Datasets:

vinesmsuic

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SwissProtCLAP_random_10k

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C0QGP6

MGKIIGIDLGTTNSCVAVMEAGEPKVITNSEGNRTTPSVVALTEGGDRLVGQTAKRQAITNPENTVFGVKRLIGRKFDSPQIQGDKKVLPYKIEASANGDTRINLRGKQHSPAEISSFILANIKKTAEDYLGEEVTEAVITVPAYFNDSQRQATKDAGKIAGLTVKRIINEPTAASLAYGLDKKGEEKIVVFDLGGGTFDVSVLEIGDGVFEVKSTNGDTHLGGEDFDLRIIDYIADEFKKSQGIDIRGDKMALQRLKEAAEKAKMELSSAVETDINLPFITADASGPKHLDVKLTRAKLESLVADLLDNLVAPCKTALKDAGLTSSDINEVVLVGGMTRMPAVQERVEKIFSKKPHKGVNPDEVVAMGAAIQAGVLQGDVHDVLLLDVTPLSLGIETLGGVMTKLIDKNTTIPTKKSQVFSTAADSQPAVSIHVLQGEREMAAGNKTLGQFELTDLPPAPRGVPQIEVTFDIDANGIVHVAAKDKATGKEQSIRITAASGLSEEEIKKMVNDAELHADEDKKKHELVDAKNTAESLIHQTEKTLKEHGDKVDAATKTAIEAACEELKKVKEGTDAAIIKEKSEALTQASHKLAEAMYQQAAQESGQTEGAAQDPKGAAQDDDVVDADFEEVKDHKK

Acts as a chaperone. By stress conditions e.g. heat shock. Belongs to the heat shock protein 70 family.

B2FI06

METVRIATRKSPLALWQSEHVADRLRQAHPGLHVELVPMSTRGDEVLDRSLAAIGGKGLFLKELELAMLRGEADCAVHSLKDVPMELDPPFALPAMLTRHDPADGFVSNLYASLDALPIGARVGTSSLRRQAQLRALRPDLELLDLRGNVNTRLAKLDNGGYDAIVLAVAGLERLGLGERIVARLQPPQWLPAPAQGAVAVECDGGNARLMALFAPLDDAATRACVEAERAMNRALHGSCHVPVAAIAQWQGDDLHLQGLVGSASDGRAVRAEAVGPANDPEGLGQRVAKLLLDDGAGELLNV

Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+) Binds 1 dipyrromethane group covalently. Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4. Monomer. The porphobilinogen subunits are added to the dipyrromethane group. Belongs to the HMBS family.

Q6LKM4

MKTNLWNGFIDVVKREVVPALGCTEPVSVALAAAIAVEKLNGTVEKITALVSPNLMKNGMGVGVPGTGMVGLPIAAAVGAIAGEANAQLEVLKNITPEDVAHAKILIDAGNVHVGVADVNNILYAKVTVTSGDEFVAVTIADSHTHVMAIEENGITTYIAEPANTATSVKKTSPFEGALLEDIYDFALNAPLEEICFIEHAAELNDALSEEGLTGKYGLQIGATFQRNVDRGLLSGGLLTDVLRRTAAASDARMDGAMKPAMSNSGSGNQGIAATMPVVVVADFLKVDKEKTIRALMLSHLTAIYIKSHQNKLSALCGATTASMGAVAGMTWLLGGDLNKINNAICSMIGDIAGIICDGAKTSCAMKVSSSAGSAVKSALMALDGIYVTGNEGIVADNADASIRNLSALANGSMTQTDVQILDIMVNK

Belongs to the UPF0597 family.

Q4WPW2

MAPASQSTYQKDERVLCFHHEILYEAKILDVRHTNAEDKKSPFEYLVHYKGWKNTWDDWVPQDRLRKFTDENRELATTLRREAEAAFRQKSTKTTLKRKAGSDRGSARDSEERQTSVPGRVTKRARDNEIEKEEHFYTRPSVRIVMPDNLKSLLVDDWENVTKNQQVVALPAKASVNQILEDFVAEEKPKRTSSADLDVLEEVIMGIKEYFDKALDKILLYRFEREQYKALRKKWEAGSGEYSEKGPLDVYGAEHLTRLFATMPELIAQTNMDLQSTNRLREELSKFTLWLSKNSDKYFATRYMTATNEYVEKSRGNPSAAATAATTRLV

Involved in deacetylation of histones, chromatin assembly and chromosome segregation. May act as a transcriptional oscillator, directing histone deacetylases to specific chromosomal domains. 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). Component of the NuA4 histone acetyltransferase complex. Belongs to the MRG family.

E3QJV4

MQVTFTLVAALAGMASAAVAGERGSFGCATHEPTLEHIEISKKLAEEEATNATLFGLAAAATITVPTYFHVVASSQTVANGYITDKMLSDQLAVMNEDFAPHGISFNLVQTTRTINPTWARDGDELAMKRSLRKGDYGALNLYFLRDIGGAFGYCYFPTTASPGSASYIRDGCTILSSTVPGGSSTNYNLGRTVTHEVGHWFGLYHTFQGGCTGSGDSIADTPAQSSPSSGCPVGRDSCPNQPGVDPIHNYMDYSIDSCYEEFTPNQQTRMYSFFNQYRA

Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Belongs to the peptidase M43B family.

A5UMB0

MVRKNQEWPDEGELIIGTVYKVLNYGAFAKLEEYHGKEAFIHISEVSSGWVKNIRDHVRENQKIVCRVLRVNPKKGHVDASLKRIREDQRTKKIQHWKIEQKAEKFLELSAKSLGKSLNDAYDEVGYELMDIFGDVYGAFETAADDGAKSLTDEGISQEWADAITEIANKNITPPEVHISGYVDIETFVPDGVDVIIEALKAAEDNGDEEEEIKVQCVGAPRYRITVKSTDYILAEKALKAAADRCIEIVEASEGNGSFLRELDS

eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. Heterotrimer composed of an alpha, a beta and a gamma chain. Belongs to the eIF-2-alpha family.

Q96D04

MAAPVVAPPGVVVSRANKRSGAGPGGSGGGGARGAEEEPPPPLQAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCRPTSLNVVRIITSELYRSLGDVLRDVDAKALVRSDFLLVYGDVISNINITRALEEHRLRRKLEKNVSVMTMIFKESSPSHPTRCHEDNVVVAVDSTTNRVLHFQKTQGLRRFAFPLSLFQGSSDGVEVRYDLLDCHISICSPQVAQLFTDNFDYQTRDDFVRGLLVNEEILGNQIHMHVTAKEYGARVSNLHMYSAVCADVIRRWVYPLTPEANFTDSTTQSCTHSRHNIYRGPEVSLGHGSILEENVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKPRSVLTSQVVVGPNITLPEGSVISLHPPDAEEDEDDGEFSDDSGADQEKDKVKMKGYNPAEVGAAGKGYLWKAAGMNMEEEEELQQNLWGLKINMEEESESESEQSMDSEEPDSRGGSPQMDDIKVFQNEVLGTLQRGKEENISCDNLVLEINSLKYAYNISLKEVMQVLSHVVLEFPLQQMDSPLDSSRYCALLLPLLKAWSPVFRNYIKRAADHLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQRDTTDKGQQLRKNQQLQRFIQWLKEAEEESSEDD

Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP. Complex of five different subunits; alpha, beta, gamma, delta and epsilon. Interacts with RGS2. Phosphorylated at Ser-544 by DYRK2; this is required for subsequent phosphorylation by GSK3B (By similarity). Phosphorylated on serine and threonine residues by GSK3B; phosphorylation inhibits its function. Polyubiquitinated, probably by NEDD4. The disease is caused by variants affecting the gene represented in this entry. Belongs to the eIF-2B gamma/epsilon subunits family. Leiden Open Variation Database (LOVD)

Q06583

MARPIADLIHFNSTTVTASGDVYYGPGGGTGIGPIARPIEHGLDSSTENGWQEFESYADVGVDPRRYVPLQVKEKRREIELQFRDAEKKLEASVQAELDKADAALGPAKNLAPLDVINRSLTIVGNALQQKNQKLLLNQKKITSLGAKNFLTRTAEEIGEQAVREGNINGPEAYMRFLDREMEGLTAAYNVKLFTEAISSLQIRMNTLTAAKASIEAAAANKAREQAAAEAKRKAEEQARQQAAIRAANTYAMPANGSVVATAAGRGLIQVAQGAASLAQAISDAIAVLGRVLASAPSVMAVGFASLTYSSRTAEQWQDQTPDSVRYALGMDAAKLGLPPSVNLNAVAKASGTVDLPMRLTNEARGNTTTLSVVSTDGVSVPKAVPVRMAAYNATTGLYEVTVPSTTAEAPPLILTWTPASPPGNQNPSSTTPVVPKPVPVYEGATLTPVKATPETYPGVITLPEDLIIGFPADSGIKPIYVMFRDPRDVPGAATGKGQPVSGNWLGAASQGEGAPIPSQIADKLRGKTFKNWRDFREQFWIAVANDPELSKQFNPGSLAVMRDGGAPYVRESEQAGGRIKIEIHHKVRVADGGGVYNMGNLVAVTPKRHIEIHKGGK

Causes breakdown of chromosomal DNA as well as complete inhibition of lipid synthesis in sensitive cells. Purified pyocin S1 makes up a complex of the two (large and small) proteins. The large protein, but not the pyocin complex, shows in vitro DNase activity. Pyocins contain N-terminal receptor-binding domain, translocation domain and C-terminal DNase domain. Belongs to the colicin/pyosin nuclease family.

P02912

MIEIIQEYWKSLLWTDGYRFTGVAITLWLLISSVVMGGLLAVILAVGRVSSNKFIRFPIWLFTYIFRGTPLYVQLLVFYSGMYTLEIVKGTDLLNAFFRSGLNCTVLALTLNTCAYTTEIFAGAIRSVPHGEIEAARAYGFSSFKMYRCIILPSALRIALPAYSNEVILMLHSTALAFTATVPDLLKIARDINSATYQPFTAFGIAAVLYLLISYVLISLFRRAERRWLQHVSSK

Part of the histidine permease ABC transporter. Also part of a lysine/arginine/ornithine transporter. Probably responsible for the translocation of the substrate across the membrane. Required to relay the ATPase-inducing signal from the solute-binding protein to HisP. The complex is composed of two ATP-binding proteins (HisP), two transmembrane proteins (HisM and HisQ) and a solute-binding protein (HisJ or ArgT). Belongs to the binding-protein-dependent transport system permease family. HisMQ subfamily.

Q9CI80

MTRYKATIAYDGTDFAGFQSQTNQRTVQKEIEKILTKLNSFEPVILQGSGRTDSGVHAFGQVIHFDLKGKVRDLERLRFGLDTQTPADIAVKKVELVPDDWHARYQKHEKTYEYYLENSITRSPFQRHSKAYFRYPLNFERMQEAMSKLVGEHDFTGFTASGSSVDDKVRTIYQAEIIRLDEENFKFIFRGNGFLYKQVRNMVGTVIKIGNDRMPVSQIDKILTSKNRDFAGPTAAPEGLYLKEVKYAENTDI

Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA Homodimer. Belongs to the tRNA pseudouridine synthase TruA family.

B2V7L6

MPRQVPIEKLRNIGIVAHIDAGKTTTTERILFYTGKTYKIGEVHEGAATMDWMEQEKERGITITSATTAAYWKGYQLNIIDTPGHVDFGVEVVRSMKALDGIVFVFASVEGVQPQSEANWRWADRFGVPRIAFVNKMDRVGANFFGVYEDMKKKLGTNPVPIQVPIGAEDNFKGVVDLFNMKAIIWEGDELGAKFEEKEIPAELIDLAQEWREKMIEAIVETDESLMEKYFAGEEIPAEDLKKALRKATIERKLVPMLCGTAFKNKGIQPMLDAVIDFLPSPVDVPPVKGANPNTGEEEARHASDDEPFCALAFKVMADPYAGQLTYFRVYSGSVKAGQTVYVSNKGKKERIGRILRMHANQREEISEVYAGDIAAAVGVDATTGDTLCDEKAPIVLEKMEFPEPVIAMAIEPKTKSDQEKLSQVLNKFMKEDPTFKVSVDPETNQTLIHGMGELHLEIIIDRMKREHKLEVNVGKPQVAYKETIKKKATAEGKFIRQSGGRGQYGHVWIDIEPNQEKEYEFVDKIVGGVIPKEFIPAVDEGIREAMNQGVVAGYPVINVKATLFDGSFHEVDSSEIAFKIAGSMAFRDAMKKADPVLLEPIMHVEVDTPEEYMGDVMGDLNRRRGRILGMEKRGNTVTIKAEVPLAEMFGYATDLRSITQGRATFVMTFERYEEVPRHIAEQVAGQRSKANA

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.

