ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
Q83906 | MSGTSESELKNLISSLHLNNGFLGIFDCRFPGFLQKSKIQTAIINTGPREQGGIHWITLALEPISYKLFIFDPLGWKDTQLIKFYNFSLNSLIKRSALNNSDRCITVERNTQSVQCTCAGSCGLFCIFFLYCFHFYKQNVFKSWLFQKLNGSTPSLIPCEPHLLHENQTFLYDFLNAKSVYFRKNYRTFIENTKTGLIKTH | Function: Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, pVIII, and pX) inside newly assembled particles giving rise to mature virions. Protease complexed to its cofactor slides along the viral DNA to specifically locate and cleave the viral precursors. Mature virions have a weakened organization compared to the unmature virions, thereby facilitating subsequent uncoating. Without maturation, the particle lacks infectivity and is unable to uncoat. Late in adenovirus infection, in the cytoplasm, may participate in the cytoskeleton destruction. Cleaves host cell cytoskeletal keratins K7 and K18.
Catalytic Activity: Cleaves proteins of the adenovirus and its host cell at two consensus sites: -Yaa-Xaa-Gly-Gly-|-Xaa- and -Yaa-Xaa-Gly-Xaa-|-Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino acid).
Sequence Mass (Da): 23194
Sequence Length: 201
Subcellular Location: Virion
EC: 3.4.22.39
|
P0DOI1 | MGNSPSYNPPAGISPSDWLNLLQSAQRLNPRPSPSDFTDLKNYIHWFHKTQKKPWTFTSGGPASCPPGKFGRVPLVLATLNEVLSNDEGAPGASAPEEQPPPYDPPAVLPIISEGNRNRHRAWALRELQDIKKEIENKAPGSQVWIQTLRLAILQADPTPADLEQLCQYIASPVDQTAHMTSLTAAIAAEAANTLQGFNPKMGTLTQQSAQPNAGDLRSQYQNLWLQAWKNLPTRPSVQPWSTIVQGPAESYVEFVNRLQISLADNLPDGVPKEPIIDSLSYANANKECQQILQGRGLVAAPVGQKLQACAHWAPKTKQPAILVHTPGPKMPGPRQPAPKRPPPGPCYRCLKEGHWARDCPTKTTGPPPGPCPICKDPSHWKRDCPTLKSKKLIEGGPSAPQIITPITDSLSEAELECLLSIPLARSRPSVAVYLSGPWLQPSQNQALMLVDTGAENTVLPQNWLVRDYPRTPAAVLGAGGISRNRYNWLQGPLTLALKPEGPFITIPKILVDTFDKWQILGRDVLSRLQASISIPEEVHPPVVGVLDAPPSHIGLEHLPPPPEVPQFPLN | Function: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus.
PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. The protease is autoproteolytically processed at its N- and C-termini.
Sequence Mass (Da): 62261
Sequence Length: 571
Domain: Gag polyprotein: Late-budding domains (L domains) are short sequence motifs essential for viral particle release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. Matrix protein p15 contains one L domain: a PPXY motif which binds to the WW domains of the ubiquitin ligase NEDD4.
Subcellular Location: Virion
|
P49860 | MPEIVKTLSFDETEIKFTGDGKQGIFEGYASVFNNTDSDGDIILPGAFKNALANQTRKVAMFFNHKTWELPVGKWDSLAEDEKGLYVRGQLTPGHSGAADLKAAMQHGTVEGMSVGFSVAKDDYTIIPTGRIFKNIQALREISVCTFPANEQAGIAAMKSVDGIETIRDVENWLRDSVGLTKSQAVGLIARFKSAIRSESEGDGNEAQINALLQSIKSFPSNLGK | Function: Protease involved in virion assembly and maturation.
PTM: Cleaves itself autocatalytically to yield the mature form of the protease.
Sequence Mass (Da): 24392
Sequence Length: 225
Subcellular Location: Virion
|
Q01267 | MKKHAIGIAALNALSIDDDGWCQLLPAGHFSARDGRPFDVTGGQGWFIDGEIAGRLVEGVRALNQDVLIDYEHNQLRKDKGLPPEQLVAAGWFNADEMQWREGEGLFIHPRWTAAAQQRIDDGEFGYLSAVFPYDTATGAVLQIRLAALTNDPGATGMKKLTALAADLPDILQQENKPMNETLRKLLARLGVTVPENADITDEQATAALTALDTLEINAGKVAALSAELEKAQKAAVDLTKYVPVESYNALRDELAQATAQSATASLSAVLDKAEQEGRIFKSERTYLEQLGGQIGVAALSAQLEKKQPIAALSAMQTTTAKIPSQEKTAVAVLSADEQAAVKALGITEAEYLKMKQEQEK | Function: Protease I is involved in virion assembly and maturation. Protease I cleaves the portal protein to yield mature procapsids competent for DNA packaging (Probable). Isoform scaffold protein Z probably helps the capsid proteins to assemble into a functional capsid (Probable).
PTM: The N-terminus is acetylated.
Sequence Mass (Da): 38893
Sequence Length: 361
Subcellular Location: Host cytoplasm
|
Q6QGD7 | MTQAAIDYNKLKSAPVHLDAYIKSIDSESKEGVVKIRGFANTISKDRAGDVIPASAWKTSNALTNYMKNPIILFGHDHRRPIGKCIDLNPTEMGLEIECEINESSDPAIFSLIKNGVLKTFSIGFRCLDAEWDEATDIFIIKDLELYEVSVVSVPCNQDSTFNLAKSMNGHDYTEWRKSFTAISSKAVPAQERNLSELEKLAIALGYVKE | Function: Serine protease involved in capsid assembly and maturation. Cleaves the major capsid protein, the decoration protein, the portal protein to yield mature procapsids competent for DNA packaging (Probable). Acts as a trigger for assembly of the capsid protein.
PTM: Cleaves itself autocatalytically to yield the mature form of the protease (Probable).
Sequence Mass (Da): 23379
Sequence Length: 210
Subcellular Location: Virion
EC: 3.4.21.-
|
P10274 | MGQIFSRSASPIPRPPRGLAAHHWLNFLQAAYRLEPGPSSYDFHQLKKFLKIALETPARICPINYSLLASLLPKGYPGRVNEILHILIQTQAQIPSRPAPPPPSSPTHDPPDSDPQIPPPYVEPTAPQVLPVMHPHGAPPNHRPWQMKDLQAIKQEVSQAAPGSPQFMQTIRLAVQQFDPTAKDLQDLLQYLCSSLVASLHHQQLDSLISEAETRGITGYNPLAGPLRVQANNPQQQGLRREYQQLWLAAFAALPGSAKDPSWASILQGLEEPYHAFVERLNIALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGHTNSPLGDMLRACQTWTPKDKTKVLVVQPKKPPPNQPCFRCGKAGHWSRDCTQPRPPPGPCPLCQDPTHWKRDCPRLKPTIPEPEPEEDALLLDLPADIPHPKNLHRGGGLTSPPTLQQVLPNQDPASILPVIPLDPARRPVIKAQVDTQTSHPKTIEALLDTGADMTVLPIALFSSNTPLKNTSVLGAGGQTQDHFKLTSLPVLIRLPFRTTPIVLTSCLVDTKNNWAIIGRDALQQCQGVLYLPEAKRPPVILPIQAPAVLGLEHLPRPPEISQFPLNQNASRPCNTWSGRPWRQAISNPTPGQGITQYSQLKRPMEPGDSSTTCGPLTL | Function: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus.
PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. The protease is autoproteolytically processed at its N- and C-termini.
Sequence Mass (Da): 71558
Sequence Length: 651
Domain: The capsid protein N-terminus seems to be involved in Gag-Gag interactions.
Subcellular Location: Virion
|
Q13523 | MAAAETQSLREQPEMEDANSEKSINEENGEVSEDQSQNKHSRHKKKKHKHRSKHKKHKHSSEEDKDKKHKHKHKHKKHKRKEIIDASDKEGMSPAKRTKLDDLALLEDLEKQRALIKAELDNELMEGKVQSGMGLILQGYESGSEEEGEIHEKARNGNRSSTRSSSTKGKLELVDNKITTKKRSKSRSKERTRHRSDKKKSKGGIEIVKEKTTRSKSKERKKSKSPSKRSKSQDQARKSKSPTLRRRSQEKIGKARSPTDDKVKIEDKSKSKDRKKSPIINESRSRDRGKKSRSPVDLRGKSKDRRSRSKERKSKRSETDKEKKPIKSPSKDASSGKENRSPSRRPGRSPKRRSLSPKPRDKSRRSRSPLLNDRRSKQSKSPSRTLSPGRRAKSRSLERKRREPERRRLSSPRTRPRDDILSRRERSKDASPINRWSPTRRRSRSPIRRRSRSPLRRSRSPRRRSRSPRRRDRGRRSRSRLRRRSRSRGGRRRRSRSKVKEDKFKGSLSEGMKVEQESSSDDNLEDFDVEEEDEEALIEQRRIQRQAIVQKYKYLAEDSNMSVPSEPSSPQSSTRTRSPSPDDILERVAADVKEYERENVDTFEASVKAKHNLMTVEQNNGSSQKKLLAPDMFTESDDMFAAYFDSARLRAAGIGKDFKENPNLRDNWTDAEGYYRVNIGEVLDKRYNVYGYTGQGVFSNVVRARDNARANQEVAVKIIRNNELMQKTGLKELEFLKKLNDADPDDKFHCLRLFRHFYHKQHLCLVFEPLSMNLREVLKKYGKDVGLHIKAVRSYSQQLFLALKLLKRCNILHADIKPDNILVNESKTILKLCDFGSASHVADNDITPYLVSRFYRAPEIIIGKSYDYGIDMWSVGCTLYELYTGKILFPGKTNNHMLKLAMDLKGKMPNKMIRKGVFKDQHFDQNLNFMYIEVDKVTEREKVTVMSTINPTKDLLADLIGCQRLPEDQRKKVHQLKDLLDQILMLDPAKRISINQALQHAFIQEKI | Function: Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF.
PTM: Phosphorylated by Clk1.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 116987
Sequence Length: 1007
Subcellular Location: Nucleus
EC: 2.7.11.1
|
O33071 | MNILSRIFARTPSLRTRVVVATAIGAAIPVLIVGTVVWVGITNDRKERLDRKLDEAAGFAIPFVPRGLDEIPRSPNDQDAIITVRRGNLVKSNFDITLPKLTNDYADTYLRGVRYRVRTVEIPAPEPTSIAVGATYDATVAETNNLHRRVLLICGFAIAAAAVFAWLLAAFAVRPFKQLAQQTRSVDAGGEAPRVEVHGATEAVEIAEAMRGMLQRIWNEQNRTKEALASARDFAAVSSHELRTPLTAMRTNLEVLATLDLADDQRKEVLGDVIRTQSRIEATLSALERLAQGELSTSDDHVPVDITELLDRAAHDATRSYPELKVSLVPSPTCIIVGLPAGLRLAVDNAVANAVKHGGATRVQLSAVSSRAGVEIAVDDNGSGVPEDERQVVFERFSRGSTASHSGSGLGLALVAQQAQLHGGTASLETSPLGGARLLLRISAPS | Function: Member of the two-component regulatory system PrrB/PrrA that is involved specifically in early intracellular multiplication of Mycobacterium and is essential for its viability. Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to the conserved aspartic acid residue in the regulatory domain of PrrA. In turn, PrrA binds to the upstream promoter regions of target genes including itself to positively regulate their expression.
