ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A7F9L8 | MDAFRGYLAAQKGQHNQAASNNPPFHSDHEMHHYGAHPNTNAAPADDYYTPYLGLRARLSQTWINRWTILLLLIIVRLLISLSTINGDIASAKTEALSACTSVENVGSAMASMPHYLSQGVNSMAAAGITKAVNGMMEMLYLTLTGVEEIVLFVIHMMTSTYMCLITLAITGSLQVAIQMIEDVGAFMNKSIDTITGDMSSGLKSFEDDLNGFLSKINIGGIFGSSTSPPKIDLSSEINKLNSIQIDPSTMDADLAKLNASLPTFDQVQNFTDSIIKLPFEEVKKLVNESKIGYKFDDSVFPVPQKKSLTFCSDNTAIQDFFIGLVKTLNIAKKIMLIVLIIAAILACVPMAYREIWGWRSMQRRAALLKAHNYTNELDILYQAHRPYTSQFGLKLSRRFKGQKNQILARWFIAYATSIPALFVLALGMAGLFTCLCQFIILRTIEKEIPALAAEVGDFAEHVVQALNNASEAWALGANSVINNTNTDINENVFGWVNTTTGAINETLNVFTDEMTKALNVTFGGTILYKPIMGVFECLVGLKVAGIEKGLTWVSDHAHVEFPEFQPDVFSLGAAASLTNSTADDNFLANPATSTTDEITDAVVKVGKKLEAVIKQEALISASLVIVYFVIVFIGFVRVVIGMCGRDKSRAEGGSGPGTLYRNGFPHQHLPVIREEKFGSNASDGWHEEHMRAGGDTIRMPFGGDGAADDLPYDGAPAPKYEASIAPVTTEMGSERLGVVPGGRANTNRGPWVRDEKGREGWEADDAQMRATSSYGFLENGDEKSSGWGLPPRRV | Function: Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 86696
Sequence Length: 795
Subcellular Location: Cell membrane
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Q4P996 | MSFHPNAVDAPPSYLHQHQAGSPLYTQNTIRPNANSTDLNSPHKPPILQPWLGLQARLFLAPISIPLISLLFVAARMLSSSNEATDSISSAKGKLLSACSAAEGTASLAASFPHFLAASTNVQLALSVTATVHSAARVFDLSMTAIQKILTYIVNSYKSLFMCFMELLVRGALAVLITAVEFISQAITAATLGIRSAIQESITGVNTLLATAVGAINDVIGVFGQHVNPPHIAVPSLTSLENITLPHEIQDGLVKLNATLPTLQQLKQSMDALIETPFEEMKREVNATLASFQFNHSVFPVPEMQNVTFCDRIDTSPLDELGNALKNVARWGLVALLLIAIVVMLIGVAWEWWKWQKEVKAVERTRSLWLAQRSSAHSDGNDKFCDNILKTENLMSLLTISQHPLISFCSLNYCKRLGIRTRRAQDRCAWLLSFLMHPASLACLFTGVLGLISVLMQAILVHSLSHHYVSSIDTSLAHLSSDIVNLVHDHTRNASVAFSTSANTVILQVEAELNDHVFRWVDTTTSTMNSTLNQFVDGLTETLTSTFGGTPFNAPLQTFVQCILGQKVQGIEKALTWIHENAYVNFSVVPADVLMLRPEQQEAVLRPVREAMLGSRDDQGGGNGVVGHVISRYMEHLHQEKILFTALIGVYAIILLIGLLAVLYATLAERRMHDDDETRKKVSRDESEEKLRSDLQAGPGGAGIARLWSRRPKLNAGCFRAFSHPPVPVSAQNPSSKIDHAARFPSSAHSSRPDPIHVTKDSISYPFQMHHSLNTSPSTRPTQPTPLQQTSNPDRDTVQSLHHASTTHNQTASTRTKEYDSWLCFLASYHDGEATVPAKAPEAVEGAQDRFHRLFGCSLRASPTVATFNHHVSAPAVSSDRAEIEVEDARFRETLDLGSMQDWIGSKSPIPPPAGRGGSHSPRNTADQLPEVQLTRSGGCVGPHSSDSTQETYAFTDSVRLPPGPQPQQKRVVSSQSISFFAW | Function: Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 107499
Sequence Length: 983
Subcellular Location: Cell membrane
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Q6C6L1 | MAMSLASQIKLWWNTQNSPTEHSSIPLLKARLSQTWLNKWTIGLLLVSIKLWMFKMSLSGQLDGAESNSERSCSALERSVSKMMSIPHYTATGMNHVIATAIQKFVSGLIKMVLLIITGVQELLIFAVNMLISTYTCLITLVVQGAVSLAVDTSKHVISFVNDTISTVVPEIEKGLNGLADGLNTATNAFVDLGNLITGKQAEEYTGQIDFVKLQLDGLKNVSIPASVNEKLDSVKDKVPDFETVKNEIESLIRKPFQTISKSMNETLATPLNVSDSLKVPALKSAQFCKDANIPEVYAKLNSGLNTGLKVIISLLLILALIMIVPVAWSEWRLWRYHEELWVEQSTVDVKQEKRHAFHTVLFQAQHKYVTMVKQKLAWGKKLYQRNLSQWYWAYILYPYMLTLLLVGLFGILAFLLQLGLLSILKSGLQSLTVPTSEVGADVTETVVREIETWKNDTNLFLNSQETHINKNLLGWVVDSTSTVNTTLSTFIDTMNNGIDSVFKDTPLHGAVQGVTKCLVTLKLQKVADGMGWVSDNAHVTLPRIDKELMSHQDIEQEASEKADYVSDGIARIIKTVEKLLFTELYIALACLGIWLFMCLIALVYVLIKSRDRTTNFEPSRELKFDMVDTSRDINVPRVLPPQITIPKPALFMRNHIPSPATDPFEEYPIRRNKSSSWLFNLKSPVLRKS | Function: Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 77376
Sequence Length: 690
Subcellular Location: Cell membrane
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P53835 | MSGFKCYLQLGDRLSQIWLNKYTLVLLLAMLKLLFFSKSIQHAIEVSETYILSNCYSIDSLYSKMTDNTPHYLGIMGNYLIEKGMEETVKATLETLSLIVYASEGLVNFAIDLYLGTYACLIVSAVDGTVDVATNITEKLISLVNDTVSSVANELDTGLNDISKIINKVIKAASKVENFFTGDDDDSNMTSSIKSVNLTISALHNLYIPSSINDKLEELSAKTPDFAQVKNTTKNLISVPFNEVRKNIKAVNASNIIGDTSVLYVPPVSLDNSTGICSSNQSEILAFYSILGHVLKIATVVCITVLICFAVGAMAPVAWNEIKLWRRLCGMRDHYMLSRQDSYTSFSSENTHELKDPFRDPPIQNGQYDVIASYQQCFQTWNTRIAGWMTNLVTFGKSPENIDPKTKQKIEWVVAYMTSERALCVLGIGLLGILVCICQFVMIALLKHKISHSLTSNDGDGVQNLLKSSTAVDIENQMSLWSVQTNKYINTTETNINQEVFGWINTTTLSVNNTVATMISDIDTTLADVFNGTLLYNPMKTVVGCAIENKLYTIEKAMTWIHDKAQLHIPRINGTQIKQALAKQTDNSTIPTASSTSAATENLLENLVNDMREGLLKILRAYHRITLGELTVALVILAVWLVQLPIALVILRLRLRKATFD | Function: Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73353
Sequence Length: 661
Subcellular Location: Cell membrane
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P19782 | MVRCHVKSPTESPPGQQGSGQQGETEHPDQARELRPEDIPVYGRTHRGRYHYRHRSHTRRRPYRRRRRRACRHRRRRRGAAGPPCAPIPGTPQASRQGSGCRRMRRRRRRCGRQL | Function: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex.
PTM: Proteolytic processing into mature chains is required for histone eviction during spermatogenesis. Transition proteins (TNP1 and TNP2) are required for processing.
Sequence Mass (Da): 13646
Sequence Length: 115
Subcellular Location: Nucleus
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Q28337 | MVRYRVRSPSERPHEEYRQLVNWQEQGRNGQEEQGLSAEGGEVYGRTHQGYSSYRRRRCSRRRRYRIHRRRSRSCRRRRRRSCRYRRRPRRGCRSRRRRRCRRY | Function: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex.
PTM: Proteolytic processing into mature chains is required for histone eviction during spermatogenesis. Transition proteins (TNP1 and TNP2) are required for processing.
Sequence Mass (Da): 13372
Sequence Length: 104
Subcellular Location: Nucleus
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P04554 | MVRYRVRSLSERSHEVYRQQLHGQEQGHHGQEEQGLSPEHVEVYERTHGQSHYRRRHCSRRRLHRIHRRQHRSCRRRKRRSCRHRRRHRRGCRTRKRTCRRH | Function: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex.
PTM: Proteolytic processing into mature chains is required for histone eviction during spermatogenesis. Transition proteins (TNP1 and TNP2) are required for processing.