B1X6P4

MKIDLNADLGEGCASDAELLTLVSSANIACGFHAGDAQIMQACVREAIKNGVAIGAHPSFPDRENFGRSAMQLPPETVYAQTLYQIGALATIARAQGGVMRHVKPHGMLYNQAAKEAQLADAIARAVYACDPALILVGLAGSELIRAGKQYGLTTREEVFADRGYQADGSLVPRSQSGALIENEEQALAQTLEMVQHGRVKSITGEWATVAAQTVCLHGDGEHALAFARRLRSAFAEKGIVVAA

Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate. 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate Forms a complex composed of PxpA, PxpB and PxpC. Belongs to the LamB/PxpA family.

Q0P8S7

MAEILCTICARGGSKGVKNKNIRKINKLEMIAYSIIQAQNSKLFKHIVISTDSDEIASVAQKYGAEVFFKREAHLANDRTAKLPVMRDALLRSEEHFKTCFETLIDLDASAPLRSSLDIKKAYESFVENDNSNLITAVPARRNPYFNLVEIQNNKVVKSKEGNFTTRQSAPKCYDMNASIYIFKRDYLLENDSVFGKNTGLFVMDESTAFDIDSELDFKIVEFLISLKNLSPKDF

Involved in biosynthesis of legionaminic acid (5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonic acid)(Leg), a sialic acid-like derivative that is incorporated into flagellin via O-linkage to Ser/Thr. Catalyzes the conversion of N,N'-diacetyllegionaminic acid (Leg5Ac7Ac) and CTP into CMP-N,N'-diacetyllegionaminic acid (CMP-Leg5Ac7Ac). CTP + N,N-diacetyllegionaminate = CMP-N,N-diacetyllegionaminate + diphosphate Belongs to the CMP-NeuNAc synthase family.

Q2S009

MLSHERRLWADGYERVAGLDEAGRGCLAGPVVAAAVIMPPQVEITAIQDSKALSEGQRLDARATIEDEAVAASIARCSPTEIDDRNILQAALEAMRRAASGCRPPPDFVLVDGNQWDRNLVDAPWPHETVVKGDAKSQSIAAASILAKTERDALMRDLHEAHPEYDWASNVGYPTQQHYDALREHGATPHHRQSFTLFRD

Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. Endonucleolytic cleavage to 5'-phosphomonoester. Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding. Belongs to the RNase HII family.

Q6XYE1

MEPTEPMEPTEPMEPTEPMEPARSAHRGGEALLRELEVLVQDVVRTSSWWERHGVDCAILALSLFALPAGFLCLRWENALVFASGITILGVCHYTLTVKGSHLATHGALTESKRWSKIWLLFFVEVCTAFTAEHATHGHVKMHHAYTNVVGLGDSSTWRLPCLNRYVYMFLAPFLLPIATPLVAVERLRKVELGTALRTLALISLGLYSHYWLLLNVSGFKNPSSALGCMFLTRSLLAHPYLHVNIFQHIGLPMFSRDNKPRRIHMMSLGVLNLARLPVLDWAFGHSIISCHVEHHLFPRLSDNMCLKVKPVVSQFLREKQLPYNEDSYLARFQLFLRRYEEFMVQAPPITELVGL

Lipid metabolism; fatty acid metabolism. Belongs to the fatty acid desaturase type 1 family. The N-terminus contains a duplication of the repeated 'MEPTEP' sequence. It is unclear whether such duplication is due to a sequencing error or a polymorphism.

D6W1L1

MLHLQPQNLLIQKTLNEAIEALRKGSPLTMDRIVSDFDYTTYHISNTAEDKSILLLSVKTKAWVSVSECQLDGSLTLLKFLADHYSSLGGVTIPSEVEPGYDYTLQITLAELVQESILQLSVLKTIILSFPFELAISKFIELSQQQPAPVEAEITGGEVAANGDNTLFTIKYRDEENIFIKPSNDRVTIIFETIFQDETDKIFGKVFLQEFVDARKRNRQIQSAPQVLYSHEPPLELKRLYQPPKVAEQSRRFITFVLFPRHFQTKELQFHSICQLTLFRNYFHYHIKCSKAYMHSRMRFRVDSFIKVLNRAKVDEDDENDELSAEGRQQARRTFTGRKIVY

Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament (By similarity). Component of the Arp2/3 complex composed of ARP2, ARP3, ARC40/p41-ARC, ARC35/p34-ARC, ARC18/p21-ARC, ARC19/p20-ARC and ARC16/p16-ARC. Present with 13400 molecules/cell in log phase SD medium. Belongs to the ARPC2 family.

Q9UNV3

MKDVPGFLQQSQNSGPGQPAVWHRLEELYTKKLWHQLTLQVLDFVQDPCFAQGDGLIKLYENFISEFEHRVNPLSLVEIILHVVRQMTDPNVALTFLEKTREKVKSSDEAVILCKTAIGALKLNIGDLQVTKETIEDVEEMLNNLPGVTSVHSRFYDLSSKYYQTIGNHASYYKDALRFLGCVDIKDLPVSEQQERAFTLGLAGLLGEGVFNFGELLMHPVLESLRNTDRQWLIDTLYAFNSGNVERFQTLKTAWGQQPDLAANEAQLLRKIQLLCLMEMTFTRPANHRQLTFEEIAKSAKITVNEVELLVMKALSVGLVKGSIDEVDKRVHMTWVQPRVLDLQQIKGMKDRLEFWCTDVKSMEMLVEHQAHDILT

Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits including PSMD13, a base containing 6 ATPases and few additional components. Belongs to the proteasome subunit S11 family.

Q965Q4

MGSVSKTVISARGASPDDEQNGTKNGISNGSEWAKCIFLFFFLFIAGMSNWAVLAYTHDYVPRESLPDIVFSLVSEQRWASSLGDFCVALCIVMLGALLVIHQHRGTILKRVVFCAGTLYAMRSVTLAATQLPSGYTDNQGRCRDQVESEAGVFFGRLFEQTIRIGFQSKDQMLCGDLLFSGHTLVMVTCSLAVAYYLPKSIKPLQWVSHVACLIGMICMTISRTHYTIDVVIAYWLSNMVFRMYHAYCEVDMCMERRKSILYSWWPCRIVDWLEQDIVPGRLENRCQLPWRRSTPRGQERGGASAESSDSSVTMCDNITTSHHQKHVSISSSSTYPLPC

Bidirectional lipid cholinephosphotransferase capable of converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. Directly and specifically recognizes the choline head group on the substrate. Also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Does not function strictly as a SM synthase (By similarity). a 1,2-diacyl-sn-glycero-3-phosphocholine + an N-acylsphing-4-enine = a 1,2-diacyl-sn-glycerol + a sphingomyelin Lipid metabolism; sphingolipid metabolism. Belongs to the sphingomyelin synthase family.

C1KWE3

MYYYLITLAVIALDQLTKWIVVQNMEIGQKIEVIPGFLYWTSYRNDGAAWSILEGHMWFFYLITVVVIGIIIYIMQKYAKGKRLFSISLAFILGGAIGNFIDRVLHQEVVDFVQTVWGNYYFPIFNVADAALSVGVVLMLVYVFVDDRKTKGIK

This protein specifically catalyzes the removal of signal peptides from prolipoproteins. Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains. Protein modification; lipoprotein biosynthesis (signal peptide cleavage). Belongs to the peptidase A8 family.

O54749

MIMFLSSLVTTFWEALHLKTLVLAVVTFLFLINILRSRHPKNYPPGPWRLPFVGNFFQIDTKQTHLVLQQFVKKYGNVFSLELGQSPVVVVSGLPLIKEMFTHLDQNFVNRFMTPVRERITGKNGLVVSNGQTWKEQRRLALMALRNFGLGKKSLEERIQEETHHLVEAIREEGGQPFNPHLKLINAVSNIICSVTFGERFDYEDCQFQELLQLLDETMHLMGSSAGQLYNGFPCIMKYLPGPHQKIFRNWGKLKLFVSHIVKKHEKDWNPDEPRDFIDAFLIEMQKDPDRTTSFNEENLISTTLDLFLGGTETTSSTLRWALLYMSSYPEIQENVQAEIDRVIGHKRQVSLSDRESMPYTNAVIHEVQRMGNIVPLNSSREVTVDTKFNGFHLPKGTMILTNLTALHRDPKEWATPEVFNPEHFLENGQFKKRESFLPFSMGKRACLGEQLAKSELFIFFSALMQKFTFKPPINEKLSLKFRMGLILSPASYRICAIPRV

an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] Belongs to the cytochrome P450 family.

Q3T0S5

MAHQFPALTSEQKKALSETARRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFTVDSSVSQSIGGVILFHETLYQKDGQGKLFRDILKEKGIVVGIKLDQGVAPLAGTNKETTVQGLDGLSERCAQYKKDGADFGKWRAVLKIDNQCPSHLAIQENANTLARYASICQQNGLVPIVEPEVIPDGSHDMEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPLPKPWKLSFSYGRALQASALAAWGGKAENKKTTQEAFMKRALANSQAAKGQYVHMGSSGSASTQSLFTASYTY

beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Homotetramer. Interacts with BBS1, BBS2, BBS4 and BBS7. In vertebrates, 3 forms of this ubiquitous glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver and aldolase C in brain. Belongs to the class I fructose-bisphosphate aldolase family.

O49606

MALKTATSGMWMTDDCKKSFMEMKWKKVHRYVVYKLEEKSRKVTVDKVGAAGESYDDLAASLPEDDCRYAVFDFDYVTVDNCRMSKIFFITWSPEASRIREKMMYATSKSGLRRVLDGVHYELQATDPTEMGFDKIQDRAK

Does not display typical F-actin depolymerizing activity. Exhibits a high ability to stabilize and cross-link actin filaments. Functions as an actin bundling protein with the highest efficiency under acidic conditions (PubMed:21570971). May play a role in the modulation of levels of histone H3 lysine 4 trimethylation and H3 lysine 9 and 14 acetylation at the FLC locus (PubMed:18830798). By auxin, gibberellin, abscisic acid (ABA) and kinetin in roots. Developmental defects, reduced plant size, early flowering and decreased number of inflorescence secondary branches. Belongs to the actin-binding proteins ADF family.

Q9NJP2

AAFAYFSGFMLDDARFSPAEIELMESVLLDNNLTMVQFVDRLRWDCHELLHRCRYHGDIMDCTQLFQLSKTFFGHCCSFNLRQHGLDFTAQAAAGGLDNGLSLILRYKDENYDALQSYSHGFKLLIQETDAFPSAHADCKFLGLNTESFATLRVVETFCSEAVKSLPISQRNCVFRHEFRLRYFSDYVYPNCELNCRAKNMVKLCGCHTYFFEFNRTKDRVCTFRDIPCLVDNFPDIITRRKKTQCNCPLTCEHFDYDVQMSNFALMLNMPVVDPFYTGIERNDAIVHIFLNSQVYRRVRVDLLSNMVTLVSHLGSAFSLFVGMSMLSLVEIIYYFTVILRRNYVQECRARQKLQTLHRRPNFGWPGDKNSNQQKSVFYIRGRN

Part of a complex that plays a role in tracheal liquid clearance. Probable role in sodium transport (By similarity). Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family.