PTM: Autophosphorylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 47796
Sequence Length: 446
Subcellular Location: Cell membrane
EC: 2.7.13.3
|
Q6J4G7 | MGKLLLILGSVIALPTFAAGGGDLDASDYTGVSFWLVTAALLASTVFFFVERDRVSAKWKTSLTVSGLVTGIAFWHYMYMRGVWIETGDSPTVFRYIDWLLTVPLLICEFYLILAAATNVAGSLFKKLLVGSLVMLVFGYMGEAGIMAAWPAFIIGCLAWVYMIYELWAGEGKSACNTASPAVQSAYNTMMYIIIFGWAIYPVGYFTGYLMGDGGSALNLNLIYNLADFVNKILFGLIIWNVAVKESSNA | Function: Light-driven proton pump.
PTM: Contains one covalently linked retinal chromophore per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27308
Sequence Length: 250
Subcellular Location: Cell membrane
|
Q66GI4 | MLRLTCFTPSFSRACCPLFAMMLKVPSVHLHHPRFSPFRFYHTSLLVKGTRDRRLILVERSRHLCTLPLAAAKQSAASPSENLSRKAKKKAIQQSPEALLKQKLDMCSKKGDVLEALRLYDEARRNGVQLSQYHYNVLLYVCSLAEAATESSPNPGLSRGFDIFKQMIVDKVVPNEATFTNGARLAVAKDDPEMAFDMVKQMKAFGIQPRLRSYGPALFGFCRKGDADKAYEVDAHMVESEVVPEEPELAALLKVSMDTKNADKVYKTLQRLRDLVRQVSKSTFDMIEEWFKSEVATKTGVKKWDVKKIRDAVVSGGGGWHGQGWLGTGKWNVKRTEMDENGVCKCCKEKLVCIDINPVETETFAASLTRLACEREVKANFNQFQEWLERHGPFDAVIDGANMGLVNQRSFSFFQLNNTVQRCQQISPSKRLPLVILHKSRVNGGPATYPKNRALLEKWKNAGALYATPPGSNDDWYWLYAAVSCKCLLVTNDEMRDHLFQLLGNSFFPRWKEKHQVRISVTREDGLKLNMPPPYSIVIQESEDGTWHVPMSVEDDLQTSRQWLCAKRSKTP | Cofactor: Binds 2 Mg(2+) or Mg(2+) ions per subunit.
Function: Endonuclease RNase P responsible for the 5' maturation of tRNA precursors. Preferentially cleaves at the unusual cleavage site, but also able to cleave at the classical cleavage site. Also involved in the maturation of mRNAs in mitochondria.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 64877
Sequence Length: 572
Subcellular Location: Mitochondrion
EC: 3.1.26.5
|
Q680B9 | MAASDQHRSRRHDESSSRPNKKKKVSRNPETNLLFNLNSCSKSKDLSAALALYDAAITSSEVRLSQQHFQTLLYLCSASITDISLQYLAIDRGFEIFDRMVSSGISPNEASVTSVARLAAAKGNGDYAFKVVKEFVSVGGVSIPRLRTYAPALLCFCEKLEAEKGYEVEEHMEAAGIALEEAEISALLKVSAATGRENKVYRYLHKLREYVGCVSEETLKIIEEWFCGEKAGEVGDNGIGSDVGMLREAVLNNGGGWHGHGWVGEGKWTVKKGNVSSTGRCLSCSEQLACVDTNEVETQKFVDSLVALAMDRKTKMNSCETNVVFSEFQDWLEKHGDYEAIVDGANIGLYQQNFVDGSFSLSQLESVMKELYRESGNNKWPLILLHKRRVKTLLENPTHRNLVEEWISNGVLYATPPGSNDDWYWLYAAAKLKCLLVTNDEMRDHIFELLGSTFFQKWKERHQVRYTFVKGNLKLEMPSPFSVVIQESEKGSWHFPVSCENNEESSRTWMCISRQSILDSPKSNGKIP | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Endonuclease RNase P responsible for the 5' maturation of tRNA precursors . Preferentially binds precursor tRNAs containing short 5' leaders and 3' trailers . Also involved in the maturation of mRNA and small nucleolar RNA (snoRNA) .
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 59228
Sequence Length: 528
Subcellular Location: Nucleus
EC: 3.1.26.5
|
F4JKB6 | MKLKKPSLPSSLLCAVPPCLSQIRLLIPRRVRVSSSTFANAKLVTLRNHTVNLHIYYCSMAGTDNRRSRHDDESPKNPNKKKKGNRNPEKSLLINLHSCSKRKDLSAALALYDAAITSSDIRLNQQHFQSLLYLCSAFISDPSLQTVAIDRGFQIFDRMVSSGISPNESSVTAVARLAAAKGDGDYAFKLVKDLVAVGGVSVPRLRTYAPALLCFCDTLEAEKGYEVEDHMDASGIVLEEAEISALLKVSAATGRENKVYRYLQKLRECVGCVSEETSKAIEEWFYGVKASEVSDNGIGSDIELLRAAVLKNGGGWHGLGWVGEGKWIVKKGNVSSAGKCLSCDEHLACVDTNEVETEDFVNSLVTLAMERKAKMNSCEPMADFSEFQEWLEKHGDYEAILDGANIGLYQQNFADGGFSLPQLEAVVKELYNKSGSKKQPLILLHKKRVNALLENPNHRNLVEEWINNNVLYATPPGSNDDWYWLYAAAKLKCLLVTNDEMRDHIFELLSNSFFQKWKERHQVRFTFVKGCLKLEMPPPFSVVIQESEKGSWHVPITSQDKEESLRSWMCITRQSS | Cofactor: Binds 2 Mg(2+) or Mg(2+) ions per subunit.
Function: Endonuclease RNase P responsible for the 5' maturation of tRNA precursors. Also involved in the maturation of mRNA and small nucleolar RNA (snoRNA).
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 64396
Sequence Length: 576
Subcellular Location: Nucleus
EC: 3.1.26.5
|
P81264 | MKAVGAWLLCLLLLGLALQGAASRAHQHSMEIRTPDINPAWYAGRGIRPVGRFGRRRAAPGDGPRPGPRRVPACFRLEGGAEPSRALPGRLTAQLVQE | Function: Stimulates prolactin (PRL) release and regulates the expression of prolactin through its receptor GPR10. May stimulate lactotrophs directly to secrete PRL.
PTM: Amidation of C-terminus is required for receptor interaction.
Sequence Mass (Da): 10544
Sequence Length: 98
Subcellular Location: Secreted
|
Q01939 | MTAAVTSSNIVLETHESGIKPYFEQKIQETELKIRSKTENVRRLEAQRNALNDKVRFIKDELRLLQEPGSYVGEVIKIVSDKKVLVKVQPEGKYIVDVAKDINVKDLKASQRVCLRSDSYMLHKVLENKADPLVSLMMVEKVPDSTYDMVGGLTKQIKEIKEVIELPVKHPELFESLGIAQPKGVILYGPPGTGKTLLARAVAHHTDCKFIRVSGAELVQKYIGEGSRMVRELFVMAREHAPSIIFMDEIDSIGSTRVEGSGGGDSEVQRTMLELLNQLDGFETSKNIKIIMATNRLDILDPALLRPGRIDRKIEFPPPSVAARAEILRIHSRKMNLTRGINLRKVAEKMNGCSGADVKGVCTEAGMYALRERRIHVTQEDFELAVGKVMNKNQETAISVAKLFK | Function: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).
PTM: N-acetylated by NAT1.
Sequence Mass (Da): 45272
Sequence Length: 405
Subcellular Location: Cytoplasm
|
Q81U45 | MKKAMLALAATSVIALSACGTSSSDKIVTSKAGDITKDEFYEQMKTQAGKQVLNNMVMEKVLIKNYKVEDKEVDKKYDEMKKQYGDQFDTLLKQQGIKEETLKTGVRAQLAQEKAIEKTITDKELKDNYKPEIKASHILVKDEATAKKVKEELGQGKSFEELAKQYSEDTGSKEKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQFGYHIIKVTDIKEPEKSFEQSKADIKKELVAKKSQDGEFMNDLMMKEIKKADVKVDDKDLKDLFEEKKADAKKEEKK | Function: Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins. Important for the secretion of the protective antigen. The three PsrA proteins in this organism show different but overlapping substrate specificities.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Location Topology: Lipid-anchor
Sequence Mass (Da): 32456
Sequence Length: 287
Subcellular Location: Cell membrane
EC: 5.2.1.8
|
P60750 | MNKTWKKAATVLAFAGIALSATACSGGKAVVTYKGGKITESQYYDKMKESQAGQSTLASMIVSDALESQYGKDVTQKQVDKEYNKYKKQYGSQFDSVLEQNGMTASTFKDNLKTNLLTEAALKHIKKITPAQEKKAWKNYQPEVTVQHILVSKKSTAEDVIKQLQDGGDFKKLAKKYSTDTATKNDAGKLPAFDSTDSTLDSSFKTAAFKLKTGEITTTPVKTQYGYHVIKMIKHPAKGTFKEHKKQIDNQIYQSMSEDQNVMRSVIATVLKRADVSIKDKDLKNVLSQYVSSDSLSK | Function: Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Location Topology: Lipid-anchor
Sequence Mass (Da): 33048
Sequence Length: 298
Subcellular Location: Cell membrane
EC: 5.2.1.8
|
Q88X05 | MKKWLIALAGVLLTFTLAGCGSKTVASTSGGKITESQYYSSMKGTSSGKQVLQQMILNKVLEKDYGSKVSTKQVTKQYNTYKSQYGSSFSTVLSQNGLTTKTFKEQLRSNLLLKEAVKDKVKITDKALKKQWKSYEPKVTVQHILVAKSATADKVLDALKKDSSQANFTKLAKKYSTDTTTKNDGGKLSAFDNTNTSYSSKFLTAAFKLKNGEYTTSAVKTSNGYEIIRMIKNPGKGKMSDHTADLKKQIWDNDMSDSTVLQNVVSKVLKGGNVSIKDNDLKDILSSYLSTSSSSSSN | Function: Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Location Topology: Lipid-anchor
Sequence Mass (Da): 32619
Sequence Length: 298
Subcellular Location: Cell membrane
EC: 5.2.1.8
|
Q92BR2 | MTKLKKVMISLVAATLLLLAGCGSSAVVKTDAGNVTQDELYEAMKTTYGNEVVQQLTFKKILEDKYTVTEKEVNAEYKKYEEQYGDSFESTLSSNNLTKTSFKENLEYNLLVQKATEANMNVSESKLKTYYKTWEPNITVRHILVDDEATAKEIQTKLKNGEKFADLAKEYSTDTATSTNGGLLDPFGPGEMDETFEKAAYALKNKDDVSGIVKSTYGYHLIQLVKKTEKGTYAKEKANVKAAYIKSQLTSENMTAALKKELKAANIDIKDSDLKDAFADYTSTSSSSSTSTSN | Function: Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Location Topology: Lipid-anchor
Sequence Mass (Da): 32552
Sequence Length: 294
Subcellular Location: Cell membrane
EC: 5.2.1.8
|
Q99405 | MKKPLGKIVASTALLISVAFSSSIASAAEEAKEKYLIGFNEQEAVSEFVEQIEANDDVAILSEEEEVEIELLHEFETIPVLSVELSPEDVDALELDPTISYIEEDAEVTTMAQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGNGHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGASGSGSVSSIAQGLEWAGNNGMHVANLSLGSPSPSATLEQAVNSATSRGVLVVAASGNSGAGSISYPARYANAMAVGATDQNNNRASFSQYGAGLDIVAPGVNVQSTYPGSTYASLNGTSMATPHVAGVAALVKQKNPSWSNVQIRNHLKNTATGLGNTNLYGSGLVNAEAATR | Cofactor: Binds 2 calcium ions per subunit.