Sequence Mass (Da): 13051
Sequence Length: 102
Subcellular Location: Nucleus
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Q9RU72 | MLVYLLPGSFDTREAHLDLLWEAGATGLEERGPNIRVYFDERTELPAEVADGEWHEEAEQDWQAEFKKNLRPVHAGRVTIVAPWQREEVPAGQLALVIEPGMAFGTGHHATTRMAVEALGELDLSGKRVLDVGTGSGVLAMAAAKLGAAQTLGVDIDPITIPIARDNARDNGLTSGIRFEEGTLGLDEDAEMFGEPYDVLVANLYAELHDLLAGEYAAQLRPGAPLILTGILTSKLPLVRDALDREGFTDVQVRTDSEGAGGEWALVTARRED | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 29548
Sequence Length: 273
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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C0QLV7 | MKWIHVNARFEADDMALAEELVAQIFFDLDLKGVVCEVPLPEPDEGFGSNALAQPDTHSISGYLPDLSTSDLLFADIKKKADALKGINVTLSTRIVDDQDWAESWKDFFFVTRITDTLVIRPSWREFEPKPGDVVIDLDPGMAFGTGTHETTAMCLALVQEQITPGASFLDVGTGSGILMIAAAKLGAGTLKGLDNDEAAVQIAGKNLEHNRISPQSFEIRCTTLDRYPHEKFDLVVANILAEVIISILPEIHSRLAPGGRAILSGIIIAWEERVKTALEDNGFTLVKTTTQGEWVALVAELV | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 33058
Sequence Length: 303
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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B8FBE9 | MQWMEIKIVFDAAEPELAQEMVSYLVMEHGAEGLEMTTPGETGMVQDGSGSSVPDSKEHSVTAFLPLDDLFEGRKADLTRALDDLKGSVLTDYSVHFSKQDDQPWETAWKAHFHPIEIGESLVIKPSWEDYENPEKRMLIELDPGMAFGTGTHPTTAVCLEMIETECLKKAPERFLDVGTGSGILMIGAYKLGARKVFGCDNDMDALEAAAKNLKGNQVHEGDFGLWLGDLLAGIVEGAFDMVAANITAEANVMLIPGLPRIMAPGSIFIASGIMAEKKDLVLEALDACRFSVERVQETGGWVGIAARMP | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 33723
Sequence Length: 310
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q24SS5 | MNWREIAVTVSSAGEEAVADLFYQLGCPGVSVEDPELLQSYVESGNWDYHDFGEIALTGTSVVKGYICEDHELQPKLRQLDEGLKELLQRFPEWVLQVKGLTVQEEDWATSWKAYFKPVRIGRHFLIKPSWEEVTPLPEDIILELDPGMAFGTGTHATTSLCLETLEETVKPDMRIFDLGTGSGILAIAAAKLGAQVEAIDLDSVAVKVAQENVELNQVADRISVRQGDLGTVLQGQADLVVANIIADVILMLIPDLKRIMKEDGEFLASGIIGHRSSDVEAGLGEHGLEVLEKKEDSGWVLLRARWQRASL | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 34405
Sequence Length: 312
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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A8ZW25 | MQWLEAGIVFETEDLFAQTAAELVCNIFYDLGLSGVVTEDPVPVSDHGVRGRVIGYLPVDEALEQTRADLEQMASGLSARHPVRCTLEFTPCDDQDWANAWKDHFFVQKIGRNIVVRPTWRDHVPEPGEVVIDLDPGMAFGTGTHPTTAMCLEMVEKHLAPGTAFLDVGTGSGILMIAAQKLGAKTVWGVDNDGVAVKIAAENLERNGIFAGGNACRIMRADLVTGVDRAFDLVTANILSEVIVALADDVGRVVVPGGLLVCSGIIEPKQAMVEAKLTACGFDIIERKTTDLWVCLVARRTP | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 32596
Sequence Length: 302
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q6AQF1 | MHTMKKWLKISIEANPLMVEVVSDYLVGIHGAGVDLAADKDENPAGQIVAFIEQAELSTADAEKCATQISVFLAEMAAVFNVASPSLVWEFLEEEDWSKNWKEHFVPFTIVPGLIIAPTWENYEAQGDELVIEMDPGMAFGTGHHATTSLSLSYLQDVVTQRGAKTVLDVGCGTGILVMGAVLFGAERGLGIDNCPDAVAAASNNVVHNHLAEKIDIGITPLSELREEYDLVVANIIHDVLASMVLELYSRVKKEGHLILSGLLADQQVDSIIEIFAREGFVLLEKGIEGEWGAVLLQKR | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 32623
Sequence Length: 300
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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A4J7F1 | MNWLEIAVHVCPEGIDMVSNIFDELGAGGVVIEDPALINRYIEANIWDHYEFPPEVLNRPQPIVKAYLPEGPNLENKLVLLQERLTGLPLDAVPTFERRQVAEEDWATAWMKYYKPVEIGQKLAVKPSWEDYVPEDGRIVLEMDPGMAFGCGNHPTTTMCMEYLEGIIQGGESVADVGTGTGILAITSAKLGAARVLAVDLDEVAVKVSQENVERNGVQDIVEVFHGNLLDKVESKVDVVIANIVANVIMILAPDVPRILKHGGYFITSGIIQFRAEEVRQKLEQTGFKILGRKEDGEWVSYLCILEG | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 34140
Sequence Length: 308
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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A5EVX5 | MTQRHWLELTLIADNDDDVLLLETALECAGAVAVTYQAANEEEIFEPEIGTTPMWSKTGVTGLFPLDTDPNAVIELLMQALGEDYPIAQHLLPESDWTRAWLEHFQPIAFGNHFWVAASEHVIEEHDAKVLRLDPGLAFGTGTHPSTAMCLHYLVNHAALHGKTVYDYGCGSGILGIAAAMMGAKAVYQTDIDPQALTASYENAQKNQVAEKIFLCEQPDLAPAVDLLVANILLEPLCALRAQFEKHLHAQSVMIFSGLLERQQQKLEQAYQDHYRIERINCRAGWILLRLTSL | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 32700
Sequence Length: 294
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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B8E1A7 | MEYFELMFKTAKELEESIVAILEDVDSIGIAIEDNFFDESILWDYIDKSFSERNYILIKAYFDRNVDIDRIIDKIRTKIKEIFGEAKVEIEYRIIREEDWTNKWKKYAKPIYLDRIVVLPSWEEIGNVEDRILIRIDPGMAFGTGNHPTTIMCIEMLQKYLKEGMDVLDVGTGSGILSIVAKKLGGDKVKGVDIDEKAIEVAKKNAEGNHVEVEFQKNDLIDGINEKYDIVVANLIAEIILKLNANVKRVLKTDGIYIVSGIVQEKLDMILNSLRESGFKLLEVKEKEDWYTVVAQNED | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 34410
Sequence Length: 299
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q2S4C3 | MDTIELTLTIPPVEHAPFLAELEEPATGFVQNDTELRAYVPAERWAAVDQKQLKARLAADGHPDALSIRPLESKNWNAVWEDTLSPVRAGPFLVCPTSVAPPSARDDATVLRIDPEMSFGTGHHATTRLALRLLAEALAPGDRVLDVGTGTGVLAIAACRIGADAARGVDTNPDAVRNARENVRRNEETDCVTVQEGSVDVASDTQYDLVAANITRRVLLELMPALVARLAPGASLLLSGLLRPQRDDIRDAVASHGLALDAEAAEEGWWAGRFARSPSP | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 29998
Sequence Length: 280
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q8EJR7 | MPWIQLRINTNSDDAETISDLLMEEGAVSITFEDGKDTPIFEPKLGETPLWRDTVVVALFEADTDLTPTIEMLKTLPFLGEHFSHKIEQIEDKDWVREWMDNYHPIQFGKRLWICPSWREVPDPTAVNVILDPGLAFGTGTHPTTALCLEWLDSLDLSNEEVIDFGCGSGILAVAALKLGAKKVTGIDIDYQAIDASKANAERNDVADQLELYLPEDQPADLKADVLVANILAGPLRELAPLIAERVKTGGKLALSGLLKEQAQEISDFYSQWFDMDEAAHKEDWSRLTGTRK | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 32678
Sequence Length: 293
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q748B2 | MTEKPEIWTIRKVLDWTRGYLAEKGVENARLETEWLLSAALGLDRVGLYVNFDKPLNPEELAACRGLVARRAKREPLQYILGTQEFCGLDFVVTPSVLIPRHDTEVIVEEALRRAPHAAAVLDIGVGSGCIAVALAKQLPHAQVVGVEQSPGAIALAQRNAERHGARVTLFEGSLFEPLGDQRFDLIVSNPPYIPTADLEALQPEVREYEPRAALDGGSDGLDFYRLIVPAAPEYLNPGGWLMVELGIGQAETVLGMFSRTGFCDCFTAQDPNGIDRVVGGRIG | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30971
Sequence Length: 284
EC: 2.1.1.297
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Q7NJS7 | MRQPADGWREQALAEARVHDIDAAEIDYLIEAVTGLDRLRVRLGGPQALEAHREKLAALWRRRIEEAMPLQYLLGTAHWRDLQLQVNPAVLIPRPESEALVDVAVDFCRSCAGARVVDLGTGSGAIAVAVARALPGATVWAVDASEAALVVAGANIERYGLSEQVHLLRGNWFVPLPTQPFDAVLSNPPYIPSAEIAALMPEVRLHEPLSALDGGSDGLDAVRQIIADAARHLRPGGILALEVMAGQGPTVVQLLARDSRYGCIRTVRDWAGIERIVVTYAWARGS | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30927
Sequence Length: 286
EC: 2.1.1.297
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Q768T3 | MSAPAQPRERSFPSIEFTDAEADAREFPSSRSRKYNYYQPSKKRATIYEDVTVDVQPDPERHLTQGWIYGFGDGPGGYPKEWTSAQSSNWHQFLDPNEEWEQSIYRNNSAVVHQVDLCLQNAKRARAYDGWNSAWLKFIERNLGAWMHAESGMGLHVFTSIQRSAPTNMINNAVCVNAAHKLRFAQDLALFNLDLSEAEEAFDGSAHKEVWQSAPEWQPTREAVERLTAIGDWAELLFCSNIVFEQLVGSLFRSELVMQVAARNGDYITPTIVGTGEYDYDRDLNYSRALFQMLARDEKHGIDNRKLFSRWMSEWFPGASTRARGLQPIWSQPADKSVTFSSSLEHAKTKFADVLAAIDVDIPEELNK | Function: Component of the propane 2-monooxygenase multicomponent enzyme system which is involved in the degradation of propane via the O2-dependent hydroxylation of propane . Under acetone induction, also able to catalyze the oxidation of phenol to yield hydroquinone .