Q8MUP5

MKSVFVCTLVLALAHHAFAGVCDSNVDYNSTLITPCLGNDIIVLWPNYLNFNTYYKCVEFGKPQLMDCPPNTYFTYYFQQCTGCDNFIPAPTCEYLKQTTDVECVPLVKPTTAAPTTLKTTPSKTTPIVTTAPPSTPVPSTIVTNKPDPTTPKTTKPPKVTTTVNPSPPTGTGPATNAPSSDIPLPPIASTVNTKYPTPPGMPPTPPSFGTPPSIVQLQN

May bind oligosaccharide structures. Larval peritrophic membrane. Expressed in all 3 larval instars but not adults or eggs. Glycosylated.

Q9BPD1

MLCLPVFIILLLLASPAAPNPLQTRIQSNLIRAGPEDANIKTDKRVISGLLASILVPLIDAIIG

Expressed by the venom duct. The mature peptide does not contain cysteine residues. Belongs to the conotoxin T superfamily.

B5BEY9

MDQKRLTHLRQLETESIHIIREVAAEFANPVMLYSIGKDSSVMLHLARKAFYPGTLPFPLLHVDTGWKFREMYAFRDRTANAYGCELLVHKNPEGVAMGINPFVHGSAKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERIYSFRDRFHRWDPKNQRPELWRNYNGQINKGESIRVFPLSNWTEQDIWQYIWLENIDIVPLYLAAERPVLERDGMLMMVDDDRIDLQPGEVIKKRMVRFRTLGCWPLTGAVESHAQTLPEIIEEMLVSTTSERQGRMIDRDQAGSMELKKRQGYF

With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD. ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3. Heterodimer composed of CysD, the smaller subunit, and CysN. Belongs to the PAPS reductase family. CysD subfamily.

Q99TP4

MRVDLNCDLGEAFGNYSFGGDHQIIPLITSANVACGFHAGDENVMNETVKLAKAHNVAVGAHPGLPDLKGFGRRNIDISNDEIYNLMIYQLGALQGFCRIHQLKINHVKPHGALYQMGAKDREIANVIAQAVYDFDPSLVLVGLANSYLISEAKNVGLITASEVFADRRYEDDGQLVSRKESDAVITDTDEALKQVLKMVKENKVISKNNKEVTLQADTICVHGDGEHALLFVSKIREILMKEGIDIQSL

Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate. 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate Forms a complex composed of PxpA, PxpB and PxpC. Belongs to the LamB/PxpA family.

Q72NU6

MKEVSVPAIKRIVLIAHDNRKEDLVNWVKTHREILSKHQLYGTGTTGKLISEETELPVYRFLSGPLGGDQQIGAKIAEGDLDIVIFFWDPLTAQPHDPDVKALLRIAVLYNVPMACNRSTADYMISSPQFTKTYKKILLSYNTKVKKD

Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate. dihydroxyacetone phosphate = methylglyoxal + phosphate Belongs to the methylglyoxal synthase family.

Q3BAH2

MDGIKYAVFTEKSIRLLGNNQYTSNVESGSTRTEIKHWVELFFGVKVIAMNSHRLPGKGRRMGPIMGHTMHYRRMIITLQPGYSIPPLIEKRT

Binds to 23S rRNA. Part of the 50S ribosomal subunit. Belongs to the universal ribosomal protein uL23 family.

C4K2Q8

MSSLVRPINLGKINHSQSTVKDYILLMKPRVMSLVIFTGFVGMWLAPYSVHPFIAGIAVVCIALGAGSAGAINMWYDRDIDSLMKRTQKRPIVRGVIESDEALSFGLITGFFAVFFMALCVNLLASFLLLFTIFYYICIYTIWLKRRSIQNIVIGGVSGALPPVIGYAAVSNTISLESSILFLIIFIWTPPHSWALALFCNDDYKNCKVPMMPAVKGTLYTKKQILIYSILLFIVSLMPFFIGMNNFIYLIISGILGVVFLYYAGSLFYDTPDNKQAKRFFAYSIFYLFFIFLLLYSTNTISTIS

Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1. Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature. Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.

Q2YV69

MINKNDIVADVVTDYPKAADIFRSVGIDFCCGGQISIEAASLEKKNVDLNELLQRLNDIEQTNTPGSLNPKFLNVSSLIQYIQAAYHEPLREEFKNLTPYVTKLSKVHGPNHPYLVELKETYDTFKNGMLEHMQKEDDVDFPKLIKYEQGEVVDDINTVIDDLVSDHIATGQLLVKMSDLTSSYEPPIVACGTWRLVYQRLKALEVLTHEHVHLENHVLFKKVS

Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions. Homodimer. Belongs to the RIC family. ScdA subfamily.

C3MHU1

MADGSSETKSSNQMWGGRFASGPDAIMEEINASIGFDKKLYAQDIRGSIAHATMLAHKGIISAEDKDKIVHGLETILSEIESGAFDFSRRLEDIHMNIEARLASLIGPAAGRLHTARSRNDQVALDFRLWVKEELQRTEKALTGLIGAFLDRAEEHAGTVMPGFTHLQTAQPVTFGHHCMAYVEMFGRDRSRVRHAIEHMDESPIGAAALAGTGFPIDRHMTAKALGFREPTRNSIDTVSDRDFALEFLSIASIAATHLSRLAEEIVIWSTPQFGFIRLSDAFSTGSSIMPQKKNPDAAELVRAKTGRINGSLIALLTVMKGLPLAYSKDMQEDKEQVFDAAESLELAIAAMTGMVRDMTVRADRMKAAAGSGYSTATDLADWLVREAGLPFRDAHHVTGRAVALAEQKGCDLADLSLADLQAINPAITDKVFDVLTVEASVASRTSFGGTAPAEVRKQIAWWRARN

2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.

B1JWS3

MSASDLTSVQAAAPQGSRQILVTSALPYANGQIHIGHLVEYIQTDIWVRTLRMHGHEVYYIGADDTHGTPIMLRAEKEGLTPKQLIDRVWTEHKRDFDSFGVSFDNFYTTDSEENRVLSENIYLALQEAGLIAEREIEQAYDPVKEMFLPDRFIKGECPKCHAKDQYGDSCEVCGSTYLPTELLNPYSVVSGATPVRKTSKHYFFRLSDPRCESFLREWVSGLAQPEATNKMREWLGDAGESKLADWDISRDAPYFGFEIPGAPGKYFYVWLDAPVGYYASFKNLCERNGIDFDAWIRPGSKAEQYHFIGKDILYFHTLFWPAMLEFSGHRTPTNVFAHGFLTVDGAKMSKSRGTFITAQSYIDTGLNPEWLRYYFAAKLNATMEDIDLNLDDFQARVNSDLVGKYVNIASRAAGFLIKRFDGRVQDSAMNHPLVAKLRDAIAQIAASYEAREYGRALRHTMELADEVNAYVDGAKPWDLAKDPANAVALHETCSVSLEAFRLLSLALKPVMPRVAEAVEAFFGIAPLAWADAAKPLSSAQPIKAYQHLMTRVDAKQIEALLAANRDSLQAEAAGAAAAGANAAKDAKSNAKAKPAAVNGADDAPISIDDFAKIDLRIAKIVACQAVEGSDKLLQLTLDVGEEKTRNVFSGIKSAYQPEQLVGKLTVMVANLAPRKMKFGLSEGMVLAASATDEKAEPGLYILEPHSGAKPGMRVK

Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met) Binds 1 zinc ion per subunit. Homodimer. Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily.

A9M1R2

MAKKYFGTDGVRGEVGQFPITPDFVLKLGYAAGQVLVQHDTDQKPTVLIGKDTRISGYMLEAALVAGFTAAGVNVIQTGPLPTPGVAYLTRALRLSAGVMISASHNAYSDNGIKFFAEGGVKLSDEIELEIEAKIDEEMKTQPSARLGRARRISGADDRYIEFCKSTFPTHSDLRGLKLVVDAANGAAYSVAPKVFHELGAQVVSIGDEPDGYNINEKCGATHTKTLQAAVLQNEADYGIALDGDGDRLMMVDKNGKVYDGDSLIYVIAKARAREGINIGGVVGTVMTNMAMEIALKEQGVDFCRAKVGDRYVLEQLNQRSWLIGGEASGHILCMDKHNTGDGIISALQVLAALQTLNQDLATVCADWQPYPQTMINVRIQKGQKWQEASKDVLAEVEKELEGKGRVVLRASGTEPVVRVMVEARQADWARDGAERIASAIGSL

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate Binds 1 Mg(2+) ion per subunit. Activated by phosphorylation. Belongs to the phosphohexose mutase family.

Q08699

MAPRKGKAPKEEQVISLGPQVADGENVFGVAHIFASFNDTFVHVTDLSGKETIARVTGGMKVKADRDESSPYAAMLAAQDVAVRCKEIGITALHVKLRATGGNRTKTPGPGAQSALRALARSGMKIGRIEDVTPIPSDCTRRKGGRRGRRL

Belongs to the universal ribosomal protein uS11 family.

Q54LT8

MRQPLICSGHSRPVSDLSFSNENSDGSFIVSACLDGSPMLRNGENGDWIGTFEGHKGAVWSSRFNSTASQALTASADYTVKLWDTLNGSEILSIEHQSIVKTADFSNNNSRVVTGGSEKILRIFDLERPNDPLLQISGHTNTIKTATWSVHNDDIVLSGGLDEVIRIWDLRSGTQVSLCAKSSITSMEFSKDRRFLVTTAGNEVTFWDAQSFYPLKVYSLPFDVNCASLHPDNSKFIAGGSDFWVHVYDFSTGNEIEVNKGHHGPVNCCRFSPDGASFASGSLDGTIRLWKGM

The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. STRAP may play a role in the cellular distribution of the SMN complex (By similarity). Part of the core SMN complex. Belongs to the WD repeat STRAP family.

A4WEY3

MTDVTVKSLATEIQTPVERLVQQFADAGIPKAADDSVTAQEKQTLLAHLNREHGSTPDKLTLQRKTRSTLSIPGTGGKSKSVQIEVRKTRTFVKRDPQEAERLAAEEQAQREAEEQAQREAVETAKREAVLKAEREAAEKAKRDANDKAKRDAAEKDKVSNQQTDEMTKTAQTEKARRENEAAELKRKAEEEARRKLEEDARRVAEEARRMAEENAGVWAEQEKAKGEEDKTDYHVTTSQHARQAEDENDREVEGNRSRTRTATKAARPQKKGNKHAESKADREEARAAGRGGKGGKRKGSSLQQGFQKPAQAVNRDVVIGETITVGDLANKMAVKGSQVIKAMMKLGAMATINQVIDQETAQLVAEEMGHKVTLRRENELEEAVMSDRDTGAAAESRAPVVTIMGHVDHGKTSLLDYIRSTKVASGEAGGITQHIGAYHVETDNGMITFLDTPGHAAFTSMRARGAQATDIVVLVVAADDGVMPQTIEAIQHAKAAQVPVVVAVNKIDKPEADMDRVKTELSQYGVMPEEWGGESQFIPVSAKAGTGIDDLLNAILLQAEVLELKAVRNGMASGAVIESFLDKGRGPVATVLVREGTLNKGDIVLCGFEYGRVRAMRNELGQEVLEAGPSIPVEILGLSGVPAAGDEVTVVRDEKKAREVALYRQGKFREVKLARQQKSKLENMFANMTDGEVHEVNVVLKADVQGSVEAISDSLLKLSTDEVKVKIIGSGVGGITETDATLAAASNAILVGFNVRADASARKVIDSESLDLRYYSVIYHLIDEVKAAMSGMLSPELKQQIIGLAEVRDVFKSPKFGAIAGCMVTEGTIKRHNPIRVLRDNVVIYEGELESLRRFKDDVNEVRNGMECGIGVKNYNDVRVGDMIEVFEIIEIQRSIA

One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex. Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.