Function: Alkaline serine protease that cleaves various substrates, including N-succinyl-Ala-Ala-Pro-Phe-pNA, N-succinyl-Ala-Ala-Pro-MetpNA, oxidized insulin B chain, casein, hemoglobin and scleroproteins, such as keratin, alpha-keratin and elastin.
Sequence Mass (Da): 38881
Sequence Length: 380
Subcellular Location: Secreted
EC: 3.4.21.-
|
P24158 | MAHRPPSPALASVLLALLLSGAARAAEIVGGHEAQPHSRPYMASLQMRGNPGSHFCGGTLIHPSFVLTAAHCLRDIPQRLVNVVLGAHNVRTQEPTQQHFSVAQVFLNNYDAENKLNDVLLIQLSSPANLSASVATVQLPQQDQPVPHGTQCLAMGWGRVGAHDPPAQVLQELNVTVVTFFCRPHNICTFVPRRKAGICFGDSGGPLICDGIIQGIDSFVIWGCATRLFPDFFTRVALYVDWIRSTLRRVEAKGRP | Function: Serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro) . By cleaving and activating receptor F2RL1/PAR-2, enhances endothelial cell barrier function and thus vascular integrity during neutrophil transendothelial migration . May play a role in neutrophil transendothelial migration, probably when associated with CD177 .
Catalytic Activity: Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala-|-Xaa- > -Val-|-Xaa-.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27807
Sequence Length: 256
Subcellular Location: Cytoplasmic granule
EC: 3.4.21.76
|
A9YWT8 | MQIQNNNYKGLIPPYILQNIYKNTSESEKDNVLMTLNHTQSLMLDSVIKTSDSIDNTDDEVVSDTLHRSIYDAKNETKLPGTLVRDEGDPDNGDVAVDNAYKYLEATYNFYKEVFNRNSLDDKGMKLIATVHYGKEYMNAYWGRGQMVFGDGDGKVFNNFTTSIDVIGHELSHGVIEKTADLIYFFQSGALNESIADVFGSLVRQHYLKQKADEASWVVGEELLAKGIKGVGIRSMKEPGKAYDDPLLGKNPQPGHMDDFKDYPIYRDNGGVHVNSGIPNKAFYNLAIKLGGYAWEKAGKIWYNTLLDKDLARDTTFLSFAKLTVKHARDLFDEDVEKATIDSWKEVGIKVKEEDKDKGKDEGKDKAETKV | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease involved in the inhibition of insect antibacterial peptides. Reduces the antibacterial activity of G.mellonella hemolymph by 50%. Reduces the antibacterial activity of cecropin A by 80% and completely inhibits cecropin B.
Sequence Mass (Da): 41773
Sequence Length: 371
Subcellular Location: Secreted
EC: 3.4.24.-
|
Q7NFT6 | MSTTPQEREKPVRVLVDNDPVPTSTEKWGKPGWFERNLARGPKTTTWIWDLHALAHDFETHTSDKEEISRKIFSAHFGHLAVVCVWLSGMFWHGAYFSNFTAWMENPLGLKPSAQTVWPVFGQEILNDPSTVAKGFEQGGIVITSGLFHLWRAVGFTTTGQLAAMSIAMLIIAALFLFAGWFHYHKRAPKLEWFQNVESMLNHHLAGLFGLGSLFWTGHLIHVALPVKAQLDAGIAPAQVNPFAGLDYGLMGQYFPKGFGPNGGLGAFFTLNWGQFTDFLTFKGGLEPATGALYLTDIAHHHLAIATLFIIAGHMYRTNWGIGHSIKEMLEAHKGPLTGEGHRGLYEVLTTSWHAQLAINLAMAGSITIIVAHHMYAMNPYPYMGTDYATQISLFTHHMWIGGFLIVGAGAHAAIFMVRDYDPVTNQNNLLDRVLRHRDAIISHLNWVTLFLGFHSFGLYVHNDTMQALGRPRDMFADFAIPLQPVFAQWIQNIHAAAPGGATAPWVGGTSPTWYTGALSSAATLQANQVLALANDKISISPIHLGTADFMVHHIFALCIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQSSAWDHVFLGLFWMYNTISVVIFHFSWKMQSDVWGTVDRSTGAVNHIIGNTDVLLGGQTVALSQYAASSININGWLRDFLWAQSSAVINSYGGPLSAYGLMFLGAHFIWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPAIQPRALSITQGRAVGVAHYLLGGIATTWAFFLARFLALP | Cofactor: PSI electron transfer chain: 5 chlorophyll a, 1 chlorophyll a', 2 phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 chlorophyll a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
Function: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6.
Catalytic Activity: hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 86419
Sequence Length: 783
Subcellular Location: Cell inner membrane
EC: 1.97.1.12
|
Q9XQV3 | MKLFFRYVNSRVWSQAGSSHFNKALAKGPKTTTWIWSLHADAHDFQQSSSESTAASVGAKVFSSGLAHFSIVFFWLGGMHFHGAYFSNYSAWLKDPKTPGSQLVWSLVGQDILNQDLGGYFQSIRVTSGFFQLWRAEGIVTQVHLKYAAAAALIGSIATLWAAYFHMHISWSSSLRTMGSLSSYNAGQLAILAGLGSISWAGHQIHIALPINRLLDSGVDPSQLPSPQDLLFKDLMQVIFPGFGVGPAVDFSIYLNQKGAASEVGLNPSTGSIYLGQIASHHFFVGITCIISGIIALLVKRSKAGSFQDAAAFNNSWHSRLSINLAIAGSLSITFAHHIYAMPVYPFCGSDYATVLSLFVHHMWIGGFFIVGAGAHASIFMIRDEGVPAGIPSAKGRLYSVNSIIQQLLAHRDIIMGHLIYVTIALGMHAFGIYIHNDTLQALGRPEDIFSDNSIQLKPLFAVWVQSLPSLFLLNTLSGDAAVTGIPGFGLEVLDGKVVTMTQELGTADFMVHHIHAFTIHCTLLILMKGVLYSRSSRLVSDKLELGFRYPCDGPGRGGTCQISPWDHVFLGVFWMYNSLSIVIFHFFWKMQSDVWGVYDVSTQKIVHLTGGDFSVNSITINGWLRNFLWSQAAEVIQSYGSGLSGYGLIFLGAHFTWAFSLMFLWSGRGYWQELIESILWAHHKLKIVPNIQPRALSITQGRAVGLVHYMLGGIGTTWAFFLARVVALSIS | Cofactor: P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
Function: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6.
Catalytic Activity: hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80332
Sequence Length: 732
Subcellular Location: Plastid
EC: 1.97.1.12
|
Q9MUK1 | XIMVEKDPVKTSFEKWAQPGHFSKALAKGPSTTTWIWNLHADAHDFDSHTNDLEDISRKIFSAHFGQLGIIFIWLSGMYFHGARFSNYEAWLNDPTHVKPSAQVVWPIVGQEILNGDVGGGFQGIQITSGFFQLWRASGITSELQLYCTAIGGLIFAGLMFFAGWFHYHKAAPKLAWFQNVESMLNHHLAGLLGLGSLAWAGHQIHVSLPINQLLDAGVDPKEIPLPHEFILNRELMAQTFPSFAKGLIPFFTLDWSEYSDFLTFRGGLNPVTGGLWLTDTAHHHLAIAVLFLVAGHMYRTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXAHHMYAMPPYPYLATDYATQLSLFTHHMWIGGFLIVGAAAHAAIFMVRDYDPTTQYNNLLDRVIRHRDAIISHLNWVCIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPVFAQWVQNTHALAPGSTAPNAAASTSPTWGGSDLVAVGGKVALAPIPLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNSISVVIFHFSWKMQSDVWGSISEEGVVNHITGGNFAQSSTTINGWLRDFLWAQASQVIQSYGSSLSAYGLLFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPVTQPRALSIIQGRAVGVAHY | Cofactor: P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
Function: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin.
Catalytic Activity: hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79952
Sequence Length: 720
Subcellular Location: Plastid
EC: 1.97.1.12
|
Q0P3K2 | MATKFPKFSQGLASDPTTRRIWFGIATAHDFETHDGMTEEKLYQKIFASHFGQLAIIFLWTSGNLFHVAWQGNFEKWGEDPLHVRPIAHTIWDPHFGQPAVEAFTRGGASAPVNIAYSGVYQWWYTIGMRTNVDLYNGSLFLLFVAGLFLFAGWLHLQPTFAPAVSWFKNAESRLNHHLSGLFGVSSLAWTGHLVHVAIPASRGETVRWDNFLTTLPHPAGLAPFFTGQWAVYAQNPDTAGHIFGTSEGAGTAILTFLGGFHPQTQSLWLTDMAHHHLAIAVVFIIAGHQYRTNFGIGHSMKEILEAHTAPSGRLGAGHTGLFDTVNNSLHFQLGLALASVGVLCSLTAQHMYSMPPYAFLAQDFTTQAALYSHHQYIAGFIMCGAFAHGAIFFIRDYDPEANKGNVLARMLEHKEAIISHLSWVSLFLGFHTLGLYVHNDVMQAFGTPEKQILIEPVFAQWIQAAQGKALYGFDILLSGDNAATAAGNSIYLPGWLAGINSSTNSLFLPIGPGDFLVHHAIALGLHTTTLILVKGALDARGSKLMPDKKDFGYSFPCDGPGRGGTCDISAWDAFYLAVFWELNTVSWTVFYFHWKHLALWQGNSAQFDESSTYIMGWLRDYLWLNSSQLINGYNPFGMNSLSVWAWMFLFGHLIYATGFMFLISWRGYWQELIETLVWAHERTPLANFVKWNDKPVALSIVQARLVGLTHFAVGFVLTYAAFVIASTSGKFG | Cofactor: P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
Function: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6.