Catalytic Activity: H(+) + NADH + O2 + propane = H2O + NAD(+) + propan-2-ol
Sequence Mass (Da): 41946
Sequence Length: 368
EC: 1.14.13.227
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P45253 | MNYKEWLAQAIADLAKKNPTENSKIDALVLLQHATGKSRTQILAFDDTEIDEKVRLKLTALLDRRLKGEPIAYILGEKEFWSLPLNVSKGTLIPRPDTEILVEKALQIALEKLEENPPHFRILDLGTGTGAIALALASELAPICQKRHIPLEIIGVDLMSDVVALAQSNAERNQLNVEFLQSRWFDNITGKFDLIVSNPPYIDAQDEHLHQGDVRFEPLSALVANDEGYADLRHIIELASSYLNSNGVLLLEHGWQQGEKVRSIFQENHWEMVETVRDYSDNERVTLGFWKK | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33055
Sequence Length: 292
EC: 2.1.1.297
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Q1II29 | MTLKQAFDSALKHLEAADTPSPRLSAELLLMFSLNCDRAYLFTYPERELTADEQARYDEAIARRCHGEPAQYITGHQEFYGRDFLVSPAVLIPRPETEHLIEAVLELAPREVRWEVLDVGTGSGCIAATLAKEFPRMKVTAVDISPEALQIAQANAARLEAQVEFRVSDLLSAIEPGRQFDMIVSNPPYVGECEADKVQRQVKDFEPHCAVFGGERGMDIIKRLAPQVWEHLKPGGWFLMEIGYSIADPVHEIMRDWTNFKVVPDLRGIPRVVVGRKPTS | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 31472
Sequence Length: 280
EC: 2.1.1.297
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Q9CHX0 | MLWIEAVRTLSADLEDPFELEFVWRNLHELNKLSWLNLMREKITDQELKLLTEVSKRLHQNEPPQYIVGWAEFRDLKLKVDERVLIPRPETEELVEMILAENEKDSLKILDIGTGSGAIAISLAQARENWSVKASDISKEALTLAAENAEINQANLEFIQSDVLDKITDSFDIIVSNPPYIAFDETYEMDNSVIKYEPDLALFAENQGLAIYQKIADQAVNHLTDNGKIYLEIGYKQGQAVQAIFQEKFTDKLVSIHQDIFGKDRMISVK | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30912
Sequence Length: 270
EC: 2.1.1.297
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Q8F987 | MQHPDSILTLLKKSEEFLKKKEIPSARLDAEILLADLLNLQRVKLYVNFERLLNETEKNAYRERILERSKNKPTAYITSQKAFYNSIFFVNENVLIPRPETEELVEKVLSDFKGNIGEQNVLDLCTGSGCIGISLKLARKDWNITLSDISKEALEVATKNAIQILGEEKHIQFLESDLFLSIPKESKFNLIVTNPPYIPISDKAEMMKDVIDYEPHLALFLENPKDFLSTLIAQAYERLVEGGKLYMEILPSLSETIISDSIAKGWENGKIEKDLSGKERFVILTR | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32679
Sequence Length: 286
EC: 2.1.1.297
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Q8Y4A9 | MTQISQLLKKAEAILFEKGLDQNAAEILLETRMGLSRSELWMEISRELEPNHEKQFEEDFARYLAGEPVQYILKTAPFYGYDFLVTEDVLIPRPETEELVACAEAFLKKHPVKNVLDVCTGSGIIAIALKKAFPEISVTASDISAPALVVARKNALLLNADVRFVETDLLEAFKQNEERFDMIVANPPYISEAEKAEMSDYVLKNEPSLALFAENDGLAIYERFVDNLKYVLNSSFWVGVEIGYTQGERVKQLFEKSYPHTTVVIHKDINSKDRYVTCSNILV | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32051
Sequence Length: 283
EC: 2.1.1.297
|
Q6F0I4 | MMNNVRKLKHNYKIMNNANIKIALDFLLENSKIGKSDAIEIISFITKIEYSEVLFSQEKVLNKKQFKKIIKISKKLAKGKPLAYILGYKIFRTHKILVNKNTLIPRMETELIVDYVNEFINSQNEKISVLDLCCGSGCIGISIAIENKDKMENVTFSDISKKALNITSKNIENNNLVNWTKVVKSDFLNSIIKQQNKFNILVCNPPYIDFNDVDVDKMTKKYEPKLALFAKDNGLFFYKEAIKNIDKFMDITKNILIVFEIGWKQEKELDVFLKQELGLKYKWKFEKDYFNNLRYLILTK | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35085
Sequence Length: 300
EC: 2.1.1.297
|
Q2RFW1 | MTLRQALGEAVRRLAAGGVERPRLEAEVLLGWACSLTRPRLLARLEEELAPAAAGRFWQAIDRRAAGYPLQYLTGHQEFMSLDFKVTPAVLIPRQDTEVVVEAVLERLDPCESYTIADCGTGSGAIALSLAHYLPRARVYATDISPAALTVAQENARKLGLAARVTLLQGDFLAPLRGLKLDALVANPPYIPTAALPGLPADVRSEPRLALDGGPDGLDAYRFLLPGAAGLLRPGGLLALEIGSDQGQAVKDLARAVGAYRNEQVLPDYAGRDRCFLAYRREE | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30475
Sequence Length: 283
EC: 2.1.1.297
|
Q6MU88 | MNNTIFNVLNKIKNTNISLNKADVYHILEHIINKDYQWIISNLDHKLTKKQIYKIDQILDLLKQNYPLAYILKSKYFYSNIFFVNKDVLIPRNESELIIDHVSEFVKNNNDLLIVDLCTGSGCLGISCALLNDQNKVILTDISYKSLKVANKNIKKFNLINTSCLNGNFIDVLIKNNLKANLIICNPPYIDINDQNIDKNVIDFEPSIALFAPNKGLYFYEILIKNIDKIVDTNKNFLIVLEFGWLQKDSIEQLLINNCLKYKWEFKKDYNDYWRNLIIKNF | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33026
Sequence Length: 282
EC: 2.1.1.297
|
P9WHV3 | MTLRQAIDLAAALLAEAGVDSARCDAEQLAAHLAGTDRGRLPLFEPPGDEFFGRYRDIVTARARRVPLQHLIGTVSFGPVVLHVGPGVFVPRPETEAILAWATAQSLPARPLIVDACTGSGALAVALAQHRANLGLKARIIGIDDSDCALDYARRNAAGTPVELVRADVTTPRLLPELDGQVDLMVSNPPYIPDAAVLEPEVAQHDPHHALFGGPDGMTVISAVVGLAGRWLRPGGLFAVEHDDTTSSSTVDLVSSTKLFVDVQARKDLAGRPRFVTAMRWGHLPLAGENGAIDPRQRRCRAKR | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32459
Sequence Length: 304
EC: 2.1.1.297
|
Q5F5B4 | MTFDEWLGLSKLPKIEARMLLQYVSEYTRVQLLTRGGEEMPDEIRQRADRLAQRRLNGEPVAYILGVREFYGRRFTVNPNVLIPRPETEHLVEAVLARLPENGRVWDLGTGSGAVAVTVALERPDAFVRASDISTPALETARKNAADLGARVEFAHGSWFDTDMPSERQWDIIVSNPPYIENGDKHLSQGDLRFEPQIALTDFSDGLSCIRTLAQGAPDRLAEGGFLLLEHGFDQGAAVRGVLAENGFSGVEILPDLAGLDRVTLGKYMKHLK | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30311
Sequence Length: 273
EC: 2.1.1.297
|
Q9CN82 | MTYQEWRQFAEHVLMKNKENDPFLDVKSESVLLLQTVTKRSKASILAFSETVLTEVELQQLAQLLMRRAKGEPIAYILGEKAFWSLSLKVSEHTLIPRPDTEVLVEHALDFAKQRVTSAHVSGELSILDLGTGTGAIALALAAELTPLTQKCGINLNILGVDRIAEAVALAKDNAKQNELKVNFLQSVWFDALNPEIRFDLIVSNPPYIDKNDPHLTQGDVRFEPLSALVAAEEGYADIRHIIEQAPLFLKPQGALLLEHGWQQAEKVRSIFQKNLWHNVATLKDYSGNERVTLGCWR | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33428