B1KE86

MSDGKSVEKEEALSVNEHLKTDSDFLRGTIQEGLDTAVTGSFSEGDQQLIKFHGFYQQDDRDLRNERKEQKLEPLYSFMLRARVAGGVCSPEQWLGVDEISSTLTSSNSIRLTTRQTFQYHGISKRNLRTLIQGLDSKALDSIAACGDVNRNVMCNPNPVESRLHEQAYYWAKQLSDQYLPRTKAYAEIWLGDDKVATSEGDDVEPVYGKTYLPRKFKMAVAVPPDNDVDVYTNDLGFVAVAEEGELVGFNLVAGGGMGSTHGEVQTFPRLADDFGFIKAEDTLKFAEAVLKVQRDWGNRSNRKLSRLKYTIVKYGYEAFKAEVEKRAGVKFEPKRDVVIGDRGDRYGWIKGVDNKWHLTLFIEGGRIKDLPGQPLQTGLREIAKIHKGDFRMTSNQNFIIASVAEEDKAEIEALARSHGLMGKLITETRGRSIACVALPTCALAMAEAERYFPDFLSKVESLQEKHGFLDQGIVIRMTGCPNGCARPFAAEIGLVGKAPGRYNLYLGASFEGTRLNKLYRENIQEAEILSELDSLFARYVAEREEGETFGNFTVRIGAVSAVIDAAKDFHEQHNHA

Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. 3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite Binds 1 siroheme per subunit. Binds 1 [4Fe-4S] cluster per subunit. Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. Alpha(8)-beta(8). The alpha component is a flavoprotein, the beta component is a hemoprotein. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.

A2STI8

MVEVQKEQVYVIPLRDVKRVPCYKRANAAIKDIRGYLEHHMKSDDVKLDKSINELVWARGSQKPPRRIRVRAMKFEDGQVQAELAEE

Belongs to the eukaryotic ribosomal protein eL31 family.

O12985

MLTDSDKKLVLQVWEKVIRHPDCGAEALERLFTTYPQTKTYFPHFDLHHGSDQVRNHGKKVLAALGNAVKSLGNLSQALSDLSDLHAYNLRVDPVNFKLLAQCFHVVLATHLGNDYTPEAHAAFDKFLSAVCTVLAEKYR

Involved in oxygen transport from the lung to the various peripheral tissues. Heterotetramer of two alpha-D chains and two beta chains. Red blood cells. In birds, the alpha-D chain occurs in a minor hemoglobin component, called hemoglobin d, which is expressed in late embryonic and adult life. Belongs to the globin family.

A0L4K6

MLILLTNDDGIASPGLQALKDALKERHDVVTLAPVKDMSGTAHAISRGEDIKLTRIAEYEVAINGTPTDCVMAGLRMVLRRPPDLLVSGINMGANVAEDLSYSATAGAAWEGALSGIPSMAVSLCGSAAPWHFESAIKVTHMVIRQWLENPLPPGTFLNVNVPNVPEYELKNPKPTRQGLRFNWPPPPVTAAGNPAFWDPTIPTPREEEFQLATDEEALRDGFTSVTALHCLFRHPHATERLKAWSLFR

Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate Binds 1 divalent metal cation per subunit. Belongs to the SurE nucleotidase family.

A4FVV8

MFRFDKEQMVIEFAGAKFGGQPGEYPTALSGTIFYARHKIVEDAKKGIFDKKAAEALINKQAEMQDITGNSAFVQVFGGTEEALVNYIDFVSEVWDGPMLLDSTSGKARMAAANRATEAGYAKQCVYNSINVAAEDEEIENLTNSDVEASIVLCFDPMDPSVGGKLNVLNDGGKTKDIGMLELAEKAGIKYPLIDVAVTPMGNGAGHAVRASFAVKAKLGLPVGSGIHNVPSAWDWLREFRKGLREEGKDQISKDVHHVCDIGANIVQTMASGDYVLYGPIDNAELAFPAVAMTDMIIAETAKEMGTATVAEHPLNKLI

Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step. MtrH catalyzes the transfer of the methyl group from methyl-tetrahydromethanopterin to the corrinoid prosthetic group of MtrA. 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + 2 Na(+)(in) = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M + 2 Na(+)(out) One-carbon metabolism; methanogenesis from CO(2); methyl-coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: step 2/2. The complex is composed of 8 subunits; MtrA, MtrB, MtrC, MtrD, MtrE, MtrF, MtrG and MtrH. Belongs to the MtrH family.

A6U816

MAILTIEELAERLPPYQAVAGLDLGTKTIGLSVSDLGRRFATPRDVIRRVKFGIDAQALLFFAEKEKVAAFVIGLPVNMDGSEGPRCQATRAFVRTMGERTDIPSVLWDERLSTVAAERVLIEMDVSRKKRADRIDSAAASFILQGALDRLALLARGASGDRDAP

Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.

A1USW8

MGLVFNNSTIVAPQAKGIIDPNTSKLIGANDQFFQDMNAELSDKGFLVTSVDSLITWARTGSLMWMSFGLACCAVEMMQCSMPHYDNERFGYAPRASPRQSDVMVVAGTLTNKMAPALRKVYDQMPEPRYVISMGSCANGGGYYHYSYSVVRGCDRIVPVDIYVPGCPPTAEALLYGILLLQKKIRRTGSIER

NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+) Binds 1 [4Fe-4S] cluster. NDH-1 is composed of 14 different subunits. Subunits NuoB, C, D, E, F, and G constitute the peripheral sector of the complex. Belongs to the complex I 20 kDa subunit family.

O23116

MGDLAMSVADIRMENEPDDLASDNVAEIDVSDEEIDADDLERRMWKDRVRLKRIKERQKAGSQGAQTKETPKKISDQAQRKKMSRAQDGILKYMLKLMEVCKVRGFVYGIIPEKGKPVSGSSDNIRAWWKEKVKFDKNGPAAIAKYEEECLAFGKSDGNRNSQFVLQDLQDATLGSLLSSLMQHCDPPQRKYPLEKGTPPPWWPTGNEEWWVKLGLPKSQSPPYRKPHDLKKMWKVGVLTAVINHMLPDIAKIKRHVRQSKCLQDKMTAKESAIWLAVLNQEESLIQQPSSDNGNSNVTETHRRGNNADRRKPVVNSDSDYDVDGTEEASGSVSSKDSRRNQIQKEQPTAISHSVRDQDKAEKHRRRKRPRIRSGTVNRQEEEQPEAQQRNILPDMNHVDAPLLEYNINGTHQEDDVVDPNIALGPEDNGLELVVPEFNNNYTYLPLVNEQTMMPVDERPMLYGPNPNQELQFGSGYNFYNPSAVFVHNQEDDILHTQIEMNTQAPPHNSGFEEAPGGVLQPLGLLGNEDGVTGSELPQYQSGILSPLTDLDFDYGGFGDDFSWFGA

Probable transcription factor that may be involved in the ethylene response pathway. Interacts with MYB72. Belongs to the EIN3 family.

Q5R974

MERREEQPGAAGAGAAPALDFTVESVEKALHQLYYDPNIENKNLAQKWLMQAQVSPQAWHFSWQLLQPDKVPEIQYFGASALPIKTSRYWSDIPTDQYESLKAQLFTQITRFASGSKIVLTRLCVALASLALSMMPDAWPCAVADMVRLFQAEDSPVDGQGRCLALLELLTVLPEEFQTSRLPQYRKGLVRTSLAVECGAVFPLLEQLLQQPSSPSCVRQKVLKCFSSWVQLEVPLQDCEALIQAAFAALQDSELFDSSVEAIVNAISQPDAQRCVNTLLKLIPLVLGLQEQLRQAVQNGDMETSHGICRIAVALGENHSRALLDQVEHWQSFLALVNMIMFCTGIPGHYPVNETTSSLTLTFWYTLQDDILSFEAEKQAVYQQVYRPVYFQLVDVLLHKAQFPSDEEYGFWSSDEKEQFRIYRVDISDTLMYVYEMLGAELLSNLYDKLGRLLTSSEEPYSWQHTEALLYGFQSIAETIDVNYSDVVPGLIGLIPRISISNVQLADTVMFTIGALSEWLADHPVMINSVLPLVLHALGNPEPSVSSVSTLKKICRECKYDLPPYAANIVAVSQDVLMKQIHKTSQCMWLMQALGFLLSALQVEEILKNLHSLISPYIQQLEKLAEEIPNPSNKLAIVHILGLLSNLFTTLDISHHEDDHEGPELRKLPVPQGPNPVVVVLQQVFQLIQKVLSKWLNDAQVVEAVCAIFEKSVKTLLDDFAPMVPQLCEMLGRMYSTIPQASALDLTRQLVHIFAHEPAHFPPIEALFLLVTSVTLTLFQQGPRDHPDIVDSFMQLLAQALKRKPDLFLCERLDVKAVFQCAVLALKFPEAPTVKASCGFFTELLPRCGEVESVGKVVQEDGRMLLIAVLEAIGGQASRSLMDCFADILFALNKHCFSLLSMWIKEALQPPGFPSARLSPEQKDTFSQQILRERVNKRRVKEMVKEFTLLCRGLHGTDYTADY

Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. 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 (By similarity). Mediates the nuclear import of UBC9, the RBM8A/MAGOH complex, PAX6 and probably other members of the paired homeobox family. Also mediates nuclear export of eIF-1A, and the cytoplasmic release of eIF-1A is triggered by the loading of import substrates onto IPO13 (By similarity). Interacts with UBC9, RAN, RBM8A, eIF-1A and PAX6. Belongs to the importin beta family.

C4LKC1

MEIRVVDHPLVSSRLTIMRDKRSTNDVFRAALSDLGMMLVYEASRDLSVDTFPVSTPVDQADGFRLTEPPIIVPIIRAGLGMVDPALSMIPDAQVGFIGLARDETTHKPVPYLEALPDDLSGRPVFLVDPMLATGGSLLHAIRLLASRGADDITCICMVAAEPGVQALKAADLPVTRLVTATIDPSLNEDAYIVPGLGDAGDRLYGPRNIDL

Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP. Allosterically activated by GTP. Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1. Belongs to the UPRTase family.

Q9UGN3

MAGAVPGAIMDEDYYGSAAEWGDEADGGQQEDDSGEGEDDAEVQQECLHKFSTRDYIMEPSIFNTLKRYFQAGGSPENVIQLLSENYTAVAQTVNLLAEWLIQTGVEPVQVQETVENHLKSLLIKHFDPRKADSIFTEEGETPAWLEQMIAHTTWRDLFYKLAEAHPDCLMLNFTVKLISDAGYQGEITSVSTACQQLEVFSRVLRTSLATILDGGEENLEKNLPEFAKMVCHGEHTYLFAQAMMSVLAQEEQGGSAVRRIAQEVQRFAQEKGHDASQITLALGTAASYPRACQALGAMLSKGALNPADITVLFKMFTSMDPPPVELIRVPAFLDLFMQSLFKPGARINQDHKHKYIHILAYAASVVETWKKNKRVSINKDELKSTSKAVETVHNLCCNENKGASELVAELSTLYQCIRFPVVAMGVLKWVDWTVSEPRYFQLQTDHTPVHLALLDEISTCHQLLHPQVLQLLVKLFETEHSQLDVMEQLELKKTLLDRMVHLLSRGYVLPVVSYIRKCLEKLDTDISLIRYFVTEVLDVIAPPYTSDFVQLFLPILENDSIAGTIKTEGEHDPVTEFIAHCKSNFIMVN

Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II (PubMed:12612062). The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex (PubMed:10199401). (Microbial infection) The NELF complex is involved in HIV-1 latency possibly involving recruitment of PCF11 to paused RNA polymerase II. The NELF complex is composed of NELFA, NELFB, NELFCD (isoform NELF-C or isoform NELF-D) and NELFE; NELFA and NELFCD form a stable subcomplex that binds primarily through NELFCD to the N-terminus of NELFB (PubMed:27282391, PubMed:12612062). Binds RNA which may help to stabilize the NELF complex on nucleic acid (PubMed:27282391). In vitro, the NELFA:NELFCD subcomplex binds to ssDNA and ssRNA in a sequence- and structure-dependent manner (PubMed:27282391). Interacts with ARAF (PubMed:11952167). Interacts with PCF11 (PubMed:23884411). Interacts with KAT8 (By similarity). Widely expressed. Expressed in heart, brain, lung, placenta, liver, skeletal and cardiac muscle, adrenal, thyroid, kidney and pancreas. Produced by alternative initiation at Met-10 of isoform NELF-C. Belongs to the NELF-D family.