Catalytic Activity: hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81346
Sequence Length: 733
Subcellular Location: Plastid
EC: 1.97.1.12
|
P12185 | MTASYLPSIFVPLVGLIFPAITMASLFIYIEQDEIL | Function: May help in the organization of the PsaL subunit.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4018
Sequence Length: 36
Subcellular Location: Plastid
|
Q0P3K0 | MAASLLPSIFVPLVGLVFPAVAMASLFLYIEKEQVS | Function: May help in the organization of the PsaL subunit.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3853
Sequence Length: 36
Subcellular Location: Plastid
|
P17230 | MRDFKTYLSVAPVLSTLWFGSLAGLLIEINRFFPDALTFPFFSF | Function: May help in the organization of the PsaE and PsaF subunits.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5077
Sequence Length: 44
Subcellular Location: Plastid
|
Q31NU0 | MDGLKRYLSSAPILATIWFAITAGILIEFNRFFPDLLFHPL | Function: May help in the organization of the PsaE and PsaF subunits.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4710
Sequence Length: 41
Subcellular Location: Cellular thylakoid membrane
|
A0T0V1 | MNDFQKYLSTAPVLLTLWMTFTAGFIIEVNRFFPDMLGLYF | Function: May help in the organization of the PsaE and PsaF subunits.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4853
Sequence Length: 41
Subcellular Location: Plastid
|
A9WSI0 | MTQQFYVSPEQVMKDRADFARKGIARGRSVVVVSSLEGIALVAENPSPSLHKIGEIYDKIAFAAVGKYNEFESLRQAGVRYADVRGYSYDRDDVTARGLASVYAQSLGAVFTAEQKPFEVELAVAEVGENQDQDHLYRLTFDGSIADETGFIAMGGQVDSVHQVVAAGWASGSSLADVVGLAVGALGAGREPVVELDAANLEIAVLDRDSETSRGVARAFRRLNANEVNDLLSPRGSGSPAE | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Sequence Mass (Da): 25828
Sequence Length: 242
Pathway: Protein degradation; proteasomal Pup-dependent pathway.
Subcellular Location: Cytoplasm
|
B1W307 | MSTPFYVSPQQAMADRAEYARKGIARGRSLVVLQYADGIVFVGENPSRALHKFSEIYDRIGFAAAGKYNEYENLRIGGVRYADLRGYTYDRDDVTARGLANVYAQTLGTIFSSAAEKPYEVELVVAEVGSEPEGDQIYRLPHDGSIVDEHGSVAVGGNSEQISTFLDQRHRDGMTLAEALKLAVQALSREPGGGEREIPAERLEVAVLDRTRPQQRKFKRIVGRQLARLLDTEAAGSTPTDAPSDTEDGDSTDGTDRADGTTDSTEETEK | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Sequence Mass (Da): 29525
Sequence Length: 270
Pathway: Protein degradation; proteasomal Pup-dependent pathway.
Subcellular Location: Cytoplasm
|
Q2TBP0 | MAAVSVYERPVGGFSFDNCRRNAVLEADFAKKGYKLPTARKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKKLVSEAIAAGIFNDLGSGSNIDLCVISKSKLDFLRPYSVPNKKGTRFGRYRCEKGTNAVLTEKVTTLEIEVLEETVQTMDTS | Function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB7 displays a trypsin-like activity.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 30009
Sequence Length: 277
Subcellular Location: Cytoplasm
EC: 3.4.25.1
|
Q54QR2 | MENLNRGGFDFDLCNRNNVLEKTGLRMKGFMKTGTTIVGVVYKGGVVLGADTRATEGPIVADKNCEKIHYIADNIYCCGAGTAADTESATALISSKLKLHKLSTGKQTRVITALTMLKQMLFKYQGHISAALILGGIDINGPSLHTIYPHGSTDQLPYVTMGSGSLAAMAVFEAKYKNDMTKEEAIALVAEAISSGIFNDLGSGSNVDVTVIEPSGVTVLRNYQTPNERKFRNNPYIFKQGTTPVLKQDIAPLSTKVVIEDIMMGQ | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 28659
Sequence Length: 266
Subcellular Location: Cytoplasm
EC: 3.4.25.1
|
Q99436 | MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS | Function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB7 displays a trypsin-like activity.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 29965
Sequence Length: 277
Subcellular Location: Cytoplasm
EC: 3.4.25.1
|
P70195 | MAAVSVFQPPVGGFSFDNCRRNAVLEADFAKKGFKLPKARKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLTTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKKLVSEAIAAGIFNDLGSGSNIDLCVISKSKLDFLRPFSVPNKKGTRLGRYRCEKGTTAVLTEKVTPLEIEVLEETVQTMDTS | Function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB7 displays a trypsin-like activity.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 29891
Sequence Length: 277
Subcellular Location: Cytoplasm
EC: 3.4.25.1
|
Q3T112 | MALLDVCGAPGGQRGDWAVPLAGSRQRSDPGHYGFSLRSPELALPRGMQPTEFFRSLGGNGESKVQIEMAHGTTTLAFKFQHGVIVAVDSRASAGNYIATLKVNKVIEINPYLLGTMSGCAADCLYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNSHAYGVMDSGYRPDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLMHQYREASQ | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides (By similarity). May participate in the generation of spliced peptides resulting from the ligation of two separate proteasomal cleavage products that are not contiguous in the parental protein (By similarity). Required for adipocyte differentiation (By similarity).
PTM: Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 30268
Sequence Length: 276
Subcellular Location: Cytoplasm
EC: 3.4.25.1
|
P28062 | MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Replacement of PSMB5 by PSMB8 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues. Involved in the generation of spliced peptides resulting from the ligation of two separate proteasomal cleavage products that are not contiguous in the parental protein . Acts as a major component of interferon gamma-induced sensitivity. Plays a key role in apoptosis via the degradation of the apoptotic inhibitor MCL1. May be involved in the inflammatory response pathway. In cancer cells, substitution of isoform 1 (E2) by isoform 2 (E1) results in immunoproteasome deficiency. Required for the differentiation of preadipocytes into adipocytes.
PTM: Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 30354
Sequence Length: 276
Subcellular Location: Cytoplasm
EC: 3.4.25.1
|
P28063 | MALLDLCGAARGQRPEWAALDAGSGGRSDPGHYSFSAQAPELALPRGMQPTAFLRSFGGDQERNVQIEMAHGTTTLAFKFQHGVIVAVDSRATAGSYISSLRMNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMLQYRGMGLSMGSMICGWDKKGPGLYYVDDNGTRLSGQMFSTGSGNTYAYGVMDSGYRQDLSPEEAYDLGRRAIAYATHRDNYSGGVVNMYHMKEDGWVKVESSDVSDLLYKYGEAAL | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. May participate in the inflammatory response pathway. Required for adipocyte differentiation . May be involved in the generation of spliced peptides resulting from the ligation of two separate proteasomal cleavage products that are not contiguous in the parental protein (By similarity).
PTM: Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 30260
Sequence Length: 276
Subcellular Location: Cytoplasm
EC: 3.4.25.1
|
Q29576 | RLYYLRNGARISVSAASKLXSNMMYQYRGMGLSMGSMICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNTYAYGVMDSGHRYDLSIEEAYDLGRRAIVHATHRD | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. May participate in the generation of spliced peptides resulting from the ligation of two separate proteasomal cleavage products that are not contiguous in the parental protein (By similarity). Required for adipocyte differentiation (By similarity).
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 11604
Sequence Length: 104
Subcellular Location: Cytoplasm
EC: 3.4.25.1
|
P28065 | MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Replacement of PSMB6 by PSMB9 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues.
PTM: Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 23264
Sequence Length: 219
Subcellular Location: Cytoplasm
EC: 3.4.25.1
|
P28076 | MLRAGAPTAGSFRTEEVHTGTTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQRIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAANVVKNISYKYREDLLAHLIVAGWDQREGGQVYGTMGGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEECRRFTTNAITLAMNRDGSSGGVIYLVTITAAGVDHRVILGDELPKFYDE | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Contributes to NFKBIA degradation and subsequently NFKB1 generation.
PTM: Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 23397
Sequence Length: 219
Subcellular Location: Cytoplasm
EC: 3.4.25.1
|
A8W3E7 | MGLPWYRVHTVVLNDPGRLLSVHIMHTALVAGWAGSMALYELAVFDPSDPVLDPMWRQGMFVIPFMTRLGITNSWGGWGIAGGTVTNPGLWSYEGVAGAHIAFSGLCFLAAIWHWVYWDLEVFYDERTGKPSLDLPKIFGIHLFLSGVACFGFGAFHVTGLYGPGIWVSDPYGLTGKVQPLKPAWGAEGFDPFVPGGIASHHIAAGTLGILAGLFHLSVRPPQRLYKGLRMGNIETVLSSSIAAVFFAAFVVAGTMWYGSATTPIELFGPTRYQWDQGYFQQEIYRRVSAGLAENQSLSETWSKIPEKLAFYDYIGNNPAKGGLFRAGSMDNGDGIAVGWLGHPIFRDKEGRELFVRRMPTFFETFPVLLVDGDGIVRADVPFRRAESKYSVEQVGVTVAFYGGELNDVSYSDPATVKKYARRAQLGEIFELDRATLKSDGVFRSSPRGWFTFGHASFALLFFFGHIWHGARTLFRDVFAGIDPDLDAQVEFGAFQKLGDPTTRRQAV | Cofactor: Binds multiple chlorophylls. PSII binds additional chlorophylls, carotenoids and specific lipids.
Function: One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56073
Sequence Length: 508
Subcellular Location: Plastid membrane
|
P48187 | MKILYSLRRFYHVETLFNGTFVLAGRDQETTGFPWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGSGGEVLDTFPYFVSGVLHLISSAVLGFGGIYHALLGPETLEESFPFFGYVWQDRNKMTTLLGIHLILLGLGAFLLVLKALYFGGVYDTWAPGGGDVRKITNLTLSPGVIFGYLLKSPFGGEGWIVSVDDLEDIIGGHVWLGSICVLGGIWHILTKPFAWARRAFVWSGEAYLSYSLGALSVFGFIACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVGSAQGPTGLGKYLMRSPTGEVIFGGETMRFWDLRAPWLEPLRGPNGLDLSRLKKDGQPWQERRSGEYMTHAPLGSLNSVGGVATEINAVNYVSPRSWLATSHFVLGFFFFVGHLWHAGRARAAAAGFEKGIDRDLEPVVYMTPLN | Cofactor: Binds multiple chlorophylls and provides some of the ligands for the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also provide a ligand for a Cl- that is required for oxygen evolution. PSII binds additional chlorophylls, carotenoids and specific lipids.