Sequence Length: 298
EC: 2.1.1.297
|
Q7VDL7 | MSFERFFSAEEILIWRKQELSKGGRAVDLDWLLDIGGGLGWSTLQELKIFQSSFHKLDLSLEELSLIWMRHLSDQIPLQHLVGKCPWRDFELKVNSSALIPRQETEILIDIALKKVDAGLMKYGRWADLGTGSGALAVALARALPLWEGHAADCCNDALALAESNINTLTENANVSLHLGDWWEPLKPWWGNFDLVVANPPYIPKTHLSELDPVVRDHEPILALSGGDDGMDSCRKVIKGAMKGLRSGGWLLLEHNFDQSEQALNLMVDSGFLEVDFENDLEGVRRFGLALRP | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32794
Sequence Length: 293
EC: 2.1.1.297
|
Q9HVC8 | MTTICTLLKDSQLPDSPSARLDTELLLAAAMGKPRSFLRTWPERIVPREANERFDDWIARRRNGEPVAYILGHQGFWSLDLEVAPHTLIPRPDTELLVETALATLAADTATVLDLGTGTGAIALALASERPLWTVTAVDRVEEAVALAERNRQRLLLENVEVRRSHWFSALDGRRFRMIVGNPPYIPASDPHLSEGDVRFEPKSALVAGSDGLDDIRQIVAQAPRHLLDEGWLLLEHGYDQGAAVRELLGARGFAGVHTLRDLGGNERITLGQWAC | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30487
Sequence Length: 276
EC: 2.1.1.297
|
Q98G94 | MADPLPEALGPLLREARARLVAAGVGDPALDARLIVEHFSGTTRTQAIADPERTIDSNAIAAIDAALGRRAGGEPVHRILGYREFYGLRLSLSPETLEPRPDTETLVEAVLPFVKAMAAREGTCRILDLGTGTGAIALALLSAVPAATATGVDISAGALATAARNAGELGLGGRFTTVQSDWFEKVSGRYHVIAANPPYIPTRDIGNLQDEVRDFDPRLALDGGVDGLNPYRIIAAEAARFLEAESRIAVEIGHTQRDEVTDIFKAAGYASVAALRDLGGNDRVLVFQWG | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30689
Sequence Length: 290
EC: 2.1.1.297
|
Q8FN87 | MTAQTSSDVTDQKTDLTRESERDEVLAKATLAKKVAPEIAQLGTGVKNQILLAAAEALLERSAEIIEANSRDIAAGRESGMAESLIDRLALDEGRIEGIAGGLRQVAGLTDPVGEVLQGRVMENGIQMRQVRVPLGVMGMVYEARPNVTVDAFGLALKSGNVALLRGSSTAVHSNTTLVGILQDVLATFDLPRETVQLLPCATRESVQDLITARGLVDVVIPRGGAGLINAVVMGATVPTIETGTGNCHFYIDGDVDVDSAIAMLINGKTRRCSVCNATETALIDSALPDVDKLRVVRALQDAGVTVHGRVAELEAFGATDVVEATENDWDSEYLSFDIAVAVVDGVDAAIEHIEKYSTHHTEAIATNNVFTAQRFADHVDAAAVMINASTAFTDGEQYGMGAEIGISTQKLHARGPMALPELTSTKWILQGTGHTRP | Function: Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
Catalytic Activity: L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 46362
Sequence Length: 438
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.41
|
Q4JWT3 | MTNSNEAQENALSPERQAERDEVLAKAKKAKEVSSQLLLNTQQKNDLLADAADALEANAADIIAANEKDIATGKERGFADSLLDRLALDTERISGIAGGLRQVIGLSDPVGEIVRGHTRPNGLRMKQVRVPLGVMGMVYEARPNVTVDAFGLAIKSGNVPLLRGSKSARHTNEKLVQILQDVAESHNLPRELVQLLPCDTHDSVQDLITARGLVDLVIPRGGAGLINAVVLGATVPTIETGTGNCHFYIDSSADIEEATKLVINGKTRRCSVCNATEVVLLDSALPDPDKIYVLQELQKAGVTLHGEKKQLDPLINDVVQAEETDWTDEYLSFDIAVAIVDGVEEAVAHINRYGTSHTEGIAARDYKTTSYFEQYVDAAAVSINTSTAWTDGEMFGFGAEIGISTQKLHARGPMGLPELTSTKWVINGEGQVRP | Function: Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
Catalytic Activity: L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 46750
Sequence Length: 434
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.41
|
A9BJ18 | MNLQEYVLNKAKKAKDTSRKFSSSSETDKIRILNYISEELMANKNYIISENQKDVESAKNTGMSSSLLDRLLLNQERITKMAEGVQKVAQLQSSVGNISQMWKRPNGLMIGKMVVPLGVIAIIYESRPNVTVDAAALCIKSGNCVVLRGGSEAIHSNNALVKIIHQAIERAGFSKDIVQFIEITDRKAVDELMKLYEYIDVLIPRGGPSLIKNTVENSMIPVIQTGAGNCHVYVDRQADLEKALKIVENAKISRPSVCNAAEKLLVHKDIAEEFLPKIYTLFEKKVELRGCEKTLKIIPQMKAAQEEDWSTEYLDYIMAVKIVDSTEEAINHINKYSTKHSEAIITENYTIAQKFLNEIDSAAVYVNASTRFTDGEEFGFGAEMGISTQKLHVRGPIGINELTTTKYIILGNGQVR | Function: Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
Catalytic Activity: L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 46409
Sequence Length: 416
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.41
|
P74935 | MVEVYARLRAAVARLAVCSAAEKDGALRAVRDALHAQREDILRANAQDLARAREAGLAAPLVARLALSEHLLEDMLRSLTVLSLQRDPIGEIIEGYTLANGLEIRKVRVPLGVVAVIYESRPNVTVDAFALAYKSGNAVLLRAGSAASYSNAPLLRAIHVGLKKAHGVVDAVAVPPVLEEKYGDVDHILRARGFIDAVFPRGGAALIRRVVEGAHVPVIETGCGVCHLYVDESANIDVALQIAENAKLQKPAACNSVETLLVHRAVARPFLHRVQEIFATCEETTRKPGGVDFFCDAESFSLLTERGARKNVFHAQAETWDREYLDYQVSVRVVPNLEEALRHIARHSTKHSEVIVTRDRARARRFHQEVDAACVYVNASSRFTDGGQFGMGAEIGVSTQKLHARGPMGLCALTTSKYLIDGEGQVRP | Function: Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
Catalytic Activity: L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 46608
Sequence Length: 428
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.41
|
Q6A9H7 | MTDQRGAICGAATLVVKVGSSSLTLPGGGIDVRRVDDLVDALSEVIAVGRRVVLVSSGAIATGFPAMGITHRPRTLAGKQAAASVGQGILLAHYASRFASHGLRVGQVLLTVNDLVRPTSYRNAWSTLDTLLGLGVVPIVNENDTVATGEIRFGDNDRLAALVAELVRAQALILLSDVDALYTAHPDSPDARRVEVVEDIDTLDVDTHKAGSGVGTGGMTTKLEAARMATCAGVPVVLAAAVDAPDVLAGVPVGTYFRPLATRRPRRLLWLADAATPQGQIVIDDGAVEALTQRHSSLLAVGVTRVHGDFQAGDPVTILASDGRVVGRGIAQFSHDEVRVMRGRSSAWLAAEMGPAASREIIHRDAMVLSRRRKAEPSSRNQKSSGSRVTS | Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
Sequence Mass (Da): 40984
Sequence Length: 391
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.11
|