Q7UM97

MAKQLLFEDHARARMLAGVEKLAKAVATTMGPTGRNVIIDKSFGGPTVTKDGVTVAKEIELEDRFENMGAKLVIEVAQKTSDLAGDGTTTATVLARAIFKEGLRNIVAGSNPTAIRRGIEKAVEAACDQLVEMGRPVSGKQEVAHVGAISANNDNVIGELLADALERVGKDGVITVEEGKSRNTEVEYVDGMQFDKGYVSPYFITDSSTMEASLEDALVLLYEKKVSNIRDLVPLLEKTAQTGQPLLIIAEDVDAEALTLLVVNKLRGTLNVCAVKAPGFGDRRKAMLGDIATLTGGTLISEDLGMQLENVTLEHLGRAKKVTVDKSNTTIVEGAGKREDIDKRVAQIRAQIEQTDSDYDKEKFQERLAKLAGGVAVISVGAETEAEMKQTKARLEDALHATRAAVEEGILPGGGVALVHCREAVEAAKKKAKGDEKIGVDIVLGALDAPMRQIADNGGIDGSVVVDEVLQKNDPKIGFNAHTGEYTDMVKAGVIDPVKVVRTALTNAASIAGLLLTTEALVTNFEQEDKDKRPVEGMVS

Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide. Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES. Belongs to the chaperonin (HSP60) family.

Q39XY3

MKVRASVKKICDKCKIIKRKGIVRVICETPKHTQRQG

Belongs to the bacterial ribosomal protein bL36 family.

Q1MPX3

MAVILLGNEHIWKLPFCRLEFVAILEKMLSFAKLQTIEVYLVSDTTIAFFNLHYMNCLGITNVLSFPMDDEDLAGSIILSVDAVCRESLLYRQPILDYCLSLLSHGIAHIAGYTHGVEMDKFCSNLLLPFKLA

Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. Binds 1 zinc ion. Belongs to the endoribonuclease YbeY family.

Q1QWA6

MNYDIADLRRDYAGETLSVESAPASPLDLFQTWFAAAREHETQDANAMTLATVDSQGLPHARVVLLKQLDDKGLVFFTNYQSHKGSELTNVPYAALVFWWPTLQRQIRIEGRVEKASAEVSDAYFANRPRDSQLGAWISQQSVEIPDRDWLEERKQRFEQVYGEQTVERPPHWGGYRVLPFLLEFWQGQPNRLHDRIRYRYHEQDAAWSKTRLAP

Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate O2 + pyridoxine 5'-phosphate = H2O2 + pyridoxal 5'-phosphate Binds 1 FMN per subunit. Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1. Homodimer. Belongs to the pyridoxamine 5'-phosphate oxidase family.

B0BA79

MFILPPPQEPLLGAHTSAAGGLHNALYEGRDIGATTVQLFTANQRQWKRRALTQEMVDQFRIALNETSLSYIMSHAGYLNNPGAPNPEILEKTRVCMHQEIADCISLGISFVNFHPGAALSDSKESCLDRAITSFSQMAPLFENHPPLVVLLETTAGQGSLIGSSFEELAYLIQGIKALIPIGVCLDTCHIFAAGYDISSVAGWEQVLKHFDAVIGLSFLRAIHLNDSVFALGKNKDRHAPIGEGCIGSDSFCFLMQDERTRMLPKYLETPGGPDLWTKEIRYLQKVC

Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products. Binds 3 Zn(2+) ions. Belongs to the AP endonuclease 2 family.

P49416

MPLPRAAFLLGLLLAAAAAESVRETETMDARWLDNVGSGDLPDDEDIGEFTPHLTSDEFDIDDTSGSGDYSDYDDAIYLTTVDTPAISDNYIPGDTERKMEGEKKNTMLDNEIIPDKASPVEANLSNKISMASTANSSIFERTEVLTALIAGGAVGLLFAVFLILLLVYRMKKKDEGSYDLGKKPIYKKAPTNEFYA

Cell surface proteoglycan that bears heparan sulfate. Regulates exosome biogenesis in concert with SDCBP and PDCD6IP. Interacts with SDOS. Belongs to the syndecan proteoglycan family.

A8JGF7

MKRNKLPGGDKYTEIKAKLRELKLSTVCEEARCPNLGECWGGGDGHTATATIMLMGDTCTRGCKFCAVKTSKAPPPLDPHEPENVSKAIAAWGLDYVVLTSVDRDDLPDGGAAHIASTIRLLKQKTEGRLLVEALVPDFQGDMGGVQTIVEAGLDVYAHNIETVERLQGQVRDRRAGWAQSLATLSAAKRVSGGRLLTKSSIMLGCGESREEVVDTLKALRANGVDVVTLGQYMRPTKKHMAVAEFVTPEAFAAYEQIAKDLGFLYVASGPMVRSSYRAGELYITNVLKGRRGGEGEGGEGQQQQQGQQQQQARAATA

Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin] Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. Belongs to the radical SAM superfamily. Lipoyl synthase family.

B5X7E4

MDDHLKLGDSGVVKNVARLGRRGQRARQAAEQTSLEEPRHVRKSSSSTSMGEGPPPKPARRQGGWAEETSGSAKSGRRPAMVQDVEDRRLRPQTPQGSDGEGDIPVIPDLDEVQEEDLNMQVAAPPSIQVNRVMTYRDLDNDLMKYSAFRTLDGEIDLKLLTKVLAPEQEVREEDVGWDWDHLFTEVSSELLTEWDQGEKEEQVCVMRTSLPKMG

Component of IFT complex A (IFT-A) involved in retrograde ciliary transport along microtubules from the ciliary tip to the base. Component of IFT complex A. Belongs to the IFT43 family.

Q1LTB4

MARYLGPKLKMSRRENIDLFLKSGVRAIDSKCKIEQPPGQHGARKPRLSDYGLQLREKQKVRRIYGILERQFRNYYQEAARLKGNTGESLLQLLESRLDNVVYRMGFGATRAESRQLVSHKAIMVNNHIVNIASYQVAINDKISIRDKAKKQSRIRASLELAEQREKPTWLEVDIVKMEGIFKKIPERIHLSAHINEHMIVELYSK

One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. With S5 and S12 plays an important role in translational accuracy. Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity. Belongs to the universal ribosomal protein uS4 family.

U6C6D6

MVGPGPTASAAAEERWQKLQEYLAAKGKLKDPNAKPYLKAKNICPKPPPSKYTPGPKKDVSNHVLPSKTTRPINIKFQTKPASITASQKPESKPPKLPSRGLTSRCFSSNTDCKQSSKPQQQPRAVSFTAGLSRNPRQCPDIQELKTKQQQQAHGGNAKCTHPETNTHAAKQPVDGFPDETNKENLPQALPKPEKPDPELHSIRKPNTGSSNQTQKGLAPKQILSKSSVTQTALKDRANKQFIRNTQIRTQAVKSRPRPTVADSTRPREKPPQTAPSHSVPAHNKTQTSKKPMTKNTQDITVNRVRYGKPNETKIESCPATEQKVKHTKPSSQLNVLQGGHNSRHPNMRQDQKPVQPHLGPQTSCVLQKSRAISQRPNLTARNFNSVIPSTPNMRANKTLNNKYNNIFQQKAQTLDSKFRKFPPQSHFLNKTAPRTQASTAAASRKGAPSATQTHPHGKKPEGEDRRKQLEEWQKSKGKTYKRPPMKFKTKRKVIEEMNTSFWKSIEREEEEKKAQLELSKKIDSTLTECLRLIEEGVLPNEIFTIVSSIPEAEKFAKFWVCKAKLLASKGTFDAIGLYEEAIQNGATPVQELQEVLNVLQDPCRSTEAVTSDTSAAGTNTTSAEELAKEESEQPCPSLTEMEPIAAAAPRIPVSEWDNHGIKLQVAPIPRICGMPEVQDMKLITPVRRSARIERTVARYPEMLQEHDVVVASLNELLEVDKTECFIFRENEALPVTLGFEVLES

Microtubule-associated protein required for mitotic spindle formation and cell-cycle progression in neural progenitor cells. Uniformly distributed along each microtubule bundle of spindles in addition to centrioles during mitosis, expression promptly diminishes at interphase. Highly expressed in regions of active neurogenesis and neural stem/progenitor cells (NSPCs), both embryonic and adult, not detected in lung, liver, kidney, heart, and skeletal muscle. At 10.5 dpc, strongly expressed in the neural progenitor cells throughout the neural tube and in the myotome. Expression is significantly lower in connective tissues compared to neural tube, but can be detected at the mitotic spindles of dividing mesenchymal cells loosely distributed in the developing limb bud. In an 12.5 dpc forelimb bud, detected in the dividing cells at the boundary region between protruding cartilage and surrounding mesenchyme (at protein level). The KEN box is required for the association with the APC/C-Cdh1 complex, ubiquitination and degradation. Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C). Belongs to the CKAP2 family.

Q1R4J1

MFYPDPFDVIIIGGGHAGTEAAMAAARMGQQTLLLTHNIDTLGQMSCNPAIGGIGKGHLVKEVDALGGLMAKAIDQAGIQFRILNASKGPAVRATRAQADRVLYRQAVRTALENQPNLMIFQQAVEDLIVENDRVVGAVTQMGLKFRAKAVVLTVGTFLDGKIHIGLDNYSGGRAGDPPSIPLSRRLRELPLRVGRLKTGTPPRIDARTIDFSVLAQQHGDNPMPVFSFMGNASQHPQQVPCYITHTNEKTHDVIRSNLDRSPMYAGVIEGVGPRYCPSIEDKVMRFAERNQHQIFLEPEGLTSNEIYPNGISTSLPFDVQMQIVRSMQGMENAKIVRPGYAIEYDFFDPRDLKPTLESKFIQGLFFAGQINGTTGYEEAAAQGLLAGLNAARLSADKEGWAPARSQAYLGVLVDDLCTLGTKEPYRMFTSRAEYRLMLREDNADLRLTEIGRELGLVDDERWARFNEKLENIERERQRLKSTWVTPSAEAAAEVNAHLTAPLSREASGEDLLRRPEMTYEKLTTLTPFAPALTDEQAAEQVEIQVKYEGYIARQQDEIEKQLRNENTLLPATLDYRQVSGLSNEVIAKLNDHKPASIGQASRISGVTPAAISILLVWLKKQGMLRRSA

NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. Homodimer. Heterotetramer of two MnmE and two MnmG subunits. Belongs to the MnmG family.

O51745

MKIGRDELVFETGFMAKQANGSVLATYGGSSVLATVCCSSNVREDLDFVPLSVEYNEKYYAAGKIPGGFIKREGKPKDKEILVSRLIDRPMRPLFDKRFGREIQVIPTTLATDQLNPPDIVGMNAAFTAVFLSDIPFNGPIAAVRMVYLNGKFIVNPSFEEIHDSDLDIVVAGSLNGITMVEGGANEVGEDILLSAIDGAHEYIKQICNAQKEFLDIVGKKEKLPLAFEEKIFEFKDELRDFVYADLKEACFVKGKLNRDKAITLLRNKSYEYFSSLEKLTDSNESLFHKAFDDFEKEIVRSSILNDNIRTDGRTPNEIRDIISEVDILSRTHGSALFTRGETQALAVTTLGTSIDEQIMDDIDGDKRLNFMLHYNFPPFSVGETGRLMTGRREIGHGHLAQRALESMVPGKNDFPYTIRVVSEVLESNGSSSMATVCAGSMSLMSAGVPVKGQVAGIAMGLISEGDKYVVLSDILGEEDHLGDMDFKVAGTKNGITGFQMDIKIENVTKDLMRDALEQARIGRIHILSIMNTVISNSRVGISKYAPKIVQLQIDIDKISLVIGSTGKTVKAITDEFEVKVQIEQNGKIILFGDDDFKMQKAKERIESIVREPKVGEIYEGTVKKINSFGAFIELTPAKEGFLSTRLKPRDSKYGSGRFGNSNRYSRFGGGGENIRGNAGLVRPPKLEEGQRIKVKIIDIDKFGKIDLEIVRDKDY

Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n) Belongs to the polyribonucleotide nucleotidyltransferase family.