Function: One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
PTM: Phosphorylated in both bundle sheath and mesophyll cells, phosphorylation increases when cells are grown under high rather than low light regimes (70 vs 900 umol photons/m-2/s).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51900
Sequence Length: 473
Subcellular Location: Plastid
|
P06414 | MKILYSQRRFYPVETLFNGTLALGGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGPGGEIVDTFPYFVSGVLHLISSAVLGFGGIYHALIGPETLEESFPFFGYVWKDKNKMTTILGIHLILLGAGAFLLVFKALYFGGIYDTWAPGGGDVRKITNLTLSPGVIFGYLLKSPFGGEGWIVSVDNLEDIIGGHVWLGSICIFGGIWHILTKPFAWARRALVWSGEAYLSYSLGAIAVFGFIACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVGSAQGPTGLGKYIMRSPTGEIIFGGETMRFWDLRAPWLEPLRGPNGLDLSKLKKDIQPWQERRSAEYMTHAPLGSLNSVGGVATEINAVNYVSPRSWLATSHFVLGFFFFVGHLWHAGRARAAAAGFEKGIDRDFEPVLSMTPLN | Cofactor: Binds multiple chlorophylls and provides some of the ligands for the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also provide a ligand for a Cl- that is required for oxygen evolution. PSII binds additional chlorophylls, carotenoids and specific lipids.
Function: One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
PTM: Phosphorylated on threonine residue(s).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51786
Sequence Length: 473
Subcellular Location: Plastid
|
Q8CM25 | MTIAIGRAPAERGWFDILDDWLKRDRFVFVGWSGILLFPCAYLALGGWLTGTTFVTSWYTHGLASSYLEGCNFLTVAVSTPANSMGHSLLLLWGPEAQGDFTRWCQLGGLWTFIALHGAFGLIGFMLRQFEIARLVGVRPYNAIAFSAPIAVFVSVFLIYPLGQSSWFFAPSFGVAAIFRFLLFFQGFHNWTLNPFHMMGVAGVLGGALLCAIHGATVENTLFQDGEGASTFRAFNPTQAEETYSMVTANRFWSQIFGIAFSNKRWLHFFMLFVPVTGLWMSAIGVVGLALNLRSYDFISQEIRAAEDPEFETFYTKNLLLNEGIRAWMAPQDQPHENFVFPEEVLPRGNAL | Cofactor: The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution . PSII binds additional chlorophylls, carotenoids and specific lipids.
Function: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. D2 is needed for assembly of a stable PSII complex.
Catalytic Activity: 2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39361
Sequence Length: 352
Subcellular Location: Cellular thylakoid membrane
EC: 1.10.3.9
|
Q85C42 | MSGNTGERPFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTENRQEVPLITGRFNSLEQVDEFTRSF | Cofactor: With its partner (PsbF) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids.
Function: This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9508
Sequence Length: 83
Subcellular Location: Plastid
|
Q2MI72 | MATQTVENSSRSGPRRTAVGDLLKPLNSEYGKVAPGWGTTPLMGVAMALFAVFLSIILEIYNSSVLLDGISMN | Function: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
PTM: Phosphorylation is a light-dependent reaction catalyzed by a membrane-bound kinase; phosphorylation occurs on Thr residue(s) in the N-terminus of the protein.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7759
Sequence Length: 73
Subcellular Location: Plastid
|
Q2PMQ6 | MATQTVEDNSRSGPRRTVVGDLLKPLNSEYGKVAPGWGTTPLMGVAMALFAIFLSIILEIYNSSILLDGISMN | Function: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
PTM: Phosphorylation is a light-dependent reaction catalyzed by a membrane-bound kinase; phosphorylation occurs on Thr residue(s) in the N-terminus of the protein.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7843
Sequence Length: 73
Subcellular Location: Plastid
|
P05146 | MATQTVESSSRSRPKPTTVGALLKPLNSEYGKVAPGWGTTPLMGVAMALFAVFLSIILEIYNSSVLLDGISMN | Function: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
PTM: Phosphorylation is a light-dependent reaction catalyzed by a membrane-bound kinase (Ref.3). Phosphorylation occurs on Thr residue(s) in the N-terminus of the protein.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7730
Sequence Length: 73
Subcellular Location: Plastid
|
Q2JUV4 | MAIRTKLGDLLRPLNSEYGKVAPGWGTTPLMAVFMVLFGIFLLIILQIYNKSLLLEDINVSWESLSF | Function: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7559
Sequence Length: 67
Subcellular Location: Cellular thylakoid membrane
|
Q8DJZ6 | METLKITVYIVVTFFVLLFVFGFLSGDPARNPKRKDLE | Cofactor: PSII binds multiple chlorophylls, carotenoids and specific lipids.
Function: One of the components of the core complex of photosystem II (PSII). May be required for formation of PSII dimers but not their subsequent stability . PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4405
Sequence Length: 38
Subcellular Location: Cellular thylakoid membrane
|
Q85CD4 | MANTTGRIPLWLIGTIAGILVIGLVGIFFYGSYSGLGSSL | Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4130
Sequence Length: 40
Subcellular Location: Plastid
|
Q85X72 | MPVIFNICLDDAFIHSNNPFFGKLPEAYAIFDPIVDVMPIIPVLSFLLAFVWQAAVSFR | Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6672
Sequence Length: 59
Subcellular Location: Plastid
|
P41598 | MFNIFLDDAFIHSNNPFFGKLPEAYAISDPIVDVMPIIPVLSFLLAFVWQAAVSFR | Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6346
Sequence Length: 56
Subcellular Location: Plastid
|
Q6YXL7 | MTQPNPNKQSVELNRTSLYWGLLLIFVLAVLFSNYFFN | Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface and is required for correct PSII assembly and/or dimerization.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4479
Sequence Length: 38
Subcellular Location: Plastid
|
A2CBT5 | MPVNNFGFLATLLFVAVPMLFLIGLYIQTNSNKS | Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3775
Sequence Length: 34
Subcellular Location: Cellular thylakoid membrane
|
Q7VDL9 | METTNFGFIISLLFVGIPTIFLVGLYISTSDGEKSSFFSDSSKGKLGPKS | Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5365
Sequence Length: 50
Subcellular Location: Cellular thylakoid membrane
|
Q7V340 | MQTLSSAPDPAVSVAVTILAVLLALTGFGLWTAFGPKAAKLTDPWDDHDD | Function: May play a role in photosystem I and II biogenesis.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5225
Sequence Length: 50
Subcellular Location: Cellular thylakoid membrane
|
Q85BG5 | MEALVYTFLLVGTLGIIFFAIFFRDPPKVPSKGVPSKGKK | Function: Seems to play a role in the dimerization of PSII.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4413
Sequence Length: 40
Subcellular Location: Plastid
|
P37256 | MEALVYTFLLVGTLGIIFFSIFFRDPPRMIK | Function: Seems to play a role in the dimerization of PSII (By similarity). Essential to maintain photosynthetic activity under adverse growth conditions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3636
Sequence Length: 31
Subcellular Location: Plastid
|
P32095 | MLLFTFTFQALVLALIIFSFILVLTLPVIFASPKGWENNKSRIWLACRFWFFLVFLIGILDGIFL | Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 7586
Sequence Length: 65
Subcellular Location: Plastid
|
A0ZZ32 | MTIAFQLAVFALIATSSILLISVPVVFASPDGWLSNKNIVFSGTSLWIGLVFLVGILNSLIS | Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6567
Sequence Length: 62
Subcellular Location: Plastid
|
Q6B8V1 | MTIIVQLLVFILVIFSTLLVVGIPVTFASPGQWEKSKNLIYTGAGIWTGLVLITGLVNSFIN | Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6721
Sequence Length: 62
Subcellular Location: Plastid
|
O78503 | MVTILQLLVSILILLSFALVVGVPVILVSPGEWERSKNLVYASAGLWFGLVIVTAAFNSFVI | Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6689
Sequence Length: 62
Subcellular Location: Plastid
|
Q06RD4 | MTLVFQLAVFALIATSSILLISVPVVFASPDGWSSNKNVVFSGTSLWIGLVFLVGILNSLIS | Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6555
Sequence Length: 62
Subcellular Location: Plastid
|
Q332Y1 | MTLAFQLAVFALIATSSILLISVPVVFASPDGWSSNKNVVFSGTSLWIGLVFLVGILNSLIS | Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6527
Sequence Length: 62
Subcellular Location: Plastid
|
Q5IHA9 | MTIAFQLAVFALIATSSILLISVPVVFASSDGWSSNKNVVFSGTSLWIGLVFLVAILNSLIS | Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6531
Sequence Length: 62
Subcellular Location: Plastid
|
O00231 | MAAAAVVEFQRAQSLLSTDREASIDILHSIVKRDIQENDEEAVQVKEQSILELGSLLAKTGQAAELGGLLKYVRPFLNSISKAKAARLVRSLLDLFLDMEAATGQEVELCLECIEWAKSEKRTFLRQALEARLVSLYFDTKRYQEALHLGSQLLRELKKMDDKALLVEVQLLESKTYHALSNLPKARAALTSARTTANAIYCPPKLQATLDMQSGIIHAAEEKDWKTAYSYFYEAFEGYDSIDSPKAITSLKYMLLCKIMLNTPEDVQALVSGKLALRYAGRQTEALKCVAQASKNRSLADFEKALTDYRAELRDDPIISTHLAKLYDNLLEQNLIRVIEPFSRVQIEHISSLIKLSKADVERKLSQMILDKKFHGILDQGEGVLIIFDEPPVDKTYEAALETIQNMSKVVDSLYNKAKKLT | Function: 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. In the complex, PSMD11 is required for proteasome assembly. Plays a key role in increased proteasome activity in embryonic stem cells (ESCs): its high expression in ESCs promotes enhanced assembly of the 26S proteasome, followed by higher proteasome activity.
PTM: Phosphorylated by AMPK.