Q3Z705 | MNGNCYKRIVIKLGTSLLTGGTGKLDHERMADLCRQIADLTRLGTEVIIVSSGAIAAGRAKMGLRHIPKDVPFKQVLAAIGQSQLMNYYDQLFSPHGLTVAQGLLTKSDLSDRSGYLNARNTLLALMELGVITIVNENDVVAVDEIQQAKFGDNDNLSAMVANLIEADLLLILTNIRGLYTADPTLHPDARLITEVKEITEELEKLAAGSSNKLGTGGMVTKLEAARLATSSGVNVIIADGHIPDIILKLASGETEGTRFMPSLHKPDSRQRWMMSGLCTRGNICIDDGAVKAIRENQKSLLAAGVQQSEGKFGRGDIVKLSDSRGKRLGYGITNYSSDDVSKIKGLHTDEINTVLAGNQGPEIIHRNNLVVI | Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
Sequence Mass (Da): 40166
Sequence Length: 373
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.11
|
Q9RTD8 | MRVVLKLGTSVLTAGTDRLHRPRLVDLMRDIAAVSAQGHEVVLVSSGAVTAGWEALGFPPRERTLAEKQLLAAVGQVQLMHLYTSLAELYGLRSAQLLLTADDFRERTRYLNARTTLEGCLSRGVLPVINENDTVAVEQIKVGDNDTLSAFVANLVEADLLLILTDAPGLYTADPRTHPDATLIPVVERVTPDIWALAGGAGSHRGTGGMHTKIQAAEIATRAGTPVVIAPGDLPEALRRVVDGEALGTRFLAHGTRLEARKRWILAEIAHGRLLLDGGAAQAVRERGSSLLPAGIRQVEGDFERGHTVRLLAPDGQELGRGLTRYRADDLRRVCGHHSREIEALLGYTYGEEAVHRDDLVLL | Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
Sequence Mass (Da): 39263
Sequence Length: 363
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.11
|
Q24XR7 | MSDLRRIVIKVGSSSLNHPEGGLDDQAIQRIAGVIAGIRQLGVECVLVSSGAVAAGVGKLGLKTKPKDMAGKQAVAAVGQGVLIEKYALALEARGLVCAQVLLSRLDLAEASRYRNAQNTLEQLLRYQVIPIINENDTVAVEELCFGDNDRLSALVAGLVHGDLLVILTDVDGLYSANPKLNPQAELIEEVEDLTQVMHIAGGAGSSMGTGGMVTKLKAAEITTRFGMGMFLLHSKRMEEIIELIQGERPLGTYFFPAAHRIMGKKRWIAYGGLSEGSIFIDEGAVKALLKGKSLLASGITGIDGVWERKELVRINNPDGIEVARGLVELSSEELEKVRGKHSEEMLATIPNLEGEEVVHRDNMTLMIE | Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
Sequence Mass (Da): 39684
Sequence Length: 369
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.11
|
Q6AK08 | MQLRREIFDKARRVVVKVGSAILTNVGGIHTSFIADLAREISYLRQSGHEVILVSSGAVAAGRKKISWQDSAPLGMKEKQALAAIGQSHLMRTYEEAFGFYELDVAQILLTHADLSHRDRYLNIRNTILTLLKFGVTPIINENDTVSVEELKFGDNDTLAALLTNLLEADICICLTDVDALYDKNPQKDPTARPLHIVTKISPEIEAMAGNSNSLFGTGGMQSKIRAAKIVFSGGGTAIIGPGRAPRVLQRLFAGEDIGTIFLPCKERMKSKKQWIAHVLKPKGTLLLDAGACKALLQGGKSLLPSGIVGISGEFDRGDSVNCCRLDGSRIAVGLVNYASVDVNAIKGLQSREIASVLKCCDNEEVIHRDNLVILS | Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
Sequence Mass (Da): 40731
Sequence Length: 376
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.11
|
Q72DJ9 | MEWTEERAAALREARCVVVKVGSAVLTTETGVNLAVIDSLAAQLSALQESGKRVVLVSSGAVAAGRSALRDCCEIAGMPHKQAASAVGQSRLMHHYDEAFARYGHLSAQVLLTRDDLRNRERFLNARNTFQALLDWGVIPVVNENDTVAVQELKFGDNDCLASLLLNVVEGDLYVNLTSASGVYADNPQTNPEAGILPCIEDVHTLDLDVMCGGKTSVGTGGMYSKLLAASRAAQLGVPTLILPGREPRILERAFSGEPVGTWVRPEARVVSRRKYWLAYQSEPSGTVTVDEGAARALLQQGGSLLPGGVCDVSGAFEPGALVRIAGPDGTVIAVGLSNYGDRDLVRIKGHRRHEVAAILGDAHFPEVVHRDNMLLDAVV | Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
Sequence Mass (Da): 40567
Sequence Length: 380
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.11
|
B8E032 | MNNWKRIVVKVGTSSITDGRGSPSGEKILSLVKECVKLIRADKELVLVSSGAIASGREIIQKLSKRKDLPAKQALSAVGQVRLMQYYSQLFSIFKQPIAQILLTAEDLRDRKRYINISQTFETLLEEKIIPIVNENDTVAVEEIKIGDNDTLSAKVACAINADLLVILSDVEGLYSEDPNISSNALLITDVYEIDESIEKIAGPGKGTGGMFTKVQAAKIVTEAGIPMILARADVENILERIVLKKEKVGTFFYPSEKHLNKRKHWMLFMAKPEGRIYIDDGAKDALLKRGKSLLPVGIKKVEGEFTRGDTVSIFDLRGEEIARGITNYDSLELDKIKGKNTEEIRNILGEDFYEEVIHRNNLVLTNRGDL | Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
Sequence Mass (Da): 41319
Sequence Length: 371
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.11
|
Q1J5F5 | MMKRQFEDVTRIVIKIGTSSLVLPTGKINLEKIDQLAFVISSLMNKGKEVILVSSGAMGFGLDILKMEKRPTNLAKQQAVSSVGQVAMMSLYSQIFAHYQTNVSQILLTRDVVVFPESLANVTNAFESLISLGIVPIVNENDAVSVDEMDHATKFGDNDRLSAVVAGITKADLLIMLSDIDGLFDKNPTIYEDAQLRSHVAVITQEIIASAGGAGSKFGTGGMLSKIQSAQMVFENKGQMVLMNGANPRDILRVLEGQPLGTWFKQIEEVRHD | Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
Sequence Mass (Da): 29729
Sequence Length: 273
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.11
|
P35082 | MSWQAYVDEHLMCEIEGHHLAAAAIVGHDGAAWAQSTAFPEFKTEDMANIMKDFDEPGHLAPTGLFLGPTKYMVIQGEPGAVIRGKKGSGGITVKKTGQALVVGIYDEPMTPGQCNMVVERLGDYLLEQGM | Function: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
PTM: Phosphorylated by MAP kinases.
Sequence Mass (Da): 14122
Sequence Length: 131
Subcellular Location: Cytoplasm
|
R9UTQ8 | MSVSAPLLDAKVRYGRDGWLPLPHTLSDPDVRKLRQRIEGISREQRPEVVLEEGSSAVRALHGCHDFDEVCARLVRLPALVGLAEQLLGGPVYVYQFKVNMKQAHEGAAWPWHQDFAFWHHEDGMGAPDAVNIAIFLDDVTDENGPLEVIPGSQHAGIVEDTARPGRERSHDWRHHVSAKLEYVVPDEIAGRLAGTFGVRRLTGPAGTAVAFHPSIIHSSSNNTSAQRRCVLLITYNRVTNTPAHPVRPPFLVSRDSTPVVPVDADRL | Cofactor: Binds 1 Fe(2+) ion.
Function: Involved in the biosynthesis of the peptidolactone antibiotic etamycin (viridogrisein) . Catalyzes the hydroxylation of free L-proline at the C-4 position to yield trans-4-hydroxy-L-proline .
Catalytic Activity: 2-oxoglutarate + L-proline + O2 = CO2 + succinate + trans-4-hydroxy-L-proline
Sequence Mass (Da): 29603
Sequence Length: 268
Pathway: Antibiotic biosynthesis.