B7HLL7

MSQSLIVALDFPGKQDVEQFLRHFEGEELFVKVGMELFYKEGPAIITYLKEKGHKIFLDLKLHDIPNTVKSAMRSLASLDVDMVNVHAAGGSSMMKAAIEGLEEGKQEGKERPICIAVTQLTSTSEAMMKKEIGIEKTLEEAVAHYAKLTKESGLDGVVCSTLEVPKLREVCGDEFVTVTPGIRLASDDVNDQVRVATPKRARELGSSYIVVGRSITKAENPLEAYKTVKQQWEGVTV

Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). H(+) + orotidine 5'-phosphate = CO2 + UMP Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. Homodimer. Belongs to the OMP decarboxylase family. Type 1 subfamily.

A1ADR7

MTNYRVESSSGRAARKMRLALMGPAFIAAIGYIDPGNFATNIQAGASFGYQLLWVVVWANLMAMLIQILSAKLGIATGKNLAEQIRDHYPRPVVWFYWVQAEIIAMATDLAEFIGAAIGFKLILGVSLLQGAVLTGIATFLILMLQRRGQKPLEKVIGGLLLFVAAAYIVELIFSQPNLAQLGKGMVIPSLPTSEAVFLAAGVLGATIMPHVIYLHSSLTQHLHGGSRQQRYSATKWDVAIAMTIAGFVNLAMMATAAAAFHFSGHTGVADLDEAYLTLQPLLSHAAATVFGLSLVAAGLSSTVVGTLAGQVVMQGFIRFHIPLWVRRTVTMLPSFIVILMGLDPTRILVMSQVLLSFGIALALVPLLIFTSDSKLMGDLVNSKRVKQTGWVIVVLVVALNIWLLVGTALGL

H(+)-stimulated, divalent metal cation uptake system. Belongs to the NRAMP family.

P95368

MTALPRYAVFGNPVAHSKSPQIHRQFALQEGVEIEYGRICADIGSFAQAVSTFFGTGGCGANVTVPFKQEAFDLADEHSERASAAGAVNTLILLENGKLRGDNTDGLGLVGDIVKVQNTEVEGKNILLLGAGGAVRGVIPVLLAQNPARIVIANRTRAKAEEVAARFGIEAVPMADLNGGFDIIINGTSGGLNGQIPDIPPDIFQNCALAYDMVYGEAAKPFLDFARQSGAKQTADGLGMLVGQAAASYALWRGFKPDIRPVIEYMKAL

Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. Homodimer. Belongs to the shikimate dehydrogenase family.

Q18B41

MKIVIDGMGGDNAPKSNVEGAVNAIKEYQVDLIITGDKDLLEKEFSNYEFDRNKLEIVHTTEIIENEDKPVKAIRSKKDSSMVVALNLVKEGKADAIISAGNTGALLAGGLFVVGRIKGIDRPCLCSAIPNVKRGMTLIADCGANADCKPKNLVEFAAMSNIYSRKVLGLENPKVALANVGLEEGKGNDLVKRSYEEIKKLDLNFIGNVEAREVINAYTDIIICDGFTGNILLKSAEGVALSVMSLIKETFMASTKSKIGALLIKDDLRKLKSFIDYSEYGGAPLLGLNGGVIKAHGSSDAKAIKNAINQGIKFSKGKVVEDINQFISKYNEENKNNEDE

Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP] Lipid metabolism; phospholipid metabolism. Homodimer. Probably interacts with PlsY. Associated with the membrane possibly through PlsY. Belongs to the PlsX family.

C1C871

MSKKLTFQEIILTLQQFWNDQGCMLMQAYDNEKGAGTMSPYTFLRAIGPEPWNAAYVEPSRRPADGRYGENPNRLYQHHQFQVVMKPSPSNIQELYLESLEKLGINPLEHDIRFVEDNWENPSTGSAGLGWEVWLDGMEITQFTYFQQVGGLATGPVTAEVTYGLERLASYIQEVDSVYDIEWADGVKYGEIFIQPEYEHSKYSFEISDQEMLLENFDKFEKEAGRALEEGLVHPAYDYVLKCSHTFNLLDARGAVSVTERAGYIARIRNLARVVAKTFVAERKRLGYPLLDEETRVKLLAEDAE

ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly) Tetramer of two alpha and two beta subunits. Belongs to the class-II aminoacyl-tRNA synthetase family.

Q9CG91

MLTKRIIPCLDIKNGKVVKGINFVGLREIGDPVELAKIYEEQCADEIVFLDITASFEEREIIGELIGRAARELSIPLTVGGGIRSIDDFRRILARGADKVSVNSAAIENPELIRQAANEFGVQCVVVAIDAKKRADHRGYDVYIKGGRENAGLDLVDWAKKCERLGAGEILLTSMDKDGTKTGYDLEMLNDVCTAVNIPVVASGGCGKISDIVEVFQNTRSDAALFASLFHYGEATVDEVKDELIKNNIPARIIKKETL

IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit (By similarity). 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. Heterodimer of HisH and HisF. Belongs to the HisA/HisF family. The histidine biosynthesis pathway is not functional in the dairy strain IL1403.

A2S2B3

MSASAVNVTPGRNVVVVGTQWGDEGKGKIVDWLTDHAQGVVRFQGGHNAGHTLIIGGKKTILRLIPSGIMREGVACYIGNGVVLSPEALFKEIGELEEAGLSVRERLFISEATTLILPYHIAIDQAREARRGAGKIGTTGRGIGPAYEDKVGRRALRVQDLFDARTFADRLRENLDFHNFVLTQYLGGAAVDFQATLDTMLGYADRLKPMVTDVSRRLYEENHAGRNLLFEGAQGTLLDIDHGTYPFVTSSNCVAGAAAAGAGVGPQKLDYILGITKAYCTRVGSGPFPSELYDADNPSRQDQIGITLANVGKEFGSVTGRPRRTGWLDAAALRRSIQINGVSGLCMTKLDVLDGLDEVKLCVGYKIDGEDVDLLPRGAAEVARCEPVYETFGGWKESTVGIDSWDALPANARAYLTRVQEVAGVPIDMVSTGPDRDETILLRHPFKV

Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate Binds 1 Mg(2+) ion per subunit. Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. Homodimer. Belongs to the adenylosuccinate synthetase family.

Q9YI20

MIQVLLVTICLAAFPYQGSSIILESGNVNDYEVVYPRKVTALPKGAVQPKYEDAMQYEFKVNGEPVVLHLGKNKQLFSKDYSETHYSPDGREITTNPPVEDHCYYHGRIENDADSTRSISACNGLKGHFKLQGETYLIEPLKLSDSEAHAVYKYENILKEDEAPKMCGVTQNWESYEPIKKASQLNLTPEQQRYNPFRFVELVLVADKGMVTKNNGDLNKIKTRMYELANNLNDIYRYMYIHVALVGVEIWSDGDKITVTPNVDDTLSSFAEWRKTHLLTRKKHDNAQLLTAIDFNGPTIGYAYIASMCHPKRSVGIVQDYSPINLVLSVVMAHEMGHNLGIHHDHSYCSCGDYACIMGATISHEPSTFFSNCSYIQCWDFIMDHNPECIVNEPLGTDIVSPPVCGNELLEVGEECDCGTPENCQNECCDAATCKLKSGSQCGHGDCCEQCKFSKSGTECRESMSECDPAEHCTGQSSECPADVFHKNGQPCLHNYGYCYNGNCPIMYHQCYALWGADVYEAEDSCFESNKKGNYYGYCRKENGKKIPCAPEDVKCGRLYCKDNSPGQNNPCKMFYSNEDEHKGMVLPGTKCGDGKVCSNGHCVDVATAY

Shows weak hemorrhagic activity. Rapidly degrades the alpha-chain of fibrinogen (FGA). Binds 1 zinc ion per subunit. Inhibited by chelating agents. Calcium ions enhance its activity, they also suppress autoproteolysis, and contribute to the stability of the enzyme against pH, heating, urea and cysteine. Optimum pH is 6.8 in the absence of calcium ions. Optimum pH is 5.6-8.5 in the presence of calcium ions. The activity is markedly reduced above 40 degrees Celsius. Calcium ions increases the thermal stability by 10 degrees Celsius. Monomer. Expressed by the venom gland. In the absence of calcium ions, is autocatalytically degraded giving 29 (p29K) and 45 kDa (p45K) fragments. In presence of calcium ions, the p45K is not detected (PubMed:10920250). The metalloproteinase domain which is released from the cleavage of the disintegrin bothropasin may be unstable. The disintegrin domain belongs to the long disintegrin subfamily. Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIIb sub-subfamily.

Q5LXP1

MGFTDETVRFNLNDGDKDEISNTLTNVYRSLAEKGYNPINQIVGYVLSGDPAYVPRYNDARNQIRKYERDEIVEELVRYYLKGNGTDL

Belongs to the UPF0297 family.

Q6AYH6

MVAAGAGVTQLLVLLLMVAAVPSRARGSGCRVGAAARGVGADGHEAEGCGTVALLLEHSFEIGDGANFQKRGSLLWNQQDGTLSATQRQLSEEERGRLRDVAAVNGLYRVRVPRRPGTLDGSEAGGHVSSFVPACSLVESHLSDQLTLHVDVAGNVVGLSVVVYPGGCRGSEVEDEDLELFNTSVHLRPPGTAPGPETAAFIERLEMEQAQKAKNPQEQKSFFAKYWMYIIPVVLFLMMSGAPDAGGQGGGGGGGSSR

Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes. Promotes angiogenesis and tissue repair in the heart after myocardial infarction. Stimulates cardiac endothelial cell migration and outgrowth via the activation of p38 MAPK, PAK and MAPK2 signaling pathways. Component of the ER membrane protein complex (EMC). Broadly expressed, with highest levels in pancreatic islets, testis and bladder. Present in the islets of Langerhans (at protein level). By glucose in pancreatic islets. Belongs to the EMC10 family.

B1X023

MVSTTSLKTTKSEDIFAAAQKLMPGGVSSPVRAFKSVGGQPIVFDHVKGAYIWDVDGNQYIDYVGTWGPAICGHAHPEVIAALHDALDRGTSFGAPCLLENVLAEMVIDAVPSIEMVRFVNSGTEACMSVLRLMRAFTGRDKIIKFQGCYHGHADMFLVQAGSGVATLGLPDSPGVPKTTTANTLTAPYNDLEAVKALFAENPDEIAGVILEPVVGNSGFVVPDGGFLQGLRELTNEYGALLVFDEVMTGFRLSYGGAQEKFGVTPDLTTLGKVIGGGLPVGAYGGRKDIMSMVAPAGPMYQAGTLSGNPLAMTAGIKTLELLQKPGTYNQLEQITQQLSEGLLKIAKEAGHQVCGGYIGAMFGLFFTEGPVRNYDDAKKSDLAKFGRFHRGMLEKGVYLAPSQFEAGFTSLAHTSEDIEKTLAAAKDVLSNL

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. Porphyrin-containing compound metabolism; chlorophyll biosynthesis. Homodimer. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.

P34355

MPLNKLIQDGDNQDLTDERFKATFDTDALAAVFHGGEDALKRIRELRDEVTKRWHLFDALPGAHRTRAERMEDVSRKLKNLMESVGEFADFTNNLDMLVIIRDVMGIEGFPLALHNLMFVPTIQNQADDEQTEWWLMDALQGKIIGTYAQTELGHGTNLGAIETTATYDKLTEEFIIHTPTTTATKWWPGGLGTSCTHVVLVANLIIDTKNYGLHPFFVPIRDRNSYSVMSGVRVGDIGTKMGVNCVDNGFLAFDNYRIPRRNMLMKHSKVSKEGLYTAPSHPKVGYTTMLYMRSEMIYHQAYYLAMAMAISIRYSAVRRQGEIKPGTQEVQILDYQTQQYRIFPGLARCFAFNTAAATVRQMTENCIKQLSHGNSDVLADLHALSCGLKAVVTHQASQSIDQARQACGGHGYSDASYLPTLYTCSVGACTYEGENMVMLLQLSKYLMKAAAKAEKGEEMAPLVAYLVKPDITETNDKFAKMLSHFEHIARHRVMHAYRQMIEEEKQGIERDYAFANHSVDWTKAARAHTKLFIARGFVKSVQEVSDEAVHDVLTTLAELYLSYELIEMSADLTANGYLSESDVQQIRHQIYDSMRKTRRNAVSIVDSFDICDRELRSVLGRRDGHVYENLYKWAQMSPLNERNLPHVEKYLKPMTSKL

Involved in the first step of peroxisomal beta-oxidation by catalyzing the desaturation of fatty acid-derived side chains. Activated by ATP (By similarity). ATP binding leads to a conformational change that promotes FAD cofactor binding and enzyme activity (By similarity). ATP binding likely occurs during acox-1.5 folding and/or dimer formation (By similarity). Lipid metabolism; peroxisomal fatty acid beta-oxidation. Homodimer. Belongs to the acyl-CoA oxidase family.