Sequence Mass (Da): 47464
Sequence Length: 422
Subcellular Location: Nucleus
|
Q84V22 | MKPRFPQNVYFLARYSYLRRFQHSQRRTFSSFLNNIRSNYSGARASPLGGSSGAGAGAGGGGTGDSKGNAFLVPGATMATILMLGALHARRLYEDKKIEEKREKGIELEFHPDIKASFLGVLPLRSISRAWGSFMSLEIPVWMRPYAYKAWARAFHSNLEEAALPLEEYTSLQDFFVRSLKEGCRPIDPDPCCLVSPVDGTVLRFGELKGNRGMIEQVKGHSYSVPALLGNNSLLPMEPEGKNESKEEAVGDKSDKSWLRVSLASPKLRENVSASPMKGLYYCVIYLKPGDYHRIHSPADWNATVRRHFAGRLFPVNERATRTIRNLYVENERVVLEGIWKEGFMALAAVGATNIGSIELFIEPELRTNKPKKKLFPTEPPEERVYDPEGLGLRLEKGKEVAVFNMGSTVVLIFQAPTANTPEGSSSSSDYRFCVKQGDRVRVGQALGRWKEE | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. Contributes only to a minor proportion of PtdEtn production.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 50560
Sequence Length: 453
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Mitochondrion
EC: 4.1.1.65
|
A0L627 | MEKSGLVAKEGYPFMAIFIGVAAVSSALSWYGIVQFVLWVLAGWCIWFFRDPERHSDAPEDAVIAPADGRVVAIREMEKGPLTDEPVRMVSIFMNVFNVHVNRAPIAGTVTKISYHPGKFVNADLDKASIENERNVLLMESPAGVKMAFQQVAGLVARRIVCRINEGTVLQRGERFGLIRFGSRVDLFFPMDAEISVKLGEMTHSGVTQMGRLKGKES | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
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 post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24131
Sequence Length: 218
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
|
Q2W9R7 | MRGEAVQAQQISLTKYLWFPINREGWPFVGLFALGALLLGQIWGPLGWAGALLTCWCAWFFRDPDRVTPTRDGLVISPADGVVQMVGMVAPPPELDMGDAPRMRISVFMSVFSVHINRCPVDGTIVKCSYRPGKFLDASLDKASADNERMSVRMSRADGREIAFVQIAGLVARRIKCDLKDGQQVRAGQRFGLIRFGSRVDVYLPDGVAPLVSLGQSIIAGETVLADLDSTEGARQGEIR | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
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 post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26267
Sequence Length: 240
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
|
Q65RD9 | MNSLEKKQITYGQRLKIAFQYAMPQIYLTQIAGWFANKRWGAVTHFVIKMFAKKYNVHMAEAAKPNFSDYATFNEFFIRQLKEYARPINQNTDALCLPADGKISQCGHIDDELLLQAKGHSFSLRDLLAGDEELTRLFKDGEFVTTYLSPRDYHRVHMPCNGTIRKMIYVPGELFSVNPFLNTHIPNLLARNERVICLFDTDFGPMVQILVGATITASISTVWEGVINPPRTGDIRTWTYEGQSAVSLAKGQEMGAFQLGSTVINLFPKNAVKLADYLQVDTVTRVGEILAYKK | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33285
Sequence Length: 294
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
|
A1U4D6 | MLDKLFVLSQYVTPQLAVSRLAGRLADSESTPALKNRVIKWFIGRYGVNMSEAAEPDFTAYPTFNAFFTRALKPGARTIDPAPETLTSPVDGAISQIGQISTDRVFQAKGQSFSLTELLGGDDERAEPFREGEFATIYLSPKDYHRIHMPMAGTLKEMVYVPGKLFSVNPVTAENVPNLFARNERVACLFDTEAGPMAMVLVGAMIVGSVETTWAGVVAPNSGKVTQWQYRGDDAVQFEKGQEMGRFRLGSTVVLVMPKGAVKWQPNQVAEKTVQLGEAFGKLNVK | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31345
Sequence Length: 286
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
|
B2HQP4 | MARRPRRSDSSSAEPTLSPQHLLALVRSTIPPIHPAGRPFIAAGLAVAGVGYRHRWARRTGLLAAGACAGFFRHPPRVPPSRAGAIVAPADGVICVIDTAAPPAELSMGDAPLPRVSIFLSVFDAHVQRAPVSGEVVAVQHRPGRFGSADLPAASDDNERNSVRIRTANGAEVVAVQVAGLVARRIVCDAHVGDKLAIGDTYGLIRFGSRLDTYLPPGTEPVVRVGQRTIAGETILADLP | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
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 post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25179
Sequence Length: 240
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
|
Q5GSL0 | MCFSLPSINKEGYLFIVVSFIVTCIAFSISWGFGVTCLFPTLLCTYFFRDPARIIPGNKDLVLSPADGVISKIEEVSYPLSTNNGEEKKFTLVSIFLSVLNVHVNRIPISGTVKEMHYKKGKFVSAMSDRSSNENEKQVIVIEYTKGKEIIVEQIAGLIARRIVCNLRVSQSVKAGERFGIIRFGSRVNIYVPTDVEIRVSEGQTVVGGETIIANLNKENTQEKLTFDLV | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
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 post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25609
Sequence Length: 230
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
|
Q8PJ17 | MSLVTSLTYVLPHRLLSSLARALAYSQTPSTKQWLIDTVTRKFGVDLSEAQEPDPHAYPTFNAFFTRALKPGARVPDADPSAVLMPADGRISQLGPVENGRIFQAKGQSFTAAELLGDEAAAAPFNDGVFATVYLSPKDYHRVHMPWTGTLRETVHVPGRLFSVGPDAVRKVPRLFARNERLVCHFDTEFGPMASVMVGALLVSGVETVWSGVEIPRYGDRITRKDYRGKGVVLEKFAEMARFNYGSTVIVLLPPGVATLDGGLAAETSVRLGQALARRQ | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30542
Sequence Length: 280
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
|
Q7YSJ4 | MKYLFIAIILILYCSFTKADQKKFLVNMYDNDPLFSPDFENANGAQTGLVKKKLGSDGKPIPANYDMKDPNGNYYIKNATTFKSWFNEVAGVSILVPFELVLTQTAGSQNYYSYSNTSFFPLNELGWYNPSIKGDYEFKKYQDSNKKEQNFHFCMHASFIMSTNCKEVFKFKGDDDVWVFINDVLVLDIGGVHGVQDGTVDMANLPEKIHDSTNSKLGNCKNGTYPFDFFYCERHTKASNCLFETNMGFTCSYYDYCGICNGKGECCTDVKLNQCYTKKCPLPNSLPNGATNYQDYMTIVPTNTCGGTDKCKIYSCNNSTGCEFKQKSCDDGDKCTKDACDSKTGYCSNIPTNPSVVTSCLKSGCDSTTGNYSTPTNCDDKDPCTIDSCINGQGCVHTKACDDEDPCTTDSCSADGKCTHTAIAKCNSDCPSCPSKKCKITSCSEDSGACNYVDMVFASPSECYKATCDPETEEAIYSPIDSSCDTSDSCFTAQCNLNKTCTRVPAINCDDNNECTTDSCSGGSCSNTAIACDDNDPCTIDTCSPSEGCIFTPIVCEQTSLCNTFTCSVGKCVPTPITCSSSVKCQDSICREGVGCVYFNRTCPPDDDCSSAYCSMETGKCISKAYDPLPFSCQSTAVKVGVGIGAAAAAGIAIGGAVAAGLAIFGGKKAYDTWKTSRGNVMTGSQSNPLYTQNQNNGNNPLYSAPAE | Function: Acts as a quorum sensing protein regulating discoidin gene expression during growth and development. D.discoideum is a single-celled amoebae and switches to multicellular development when food becomes limited. As the growing cells reach a high density, they begin expressing discoidin genes. The ability of psiF/dicA to induce discoidin gene expression when present in conditioned medium, suggests that it allows cells to sense their local density.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 76482
Sequence Length: 708
Subcellular Location: Membrane
|
P0DPA7 | MIAVLFSFVIAGCIYYIVSRRVRRSRLPPGPPGIPIPFIGNMFDMPEESPWLTFLQWGRDYNTDILYVDAGGTEMVILNTLETITDLLEKRGSIYSGRLESTMVNELMGWEFDLGFITYGDRWREERRMFAKEFSEKGIKQFRHAQVKAAHQLVQQLTKTPDRWAQHIRHQIAAMSLDIGYGIDLAEDDPWLEATHLANEGLAIASVPGKFWVDSFPSLKYLPAWFPGAVFKRKAKVWREAADHMVDMPYETMRKLAPQGLTRPSYASARLQAMDLNGDLEHQEHVIKNTAAEVNVGGGDTTVSAMSAFILAMVKYPEVQRKVQAELDALTNNGQIPDYDEEDDSLPYLTACIKELFRWNQIAPLAIPHKLMKDDVYRGYLIPKNTLVFANTWAVLNDPEVYPDPSVFRPERYLGPDGKPDNTVRDPRKAAFGYGRRNCPGIHLAQSTVWIAGATLLSAFNIERPVDQNGKPIDIPADFTTGFFRHPVPFQCRFVPRTEQVSQSVSGP | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product . The first step in the pathway is the decarboxylation of L-tryptophan to tryptamine by the decarboxylase psiD . 4-hydroxy-L-tryptophan is accepted as substrate by psiD as well . The cytochrome P450 monooxygenase psiH then converts tryptamine to 4-hydroxytryptamine . The kinase psiK catalyzes the 4-O-phosphorylation step by converting 4-hydroxytryptamine into norbaeocystin . The methyltransferase psiM then catalyzes iterative methyl transfer to the amino group of norbaeocystin to yield psilocybin via a monomethylated intermediate, baeocystin .
Catalytic Activity: AH2 + O2 + tryptamine = 4-hydroxytryptamine + A + H2O
Sequence Mass (Da): 57515
Sequence Length: 508
Pathway: Secondary metabolite biosynthesis.
EC: 1.14.99.59
|
P0DPA8 | MAFDLKTEDGLITYLTKHLSLDVDTSGVKRLSGGFVNVTWRIKLNAPYQGHTSIILKHAQPHMSTDEDFKIGVERSVYEYQAIKLMMANREVLGGVDGIVSVPEGLNYDLENNALIMQDVGKMKTLLDYVTAKPPLATDIARLVGTEIGGFVARLHNIGRERRDDPEFKFFSGNIVGRTTSDQLYQTIIPNAAKYGVDDPLLPTVVKDLVDDVMHSEETLVMADLWSGNILLQLEEGNPSKLQKIYILDWELCKYGPASLDLGYFLGDCYLISRFQDEQVGTTMRQAYLQSYARTSKHSINYAKVTAGIAAHIVMWTDFMQWGSEEERINFVKKGVAAFHDARGNNDNGEITSTLLKESSTA | Function: 4-hydroxytryptamine kinase; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product . The first step in the pathway is the decarboxylation of L-tryptophan to tryptamine by the decarboxylase psiD . 4-hydroxy-L-tryptophan is accepted as substrate by psiD as well . The cytochrome P450 monooxygenase psiH then converts tryptamine to 4-hydroxytryptamine . The kinase psiK catalyzes the 4-O-phosphorylation step by converting 4-hydroxytryptamine into norbaeocystin . The methyltransferase psiM then catalyzes iterative methyl transfer to the amino group of norbaeocystin to yield psilocybin via a monomethylated intermediate, baeocystin . 4-hydroxy-6-methyl-l-tryptophancan also be converted the decarboxylase PsiD, kinase PsiK, and methyltransferase PsiM into respectively 6-methyl-norbaeocystin, 6-methylbaeocystin, and 6-methylpsilocybin . PsiK kinase can also turn psilocin into psilocybin . This activity may represent a protective mechanism to rephosphorylate the unstable psilocin to the stable psilocybin in case of intracellular ester cleavage . Moreover, psiK is able to O-phosphorylate the quaternary amine 4-hydroxy-N,N,N-trimethyltryptamine (4-OH-TMT) to yield aeruginascin, another bioactive compound found in Psilocybe species .
Catalytic Activity: 4-hydroxytryptamine + ATP = 4-hydoxytryptamine 4-phosphate + ADP + H(+)
Sequence Mass (Da): 40442
Sequence Length: 362
Pathway: Secondary metabolite biosynthesis.