EC: 1.14.11.57
|
O07509 | MTPDTSMKRVVVKIGSSSLTSLHGEISIRKLEALVDQVVKLKDAGYEVILVSSGAVAAGYRKLGFIQRPEKLPEKQASASIGQGLLMEAYSKLFLAHGYVASQILITRSDFSDEYRYNNVRNTMNVLLERGIIPIINENDTVTVNRLKFGDNDTLAAKVAGLIDADMLVILSDIDGLYDGNPRTNPEAKKIQRVSEITPDIEACAGDTGSIVGTGGMRSKLDAFKIVMASGIKGFLGQADAGDILYHAVHEQAEGTYFEAEGTLPLNQKEQWIAFNSGPEGEMILSDDCSRKITNGQSSLYLDGVQKIKGKFKSGSVVRLMDSKGTEIGLGIVNYSSVQLQEPEKKKELTNRALIDQEAFVCHVDFSLPVN | Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
Sequence Mass (Da): 40354
Sequence Length: 371
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.11
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Q9P7C7 | MSRRTRSRSPPRRSYNRERRDYRKYDDSEDQKGARYNRYVDDVSSRRDRHDSFRSHESNKIRRDNSWKHDKYSYEKRYQERDREYARSKNIPDQYIGRSPRPTSHRHAEEKEVDNKTKSDETNPVLQGSATEIKPQPRRSRFDRTERVGASLSVSEIQSENPRVDVIPKDKAVENNHQRNAEKPVASDKITDAKLLARLERVRAWKESKAKQEASKKEEHKLNTKPQVTAKDQNAMPSTGISGFEINRQKDTSDMKRNNRVHMDDEDGPRRMNLEDYQELWDQEDRGMLGNEQAASMEEDEVDPLDAYMASLVGTTDTIRPGLLNTEVIDPNANDDERMVISETLEEEENLLALAAKRSKKKDVITVDHSKINYEDFKKDFYVEPEELKNLSPAEVDELRASLDGIKIRGIDCPKPVTSWSQCGLSAQTISVINSLGYEKPTSIQAQAIPAITSGRDVIGVAKTGSGKTIAFLLPMFRHIKDQRPLKTGEGPIAIIMTPTRELAVQIFRECKPFLKLLNIRACCAYGGAPIKDQIADLKRGAEIVVCTPGRMIDVLSANAGRVTNLHRCTYLVLDEADRMFDLGFEPQVMRIINNIRPDRQTVLFSATFPRAMEALARKVLKKPVEITVGGRSVVASEVEQIVEVRPEESKFSRLLELLGELYNNQLDVRTLVFVDRQESADALLSDLMKRGYTSNSIHGGKDQHDRDSTISDYKAGVFDVLIATSVVARGLDVKSLQLVVNYDCPNHMEDYVHRVGRTGRAGHTGVAVTFITPEQEKYAVDIAKALKMSKQPVPKELQTLASQFLEKVKAGKEKAAGGGFGGKGLSRLDETRNAERKMQRKAYGEDEEDVETEAEAKSPLEKITPEKSTGDPTLDRVRAAVGGIAARAFANQTAQSNKLTQPISIIKTDGDEYKAKMEINDYPQQARWAVTNNTNIVHVTELTGTSITTKGNFYLPGKNPEPGEEKLYLWIEGPSELVVNRAITELRRLLLEGINHSLEGGNKPSASGRYTVV | Function: ATP-dependent RNA helicase involved in pre-spliceosome/complex A assembly and mRNA splicing . Bridges U1 and U2 snRNPs during pre-spliceosome assembly and enables stable U2 snRNP association with intron RNA . Through its helicase activity probably catalyzes an ATP-dependent conformational change of U2 snRNP .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 114213
Sequence Length: 1014
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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O60508 | MSAAIAALAASYGSGSGSESDSDSESSRCPLPAADSLMHLTKSPSSKPSLAVAVDSAPEVAVKEDLETGVHLDPAVKEVQYNPTYETMFAPEFGPENPFRTQQMAAPRNMLSGYAEPAHINDFMFEQQRRTFATYGYALDPSLDNHQVSAKYIGSVEEAEKNQGLTVFETGQKKTEKRKKFKENDASNIDGFLGPWAKYVDEKDVAKPSEEEQKELDEITAKRQKKGKQEEEKPGEEKTILHVKEMYDYQGRSYLHIPQDVGVNLRSTMPPEKCYLPKKQIHVWSGHTKGVSAVRLFPLSGHLLLSCSMDCKIKLWEVYGERRCLRTFIGHSKAVRDICFNTAGTQFLSAAYDRYLKLWDTETGQCISRFTNRKVPYCVKFNPDEDKQNLFVAGMSDKKIVQWDIRSGEIVQEYDRHLGAVNTIVFVDENRRFVSTSDDKSLRVWEWDIPVDFKYIAEPSMHSMPAVTLSPNGKWLACQSMDNQILIFGAQNRFRLNKKKIFKGHMVAGYACQVDFSPDMSYVISGDGNGKLNIWDWKTTKLYSRFKAHDKVCIGAVWHPHETSKVITCGWDGLIKLWD | Function: Required for pre-mRNA splicing as component of the activated spliceosome . Plays an important role in embryonic brain development; this function does not require proline isomerization .
PTM: Undergoes isomerization of the peptide bond between Gly-94 and Pro-95. The reaction is catalyzed by PPIL1.
Sequence Mass (Da): 65521
Sequence Length: 579
Subcellular Location: Nucleus
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Q96HE9 | MPKFKQRRRKLKAKAERLFKKKEASHFQSKLITPPPPPPSPERVGISSIDISQSRSWLTSSWNFNFPNIRDAIKLWTNRVWSIYSWCQNCITQSLEVLKDTIFPSRICHRELYSVKQQFCILESKLCKLQEALKTISESSSCPSCGQTCHMSGKLTNVPACVLITPGDSKAVLPPTLPQPASHFPPPPPPPPLPPPPPPLAPVLLRKPSLAKALQAGPLKKDGPMQITVKDLLTVKLKKTQSLDEKRKLIPSPKARNPLVTVSDLQHVTLKPNSKVLSTRVTNVLITPGKSQMDLRKLLRKVDVERSPGGTPLTNKENMETGTGLTPVMTQALRRKFQLAHPRSPTPTLPLSTSSFDEQN | Function: Plays a critical role in cell cycle progression.
PTM: Ubiquitinated (Probable). Rapidly degraded by the proteasome; degradation may involve FBXW7-specific phosphorylated phosphodegron motifs.
Sequence Mass (Da): 40085
Sequence Length: 360
Subcellular Location: Cytoplasm
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P62191 | MGQSQSGGHGPGGGKKDDKDKKKKYEPPVPTRVGKKKKKTKGPDAASKLPLVTPHTQCRLKLLKLERIKDYLLMEEEFIRNQEQMKPLEEKQEEERSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLNHKVHAVIGVLMDDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMKVTNEDFKKSKENVLYKKQEGTPEGLYL | 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. PSMC1 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides.
Location Topology: Lipid-anchor
Sequence Mass (Da): 49185
Sequence Length: 440
Subcellular Location: Cytoplasm
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Q9D9M0 | MKRWKDRRTGLLLPLVLLLFGACSSLAWVCGRRMSSRSQQLNNASAIVEGKPASAIVGGKPANILEFPWHVGIMNHGSHLCGGSILNEWWVLSASHCFDQLNNSKLEIIHGTEDLSTKGIKYQKVDKLFLHPKFDDWLLDNDIALLLLKSPLNLSVNRIPICTSEISDIQAWRNCWVTGWGITNTSEKGVQPTILQAVKVDLYRWDWCGYILSLLTKNMLCAGTQDPGKDACQGDSGGALVCNKKRNTAIWYQVGIVSWGMGCGKKNLPGVYTKVSHYVRWISKQTAKAGRPYMYEQNSACPLVLSCRAILFLYFVMFLLT | Function: Probable serine protease.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 35883
Sequence Length: 321
Subcellular Location: Membrane
EC: 3.4.21.-
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Q2L4Q9 | MKWCWGPVLLIAGATVLMEGLQAAQRACGQRGPGPPKPQEGNTVPGEWPWQASVRRQGAHICSGSLVADTWVLTAAHCFEKAAATELNSWSVVLGSLQREGLSPGAEEVGVAALQLPRAYNHYSQGSDLALLQLAHPTTHTPLCLPQPAHRFPFGASCWATGWDQDTSDAPGTLRNLRLRLISRPTCNCIYNQLHQRHLSNPARPGMLCGGPQPGVQGPCQGDSGGPVLCLEPDGHWVQAGIISFASSCAQEDAPVLLTNTAAHSSWLQARVQGAAFLAQSPETPEMSDEDSCVACGSLRTAGPQAGAPSPWPWEARLMHQGQLACGGALVSEEAVLTAAHCFIGRQAPEEWSVGLGTRPEEWGLKQLILHGAYTHPEGGYDMALLLLAQPVTLGASLRPLCLPYPDHHLPDGERGWVLGRARPGAGISSLQTVPVTLLGPRACSRLHAAPGGDGSPILPGMVCTSAVGELPSCEGLSGAPLVHEVRGTWFLAGLHSFGDACQGPARPAVFTALPAYEDWVSSLDWQVYFAEEPEPEAEPGSCLANISQPTSC | Function: In vitro can degrade the fibrinogen alpha chain of as well as pro-urokinase-type plasminogen activator.
Sequence Mass (Da): 58410
Sequence Length: 553
Subcellular Location: Secreted
EC: 3.4.21.-
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Q8LBL5 | MAETMKDITMKNDESQEEEIPDQFLCCVCLELLYKPIVLSCGHLSCFWCVHKSMNGFRESHCPICRDPYVHFPSVCQKLYFLLKKMYPLAHKKREEQVLKEEQERECFSPQIDLVLDLSVCSGDSLNVSDKQKVEECSNAANLLSSSSSRGDIPCIPKNQEPTDAKALNVHENELLKDNKVSKQISKDDLLCSACKELLVRPVVLNCGHVYCEGCVVDMAEESEKIKCQECNVCDPRGFPKVCLILEQLLEENFPEEYNSRSSKVQKTLAHNSKGNIQSYLKEGPSLSNDNNNDDPWLANPGSNVHFGAGCDSCGVYPIIGDRYRCKDCKEEIGYDLCKDCYETPSKVPGRFNQQHTPDHRLELARSPQVLINFNSIGILLGPVISNEGMDTDEGEEGPPGSSNESSSTE | Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. Functions in the N-end rule pathway of protein degradation, where it specifically recognizes and ubiquitinates proteins with a N-terminal bulky aromatic amino acid (Phe). Does not act on aliphatic hydrophobic and basic N-terminal residues (Arg or Leu) containing proteins.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 45937
Sequence Length: 410
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q99132 | MKSRPICSVIPPYILHRIIANGTDEQRHCAQQTLMHVQSLMVSHHPRPEPHEKLPAGQANRSIHDAEQQQQLPGKLVRAEGQPSNGDIAVDEAYSYLGVTYDFFWKIFQRNSLDAEGLPLAGTVHYGQDYQNAFWNGQQMVFGDGDGKIFNRFTIALDVVAHELTHGITENEAGLIYFRQSGALNESLSDVFGSMVKQYHLGQTTEQADWLIGAELLADGIHGMGLRSMSHPGTAYDDELLGIDPQPSHMNEYVNTREDNGGVHLNSGIPNRAFYLAAIALGGHSWEKAGRIWYDTLCDKTLPQNADFEIFARHTIQHAAKRFNHTVADIVQQSWETVGVEVRQEFL | Cofactor: Binds 1 Ca(2+) ion per subunit.