P60999

MKDLTLNDLPIREELRGQSAYGAPQLDVDVRLNTNENPYPPSEALVEELARVVAEQASNLNRYPERDAVELRTELARYITKCTGVPVTYEQLWAANGSNEVLQQLLQAFGGPGRTVLGFQPSYSMHPILAQGTQTTFINCPRDKEFRIDVDAALAAITTHQPNIVFVTTPNNPTGDVTSLDTIKKILDVAPGIVIVDEAYAEFSEQPSAISLLENYPTKLVVSRTMSKAFDFAGGRLGYFVAHKAFIDAVMLVRLPYHLSQLSQAAAIVALRHSEETLATVAKLVAERKRVQQGLLELGFEIVPSESNFLFFGHFEDQHAAWQAFLDRKVLIRDVSVSGYLRATVGLPEENDAFLNAAREVAQQFL

2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. Homodimer. Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.

Q02T66

MSMQDPLADMLTRIRNAQMAEKTVVSMPSSKLKAAVAKVLKDEGYIADFQISSEVKPQLSIELKYFEGKPVIEEVKRISRPGLRQYKSVEQLPKVRGGLGVSIVSTNKGVMTDRAARAAGVGGEVLCTVF

One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. Part of the 30S ribosomal subunit. Contacts proteins S5 and S12. Belongs to the universal ribosomal protein uS8 family.

Q6GED9

MSKINDINDLVNATFQVKKFFRDTKKKFNLNYEEIYILNHILRSESNEISSKEIAKCSEFKPYYLTKALQKLKDLKLLSKKRSLQDERTVIVYVTDTQKANIQKLISELEEYIKN

Negative regulator of sarA transcription at late exponential and stationary growth phases. It contributes to the modulation of target genes downstream of the sarA regulatory cascade. Also, positively regulates expression of primary transcripts RNAII and RNAIII generated by agr (virulence accessory gene regulator) locus (By similarity). Homodimer. Belongs to the SarA family.

Q5PH16

MQKYTSEARQLLALAIPVILAQVAQTAMGFVDTVMAGGYSATDMAAVAIGTSIWLPAILFGHGLLLALTPVIAQLNGSGRRERIAHQVRQGFWLAGFVSVLVMIVLWNAGYIIRSMHNIDPALADKAVGYLRALLWGAPGYLFFQVARNQCEGLAKTKPGMVMGFLGLLVNIPVNYIFIYGHFGMPELGGIGCGVATAAVYWVMFIAMLSYIKHARSMRDIRNEKGFGKPDSVVMKRLIQLGLPIALALFFEVTLFAVVALLVSPLGIVDVAGHQIALNFSSLMFVLPMSLAAAVTIRVGYRLGQGSTLDAQTAARTGLGVGICMAVVTAIFTVTLRKHIALLYNDNPEVVALAAQLMLLAAVYQISDSIQIIGSGILRGYKDTRSIFFITFTAYWVLGLPSGYILALTDLVVDRMGPAGFWMGFIIGLTSAAVLMMLRMRYLQRQPSAIILQRAAR

Multidrug efflux pump that functions probably as a Na(+)/drug antiporter. Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family. MdtK subfamily.

A7Z5N6

MKSFYHYLMKYRHPKPQDAISQFANQAYEDHGFPKTSSDYHELSSYLELSADYLETMATFDEAWEKYETEVHHA

Belongs to the UPF0346 family.

A5ISM8

MKIIHTADWHLGKILNGKQLLEDQAYILDMFVEKMKEEEPDIIVIAGDLYDTTYPSKDAIMLLEQAIGKLNLELRIPIIMISGNHDGKERLNYGASWFEHNQLFIRTDFTSINSPIEINGVNFYTLPYATVSEMKHYFEDDTIETHQQGITRCIETIAPEIDEDAVNILISHLTVQGGKTSDSERPLTIGTVESVQKGVFDIFDYVMLGHLHHPFSIEDDKIKYSGSLLQYSFSEAGQAKGYRRLTINDGIINDVFIPLKPLRQLEIISGEYNDVINEKVHVKNKDNYLHFKLKNMSHITDPMMSLKQIYPNTLALTNETFNYNEENNAIEISEKDDMSIIEMFYKHITDKELSDIQSKKIKNILENELRKED

SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity (By similarity). Heterodimer of SbcC and SbcD. Belongs to the SbcD family.

Q9Z616

MSYRSFSFLPNIDQNSVFSNRFNQIDKIFSTLTGEKPLSDTPAYNLFQIDEHKYELILSIPGYEEKELDISVHNSQLTVQGKKQNQENDDKKIKKYLHKGIIFNDFSLNFNFDHKIQVKKAELFSGLLKINFECRVPDEEKPKKIFINIPNKVKEIEKNKI

Belongs to the small heat shock protein (HSP20) family.

Q1JIJ4

MTVTGIIAEFNPFHNGHKYLLETAEGLKIIAMSGNFMQRGEPALIDKWIRSEMALKNGADIVVELPFFVSVQSADYFAQGAIDILCQLGIQQLAFGTEDVIDYQKLIKVYEKKSKQMTAYLSTLEDTLSYPQKTQKMWEIFAGVKFSGQTPNHILGLSYAKASAGKHIQLCPIKRQGAAYHSKDKNHLLASASAIRQHLNDWDFISHSVPNAGLLINNPHMSWDHYFSFLKYQILNHSDLTSIFQVNDELASRIKKAIKVSQNIDHLVDTVATKRYTKARVRRILTYILVNAKEPTLPKGIHILGFTSKGQAHLKKLKKSRPLITRIGAETWDEMTQKADSIYQLGHQDIPEQSFGRIPIIIKNERLN

Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34. acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP + diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met) Belongs to the TmcAL family.

Q8MKJ3

MADYHNNYKKNDELEFVRTGYGKDMVKVLHIQRDGKYHSIKEVATSVQLTLSSKKDYLHGDNSDIIPTDTIKNTVHVLAKFKGIKSIEAFGVNICEYFLSSFNHVIRAQVYVEEIPWKRLEKNGVKHVHAFIHTPTGTHFCEVEQLRSGPPVIHSGTKDLKVLKTTQSGFEGFIKDQFTTLPEVKDRCFATQVYCKWRYHQCRDVDFEATWGTIRDLVLEKFAGPYDKGEYSPSVQKTLYDIQVLSLSRVPEIEDMEISLPNIHYFNIDMSKMGLINKEEVLLPLDNPYGKITGTVKRKLSSRL

Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. H2O + O2 + urate = 5-hydroxyisourate + H2O2 Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3. Belongs to the uricase family.

Q6D0C7

MKDLSIRIAVVGAGGRMGRQLIQAIEQMDGVVLGAALERSGSSLLGSDAGELAGLGKNGITVNESLDAVQNDFDILIDFTRPEGTLAHLAFCRLHRKGMIIGTTGFDDAGKAAIKQAAQDIGIVFAANFSVGVNVMLKLLEKAAKVMGDYTDIEIIEAHHRHKVDAPSGTALAMGEVIADALGRDLKSCAVYTREGHTGERDPKSIGFATVRAGDIVGEHTAMFADIGERVEITHKASSRMTFANGAVRAAIWISSKESGIFDMRDVLSLDDL

Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. Homotetramer. Belongs to the DapB family. Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.

B7GKG6

MRNEMHLQFSALSQNESFARVTVAAFVAQLDPTLDELTEIKTVVSEAVTNAIIHGYENDPSGVVYISVIIEGHTVHLTIRDHGKGIENVEEARQPLFTTKPELERSGMGFTIMENFMDEVNIYSKVNEGTTVELIKHLTKSKALCN

Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Belongs to the anti-sigma-factor family.

Q2ST23

MSEHLIVKNKKAYFNYEIIQTYQAGIVLNGPEIKSIRNHDVSINEAFVLIRKKEIYILNMNVKKYQFANYIKGLEETRTRKLLLHKKEIIKILNKIKQENLTIIPIKLYFKNDYVKLEIALAKGKKLHDKRQTIKKRDTERKELRDYK

Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation. The tmRNA-SmpB complex associates with stalled 70S ribosomes. Belongs to the SmpB family.

Q14A44

MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAGLTADARVVISRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGIPRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAISNDKEAIKLAIKALLEVVQSGGKNIELAIIRRDQPLKMFSAKEIELEVSEIEREKDEAEKTKSKKST

Component of the spermatoproteasome, a proteasome specifically found in testis that promotes acetylation-dependent degradation of histones, thereby participating actively to the exchange of histones during spermatogenesis (PubMed:23706739, PubMed:31358751, PubMed:31437213). The proteasome is a protein complex that degrades unneeded or damaged proteins by proteolysis, a chemical reaction that breaks peptide bonds (Probable). Required for 20S core proteasome assembly, essential for the degradation of meiotic proteins RAD51 and RPA1 at late prophase I and the progression of meiosis I during spermatogenesis (PubMed:31358751). Localizes to the synaptonemal complex, a 'zipper'-like structure that holds homologous chromosome pairs in synapsis during meiotic prophase I (PubMed:31437213). Component of the outer alpha-ring of the 20S proteasome core which is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure (PubMed:23706739, PubMed:31358751). The catalytic chamber with the active sites is on the inside of the barrel (Probable). Interacts with canonical subunits of the spermatoproteasome, including proteasome activators PSME4 (also called PA200) and PSME3 (also called PA28-gamma) (PubMed:31437213). Interacts with proteasome-interacting proteins chaperones including CCT6B and CCT2, ubiquitin ligases (TRIP12, NEDD4, TRIM36 and RAD18), and ubiquitin specific proteases such as USP9X, USP34, USP5 and USP47 (PubMed:31437213). Interacts with meiotic proteins cyclin dependent kinase CDK1 and the ATPase TRIP13 as well as proteins of the synaptonemal complex SIX6OS1 and SYCE3 (PubMed:31437213). Localizes to the central region of the synaptonemal complex. In testes, expressed in spermatocytes at the pachytene stage (weakly in early pachynema and strongly in late pachynema), and its expression persisted thereafter throughout spermatogenesis. Knockout mice were obtained according to the expected Mendelian ratios and showed no obvious phenotypes with respect to viability and development; however males show infertility (PubMed:31358751, PubMed:31437213). PSMA8-null spermatocytes exhibit delayed M-phase entry and are finally arrested at this stage, resulting in male infertility (PubMed:31358751, PubMed:31437213). Belongs to the peptidase T1A family. Predicted to have endopeptidase activity (By similarity). However, as it is located in the outer alpha-ring, it is suggested to lack catalytic activity and preferentially interact with regulatory complexes such as PSME4/PA200.

A0A144A3J2

MSYNDGSEEENDSNTYIHDEKKKKKKKNNKNAYALINEVNYSQEDEQEVIHNTNSEDETSNRKGNGCVYSLSDQNVEDHIISLPEYLDLINNNNNNSNSYKMKKEKKKKKKKKKNQTDEENMKNKKDHIYQNNITNQQNDIKNDYKKINHHNMNNKKNKIFCQDDQNIFNINHTFQIHETVQNNLIIPPSETCLASDIIQPSDTTQSNTYLNEATASQNDDNNNEDSSNEMGMFKKIFYRIKKIIVDKKGTPITNENDVDNDMCELNVMENNMNNIHSNNNNISTHMDDVIEDESNEEVFVINRNTDGYINTRENINVSTHVTRQMINLSELNPNDLLCNVSEYEEGQNINSLWNDNNNNNNNNNNNFLVGSLNALHPINHNLRNENIHNDNINNTHINYDNNNSYESPIHILSFSFKNIYNKISSYINEHITHIKEKIKKYWLERVQEANTQLNSPRPVHTRNTTNINTNININEDENDDPSCVQILFFMGLICKFPILWIIGSIVFCITPSEHRKTKTWSLVNTFFALLSIIYFITTTNFRLRKPTFFVILEQNVENKNTYPKGILKYNNMIHHKHIIIDQSSLHKWKDLHTNKVYKTSENYFLNRNFLSSQKPDSNILLSDTIYKLLNRIQVTVTFGKGNIYSSDNIEKIKPFFQNLRINMDPISYDKLTMTDEDIPDDFFGSGLRCERTYNNHNQNINEPQQNKEKEKWYLFWKEEEINNSHNKNIYNISIPVGEIFFFKSEYNCRIAFLYPKSILYDQNDIPSNFVEIQKIIIKPF

Possible candidate for an effective malaria vaccine as determined by epitope response in sera.