EC: 2.7.1.-
|
P0DPA9 | MHIRNPYRTPIDYQALSEAFPPLKPFVSVNADGTSSVDLTIPEAQRAFTAALLHRDFGLTMTIPEDRLCPTVPNRLNYVLWIEDIFNYTNKTLGLSDDRPIKGVDIGTGASAIYPMLACARFKAWSMVGTEVERKCIDTARLNVVANNLQDRLSILETSIDGPILVPIFEATEEYEYEFTMCNPPFYDGAADMQTSDAAKGFGFGVGAPHSGTVIEMSTEGGESAFVAQMVRESLKLRTRCRWYTSNLGKLKSLKEIVGLLKELEISNYAINEYVQGSTRRYAVAWSFTDIQLPEELSRPSNPELSSLF | Function: N-methyltransferase; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product . The first step in the pathway is the decarboxylation of L-tryptophan to tryptamine by the decarboxylase psiD . 4-hydroxy-L-tryptophan is accepted as substrate by psiD as well . The cytochrome P450 monooxygenase psiH then converts tryptamine to 4-hydroxytryptamine . The kinase psiK catalyzes the 4-O-phosphorylation step by converting 4-hydroxytryptamine into norbaeocystin . The methyltransferase psiM then catalyzes iterative methyl transfer to the amino group of norbaeocystin to yield psilocybin via a monomethylated intermediate, baeocystin . 4-hydroxy-6-methyl-l-tryptophancan also be converted the decarboxylase PsiD, kinase PsiK, and methyltransferase PsiM into respectively 6-methyl-norbaeocystin, 6-methylbaeocystin, and 6-methylpsilocybin .
Catalytic Activity: 4-hydoxytryptamine 4-phosphate + S-adenosyl-L-methionine = 4-hydroxy-N-methyltryptamine 4-phosphate + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34434
Sequence Length: 309
Pathway: Secondary metabolite biosynthesis.
EC: 2.1.1.-
|
P61289 | MASLLKVDQEVKLKVDSFRERITSEAEDLVANFFPKKLLELDSFLKEPILNIHDLTQIHSDMNLPVPDPILLTNSHDGLDGPTYKKRRLDECEEAFQGTKVFVMPNGMLKSNQQLVDIIEKVKPEIRLLIEKCNTVKMWVQLLIPRIEDGNNFGVSIQEETVAELRTVESEAASYLDQISRYYITRAKLVSKIAKYPHVEDYRRTVTEIDEKEYISLRLIISELRNQYVTLHDMILKNIEKIKRPRSSNAETLY | Function: Subunit of the 11S REG-gamma (also called PA28-gamma) proteasome regulator, a doughnut-shaped homoheptamer which associates with the proteasome. 11S REG-gamma activates the trypsin-like catalytic subunit of the proteasome but inhibits the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits. Facilitates the MDM2-p53/TP53 interaction which promotes ubiquitination- and MDM2-dependent proteasomal degradation of p53/TP53, limiting its accumulation and resulting in inhibited apoptosis after DNA damage. May also be involved in cell cycle regulation. Mediates CCAR2 and CHEK2-dependent SIRT1 inhibition .
PTM: Phosphorylated by MAP3K3 (By similarity). Phosphorylation at Ser-247 promotes its association with CCAR2.
Sequence Mass (Da): 29506
Sequence Length: 254
Domain: The C-terminal sequences affect heptamer stability and proteasome affinity.
Subcellular Location: Nucleus
|
Q9GP84 | MRFISIFLIIVALCVSSSWAFNFTDQPNSFRISGTGCGSGTTTVYFSTDGRCNSACGGSIRIKGEGNNVPNQQFTLNDYSKNVTNCSGTSNVASFRCPALVNTTSPTFTVNVGNSAYHVTCQYAQVTETPAGNSADKVAVGIAIIFGALISLLAL | PTM: The GPI-like-anchor contains a phosphoceramide group, rather than a phosphatidyl group.
Location Topology: Lipid-anchor
Sequence Mass (Da): 16273
Sequence Length: 155
Subcellular Location: Cell membrane
|
P23857 | MFKKGLLALALVFSLPVFAAEHWIDVRVPEQYQQEHVQGAINIPLKEVKERIATAVPDKNDTVKVYCNAGRQSGQAKEILSEMGYTHVENAGGLKDIAMPKVKG | Function: The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspE catalyzes the sulfur-transfer reaction from thiosulfate to cyanide, to form sulfite and thiocyanate. Also able to use dithiol (dithiothreitol) as an alternate sulfur acceptor. Also possesses a very low mercaptopyruvate sulfurtransferase activity.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 11475
Sequence Length: 104
Subcellular Location: Periplasm
EC: 2.8.1.1
|
P32696 | MLELLFVIGFFVMLMVTGVSLLGIIAALVVATAIMFLGGMLALMIKLLPWLLLAIAVVWVIKAIKAPKVPKYQRYDRWRY | Function: Effector of the phage shock response.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 9023
Sequence Length: 80
Subcellular Location: Cell inner membrane
|
P94512 | MKAVFFDLDDTLLWDEKSVRTTFAETCLQAEKKYGLAPEEFEAAVREAARELYMSYETYPYTVMIGINPFEGLWSNFSEPISEGFQKLNKIVPEYRRNAWTNGLKALGIDDPAYGEYLGEFFAAERRKRPFVYDETFAVLDQLKGKYELLLLTNGDPSLQKEKLAGVPELAPYFNEIVISGAFGKGKPDVSIFEHCLKLMNIEKDDAIMVGDNLNTDILGASRAGIKTVWINRTDKKNETDVKPDYIISSLHDLFPILEK | Function: Catalyzes the last step of the phosphorylated serine biosynthetic pathway, i.e. dephosphorylation of O-phospho-L-serine to form L-serine. To a lesser extent, is also able to dephosphorylate phosphothreonine, phosphoethanolamine, and histidinol phosphate in vitro.
Catalytic Activity: H2O + O-phospho-L-serine = L-serine + phosphate
Sequence Mass (Da): 29581
Sequence Length: 260
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
|
Q72H00 | MKLLLLDLDDTLLQDLPVSRAVLEDLGRKAGVEGFFARVKARAEALFREAPFYPWAEAIGHSALEALWARYSTPGLEALAAWAGPFRERVFREALEEAGGAPERARELAEAFFRERRRYPLYPEAEAFLAEARRRGLALALLTNGVPDLQREKLVGAGLAHHFSLVLISGEVGIGKPDPRLFRMALCAFGVAPEEAAMVGDNPQKDVRGARLAGVRAVWVDRGLRPEDPEASPDLRVGDLREVFLAEAL | Function: Catalyzes the last step of the phosphorylated serine biosynthetic pathway, i.e. dephosphorylation of O-phospho-L-serine to form L-serine. Is also able to dephosphorylate O-phospho-D-serine with similar efficiency. Displays a poor activity on L-phosphothreonine, and cannot use L-phosphotyrosine, pyridoxal phosphate, glucose 6-phosphate, or fructose 6-phosphate as substrates.
Catalytic Activity: H2O + O-phospho-L-serine = L-serine + phosphate
Sequence Mass (Da): 27436
Sequence Length: 249
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
|
G4YRX5 | MRLTYVLLVAVTTLLVSCDATKPSTEATAVSKRLLRFVEAADEEERRIDFSPEKLRKMLGDETYRLKKFGKWDSDGHTFDGLKHYLLLSDSSMVKLRNMYKAWLEQ | Function: Secreted effector that possesses RNA silencing suppression activity by inhibiting the biogenesis of small RNAs in the host plant to promote enhanced susceptibility of host to the pathogen during infection . Interferes with secondary siRNA production by associating with host nuclear protein PINP1 that acts as a regulator of the accumulation of both microRNAs and endogenous small interfering RNAs .
Sequence Mass (Da): 12304
Sequence Length: 106
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellular Location: Secreted
|
Q07800 | MGFISSILCCSSETTQSNSNSAYRQQQSSSLNKNRSVKHSNTKSRTRGVHQTNSPPSKTNSAATFSSTERSTGKSGISTNDNEKKKPSSPTAAVTATTTNNMTKVEKRISKDDLYEEKYEVDEDEEIDDEDNRRSRGIVQEKGDAVKDTSRQKKQQQQQQQQSQPQPQPQSQSQSQSQSQSQQRGPTVQVSSDHLIQDMNLSRVSSSSQASETSNDADDEDDEDEEYIDLTLLQQGQYHAPGYNTLLPPQDESTKGKKCLILDLDETLVHSSFKYLRSADFVLSVEIDDQVHNVYVIKRPGVEEFLERVGKLFEVVVFTASVSRYGDPLLDILDTDKVIHHRLFREACYNYEGNYIKNLSQIGRPLSDIIILDNSPASYIFHPQHAIPISSWFSDTHDNELLDIIPLLEDLSVKTSLDVGKILDVTI | Function: Has phosphatase activity in vitro. Involved in the response to sodium and lithium ion stress (but not to potassium or sorbitol stress) by inducing transcription of the sodium pump ENA1/PMR2. Acts through a calcineurin-independent pathway and is functionally redundant with PSR2. Also involved in the general stress response; acts together with WHI2 to activate stress response element (STRE)-mediated gene expression, possibly through dephosphorylation of MSN2.
Sequence Mass (Da): 47931
Sequence Length: 427
Subcellular Location: Cell membrane
EC: 3.1.3.-
|
D0NRS4 | MGCRYAVLALAVAYFAGSIAANDSQIVAVKGPASIRFTPAIHVVRGRFLRAANTADERNEDRGINLKSMPGFEKIASLFTKKNTPGPLLSWFEKKKSPDYVFLKLKINKGKQQLFDHPDWNVWVQYTTSVVKSDPEEAMIAALRTHYTDDILSKLLESAKNVPKTSGLATKMQMEHWVASKTPSQMFQFLRLDKVRNGVLDDPTLSIWINYMKLYNSKPVNKKQQVTLVSMLTTHYKDRGVLDIIEAAKKVPKTAPAARQLEMEQIQFWLKNGKSPDELLTVLSLDKAGNQLLASPRFKFWSKYVDNYNRDFPDEATTVMATLRNQLGDEDITPILIAAGKVPSTEKAAAKLQAEQFKSWLRENEDPAKVFQLLKLDNSADDLLGSPQFKLWGKYVEDLNLKPEHNDLQVSIITILRKNYGDDVLGNMVLAGKKAPSTSFMARRLEDELYKGWIAAGSSPDGVFKHLKFDKAGENVIQSPLWGLYTKFLEHYYKSFPTPMMSALAKGYDGDALAKLLIAAEKIPTSNTLATKLQTGQIQRWLDDKDQPGKIFKALLLDDMADDILTSPLFNTWTRYLDEFNKKFPDEKVSMTDTFRTSLDDETLKSLLITAKELPDMKTLSTKLQTVQIERWLASKTSPEDAFAVLALNKAGGNVLSKPLLNTWAAYLESFNAKFPRSRVSMIDTFREFFGDKALLTTLAAAKEVESTKKVATSLQDSLLSKWVLAKKPPSGVAKLVGTDEAGAKLLKTYTTKYMERYGQ | Function: Secreted effector that possesses RNA silencing suppression activity by inhibiting the biogenesis of small RNAs in the host plant to promote enhanced susceptibility of host to the pathogen during infection . Interferes with secondary siRNA production by associating with host dsRNA-binding protein DRB4 (By similarity). Inhibits the host salicylic acid pathway during infection (By similarity).