Sequence Mass (Da): 38828
Sequence Length: 347
Subcellular Location: Secreted
EC: 3.4.24.-
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P83264 | MPRRRRRASRPVRRRRRARRSTAVRRRRRVVRRRR | Function: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex.
PTM: Phosphorylated in immature sperm. Dephosphorylated in mature sperm allowing a stronger interaction with DNA.
Sequence Mass (Da): 4665
Sequence Length: 35
Subcellular Location: Nucleus
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P80001 | MKVAANSSKMLAEKLELMKGGRRRRRRSRRRRRRSRRRSRSPYRRRYRRRRRRRRRRSRRRRYRRRRSYSRRRYRRRR | Function: Cuttlefish spermiogenesis is characterized by a double nuclear protein transition: histones -> spermatid-specific proteins (T1/T2) -> protamines (SP1/SP2). The protamines compact sperm DNA into a highly condensed, stable and inactive complex.
PTM: Phosphorylation occurs at different degrees. The triphosphorylated form may be predominant in T1. SP1 appears to be phosphorylated in elongated spermatids, but dephosphorylated in mature sperm cells.
Sequence Mass (Da): 10632
Sequence Length: 78
Subcellular Location: Nucleus
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P58309 | MPPGRPEVYQERFDIVQPHCSSEHTISLNTDFSKAAFGSATGLVAKAASQTTTAIWNLHADAHDFSNSSYLSKQVFAANLAHIGVAFIWLSGMHFHGAYFSNYLDWLQDPSIAPTAQQVSNIANQSVLNPIRVTSGFFNLWLAEGITSTYQLKVIAAFGLIASALCFLGSYFHMHSSTSFTRVLNTKLTSLSTHHLVGLLGLGSLAWAGHLIHISLPVNILMNAGVAVPSPHSLLSSKAVATIVEQLSFSALTSSDGYVWQPLVYSAMHHFALALVLIVGSVLGPLSTASNPLMSFTVGSSWHLVLGVQLFVTGTASVLYAQMSNAYPVYPYLLTDHPTVVSLFVHHMWIGGFFLVGAFAHLSIGLVRDTLPQSFSVVLTQRDIILGHLTWVVAFLGVHSFGLYVHNDTMQALGRPDDMFSDNAISLLPVFARWSTLTLNSTGSAVSVLGVELSTADFMVTHIHAFTIHTTVLILVKGFLYARSSRLVNDKYKLDFRYPCDGPGRGGTCQISPWDHVFLGLFWMYNSISVVIFHFFWEYQSNLASIKASAGGSIRALASDFELNSINTNGWLRNFLWSGAAQVIQSYGSPLAAYGLTFPASHFVWALSLMFLFSGRGYWQELIESVLWAHHKLYVVPHIQPRALSITSGRAVGFTHYLLGGIGSTWSFFLARIVATAG | 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): 74079
Sequence Length: 678
Subcellular Location: Plastid
EC: 1.97.1.12
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P56766 | MIIRSPEPEVKILVDRDPIKTSFEEWAKPGHFSRTIAKGPDTTTWIWNLHADAHDFDSHTSDLEEISRKVFSAHFGQLSIIFLWLSGMYFHGARFSNYEAWLSDPTHIGPSAQVVWPIVGQEILNGDVGGGFRGIQITSGFFQIWRASGITSELQLYCTAIGALVFAALMLFAGWFHYHKAAPKLAWFQDVESMLNHHLAGLLGLGSLSWAGHQVHVSLPINQFLNAGVDPKEIPLPHEFILNRDLLAQLYPSFAEGATPFFTLNWSKYSEFLTFRGGLDPVTGGLWLTDIAHHHLAIAILFLIAGHMYRTNWGIGHGIKDILEAHKGPFTGQGHKGLYEILTTSWHAQLSLNLAMLGSLTIIVAHHMYSMPPYPYLATDYATQLSLFTHHMWIGGFLIVGAAAHAAIFMVRDYDPTNRYNDLLDRVLRHRDAIISHLNWVCIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPVFAQWIQNTHALAPGVTAPGETASTSLTWGGGELVAVGGKVALLPIPLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNAISVVIFHFSWKMQSDVWGSISDQGVVTHITGGNFAQSSITINGWLRDFLWAQASQVIQSYGSSLSAYGLFFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPATQPRALSIIQGRAVGVTHYLLGGIATTWAFFLARIIAVG | 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): 83231
Sequence Length: 750
Subcellular Location: Plastid
EC: 1.97.1.12
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Q9MUJ4 | DIVEKDPVKTSFERWAQPGHFSKNLAKGPSTTTWIWNLHADAHDFDSHTNDLEDISRKIFGAHFGQLAIIFIWLSGMYFHGARFSNYEAWLNDPTHVKPSAQVVWPIVGQEILNGDVGGGFQGIQITSGFFQLWRASGITNELQLYCTAVGALIFAGLMFFAGWFHYHKAAPKLAWFQNVESMLNHHLAGLLGLGSLGWAGHQIHVSLPINQLLDAGVDSKEVPLPHEFILNREILTQAYPSFAKGLIPFFTLDWSEYSDFLTFRGGLNPVTGGLWLTDTAHHHLAIAVLFLVAGHMYRTNWGIGHSTREILEAHKGPFTGEGHKGLYEILTSSWHAQLAINLAMLGSLTIIVSHHMYAMPPYPYLATDYATQLSLFTHHMWIGGFLVVGAAAHAAIFMVRDYDPTTQYNNLLDRVIRHRDAIISHLNWVCIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPIFAQWVQNTHALAPGSTAPNAAAATSLTWGGSNLVAVGGKIAISPITLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNSISVVIFHFSWKMQSDVWGSISEQGVINHITGGNFAQSSTTINGWLRDFLWAQASQVIQSYGSSLSAYGLLFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPVTQPRALSIIQGRAVGVTHT | 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): 79747
Sequence Length: 719
Subcellular Location: Plastid
EC: 1.97.1.12
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Q06J42 | MAIDVSNQNDDLVKVVVDVDPVPTDFERWAKPGHFSRSLSKGPLTTTWIWNLHADVHDFDGYSTNLQDISRKIFSAHFGQLGIIFIWLSGMYFHGARFSNYEAWLSNPAKIKPSAQVVWPIVGQDILNGDVGDGFRGVQITSGLFHVWRASGITNELELFSTAIGGLVMAFLMFFAGWFHYHKAAPKLQWFQNAESMLNHHLSGLLGLGSLSWAGHQIHIAIPINKLLDKGVSASEIPLPHEFLVDKTQMINIFPSFEKGLTPFFTLNWKEYSDFLTFQGGLDPQTGSLWLTDIAHHHLAIAVLFIVAGHMYKTNWSIGHRLKEILEGHKVLSVSKGHSGLYEIFTTSWHAQLSLNLAMLGSLSIIVAHHMYAMPPYPYISVDYATQLSLFTHHMWIGGFCIVGAGAHASIFMVRDYNPADNYNNLLDRIICQRDAIISHLNWACIFLGLHSFGLYIHNDTMSALGRSDDMFSDTAIQLQPIFSQFIQRIHYMTIESTAPYVSHGTSPAWGGDIVAINGKIAMMPISLGTSDFMVHHIHAFTIHVTVLILLKGVLFSRNSRLIPDKSNLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNSLSIVIFHFSWKLQSDVWGNVNSSVVSHITRGNFAQSANTINGWLRDFLWSQSSQVIQSYGSSLSAYGLIFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPAIAPRALSITQGRAVGVAHYLLGGIGTTWSFFLARIISVN | 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): 83932
Sequence Length: 751
Subcellular Location: Plastid
EC: 1.97.1.12
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P12154 | MTISTPEREAKKVKIAVDRNPVETSFEKWAKPGHFSRTLSKGPNTTTWIWNLHADAHDFDSHTSDLEEISRKVFSAHFGQLGIIFIWLSGMYFHGARFSNYEAWLSDPTHIKPSAQVVWPIVGQEILNGDVGGGFQGIQITSGFFQLWRASGITSELQLYTTAIGGLVMAAAMFFAGWFHYHKAAPKLEWFQNVESMLNHHLGGLLGLGSLAWAGHQIHVSLPVNKLLDAGVDPKEIPLPHDLLLNRAIMADLYPSFAKGIAPFFTLNWSEYSDFLTFKGGLNPVTGGLWLSDTAHHHVAIAVLFLVAGHMYRTNWGIGHSMKEILEAHRGPFTGEGHVGLYEILTTSWHAQLAINLALFGSLSIIVAHHMYAMPPYPYLATDYGTQLSLFTHHTWIGGFCIVGAGAHAAIFMVRDYDPTNNYNNLLDRVIRHRDAIISHLNWVCIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPVFAQWIQNTHFLAPQLTAPNALAATSLTWGGDLVAVGGKVAMMPISLGTSDFMVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNSLSIVIFHFSWKMQSDVWGTVTASGVSHITGGNFAQSANTINGWLRDFLWAQSSQVIQSYGSALSAYGLIFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPAIQPRALSITQGRAVGVAHYLLGGIATTWSFFLARIISVG | 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): 83154
Sequence Length: 751
Subcellular Location: Plastid
EC: 1.97.1.12
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A0T0L9 | MAISSTDRRSKNVQIFVEKDAVETSFAKWAQPGHFSRTLAKGPKTTTWIWNLHADAHDFDSQTSSLEEVSRKIFSAHFGQLSVIFLWISGMHFHGAYFSNYSAWLTDPVNIKQSSQVVWPIVGQEILNGDVGGNFQGIQTTSGWFQMWRAEGITSEVELYWIAIGGLAMSAIMLFAGWFHYHKAAPKLEWFQNAESMMNHHLAGLLGLGCLSWSGHQIHVALPINKLLDAGVAPQEIPLPHEFLINRELMSQLYPSFSKGLAPFFSGHWGEYSDFLTFKGGLNPVTGGLWLSDIAHHHLALAVLFIFAGHMYRTNWGIGHSMKEILEAHKGPFTGEGHKGLYEILTTSWHAQLAINLAMMGSLSIIVAHHMYAMPPYPYIATDYATQLSLFTHHMWIGGFCVTGGAAHAAIFMVRDYTPANNYNNLLDRVLRHRDSIIAHLNWVCIFLGCHAFGFYIHNDTMRALGRPQDMFSDKAIQLQPIFAQWIQNIHLLAPGTTAPNALATTSYAFGGEVVEVGGKIAMMPIQLGTADFMVHHIHAFTIHVTVLILLKGVLYARSSKLIPDKANLGFRFPCDGPGRGGTCQSSSWDHVFLGLFWMYNSISVVIFHFSWKMQSDVWGTISPDGSISHITGGNFAKGAITINGWLRDFLWSQASQVIQSYGSAASAYGLIFLGAHFIWAFSLMFLFSGRGYWQELIESIVWAHNKLNFAPAIQPRALSITQGRAVGLAHYLLGGIGTTWAFFLARAVSIS | 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): 83596