A1QZH4

MSRKSKKIKKKVFKDSKYDSQVIAKFVNRMMYDGKKSISEAIVYNSIDLLAEKTEEVDKVAAFSKALDNVKPLVEVRSRRVGGATYQVPVEVREERREALAMKWIIAAARKASGKSMQEKLGNELVNSYNSTGVAFKKREDTHRMAEANRAFTHYRW

One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA. Part of the 30S ribosomal subunit. Contacts proteins S9 and S11. Belongs to the universal ribosomal protein uS7 family.

Q87E80

MNSSCEKIFGVLRSPRVSEKSSRLQEISNVYVFEVSSDATKIDVKNAVERLFDVKVGVVRVLNVKGKSKSFRNRGGSRSGWRKAYVRLIDGQSIDVASSV

One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome. Part of the 50S ribosomal subunit. Contacts protein L29, and trigger factor when it is bound to the ribosome. Belongs to the universal ribosomal protein uL23 family.

Q4L7Z5

MQELKTLLDELKSQSFFNENEICVIGCSTSEVIGQKIGSVGSMEVAEAIFNALEEVKQDTGVSFAFQGCEHINRAVTIEREDFNPLTMEEVTVVPDVHAGGSLATYAYKHMNDPIVVEHISVPKGIDIGQTLIGMHIKHICVPVRTSVKQVGEAIVTIATSRPKKIGGERAKYE

Belongs to the UPF0340 family.

P36842

MSVTTQQPAVVPLPSSPRLPIESHAGPRSTQLPPSPPETVNGDDPKSITSTPAEPDFPLPPPANPKPQVLDIDKPTPDAHVPRDPRLIRLTGVHPFNTEPPLTDLYNEGFLTSPELFYVRNHGAVPEVQDEECLDWEFSIEGMVANPLKITLRQLLEEYENVTYPVTLVCAGNRRKEQNVVRKSKGFAWGAAGVSTALFTGVVMKDVIERAKPLRKAKYVCMEGADKLPNGYYGTSVKLNWVMDPNRGIMLAHKMNGENLSLDHGKPLRAVVPGQIGGRSVKWLKKLIVTAEPSDNWYHIYDNRVLPTMVDPDEAAKNPKWWMDERYAIYDLSPNSAIAFPAHEEKVVLASAENSYNVRGYAYSGGGRRITRCEVSLNKGKNWRLANIDYAEDKYRDFEGRELFGARLDMDWRETSFCWCFWNLDIATAELRDANDILVRAMDEAMCIQPRDMYWSVLGMMNNPWYRITIHHEGDVLRFEHPTQPALIPGGWMERVKKAGGNLTNGQWGEQIEGQELENTAVEEVKEIKMTKDGVNRIVELDELKWHESAEYPWFVVNDEVYDGTSFLEGHPGGAQSIISAAGLDASDEFMAIHSETAKAMMPAYHIGTLSPTASKQLSLEEPTSKQASSSSLRPTFLDSRTWSKALLSSKTKVSWDTRIFRFKLDHASQTLGLPTGQHLMIRLRDPVTREAIIRSYTPISQISEQGFCDVLIKIYADAPGREGGKMTKALDSIPCGHWVDMKGPIGKFEYLGKGVCSINGNERRVRSMKMICGGSGITPIYQVLRAILQDSADSTHCTVLNGNRLEEDILCREDLDRFAEENGERCTLVHTLTQAAEGWTGRRGRIGEELLKEFCGTEEDGLVLVCGPEGLERSVKGLLSGMAWRDDDVIFF

Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria. H2O + NADP(+) + nitrite = H(+) + NADPH + nitrate Binds 1 FAD. Binds 1 heme group. The heme group is called cytochrome b-557. Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. Homodimer. Belongs to the nitrate reductase family.

Q9URT7

MTIPDKQLAAVFHTHGGPENVKFEEVPVAEPGQDEVLVNIKYTGVCHTDLHALQGDWPLPAKMPLIGGHEGAGVVVKVGAGVTRLKIGDRVGVKWMNSSCGNCEYCMKAEETICPHIQLSGYTVDGTFQHYCIANATHATIIPESVPLEVAAPIMCAGITCYRALKESKVGPGEWICIPGAGGGLGHLAVQYAKAMAMRVVAIDTGDDKAELVKSFGAEVFLDFKKEADMIEAVKAATNGGAHGTLVLSTSPKSYEQAAGFARPGSTMVTVSMPAGAKLGADIFWLTVKMLKICGSHVGNRIDSIEALEYVSRGLVKPYYKVQPFSTLPDVYRLMHENKIAGRIVLDLSK

a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH a secondary alcohol + NAD(+) = a ketone + H(+) + NADH Binds 2 Zn(2+) ions per subunit. Homotetramer. Belongs to the zinc-containing alcohol dehydrogenase family.

Q07015

MDDFSRDTENFVCWLKTTAEIEVSPKIEIKDLCCDNQGRAVVATQKIKKDETLFKIPRSSVLSVTTSQLIKDYPSLKDKFLNETGSWEGLIICILYEMEVLQERSRWAPYFKVWNKPSDMNALIFWDDNELQLLKPSLVLERIGKKEAKEMHERIIKSIKQIGGEFSRVATSFEFDNFAYIASIILSYSFDLEMQDSSVNENEEEETSEEELENERYLKSMIPLADMLNADTSKCNANLTYDSNCLKMVALRDIEKNEQVYNIYGEHPNSELLRRYGYVEWDGSKYDFGEVLLENIVEALKETFETNTEFLDRCIDILRNNANIQEFLEGEEIVLDSYDCYNNGELLPQLILLVQILTILCQIPGLCKLDIKAMERQVERIVKKCLQLIEGARATTNCSATWKRCIMKRLADYPIKKCVSIEKPSKGNSLTREELRDVMARRVLKSEIDSLQVCEETIDKNYKVIPDEKLLTNILKRKLTEEEKSSVKRPCVKK

S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates 60S ribosomal protein L42 (RPL42A and RPL42B) at 'Lys-55'. Present with 4010 molecules/cell in log phase SD medium. Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SETD6 subfamily.

B8D8E9

MKIYLKFKSYNKRICKLLQLFKLEHDQNCSMGLLINHNSLELYNRDNVNQKPIKVDFTSKKNHYRCHHFRRKNEVLYRVSGIKNSYFPTVLDATAGLGNDAFIFSFLGCKVIMIERHPIVAALLKDGLQRGYQDKKIGHWLQTRLHLIVNDSLKMLEIPILQPDVIYLDPMYPFYHKKSLPKKDMQFFRQLIGHNYDSKKLLEVSRKLAKNRIIVKRPYYAKPLSEDKVNHIVTTRNHRFDIYQPF

Specifically methylates the guanosine in position 1516 of 16S rRNA. guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine Belongs to the methyltransferase superfamily. RsmJ family.

Q5V6B8

MKSKYTARPEGKQSGQGLVFDSVTKRFGGKVAVRDVSLKLEAGERVAVIGPSGAGKTTLLRLAAGALQPDVGTVRFDGSSSTGSTATLAYQGETLVDRRTALSNVLTGRLGALSWLRGFIEPLLPQHPEPALERLDAVGLVGRADVPVKSLSAGERQRVAFARALMQDAEVVLADEPTANLDPSSRRNVIDVLDAALDGELLVTVLHEVDLALEHFDRIVGMADGRVRFDTPARAVTDDQLDALFAAGASTPGTDAERTGTEKESDIPVPWYV

Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system (By similarity). ATP + H2O + phosphonate(out) = ADP + H(+) + phosphate + phosphonate(in) The complex is composed of two ATP-binding proteins (PhnC), two transmembrane proteins (PhnE) and a solute-binding protein (PhnD). Belongs to the ABC transporter superfamily. Phosphonates importer (TC 3.A.1.9.1) family.

Q7RVH7

MATHNIVVFGGDHCGPEVVLEAIKVLKAIETNSPSAGKFNLQNHLLGGASIDKHNDPLTDEALNAAKAADAVLLGAIGGPEWGTSSTVRPEQGLLKLRKELGTYGNLRPCNFASESLVDSSPLKAEVCRGTDFIVVRELTGGIYFGDRTEDDGSGYACDTEPYSRAEIVRIARLAGFLALAKNPPAKVWSLDKANVLATSRLWRKTVTDVISKEFPQLQLEHQLIDSAAMLLVKNPRALNGVVITSNLFGDIISDEASVIPGSIGLLPSASLGGIPDGKGKCNGIYEPIHGSAPDISGKGIVNPVGTILSVAMMLRYSLNLPKEADAVEAAVKAAIDNGTKTKDLGGNATTSDMGNAVVAELEKILKA

Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH Binds 1 Mg(2+) or Mn(2+) ion per subunit. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4. Homodimer. Belongs to the isocitrate and isopropylmalate dehydrogenases family.

P32416

FLPLIAGLLGKLF

Shows hemolytic activity. Expressed by the skin glands.

A3MHN9

MKSTRPFHPTPVITIDGPTASGKGTVAALVAAHLGFHLLDSGALYRLAALASIRYQVEPDDADALASLVDGLHITFREGCAQLDGVDVSDEIRAEAVGNRASAIAVHASVRAALVARQRAFRKTPGLVADGRDMGTLIFPDAVLKVFLTASVEARAARRHKQLMQKGFSANIDNLLQDLRERDARDSNRAAAPLKPAADAKPLDTSALTIEQSVEQVLAWYRELGQPA

ATP + CMP = ADP + CDP ATP + dCMP = ADP + dCDP Belongs to the cytidylate kinase family. Type 1 subfamily.

A3D7J4

MTDLKKAAQRAIELMDLTTLNDDDTDQKVIYLCHKAKTAAGNTAAICIYPRFIPIARKTLDEIGAEDIQIATVTNFPHGNDDIAIAVLETRAAVAYGADEVDVVFPYRALMEGNETIGFELVKACKEACGEVLLKVIIESGVLADPALIRRASELSIDAGADFIKTSTGKVPVNATLEAAEIMLTVISEKNTQVGFKPAGGVRDAAQAAEFLGVAERILGADWVSPRTFRFGASSLLNSLLHTLELADAPKPTQGY

Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate. 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2. Belongs to the DeoC/FbaB aldolase family. DeoC type 2 subfamily.

P17333

MANKLFLVSATLAFFFLLTNASIYRTIVEVDEDDATNPAGPFRIPKCRKEFQQAQHLKACQQWLHKQAMQSGSGPSWTLDGEFDFEDDMENPQGPQQRPPLLQQCCNELHQEEPLCVCPTLKGASKAVKQQVRQQQGQQGQQLQQVISRIYQTATHLPKVCNIPQVSVCPFQKTMPGPSY

The small, basic, water-soluble napins are one of the two major kinds of storage proteins synthesized in the seed during its maturation. The mature protein consists of a small and a large chain linked by disulfide bonds. Cotyledons and the axis. Belongs to the 2S seed storage albumins family.

G0IQG1

MEFMHNLIPTVIEHTGNYERVFDIYSRLLRERIIFLSGEINDPKADTVIAQLLFLESEDSNKDIYLYLNSPGGSITAGLAIYDTMQYIKPDVRTICIGQAASMGAFLLAAGAKGKRESLTYSRIMIHQPWGGISGQASDINIQANEILRLKKLIIDIMSNQIGVDKEKLALDMERDYFMTSSDALKYGLIDNILVRE

Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs). Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes. Belongs to the peptidase S14 family. Truncated N-terminus.