Sequence Mass (Da): 85357
Sequence Length: 760
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellular Location: Secreted
|
G5ADB3 | MRLQCVVLFAALTLVAATHAPPNVKTVLSAEQHDIPVKRLLRPGNPAGKEDEERGINFSSVPGFEKLANLLKPKPGLKKLLKWADAKKPPETVFTRLRLDKTGTQLFDNTDFPVWAAYTRSVAQTDSEASAVMLKTLVSRYSDEVLSGMIAAAKKSSKTESIATKLETEQMRTWLAAKKTPDDMFLVFKLNKAGDDILSSPLLSAWTNYMKLSNKENPKAQTTLIATMTKHYGDSGVSQILAAARKSPATQSTAKRLEAEQVQLWLKKGRTPDDTFTLLSLDRAGDDLLASPQFNTWMKYINYYNKENPDEKTTVLAKLMTHFDDEELTPILVVARKVPSTESTAAKLQAEQFKNWLSADKSPEEAFTLLQLDKAGDDLLTNPQLTNWLKYTENFNLNKEINEQVTAIQVFRAQYVDDSRIANMVIAAEKVPNTQAIAKRVEDELFKGWTVVLNKPDDVFINLKLETVGENVFESPLWSFYTKFLEKYNTANPGKEQTMISGLARGYNDVTLTNMLLKAKEAPSTKTLATKLEDELVQYWLADKKLPDKLFGYLELKESVDGILTNPVFNVWLKYLNAFNDKAPVKKALMIDTLKSAFGDVAVSNMLFAAKKDPGTAKVAATLQTALLSKWVLEKKTPGQVSAILKEGAGADVSAKLLATYSAKFKVRWG | Function: Secreted effector that possesses RNA silencing suppression activity by inhibiting the biogenesis of small RNAs in the host plant to promote enhanced susceptibility of host to the pathogen during infection . Interferes with secondary siRNA production by associating with host dsRNA-binding protein DRB4 . Inhibits the host salicylic acid pathway during infection .
Sequence Mass (Da): 74613
Sequence Length: 670
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellular Location: Secreted
|
Q07949 | MGFIANILCCSSDTSKTHRQRQPPETNHNRNRNRKHSSNKAQTQGRKQKATPNGDKMQYSTPEILLSSSDSGSNAGSKTMQENGNSGNGKLAPLSRDHSNNSYDEEKEYEDYNEGDVEMTEVNNAGEEEEEDDEAKEKQDHVVHEYNVDADRNSSINDEAPPQQGLYQVGQEDMNPQYVASSPDNDLNLIPTTEEDFSDLTHLQPDQYHAPGYDTLLPPKLQEFQQKKCLILDLDETLVHSSFKYMHSADFVLPVEIDDQVHNVYVIKRPGVDEFLNRVSQLYEVVVFTASVSRYANPLLDTLDPNGTIHHRLFREACYNYEGNYIKNLSQIGRPLSETIILDNSPASYIFHPQHAVPISSWFSDTHDNELLDIIPLLEDLSSGNVLDVGSVLDVTI | Function: Probable phosphatase. Involved in the response to sodium and lithium ion stress (but not to potassium or sorbitol stress) by inducing transcription of the sodium pump ENA1/PMR2. Acts through a calcineurin-independent pathway and is functionally redundant with PSR1. Also involved in the general stress response; acts together with WHI2 to activate stress response element (STRE)-mediated gene expression, possibly through dephosphorylation of MSN2.
Sequence Mass (Da): 44772
Sequence Length: 397
Subcellular Location: Cell membrane
EC: 3.1.3.-
|
P31075 | METTMTRRDFLKSAGAAGAAGLVWSQTIPGTLGALEKQEIKGSAKFVPSICEMCTSSCTIEARVEGDKGVFIRGNPKDKSRGGKVCARGGSGFNQLYDPQRLVKPIMRVGERGEGKWKEVSWDEAYTFIAKKLDEIKQKHGAHTVAFTARSGWNKTWFHHLAQAYGSPNIFGHESTCPLAYNMAGRDVFGGSMNRDFAKAKYIINMGHNVFEGIVISYVRQYMEAIENGAKVVTLEPRLSVMAQKASEWHAIKPGHDLPFVLGFMHTLIFENLYDKKFVQKYCTGFEELKASIEPCTPEKMALECDIPADTIKRLAREFAKAAPKAIFDFGHRVTFTPQELELRRAMMMVNALVGNIERDGGMYFGKNASFYNQFLGEEDPKAKGLKKPKTPAYPKVEVPRIDRIGEKDGEFFLANKGEGIVSLVPKATLNELPGVPCKIHGWFIVRNNPVMTQTNADTVIKALKSMDLVVCVDIQVSDTAWFADVVLPDTTYLERDEEFTAGGGKNPSFGIGRQKVVEPLGDAKPGWKIAKELSEKMGLGEYFPWKDIEDYRLQQVDGDLDLLAKLKKDGSASFGVPLMLQEKKSVAEFVKKFPGAASKVNEEGLIDFPKKIQLFSPKLEEVSGKGGLGYEPFKYKEEDELYFVQGKTPVRSNSHTGNVPWLNNLMEYDAIWIHPKTASKLGIKNGDAIELYNKFSSQKSKALITEGVREDTLFGYFGFGHVSKDLKRAYGKGVNSNALMPSFTSPNSGMDLHVFGVKVKKA | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Component of the phosphorylative electron transport system with polysulfide as the terminal acceptor.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Sequence Mass (Da): 84751
Sequence Length: 763
|
P08456 | MVESDEDFAPQEFPHTDTDVIVNEHRDENDGYASDEVGGTLSRRASSIFSINTTPLAPPNATDIQKFTSDEHHFSMMRNLHMADYITMLNGFSGFYSIVSCLRFTLTGKPHYVQRAHFFILLGMCFDFLDGRVARLRNRSSLMGQELDSLADLVSFGVAPAAIAFAIGFQTTFDVMILSFFVLCGLARLARFNVTVAQLPKDSSTGKSKYFEGLPMPTTLALVLGMAYCVRKGLIFDNIPFGIFREDQILEFHPIILVFFIHGCGMISKSLKIPKP | Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30805
Sequence Length: 276
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 1/2.
Subcellular Location: Microsome membrane
EC: 2.7.8.8
|
Q12355 | MQLHSLIASTALLITSALAATSSSSSIPSSCTISSHATATAQSDLDKYSRCDTLVGNLTIGGGLKTGALANVKEINGSLTIFNATNLTSFAADSLESITDSLNLQSLTILTSASFGSLQSVDSIKLITLPAISSFTSNIKSANNIYISDTSLQSVDGFSALKKVNVFNVNNNKKLTSIKSPVETVSDSLQFSFNGNQTKITFDDLVWANNISLTDVHSVSFANLQKINSSLGFINNSISSLNFTKLNTIGQTFSIVSNDYLKNLSFSNLSTIGGALVVANNTGLQKIGGLDNLTTIGGTLEVVGNFTSLNLDSLKSVKGGADVESKSSNFSCNALKALQKKGGIKGESFVCKNGASSTSVKLSSTSKSQSSQTTAKVSKSSSKAEEKKFTSGDIKAAASASSVSSSGASSSSSKSSKGNAAIMAPIGQTTPLVGLLTAIIMSIM | Function: Has a partially redundant function to ECM33 in cell wall integrity. May be involved in a repair mechanism activated in response to cell wall damage.
PTM: Extensively N- and O-mannosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 45777
Sequence Length: 444
Subcellular Location: Cell membrane
|
Q39195 | MASMTMTATFFPAVAKVPSATGGRRLSVVRASTSDNTPSLEVKEQSSTTMRRDLMFTAAAAAVCSLAKVAMAEEEEPKRGTEAAKKKYAQVCVTMPTAKICRY | Function: May be a component of the oxygen-evolving complex.
PTM: The maturation of the PSII-T precursor to its final form occurs through a two step process. First, a stromal intermediate is formed, which, upon translocation into the thylakoid membrane, is processed to the mature protein (By similarity).
Sequence Mass (Da): 11028
Sequence Length: 103
Subcellular Location: Plastid
|
B3EWI4 | MASITMMSSFLGGSTVAPAKVPSANRRGVVMVKAMHEGENNVVISKNEESKNSGRRELFFAMAAAAACSVAKTAMADEEPKRGTPEAKKKYSSVCVTNPTARICRY | Function: May be a component of the oxygen-evolving complex.
PTM: Disulfide bond.
Sequence Mass (Da): 11317
Sequence Length: 106
Subcellular Location: Plastid
|
P9WG11 | MSPSMSIEALDQPVKPVVFRPLTLRRRIKNSVATTFFFTSFVVALIPLVWLLWVVIARGWFAVTRSGWWTHSLRGVLPEQFAGGVYHALYGTLVQAGVAAVLAVPLGLMTAVYLVEYGTGRMSRVTTFTVDVLAGVPSIVAALFVFSLWIATLGFQQSAFAVALALVLLMLPVVVRAGEEMLRLVPDELREASYALGVPKWKTIVRIVAPIAMPGIVSGILLSIARVVGETAPVLVLVGYSHSINLDVFHGNMASLPLLIYTELTNPEHAGFLRVWGAALTLIIVVATINLAAAMIRFVATRRRRLPL | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33498
Sequence Length: 308
Subcellular Location: Cell membrane
|
P0A627 | MGESAESGSRQLPAMSPPRRSVAYRRKIVDALWWAACVCCLAVVITPTLWMLIGVVSRAVPVFHWSVLVQDSQGNGGGLRNAIIGTAVLAIGVILVGGTVSVLTGIYLSEFATGKTRSILRGAYEVLSGIPSIVLGYVGYLALVVYFDWGFSLAAGVLVLSVMSIPYIAKATESALAQVPTSYREAAEALGLPAGWALRKIVLKTAMPGIVTGMLVALALAIGETAPLLYTAGWSNSPPTGQLTDSPVGYLTYPIWTFYNQPSKSAQDLSYDAALLLIVFLLLLIFIGRLINWLSRRRWDV | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32236
Sequence Length: 301
Subcellular Location: Cell membrane
|
P07654 | MAMVEMQTTAALAESRRKMQARRRLKNRIALTLSMATMAFGLFWLIWILMSTITRGIDGMSLALFTEMTPPPNTEGGGLANALAGSGLLILWATVFGTPLGIMAGIYLAEYGRKSWLAEVIRFINDILLSAPSIVVGLFVYTIVVAQMEHFSGWAGVIALALLQVPIVIRTTENMLKLVPYSLREAAYALGTPKWKMISAITLKASVSGIMTGILLAIARIAGETAPLLFTALSNQFWSTDMMQPIANLPVTIFKFAMSPFAEWQQLAWAGVLIITLCVLLLNILARVVFAKNKHG | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32322
Sequence Length: 296
Subcellular Location: Cell inner membrane
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.