine synthesis (PubMed:19286980). {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000269|PubMed:19286980}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14113 | SDE2_SCHPO | MECKTVFLNGDFLKNSVNVNLNRLATVETLLRHVLGDSYETVLERAYLTHQSRIVHPDIQLCKLEGKSTSAHLNLTLCTRVLGGKGGFGSQLRAAGGRMSKKRNEQENQDSCRDLDGNRLGTIRQAKELSEYLAKKPAETRAKKEAKKQKLNKVLAADSSSSRFDDHEYLEDLEQSVSNVRDAFQNSLLYRRGSTSASSFSSGSNGATTDEPAEKEARNNNSSINSWSRRMQASESSNEAEGEDSESQTSKSLYEWDDPLYGL | null | null | cell cycle [GO:0007049]; mRNA cis splicing, via spliceosome [GO:0045292] | cytosol [GO:0005829]; nucleus [GO:0005634]; post-mRNA release spliceosomal complex [GO:0071014]; spliceosomal complex [GO:0005681] | null | PF13019; | null | SDE2 family | PTM: The N-terminal UBL (ubiquitin-like) propeptide is cleaved at Gly-84 by the deubiquitinating enzymes ubp5 and ubp15; the resulting mature sde2 associates with spliceosomes. {ECO:0000269|PubMed:28947618, ECO:0000269|PubMed:36095128}.; PTM: Polyubiquitinated; ubiquitination is partially dependent on ubr11. {ECO:0000269|PubMed:28947618}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28947618}. Nucleus {ECO:0000269|PubMed:28947618}. Note=The unprocessed form localizes to the nucleus. Following cleavage in the nucleus, the C-terminal sde2 remains nuclear, whereas the N-terminal UBL appears to disperse throghout the cell. {ECO:0000269|PubMed:28947618}. | null | null | null | null | null | FUNCTION: Plays a role in pre-mRNA splicing by facilitating excision of introns featuring relatively long (>21 nucleotides) spacing between the branchpoint and 3'-splice site (ss) (PubMed:36095128). Recruits cactin to the spliceosome which may enable folding of RNA between the branchpoint and 3'-ss, to guide the splice site towards the spliceosome's catalytic center (PubMed:36095128). Required for proper chromatin organization by assisting splicing of components involved in genomic stability and telomere organization (PubMed:21333630, PubMed:28947618, PubMed:36095128). {ECO:0000269|PubMed:21333630, ECO:0000269|PubMed:28947618, ECO:0000269|PubMed:36095128}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14114 | ATD2_SCHPO | MKEEASEHGGSADETQELSPVSDSSDEMPNNAKRRRRSQSMIANKRIHQAFQEDEGDEDWEEEEHKPKAKRRYNTRSNESFSEGDDEPFEVSESSALEDELSDSEDSFIRSVRSKPKYKPGTRRSTRLRNRRSQDEEESEEEHRPILRERTSRINYSVPLAFPPVDEMDGDPSSQVNQSRSRKTHSELAITKLLRQQVSSFMPYIDSSGSESESDNTRIKKSSAKTIKALTDPANSGGPPDFGRIREKSDLADSDPLGVDSSLSFESVGGLDNYINQLKEMVMLPLLYPEIFQRFNMQPPRGVLFHGPPGTGKTLMARALAAACSSENKKVSFYMRKGADCLSKWVGEAERQLRLLFEEAKSTQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGMESRGQVIIIGATNRPDAVDPALRRPGRFDREFYFPLPDRDARKKIIEIHTRNWDPPVPEWLCSMLAEKSKGYGGADLRALCTEAALNSIKRTYPQLYRSTKRLQIDPKTIKVKVKDFVMSMKRMIPSSERSSISPSKPLSPELKPLLNEAFQDIEKTLQKLMPVASKLNPLEEVMYDDPKENDFEYQQRLETFETLRIYKPRFLICGRKGLGQTALGPAILQQYEGVHVQSFDMSTLLQDSTQSIETSIIHLFLEVRRHTPSIIYIPDIDNWLNVLPLTAITTFSSMLERLDFSDQILFLALSSSPLSELHPQLREWFSSKQSVYSLQYPTRDSIIAFFQPILELIKASPTELPGGIPRKRRVLPELPLAPDPPPFTSQKITLKQTKQADMRLLNKLKIKLNALLGSLRARYRKFKKPLIDFNDIYCVDPETGHSYRSREECHYEFVDDVVKQIGSDQKFSMMSLEEIEKRTWDNCYCTPKQFVHDIKLILRDALQLEDSETIKRAQEMYANVLLGVEDMEDDQFSQRCERMALREAERRKLRHGKLQKHLDETKADMQFTSEKPSVDESITEVDDAIKDGPPVLAETLTNSLMEDVGPENVDMDIEDNEIFTNQSTMSVPSMLVENEESPKPDEYIDQKDKVQSPLLNGKSPVGVPSEAALRVSTDVSTNISSNGRADIPVDTLITSPADVPNNAPTDAHNITSADGHIENIEQEVVFPDLVFDEDRLTPLKQLLIDSTTGFTVDQLLHLHSFLYQIIWNTKSEWNRNSVVDECERAVKEFMINALQ | 3.6.1.- | null | nucleosome assembly [GO:0006334]; positive regulation of transcription by RNA polymerase II [GO:0045944]; transcription initiation-coupled chromatin remodeling [GO:0045815] | chromatin [GO:0000785]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent H3-H4 histone complex chaperone activity [GO:0140665]; chromatin binding [GO:0003682]; histone binding [GO:0042393] | PF00004;PF17862; | 1.10.8.60;1.20.920.10;3.40.50.300; | AAA ATPase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:26582768}. Chromosome {ECO:0000269|PubMed:26582768}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:31848341}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000269|PubMed:31848341}; | null | null | null | null | FUNCTION: ATPase histone chaperone which facilitates loading of histone H3-H4 onto DNA in an ATP-dependent manner (PubMed:31848341, PubMed:33658433). Plays a genome-wide role in nucleosome organization and establishment of chromatin (PubMed:26582768, PubMed:31848341). Also plays a role in heterochromatin assembly by stabilizing recruitment of the histone methyltransferase clr4 to methylated histone H3, to promote the transition from H3K9me2 to H3K9me3 (PubMed:32269268). {ECO:0000269|PubMed:26582768, ECO:0000269|PubMed:31848341, ECO:0000269|PubMed:32269268, ECO:0000269|PubMed:33658433}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14122 | CUL4_SCHPO | MPPEAKRIVVKGFDPRKSRQRQETYYVTMIDRLNMALQVVMAGLGLKTGYQELYSGVENLTRADQASRCFNILQHHMSSGIQLLKDSAESFIQLEGTETDTNACTVVVGCWNKWLERVEIVQNIFYYMDKTFLSHHPDYPTIEELSLSLFREKLMAVKNIQIPFLNSLLQSFENLHSSKSTDHAYLQDAMLMLHRTEMYSSVFVPMYLVMLSRFYDTESSQKIQELPLEEYLEYAMSSLEREDAYVEKFDIVRDKKSIRETVQRCLITSHLDTLTKGISQFIEKRDAHSCKLLYALLQFNHETEYLIQPWSDCLVDVGFKLVNDESKDDTLVQELLSFHKFLQVVVDESFLHDETLSYAMRKAFETFINGAKGSQREAPARLIAKYIDYLLRVGEQASGGKPLKEVFSEILDLFRYIASKDIFEAYYKLDIAKRLLLNKSASAQNELMLLDMLKKTCGSQFTHSLEGMFRDVNISKEFTSSFRHSKAAHNLHRDLYVNVLSQAYWPSYPESHIRLPDDMQQDLDCFEKFYLSKQVGKKISWYASLGHCIVKARFPLGNKELSISLFQACVLLQFNNCLGGEGISYQDLKKSTELSDIDLTRTLQSLSCARIRPLVMVPKSKKPSPDTMFYVNEKFTDKLYRVKINQIYLKEERQENSDVQEQVVRDRQFELQASIVRVMKQKEKMKHDDLVQYVINNVKDRGIPLVSDVKTAIEKLLEKEYLEREDNDIYTYVT | null | null | DNA damage response [GO:0006974]; nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts [GO:0033621]; pericentric heterochromatin formation [GO:0031508]; protein localization [GO:0008104]; protein ubiquitination [GO:0016567]; regulatory ncRNA-mediated heterochromatin formation [GO:0031048]; silent mating-type cassette heterochromatin formation [GO:0030466]; subtelomeric heterochromatin formation [GO:0031509]; transcription-coupled nucleotide-excision repair [GO:0006283]; ubiquitin-dependent protein catabolic process [GO:0006511] | chromosome, telomeric region [GO:0000781]; CLRC complex [GO:0043494]; Cul4-RING E3 ubiquitin ligase complex [GO:0080008]; cytosol [GO:0005829]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721] | ubiquitin protein ligase binding [GO:0031625] | PF00888;PF10557; | 1.20.1310.10;1.10.10.10; | Cullin family | PTM: Neddylated; enhancing the ubiquitin-ligase activity. {ECO:0000250|UniProtKB:P47050}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18345014}. Chromosome {ECO:0000269|PubMed:18345014}. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Required, indirectly, for activation of ribonucleotide reductase through the degradation of the protein spd1, thereby supplying deoxyribonucleotides for DNA replication and repair. Also has a role as a scaffold for assembling ubiquitin ligases (PubMed:12695334). Component of the Clr4 methyltransferase complex (ClrC) which contributes to the establishment of heterochromatin by specifically methylating histone H3 to form H3K9me (PubMed:16024659, PubMed:16127433, PubMed:18345014). ClrC preferentially ubiquitylates H3K14 and ClrC-mediated H3 ubiquitination promotes clr4 methyltransferase activity for the methylation of H3K9 (PubMed:31468675). H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci (PubMed:16024659). {ECO:0000269|PubMed:12695334, ECO:0000269|PubMed:16024659, ECO:0000269|PubMed:16127433, ECO:0000269|PubMed:18345014, ECO:0000269|PubMed:31468675}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14129 | RAD55_SCHPO | MLSSQHRLVTQPAIRAYEAFSAPGFGFNSKLLDDAFGGSGLKRGYISEVCGAPGMGKTSLALQITANALLSGSRVIWVETCQPIPMERLRQLLDNHVPSSQDEEEKCDTDELLNLLDVVYAPNLVNILAFLRNFDQEKHLKEIGLLIIDNLSMPIQLAYPTSPEDYAYLRLRRNTSKKSSLSDSSQKENTLTLNKENEFSSKDDSNFAFHNSSTKTTINRRKKAIGTISSLLSKITSSCYVAIFVTTQMTSKVVSGIGAKLIPLLSTNWLDNLSYRLILYSRHSTEESKDGQSRPSHQLLRYAFMAKQPPAHSAESELAFQLTSTGIQDYQSIPTNSSQRRKRSILECES | null | null | DNA damage response [GO:0006974]; DNA strand invasion [GO:0042148]; double-strand break repair via homologous recombination [GO:0000724]; meiotic DNA recombinase assembly [GO:0000707]; meiotic joint molecule formation [GO:0000709]; reciprocal meiotic recombination [GO:0007131] | cytosol [GO:0005829]; nucleus [GO:0005634]; Rad51B-Rad51C-Rad51D-XRCC2 complex [GO:0033063]; Rad51C-XRCC3 complex [GO:0033065]; replication fork [GO:0005657]; site of double-strand break [GO:0035861] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent DNA damage sensor activity [GO:0140664]; crossover junction DNA endonuclease activity [GO:0008821]; four-way junction DNA binding [GO:0000400] | null | 3.40.50.300; | RecA family, RAD55 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Required for radiation resistance and meiotic viability and acts in recombination and recombinational DNA repair pathways. {ECO:0000269|PubMed:10430583}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14132 | PIT1_SCHPO | MKKYLWGTPTTNTVFTGKQPKYTKEVRKCISIDEVYNVVRKVGDGTFGSVYLATTKTPSKEVVAIKSMKKKLAKVSDATRLREVHSLLRLSENENIVNIFDLYIDQFRCLHIVMEFLDCNLYQLISTRKNDPLTLEQVQDIMRQIFKGLNHIHTNGFFHRDMKPENILISSNSDSSSFNVKIADFGLAREINSRPPYTEYVSTRWYRAPELLLRDSYYSFPVDIYAAGCMAFEIATLQPIFPGNDDFDQLYKMCEILGSPDEQSQNTGDKGGGIWDRAELLANKLGISLPKMAPLDFGDLFSPPWNLAFASMLSQLLKWDPAKRPTAEMCLDLEFCRVSAPADAVASKEEVNKNTDFRVSISYFPSSSSIPDECNTEEESRINPSTSKFLKQLNKGFNGFTKPFRKSRKQSKNRKNKSSVATQFSEESEDIADSITSSTFFPVLPQIRPSTPLNLKLRNFIISSSEDSTSPKAKEFDRPLPSTEFLVAINKSQEALLNNSPNSKSGSTQLSASTCLSDLISPQLSILSHEDKRENQSVNSESSKYSPRSSNHSPTLHSKDLHRDMATVNNYAKSPPSFHATQDLLRKTLAYTNSSGTSTVLSNDSSAISSTFLDRDFPDFGITSLAGSLTLPDSKIIDRSKTHVSTQLLP | 2.7.11.1 | null | ascospore formation [GO:0030437]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; regulation of meiotic nuclear division [GO:0040020]; signaling [GO:0023052] | cell division site [GO:0032153]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; | null | null | null | null | FUNCTION: Protein kinase which is essential for spore formation. {ECO:0000269|PubMed:10747048}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14139 | HRP3_SCHPO | MSTSAIALALSSSKAIEQLDHVQTETPNLKQEMSESPSNSGVASKRKLQSTEWLDPELYGLRRSGRTRSNPGRYVDTDDQEDVFPSKHRKGTRNGSSFSRHRTIRDLDDEAESVTSEESESDDSSYGGTPKKRSRQKKSNTYVQDEIRFSSRNSKGVNYNEDAYFESFEEEEEEEMYEYATEVSEEPEDTRAIDVVLDHRLIEGHDGSTPSEDYEFLIKWVNFSHLHCTWEPYNNISMIRGSKKVDNHIKQVILLDREIREDPTTTREDIEAMDIEKERKRENYEEYKQVDRIVAKHLNSDGSVEYLVKWKQLLYDFCTWEASSIIEPIAATEIQAFQEREESALSPSRGTNYGNSRPKYRKLEQQPSYITGGELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQETLALWASDMNCISYLGNTTSRQVIRDYEFYVDGTQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRLLITGTPLQNNIRELAALVDFLMPGKFEIREEINLEAPDEEQEAYIRSLQEHLQPYILRRLKKDVEKSLPSKSERILRVELSDLQMYWYKNILTRNYRVLTQSISSGSQISLLNIVVELKKASNHPYLFDGVEESWMQKINSQGRRDEVLKGLIMNSGKMVLLDKLLSRLRRDGHRVLIFSQMVRMLDILGDYLSLRGYPHQRLDGTVPAAVRRTSIDHFNAPNSPDFVFLLSTRAGGLGINLMTADTVIIFDSDWNPQADLQAMARAHRIGQKNHVMVYRLLSKDTIEEDVLERARRKMILEYAIISLGVTDKQKNSKNDKFSAEELSAILKFGASNMFKAENNQKKLEDMNLDEILEHAEDHDTSNDVGGASMGGEEFLKQFEVTDYKADVSWDDIIPLTEREKFEEEDRLREEEEALKQEIELSSRRGNRPYPSSAVESPSYSGTSERKSKKQMLKDEVLLEKEIRLLYRAMIRYGSLEHRYNDIVKYADLTTQDAHVIKKIAADLVTASRKAVSAAEKDLSNDQSNNKSSRKALLITFKGVKNINAETLVQRLNDLDILYDAMPTSGYSNFQIPMHVRSVHGWSCQWGPREDSMLLSGICKHGFGAWLEIRDDPELKMKDKIFLEDTKQTDNSVPKDKENKEKKVPSAVHLVRRGEYLLSALREHHQNFGIKSSPAISTNGKTQPKKQTANRRQSGKPNVKSAQKIESATRTPSPAISESRKKPSSKDTKIETPSREQSRSQTASPVKSEKDDGNVSLNAEQKARCKELMYPVRKHMKRLRKDSSGLGRAELVKLLTECLTTIGKHIEKTVNDTPSEEKATVRKNLWMFACYFWPKEEVKYTSLISMYEKMK | 3.6.4.- | null | nucleosome disassembly [GO:0006337]; nucleosome organization [GO:0034728]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription initiation-coupled chromatin remodeling [GO:0045815] | chromatin [GO:0000785]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; nucleosome binding [GO:0031491] | PF18196;PF13907;PF00385;PF00271;PF00176; | 2.40.50.40;6.10.140.1440;1.10.10.60;3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12127990}. | null | null | null | null | null | FUNCTION: Involved in heterochromatin silencing. Required for transcriptional repression at the silence loci of mat3, where it has a direct role as a chromatin remodeling factor. {ECO:0000269|PubMed:12127990}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14140 | SEM1_SCHPO | MSRAALPSLENLEDDDEFEDFATENWPMKDTELDTGDDTLWENNWDDEDIGDDDFSVQLQAELKKKGVAAN | null | null | double-strand break repair via homologous recombination [GO:0000724]; mRNA export from nucleus [GO:0006406]; proteasome assembly [GO:0043248] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; proteasome complex [GO:0000502]; proteasome regulatory particle, lid subcomplex [GO:0008541] | ion binding [GO:0043167]; molecular adaptor activity [GO:0060090] | PF05160; | null | DSS1/SEM1 family | null | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. | null | null | null | null | null | FUNCTION: Versatile protein that might stabilize multiple protein complexes involved in diverse pathways. Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis (PubMed:16149916). Acts as a ubiquitin receptor of the 26S proteasome, by interacting with ubiquitin chains linked by 'Lys-63' and 'Lys-48' (PubMed:25306921). Involved in nuclear export of specific sets of mRNAs (PubMed:18023413). Links the mRNA adapter mlo3 to rae1 for targeting mRNA-protein complex to the proteins of the nucleoporin complex (NPC) (PubMed:15990877). Involved in recombinational repair of DNA. Plays a critical role in linking repair and checkpoint factors to damaged DNA sites by specifically recruiting rad24 and cdc25 to the DSBs (PubMed:20231270). {ECO:0000269|PubMed:15990877, ECO:0000269|PubMed:16149916, ECO:0000269|PubMed:18023413, ECO:0000269|PubMed:20231270, ECO:0000269|PubMed:25306921}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14148 | INO80_SCHPO | MDPSRETFDGSTRDSYKPPNGAEMMGQSELNTQNRIPYNTSANNRNWQIPLYWQQRGNEFQASPPPPLGYVTPEYGATGTPVNANNASRVDYATTAANVPEEYANDYSSELAYIHNVNDMPHVDGLSNHSPATQPDLFETPAQSDPILFSSYPHAAQARVDPSISKDLYNMVPRPDANTVSPHAARSASSLPVPKEASETPFRDASTDLFDEHAHAAPMHSSISISTLLSDSDRYEPHVSLTENISPVMAPSIDARLSQTILRGLPPAQKLSPNSSQSQITHNRRKHKLPLNATTNNSVVLTPDTSPLLDSDEVVSDDDSNEQQTMMMKFNYLQHLRNKRDEAVHAEKRRLLDIRGSIHDRLVCRYENRYNKLHASEYNHHHDWAVRQAIREEVAAVEAAKIRADEEKKKKEREEQVRLLQESADKDAEMNEASTATSENEDLKDDLSLADLSSKKTANSQATENNNTPSKAKVKAESKVRSKAKSDKSRAKLSSDTNKDSEKNDNNDASLQSAGVASDGESSPETPLTKASKSKKAKASKLANDTSKNANGETKSTPKKSKKKTSKAQQEANSTTAEGKEKLSGDSTETGNSTNKEASTEDTKANATASAPNKKKKTVETLQQQVIKEIARKEIPRVYKIIQQNQYNRSTNARKTSQLCGREARRWQFRTIKNNKDMQTKAKRAMRETMVFWKRNERVERDLRKKAEREALDRAKKEEELRESRRQARKLDFLITQTELYSHFVGRKMDREQDLPSATNTASVSEINFDSDEEEDIRRLAVESAQEAVQKAREHSQLFDANRQQSPNNSSSDMNEGEMNFQNPTLVNAFEVKQPKMLMCKLKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSISVMAYLAETHNIWGPFLVIAPASTLHNWQQEITRFVPKLKCIPYWGSTKDRKILRKFWCRKNMTYDENSPFHVVVTSYQLVVLDAQYFQSVKWQYMILDEAQAIKSSSSSRWKSLLAFKCRNRLLLTGTPIQNTMQELWALLHFIMPSLFDSHNEFSEWFSKDIESHAQSNTQLNEQQLKRLHMILKPFMLRRVKKNVQSELGEKIEKEVYCDLTQRQKILYQALRRQISIAELLEKAILGGDDTVASIMNLVMQFRKVCNHPDLFEREDVRSPLSLATWSKSIYINREGNFLDVPYNTRNFITFSIPRLLYEQGGILSVPGLNTSRGFETKYLYNLMNIWNPEYTNDSIKSNPEGSPFSWLRFVDESPQTLFQTFQNPVVHYLDEAEASSSLKEEQLCRQEFCYGKDYSNVRKMLLLPKSITKVDVLGSDFKEDSPFYHLTHVLEESDSQLDLTLLDSVLVQRASAPPIDIYCPGSRQFTVLQSRFQRDHLWSHYLYQPLKGEEDLIINNQAVSKLPIPRKPLLPSFGIAKGSYSNVRIPSMLRFIADSGKLSKLDKLLVELKANDHRVLIYFQMTRMIDLMEEYLTFRQYKYLRLDGSSKISQRRDMVTEWQTRPELFVFLLSTRAGGLGINLTAADTVIFYDSDWNPSIDSQAMDRAHRIGQQKQVTVYRFITRGTIEERIVIRAKEKEEVQKVVISGGETRPTKQMDLKGNSREMVSWLLEE | 3.6.4.- | null | CENP-A containing chromatin assembly [GO:0034080]; chromatin remodeling [GO:0006338]; DNA repair [GO:0006281]; transcription initiation-coupled chromatin remodeling [GO:0045815] | chromatin [GO:0000785]; Ino80 complex [GO:0031011] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; DNA binding [GO:0003677]; histone binding [GO:0042393] | PF13892;PF00271;PF00176; | 3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00746}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P53115}; | null | null | null | null | FUNCTION: ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair. {ECO:0000255|PROSITE-ProRule:PRU00746}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14156 | PP2C4_SCHPO | MSIRFLKRLRAPLYIQNAYCSKNYFYRSFIQYYSPSNGPYLKISMNKAPQSLGLCTARGDSPTNQDRMAYGYLNNLKDTTNRDSPFFYGLFDGHGGTECSEFLSTNLGKIIENQDLNDTEKILKEVHSVGGYMAGLKPPFSLRTVLQSRDEDLLWRARLYYSFLQADMDYLTNYARPSPDSAVPGAVGTVAIITSKNNLSYWESDSYIIHLAHVGDTRALLCDSRTGRAHRLTFQHHPADVEEARRLRRYNMGFSRDSFGQKRFAWVANTRSFGDGYKLKKLGVVAEPQLTSIHSLRDDWSFLTLLSDGITDVVSDDEVVDIIKLSESPQDAANNIIRYAQNVGAVDDITCLVVRLPGWKKRTINDFTKNLRLEKSAYHPRRS | 3.1.3.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250}; | cellular response to oxidative stress [GO:0034599]; positive regulation of autophagosome maturation [GO:1901098]; positive regulation of vacuole fusion, non-autophagic [GO:0061191]; regulation of aerobic respiration [GO:1903715]; signaling [GO:0023052] | cytoplasm [GO:0005737]; fungal-type vacuole membrane [GO:0000329]; mitochondrial matrix [GO:0005759] | [pyruvate dehydrogenase (acetyl-transferring)]-phosphatase activity [GO:0004741]; MAP kinase phosphatase activity [GO:0033549]; metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722] | PF00481; | 3.60.40.10; | PP2C family | null | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10436019}; Peripheral membrane protein {ECO:0000269|PubMed:10436019}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; | null | null | null | null | FUNCTION: Has a role in the regulation of vacuole fusion. {ECO:0000269|PubMed:10436019}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14157 | MYO3_SCHPO | MSYLSKNGSNDNNNIIKKLVDAEKHCNAVKDASFDERTWIWIPDSKESFVKAWIVEDLGEKYRVKLERDGSERIVDGFDAEKVNPPKFDMVDDMAALTCLNEPSVVNNLTQRYEKDLIYTYSGLFLVAVNPYCHLPIYGDDVVRKYQSKQFKETKPHIFGTADAAYRSLLERRINQSILVTGESGAGKTETTKKVIQYLTSVTDASTSDSQQLEKKILETNPVLEAFGNAQTVRNNNSSRFGKFIRIEFSNNGSIVGANLDWYLLEKSRVIHPSSNERNYHVFYQLLRGADGSLLESLFLDRYVDHYSYLKNGLKHINGVDDGKEFQKLCFGLRTLGFDNNEIHSLFLIIASILHIGNIEVASDRSGQARFPSLTQIDQLCHLLEIPVDGFVNAALHPKSKAGREWIVTARTREQVVHTLQSLAKGLYERNFAHLVKRLNQTMYYSQSEHDGFIGVLDIAGFEIFTFNSFEQLCINFTNEKLQQFFNHYMFVLEQEEYTQERIEWDFIDYGNDLQPTIDAIEKSEPIGIFSCLDEDCVMPMATDATFTEKLHLLFKGKSDIYRPKKFSSEGFVLKHYAGDVEYDTKDWLEKNKDPLNACLAALMFKSTNSHVSSLFDDYSSNASGRDNIEKKGIFRTVSQRHRRQLSSLMHQLEATQPHFVRCIIPNNLKQPHNLDKSLVLHQLRCNGVLEGIRIAQTGFPNKLFYTEFRARYGILSQSLKRGYVEAKKATITIINELKLPSTVYRLGETKVFFKASVLGSLEDRRNALLRVIFNSFSARIRGFLTRRRLYRFNHRQDAAILLQHNLRQLKLLKPHPWWNLFLHLKPLLGTTQTDEYLRRKDALINNLQNQLESTKEVANELTITKERVLQLTNDLQEEQALAHEKDILVERANSRVEVVHERLSSLENQVTIADEKYEFLYAEKQSIEEDLANKQTEISYLSDLSSTLEKKLSSIKKDEQTISSKYKELEKDYLNIMADYQHSSQHLSNLEKAINEKNLNIRELNEKLMRLDDELLLKQRSYDTKVQELREENASLKDQCRTYESQLASLVSKYSETESELNKKEAELVIFQKEITEYRDQLHKAFQNPEKTHNINDVKSGPLNSDENIYSTSSTTLSILKDVQELKSLHTKEANQLSERIKEISEMLEQSIATEEKLRRKNSELCDIIEALKYQIQDQETEIISLNADNLDLKDTNGVLEKNASDFIDFQGIKSRYEHKISDLLNQLQKERCKVGLLKQKTENRSVTQHTLDGNSPHPSFEEKHSGDPLKRIDGNNDDRKIDNKLLKTISKSLDALQLTVEEELSNLYSLSKDLSFTDISGHIPNSIRKLEKGLSTLSELKERLNASNSDRPSPDIFKDTQAIMNSRKLLSNPNSDAQSGLISSLQKKLYNPESNMEFTGLKPLSPSKISNLPSSQPGSPSKRSGKMEALIRNFDQNSSIPDPFIVNQRNSVLQTEFEKINLKLKEATKSGILDNKDLSKFSELIQSLLKENEELKNLTTSNLGSDDKMLDFAPLLEDVPNNTRNQIKGFVEKAISSKRAIAKLYSASEEKLFSTEKALREITKERDRLLHGLQGPSVPTSPLKAPTASQLIIPNFDGSITNYSGEEETEWLQEEVNIMKIKELTSTVNKYREQLAMVQSLNEHAESSLSKAERSKNYLTGRLQEVEELARGFQTTNADLQNELADAVVKQKEYEVLYVEKSNDYNTLLLQKEKLMKQIDEFHVIRVQDLEEREKKDQLLFQRYQKELNGFKVQLEEEREKNLRIRQDNRHMHAEIGDIRTKFDELVLEKTNLLKENSILQADLQSLSRVNNSSSTAQQNAQSQLLSLTAQLQEVREANQTLRKDQDTLLRENRNLERKLHEVSEQLNKKFDSSARPFDEIEMEKEVLTLKSNLAQKDDLLSSLVERIKQIEMFALKTQKDSNNHREENLQLHRQLGVLQKEKKDLELKLFDLDLKTYPISTSKDVRMLQKQISDLEASFAASDIERIKGIDECRNRDRTIRQLEAQISKFDDDKKRIQSSVSRLEERNAQLRNQLEDVQASETQWKFALRRTEHALQEERERVKSLETDFDKYRSLLEGQRVKRSESRLSMRSNRSPSVLR | null | null | mitotic actomyosin contractile ring assembly [GO:1903475]; mitotic actomyosin contractile ring contraction [GO:1902404]; mitotic cytokinesis [GO:0000281]; nuclear migration during mitotic telophase [GO:0090561] | cell division site [GO:0032153]; cytoplasm [GO:0005737]; gamma-tubulin ring complex [GO:0000931]; medial cortex [GO:0031097]; mitotic actomyosin contractile ring [GO:0110085]; mitotic actomyosin contractile ring, proximal layer [GO:0120104]; myosin filament [GO:0032982]; myosin II complex [GO:0016460] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microfilament motor activity [GO:0000146] | PF00063;PF02736; | 1.10.10.820;1.20.5.4820;1.20.58.530;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | null | null | null | null | null | null | FUNCTION: Stabilizes the F-actin cables forming the F-actin ring that surrounds the nucleus during interphase. May work in conjunction with myo2. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14164 | EIF3C_SCHPO | MSRFFKGGSSDSDAESVDSSEENRLTSSRLKKQDDSSSEEESSEEESASSSESESSEEESESEESEVEVPKKKAVAASEDSESDSESSEEEEETESEEDSEVSDESESESESESESEEESESEEESDESERSGPSSFLKKPEKEEAKPAGLKFLRGESSEESSDEEEGRRVVKSAKDKRYEEFISCMETIKNAMSSNNWIVVSNEFDHLNKVSQKCKEAGRNPPPYIEFLSALDQKLESADKAFIKSLDAANGRAFNALKQRVRKNNRQFQSDIDRYRKDPEGFMKPAELNEIPKPAGKAGQDEVIVDGVATRGIVAPTEGLGKPEEITPADIFKYLRAIFEARGKKSTDRSEQIRLLEKLSTIAVTDYQRLRVKVALLAVRFDINTGSGQYMPIDQWNAALTELHSILDIFDANPKIVIVEQVEDENEEEEEAIAAAENNNGVIQVQGSVVSFLERLDDEFTRSLQMIDPHTPEYIDRLKDETSLYTLLVRSQGYLERIGVVENTARLIMRRLDRVYYKPEQVIRANEEVAWRSFPPTFDLTITPRATTTTPDILIHSLCVYLYNNGVSLLRTRAMLCHIYHEALQNRFYKARDMLLMSHLQDSVHAADIATQILHNRTMVQIGLCAFRNGMVQETQYALQDISTTGRVKELLGQGIQAPKFGQFTPDQDRLDKQLVLPFHMHINLELLECVYLTCSMLMEIPAMAAASSTASDSRKRVISRPFRRMLEYIDRQLFVGPPENTREYIMQASKALADGEWRRCEEFIHAIKIWSLMPDADKIKQMLSEKIREEGLRTYLLAYAAFYDSVSLEFLATTFDLPVQRVTVIVSRLLSKREIHAALDQVHGAIIFERVEINKLESLTVSLSEKTAQLNEANEKLYEQKTQHTNPQENRRRDKGGSVKRRNERTENRNRSDMN | null | null | formation of cytoplasmic translation initiation complex [GO:0001732]; translational initiation [GO:0006413] | cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; eukaryotic translation initiation factor 3 complex, eIF3e [GO:0071540]; eukaryotic translation initiation factor 3 complex, eIF3m [GO:0071541] | RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743]; translation initiation factor binding [GO:0031369] | PF05470;PF01399; | 1.10.10.10; | EIF-3 subunit C family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03002}. | null | null | null | null | null | FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. {ECO:0000255|HAMAP-Rule:MF_03002}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14170 | POP2_SCHPO | MSLSRCPTDNSSSRINSSVPLINSSSPATPPESFDPQVFPSSLIHGDNLLPQDDQIASDPRSESNSCNGNTSSSLPCTDSYQYPLKHSCTPSFLRKFNESIENVSYKCLDHSPPDSVPGDFSISLVPQRNFLYSHSSLPPKIISIDRNNRIKLDNSISSNSDNFPPSPKVDTSNTVSPGSKPISEDLEDLNLQSIVQTFEDLPEGIQSYAFFQLLRSCNRQSMRLLLNECEPLLKKDILSNLPFSIVQSILLNLDIHSFLSCRLVSPTWNRILDVHTSYWKHMFSLFGFQINENDWKYANPNLNRPPFLHNDQISDDYFPEIFKRHFLNRKRWLFPSIPPSHLSFPIHVPNFMITSLLLHKDRIITTSGSGTIQIHNAITGVLEARLEGHKEGVWAVKIHENTLVSGSIDKTVRVWNIEKAKCTHIFRGHISIIRCLEILVPSRLIRHGVEIVEPDQPYIVSGSRDHTLRVWKLPKNTDPPYLPDNTNSIDRWEKNPYFVHTLIGHTDSVRTISGYGDILVSGSYDSSIRIWRVSTGECLYHLRGHSLRIYSVLYEPERNICISGSMDKSIRVWDLSTGTCKYVLEGHDAFVTLLNVFQNRLISGSADSTIRIWDLNTGKPLMVLPSNSGYISSFVSDEHKIISGNDGSVKLWDVRTGKLLRFLLTDLTKIWHVDFDAMRCVAAVQRDDQAYLEVINFSGSRP | null | null | negative regulation of mitotic DNA replication initiation [GO:1903467]; protein polyubiquitination [GO:0000209]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146] | cytoplasm [GO:0005737]; nuclear SCF ubiquitin ligase complex [GO:0043224]; SCF ubiquitin ligase complex [GO:0019005]; Set1C/COMPASS complex [GO:0048188] | histone binding [GO:0042393]; protein-macromolecule adaptor activity [GO:0030674]; ubiquitin ligase-substrate adaptor activity [GO:1990756] | PF00646;PF00400; | 1.20.1280.50;2.130.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12167173}. Nucleus {ECO:0000269|PubMed:12167173}. | null | null | null | null | null | FUNCTION: Involved in maintenance of ploidy through proteasome dependent degradation of CDK inhibitor rum1 and S-phase initiator cdc18. Functions as a recognition factor for rum1 and cdc18, which are subsequently ubiquitinated and targeted to the 26S proteasome for degradation. Together with pop1, required for cig2 instability during G2 and M phase and cig2 degradation in exponentially growing cells. {ECO:0000269|PubMed:12167173, ECO:0000269|PubMed:14970237, ECO:0000269|PubMed:9653157, ECO:0000269|PubMed:9990507}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14174 | SPT20_SCHPO | MERNNGLGDYTYRYHGKELSLDDFQNKQGIESSDDAFLSKIYENVSNFNVPRKLHDIEHKFSKEEPSLILHIHKFHFRFEQQDGAFTYNGPVKSILQYIRMELIPPDCLEVFRNSDVKFYDGCLTVRIIDHRQSPSADQTVQPQPGSTNQQQQNNTNPINNQPEDTKPNTNSPPVYHTVLRPTPETLWQDLCLLSESFANSLSDEAVLTLESNILLASEAPLFLTPAKSKAEMIQFMNQLADSAPPCTRKKPQGSAQLADEEAERLEKENLLLLMDDQRKRDFQPTFQRLQFIENVRRKRAILQQRQMQMQQQQKAQQQQSPKAQQPPAHLVQSAPVQRKTTPKIQRLPPSSIQIPPPKPMQKFPANAASSESPPNATGNFLPSGPVPANEPMLKRESVDLIKIRQLAILFQQRASQLKARGATREQITEILNRQAIAAGTDLATVMTVARNLHFQQLQMRQQQQQQQMKAER | null | null | regulation of transcription by RNA polymerase II [GO:0006357]; septin ring organization [GO:0031106]; transcription initiation-coupled chromatin remodeling [GO:0045815] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; medial cortex septin ring [GO:0036391]; nucleus [GO:0005634]; SAGA complex [GO:0000124] | transcription coactivator activity [GO:0003713] | PF12090; | null | SPT20 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}. | null | null | null | null | null | FUNCTION: Functions as a component of the transcription regulatory histone acetylation (HAT) complex SAGA. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation and deubiquitination. SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). {ECO:0000269|PubMed:19056896}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14187 | SPP42_SCHPO | MASLPPGNPPPPPPPPGFEPPSQPPPPPPPGYVKKRKNKTPAQSGNLEKQLNERARKWRASQKSKFGVKRKQGYVQTEKADLPPEHLRKIMKDRGDMSSRKFRADKRSYLGALKYLPHAVLKLLENMPMPWEEYREVKVLYHVTGAITFVNESPRVIEPHFIAQWGTMWMMMRREKRDRKNFKRLRFPPFDDEEPPFSIDQLLDLEPLEAIRMDLDEEDDAPVMDWFYENKALEDTPHVNGPTYRRWKLNLPQMANLHRLGYQLLSDLRDDNYFYLFNDNSFFTAKALNVAIPGGPKFEPLYKDEAPEMEDWNEFNDIYKLIIRHPIKTEYRIAFPYLYNSRARSVALSEYHQPSNVFVPPEDPDLPAFFWDPIINPITSRQLTLHELDTSPEDSAIEEDPNFEIPFDPFFHSEDIEFEHTASALILLWAPHPFNKRSGATKRAQDVPLIKHWYLEHCPPNQPVKVRVSYQKLLKSHVMNKLHMAHPKSHTNRSLLRQLKNTKFFQSTSIDWVEAGLQVCRQGYNMLQLLIHRKGLTYLHLDYNCNLKPTKTLTTKERKKSRFGNAFHLMREILRLTKLIVDSHVQYRLGNIDAYQLADGLHYIFNHVGQLTGMYRYKYRLMRQIRACKDFKHLIYYRFNTGPVGKGPGCGFWAPSWRVWLFFLRGIVPLLERWLGNLLARQFEGRHSTGVAKQITKQRVDSHQDLELRAAVMNDILDMIPEGIRQGKSKTILQHLSEAWRCWKANIPWKVPGLPAPIENMILRYVKSKADWWTSVAHFNRERIRRGATVDKTVAKKNLGRLTRLWLKAEQERQHNYLKDGPYVTADEAVAIYTTFVHWLESRRFQPIPFPPLSYKHDTKLLVLALERLKEAYSVKGRLNQSQREELALVEQAYDNPHEMLSQIKRRLLTMRTFKEVGIEFMDMYSHLIPVYSVDPMEKICDAYLDQYLWFEADRRHLFPSWVKPSDSEPPPLLVYKWCQGINNLTDVWETSNGECNVLMETRLSKVFEKVDLTLLNRLMSLLMDTNLASYASAKNNVVLSYKDMSHTNSYGLVRGLQFSSFIWQFYGLVLDLLILGLQRATEIAGPADAPNDFLHFKDQATETSHPIRLYTRYIDKVYIMFRFTDEESRDLIQRFLNENPDPTNSNVVNYSKGKKNCWPRDARMRLMKHDVNLGRAVFWEIRNRLPRSLTTLEWEDTFPSVYSKDNPNLLFSMTGFEVRILPKIRQNEEFSLKDGVWNLTDNRTKQRTAQAFIRVTEDGINQFGNRIRQILMSSGSTTFTKIANKWNTALIALMTYYREAAISTPELLDLLVKCESKIQTRVKISLNSKMPSRFPPAVFYSPKELGGLGMLSMGHVLIPQSDLRWSKQTDTGITHFRSGMTTNGEHLIPNLYRYIQPWESEFIDSQRVWAEYAMKRQEALQQNRRLTLEDLEDSWDRGIPRINTLFQKDRHTLAYDKGWRVRTEFKQYQLLKNNPFWWTSQRHDGKLWQLNNYRVDVIQALGGVEGILEHTMFKATGFPSWEGLFWEKASGFEESMKFKKLTNAQRSGLNQIPNRRFTLWWSPTINRANVYVGFQVQLDLTGIMMHGKIPTLKISLIQIFRSHLWQKIHESVVWDLCQVLDQELESLQIETVQKETIHPRKSYKMNSSCADILLLAAYKWNVSRPSLLNDNRDVLDNTTTNKYWIDVQLRFGDYDSHDIERYTRAKFLDYSTDAQSMYPSPTGVLIGIDLCYNMHSAYGNWIPGMKPLIQQSMNKIMKANPALYVLRERIRKGLQLYASEPQEQYLSSSNYAELFSNQIQLFVDDTNVYRVTIHKTFEGNLTTKPINGAIFIFNPRTGQLFLKVIHTSVWAGQKRLGQLAKWKTAEEVAALIRSLPVEEQPRQIIVTRKGMLDPLEVHLLDFPNITIKGSELQLPFQAIIKLDKINDLILRATEPQMVLFNLYDDWLQSVSSYTAFSRLILILRALNVNTEKTKLILRPDKSIITKENHVWPNLDDQQWLDVEPKLRDLILADYAKKNNINVASLTNSEVRDIILGMTITAPSLQRQQIAEIEKQGRENAQVTAVTTKTTNVHGDEMVVTTTSAYENEKFSSKTEWRNRAISSISLPLRTKNIYVNSDNISETFPYTYILPQNLLRKFVTISDLRTQVAGYMYGKSPSDNPQIKEIRCIALVPQLGSIRNVQLPSKLPHDLQPSILEDLEPLGWIHTQSSELPYLSSVDVTTHAKILSSHPEWDTKAVTLTVSYIPGSISLAAYTVSKEGIEWGSKNMDINSDEAIGYEPSMAEKCQLLLSDRIQGFFLVPEEGVWNYNFNGASFSPKMTYSLKLDVPLPFFALEHRPTHVISYTELETNDRLEEDMPDAFA | null | null | spliceosomal conformational changes to generate catalytic conformation [GO:0000393]; spliceosomal tri-snRNP complex assembly [GO:0000244] | catalytic step 2 spliceosome [GO:0071013]; post-mRNA release spliceosomal complex [GO:0071014]; Prp19 complex [GO:0000974]; spliceosomal complex [GO:0005681]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U5 snRNP [GO:0005682] | cysteine-type deubiquitinase activity [GO:0004843]; metallopeptidase activity [GO:0008237]; pre-mRNA intronic binding [GO:0097157]; U1 snRNA binding [GO:0030619]; U2 snRNA binding [GO:0030620]; U5 snRNA binding [GO:0030623]; U6 snRNA binding [GO:0017070] | PF01398;PF08082;PF08083;PF08084;PF12134;PF10598;PF10597;PF10596; | 1.20.80.40;3.30.420.230;3.90.1570.40;3.40.140.10;3.30.43.40; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Involved in pre-mRNA splicing. May be involved in endoplasmic reticulum-associated protein degradation (ERAD) and required for growth at low and high temperatures (By similarity). Required for pre-spliceosome formation, which is the first step of pre-mRNA splicing. This protein is associated with snRNP U5. Has a role in branch site-3' splice site selection. Associates with the branch site-3' splice 3'-exon region. {ECO:0000250, ECO:0000269|PubMed:16133344}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14188 | IQG1_SCHPO | MDVNVGLSRLQSQAGAPVGTKGSNTRLAAKQRETLQAYDYLCRVDEAKKWIEECLGTDLGPTSTFEQSLRNGVVLALLVQKFQPDKLIKIFYSNELQFRHSDNINKFLDFIHGIGLPEIFHFELTDIYEGKNLPKVIYCIHALSYFLSMQDLAPPLIKSDENLSFTDEDVSIIVRRLRQSNVILPNFKALSADFMLRASPVSSRTPSPTRFPKHARFQTLNSSDSASIYSSPYTSPTLEFSKKDASARSDILKMHRRTKSATPSLEQFNEPYKQTLPSHSIEFEDSFFQPPSQKGHMQRSFLTTFSAPTRRREALFSTTSGLSQRSPVDEKIVNAIQACGRGVLVRLRLVDMLQSLVEQSSSVVLLQAVIRGYISRNTYRIRKKAYDELVNWVTSIQSISRAYLIRAQYRKVVLQEEATKSIQTLQSIIRGGFYRRKYHSLIERLDLFTPSFVLIQSSALGFLTRHAIVNMLDNLYNYIPLFNRMQSILRANMFRNEWSNFLDSVQSFPVSFHSICKGRLIRDSINRLNGSLLGELDNFIKLQNLSRGFMIRRAFKEKLEKLKASTSSFIALQAIVRAFLLRKNLESIYDSFQKSHLSVIKAQSLYRGFITRTKIDYCNDYLLKRLPDIVFMQSAVRAILLRDDVNYTEVQLDSFIPEIVLLQSLIRGYLSRNKFSRKLQNFHKNMENPIVAKSIFRGRQEGLAYRELATAKNPPVMTVKNFVHLLDDTNFDFEEEVLLEKMRKEIVQQVRDNEEIEVHINELDVKIALLVKNKISLDDVLKHHNKYKFGKQSTEYLKINTLSMKSLNNSSRKFLELYQCFFYVLQTNEMYLANYFQALKTEGTSSVKIRHAVYLVLQIFGHGSNRREEVLLLRFISQVIKLEAALVNSSQDLLSDDCVWKLLFTGYRGDVREVKLWKTILGRIHKVLVADNHLDFEINPLTLFKSFNPEVASQTDSPKLTLSLAMQHPPTRNLYVSRLRELRKLCQSFLVALSKNIENIPYALCYTAAQLKNSLQRYFPAAHKEEIFGVIGKFVYWAYVAPVLVSPDNFKLVDGSITALQRKNLYTLSSILSEIFSIESCDSKQLGFFRPLSEFIEVSKQDTMLMLERLVDVVDPEVYFEFDAFEDLVNTKRPVIYMKRDDILGIYSSIAYVIDSIAPPDVNDPLRAVVNSLGPVSEQDNDFVQDETDVKLELNPKFCTIENPVAQERTLIVQTKRYILFIIRIQNGLNLLEILVKPVTDSDEAAWQNLLAEESEKNARNYDLFDDSIFSMSFAELKYTALSNIVEMEKLGFANRRNNYQDMVNSIALDIRNKSRRRMQRQRELDAGHQSLLNLREKRAFLDSQLKSYNEYIEQAMETLQSKKGKKKLIPFSKQYFHMRDLRKSGRVPRFGSFKYPALKLYDRGVLVSISHMPQKEKLYITISADEVGKFILEATSPTVKVSSPRCELHLDDLLSAQYNKVLTLDVLDGRLKLNTNMFLHLIFSKFYS | null | null | actomyosin contractile ring assembly actin filament bundle convergence [GO:0071520]; mitotic actomyosin contractile ring assembly [GO:1903475]; mitotic actomyosin contractile ring assembly actin filament organization [GO:1903479]; mitotic actomyosin contractile ring contraction [GO:1902404] | cell cortex [GO:0005938]; cytoplasm [GO:0005737]; medial cortical node [GO:0071341]; mitotic actomyosin contractile ring [GO:0110085]; mitotic actomyosin contractile ring, proximal layer [GO:0120104]; mitotic spindle pole body [GO:0044732]; nuclear envelope [GO:0005635]; spindle pole body [GO:0005816] | actin filament binding [GO:0051015]; calmodulin binding [GO:0005516]; cytoskeletal anchor activity [GO:0008093]; GTPase activator activity [GO:0005096] | PF00307;PF00612;PF00616;PF03836; | 1.20.5.190;1.10.418.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus envelope. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Localized to the F-actin ring and spindle pole body during interphase and mitosis. Also found in septum. | null | null | null | null | null | FUNCTION: Component of the contractile F-actin ring; required for its construction following assembly of F-actin at the division site. {ECO:0000269|PubMed:9635188}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14194 | GGT2_SCHPO | MSPTDTTPLLYSWDDQSRHQDPDWHKLRNYHGAWYRRISRRRFSQFIFAFGLMTLFVLVYSISSNLHTPTQFTGHKVRGRRGAVASEVPVCSDIGVSMLADGGNAVDAAIASTFCIGVVNFFSSGIGGGGFMLIKHPNETAQSLTFREIAPGNVSKHMFDKNPMLAQVGPLSIAIPGELAGLYEAWKSHGLLDWSKLLEPNVKLAREGFPVTRAMERVLKLPEMAHLLKDPIWQPILMPNGKVLRAGDKMFRPAYAKTLEIIANKGIEPFYRGELTNSMVKFIQDNGGIVTVEDFGNYSTVFADALHTSYRGHDVYTCTLPTSGPALIEGLNILDGYPLNTPSLAFPKRLHLEVEAMKWLSAGRTQFGDPDFLPLDHLDVVSKLLSKEFASQIRNNISLSKTYPWEHYNPSYDLPISHGTTHVSTVDSNNLAVSITSTVNLLFGSQLMDPVTGVVFNDQMDDFSIPGASNAFNLSPSPWNFIEPFKRPQSSSAPTILTDINGDFEMALGASGGSRIVTAVLDSIIKRIDMDYDIESMVASARPHHQLLPDILILESGFSKSVATRMKKYGHKVWRLKQHDTPLSQIQAVTRHHSEYYGMSDPRKYGQAAAY | 2.3.2.2; 3.4.19.13 | null | cellular detoxification [GO:1990748]; glutathione catabolic process [GO:0006751]; proteolysis [GO:0006508] | fungal-type vacuole [GO:0000324]; plasma membrane [GO:0005886]; vacuolar membrane [GO:0005774] | glutathione hydrolase activity [GO:0036374]; leukotriene C4 gamma-glutamyl transferase activity [GO:0103068] | PF01019; | 1.10.246.130;3.60.20.40; | Gamma-glutamyltransferase family | PTM: Cleaved by autocatalysis into a large and a small subunit. {ECO:0000250}. | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide]; Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795, ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599, ChEBI:CHEBI:78608; EC=2.3.2.2; Evidence={ECO:0000305|PubMed:15920625}; CATALYTIC ACTIVITY: Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13; CATALYTIC ACTIVITY: Reaction=an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779, ChEBI:CHEBI:143103; EC=3.4.19.13; | null | PATHWAY: Sulfur metabolism; glutathione metabolism. | null | null | FUNCTION: Catalyzes the transfer of the gamma-glutamyl moiety of glutathione (GSH) and other gamma-glutamyl compounds to amino acids and peptides. Major GSH-degrading enzyme, catalyzing the hydrolytic release of L-glutamate from GSH. Plays a role in the turnover of the vacuolar GSH, serving as an alternative nitrogen source during nitrogen starvation (By similarity). {ECO:0000250, ECO:0000269|PubMed:15920625}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14213 | EPR1_SCHPO | MNNPFKDMDCYEILQVNHDSDLQEIKANYRKLALQYHPDRNPGIEDYNEIFSQINAAYNILSNDDKRKWHEKDYLRNQYSVQIEDVLQHLQTIEKIPFESTSAFVERLRQDEKIAGSTDDLPTLGDTTWLWTYAKPIYQKWLRFSTKKSFEWEALYNEEEESDAATRRLMKRQNQRQIQYCIQRYNELVRDLIGKACDLDPRRKNVVKLSDGERYNSLQEASRKQSERDRRQYQETFKNQSIASWTIIDQEETSSDDESLSKEIVNSNPIMCMVCNKNFRSQNQLENHENSKKHKKNLRKMNQEIKKHAKEAQKNAESNKQPEDAPSESPYSNKVSSSDFYTRSFEEIEKTFTFVEISDNEFYTASEDGFLNEDDKLDQD | null | null | meiotic cell cycle [GO:0051321]; nucleophagy [GO:0044804]; reticulophagy [GO:0061709] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; phagophore assembly site [GO:0000407] | endoplasmic reticulum-autophagosome adaptor activity [GO:0140506]; nucleic acid binding [GO:0003676]; zinc ion binding [GO:0008270] | PF00226;PF12171; | 3.30.160.60;1.10.287.110; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:16823372, ECO:0000269|Ref.5}. Preautophagosomal structure {ECO:0000269|Ref.5}. Note=Accumulates at the preautophagosomal structure when autophagy occurs. {ECO:0000269|Ref.5}. | null | null | null | null | null | FUNCTION: Reticulophagy receptor required for autophagosomal sequestration of endoplasmic reticulum (ER) membranes during ER stress (Ref.5). Confers resistance to ER stress by promoting the autophagic degradation of the ER (ER-phagy or reticulophagy) (Ref.5). Acts as a bridging molecule to mediate the association between atg8 on the autophagic membrane and the vesicle-associated membrane protein-associated proteins (VAPs) scs2 and scs22 on the ER (Ref.5). May play a role in meiosis (PubMed:16303567). {ECO:0000269|PubMed:16303567, ECO:0000269|Ref.5}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14214 | TRM10_SCHPO | MENKDALDIGKDDTNTSEADVSKNETQEQPVLSKSALKRLKRQQEWDAGREKRAEMRREKKRLRKEERKRKIEAGEVVKSQKKRIRLGKVVPSSIRIVLDCAFDDLMNDKEINSLCQQVTRCHSANRTALHPVELFATNFGGRLKTRQDFVLKGQQNNWKRYNPTTKSYLEEFESQKEKLVYLSADSDNTITELDEDKIYIIGAIVDKNRYKNLCQNKASEQGIKTAKLPIDEYIKITDRKILTVNQVFEILSLWLEYRDWEKAFMEVIPKRKGILLKSDESFDVSEDTRSQSNQSDSELEKEN | 2.1.1.221 | null | tRNA N1-guanine methylation [GO:0002939] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | tRNA (guanosine(9)-N1)-methyltransferase activity [GO:0052905]; tRNA binding [GO:0000049] | PF01746; | 3.40.1280.30; | Class IV-like SAM-binding methyltransferase superfamily, TRM10 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q12400}. Nucleus {ECO:0000250|UniProtKB:Q12400}. | CATALYTIC ACTIVITY: Reaction=guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43156, Rhea:RHEA-COMP:10367, Rhea:RHEA-COMP:10368, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.221; Evidence={ECO:0000269|PubMed:24081582}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.2 uM for tRNA(Gly) {ECO:0000269|PubMed:24081582}; Note=kcat is 0.16 min(-1) for tRNA(Gly) (m1G9)-methylation. {ECO:0000269|PubMed:24081582}; | null | null | null | FUNCTION: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA. {ECO:0000269|PubMed:24081582}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14215 | PRI1_SCHPO | MTVQIDELDDKDLDEIIANGTLDGAKQGAVDSETMIQYYRHLFPWKYLFQWLNHGPVVTNDFAHREFAFTLPNDAYIRYLSFSNWEELKKEALNLCPSRFEVGPVYSANPRDRKTIRKSTFHPLKKELVFDIDMTDYDDVRTCCSKTNICEKCWPFITIAVQVLDICFHEDFGFKHILWVYSGRRGIHAWICDEIACSLDDRSRRMIASYLQVVVGNPQGGVRLINNLKRPLHPHLTRSLNILKSAFVKIVLEDQDPWASKEGAENLLKLLPDKDLASALRKKWEVDPERSSKNKWSDIDTVLASGSIASISPSVIAIAKQDIVLTYLYPRLDVEVSRHLNHLLKSPFCVHPGTSRVCVPIDIERMDSFNPLKVPTVNDLLQELDKNSQNDNGHGPTMETNTTENQKDNARGQSNKGHGFSTSLNPYTLYFKSFSSQLFKETVGNKRKHENLEF | 2.7.7.102 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P49642}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P49642}; | DNA replication initiation [GO:0006270]; DNA replication, synthesis of RNA primer [GO:0006269] | alpha DNA polymerase:primase complex [GO:0005658]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA primase activity [GO:0003896]; metal ion binding [GO:0046872] | PF01896; | 3.90.920.10; | Eukaryotic-type primase small subunit family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11160827}. | CATALYTIC ACTIVITY: Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.; EC=2.7.7.102; Evidence={ECO:0000250|UniProtKB:P49642}; | null | null | null | null | FUNCTION: Catalytic subunit of the DNA primase complex and component of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex - primosome/replisome) which play an essential role in the initiation of DNA synthesis (By similarity). During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit pol1, an accessory subunit spb70/pol12 and two primase subunits, the catalytic subunit spp1/pri1 and the regulatory subunit spp2/pri2) is recruited to DNA at the replicative forks (By similarity). The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands (By similarity). {ECO:0000250|UniProtKB:P49642}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
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