Sequence Length: 752
Subcellular Location: Plastid
EC: 1.97.1.12
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Q9AL93 | FDSHTSDLEDVSRKIFSAHFGHLAVIFIWLSGAYFHGARFSNYTAWLSDPISIKPSAQVVWPFRSIFGQEILNGDVGGGFHGIQITSGLFHLWRACGITHSSELYATAIGALVMAGLMLFAGWFHYHKAAPKLEWFQNVESMLNHHLSVLLGCGSLGWAGHLIHISLPVNALLDAGVSPADIPLAKDYVLDAGYMAKFSQLCRGLNPFFTLNWGVYSDFLTFKGGLNPQTGSLWLTDIAHHQLAIAVLFIIAGHMYRTNWGIGHDMKALLDGHKGPVGEVGTGHAGLYEILTTSWHAQLAINLALLGSLSIIVAHHMYAMPPYPYLAIDYPTQLSLFTHHVWIGGFLIVGAGAHAAIFMIRDYDPAKNVDNLLDRVIRHRDAIISHLNWVCIWLGFHSFGLYIHNDTMRALGRPQDMFSDSAIQLQPIFAQGIQSIQAAVAGSAQAPWVGAATSPVWGGDTIAVGGKVAMSAIPLGTADFMVHHIHAFTIHVTVLILLKGVLYARNSRLVPDKAELGFAFPCDGPGRGGTCQVSAWDHVFLGLFWMYNSLSIVIFHFSWKMQSDVWGTVYPDGSVLNITVGNFAESALTINGRLRDFLWAQAASVINSYGSALSAYGLMFLAAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPAIQPRALSITQGRAVGVAHYLLGGIATTWAFFLARIISVG | 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 (By similarity).
Catalytic Activity: hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76532
Sequence Length: 699
Subcellular Location: Cellular thylakoid membrane
EC: 1.97.1.12
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P62090 | MSHSVKIYDTCIGCTQCVRACPTDVLEMIPWDGCKAKQIASAPRTEDCVGCKRCESACPTDFLSVRVYLWHETTRSMGLAY | Cofactor: Binds 2 [4Fe-4S] clusters. Cluster 2 is most probably the spectroscopically characterized electron acceptor FA and cluster 1 is most probably FB.
Function: Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. 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.
Catalytic Activity: hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 9038
Sequence Length: 81
Subcellular Location: Plastid
EC: 1.97.1.12
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Q2JXQ1 | MAIQRGAKVRVLRKESYWYRDVGTVAAVDTSGILYPVIVRFDKINYYNINTNNFREDELEVVEEPKPKAKASS | Function: Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 8424
Sequence Length: 73
Subcellular Location: Cellular thylakoid membrane
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P12975 | MALNRGDKVRIKRTESYWYGDVGTVASVEKSGILYPVIVRFDRVNYNGFSGSASGVNTNNFAENELELVQAAAK | Function: Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 8145
Sequence Length: 74
Subcellular Location: Cellular thylakoid membrane
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P0A423 | MVQRGSKVKILRPESYWYNEVGTVASVDQTPGVKYPVIVRFDKVNYTGYSGSASGVNTNNFALHEVQEVAPPKKGK | Function: Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 8389
Sequence Length: 76
Subcellular Location: Cellular thylakoid membrane
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P20900 | MVQRGSKVKILRPESYVYNEVGTVAS | Function: Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 2911
Sequence Length: 26
Subcellular Location: Cellular thylakoid membrane
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Q9SHE8 | MSLTIPANLVLNPRSNKSLTQSVPKSSARFVCSDDKSSSSTPQSMKAFSAAVALSSILLSAPMPAVADISGLTPCKDSKQFAKREKQQIKKLESSLKLYAPESAPALALNAQIEKTKRRFDNYGKYGLLCGSDGLPHLIVNGDQRHWGEFITPGILFLYIAGWIGWVGRSYLIAISGEKKPAMKEIIIDVPLASRIIFRGFIWPVAAYREFLNGDLIAKDV | Function: Participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24173
Sequence Length: 221
Subcellular Location: Plastid
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P62596 | MRDIKTYLSVAPVLSTLWFGALAGLLIEINRLFPDALSFPFF | Function: May help in the organization of the PsaE and PsaF subunits.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4745
Sequence Length: 42
Subcellular Location: Plastid
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B0JUV4 | MEGLTKFLSSAPVLIMALLTFTAGILIEFNRFYPDLLFHPLG | Function: May help in the organization of the PsaE and PsaF subunits.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4699
Sequence Length: 42
Subcellular Location: Cellular thylakoid membrane
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O65107 | AMRNAIEGMNGKELDGRNITTTGSAKATIFDEYLEKSKANKELNDKKRLATSGANFARAYTVEFGSCQFPYNFTGCQDLAKQKKVPFISDDLEIECEGKEKFKCGSNVFWKW | Function: May function in mediating the binding of the antenna complexes to the PSI reaction center and core antenna.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12621
Sequence Length: 112
Subcellular Location: Plastid
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P82339 | SVFDEYLEKSKANK | Function: May function in mediating the binding of the antenna complexes to the PSI reaction center and core antenna.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 1658
Sequence Length: 14
Subcellular Location: Plastid
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Q9SBN5 | MAVAMRAQCAKVQAARPARATTVVCRASAQSRRELLGLGVLLGAAALAPAANAGVVEDLLAKSAANKALNNKKRLATSYANLARSRTVYDGTCQFPENFFGCEELAFNKGVKYIAEDLKIECEGKDAKSCGSKFTLRSK | Function: May function in mediating the binding of the antenna complexes to the PSI reaction center and core antenna.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14759
Sequence Length: 139
Subcellular Location: Plastid
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Q949Q5 | MAATFATPSTVIGLGGSSITTKPFSSSFLKPTLSAKNPLRLAGASGGRVTCFERNWLRRDLNVVGFGLIGWLAPSSIPAINGKSLTGLFFDSIGTELAHFPTPPALTSQFWLWLVTWHLGLFLCLTFGQIGFKGRTEDYF | Function: Involved in the balancing of excitation energy between the two photosystems I (PSI) and II (PSII).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15144
Sequence Length: 140
Subcellular Location: Plastid
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C7LYP8 | MSMPFYVAPEQLMKDRADYARKGIARGRALIGAVWEGGIIIVAENPSRSLHKLSEIYDRIAFGGVGKYNEFDQLRVAGIRHADLKGYAYAREDVDARSLANLYAQYLGTVFTHEMKPLEVEILVAELGNGHRESQLFQILYDGTVMDEREFAVLGGDADAIAERFRALYDASGPRERLLQSARDALSGQRPPIGADDLEVVVLEDRGERRCFRRLEVDEVREALGDQPEGSA | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Sequence Mass (Da): 25904
Sequence Length: 232
Pathway: Protein degradation; proteasomal Pup-dependent pathway.
Subcellular Location: Cytoplasm
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Q8H0S9 | MDAPKEIFLKNYTKPDYYFETVDLSFSLGEEKTIVSSKIKVSPRVKGSSAALVLDGHDLKLLSVKVEGKLLKEGDYQLDSRHLTLPSLPAEESFVLEIDTEIYPHKNTSLEGLYKSSGNFCTQCEAEGFRKITFYQDRPDIMAKYTCRVEGDKTLYPVLLSNGNLISQGDIEGGRHYALWEDPFKKPCYLFALVAGQLVSRDDTFTTRSGRQVSLKIWTPAEDLPKTAHAMYSLKAAMKWDEDVFGLEYDLDLFNIVAVPDFNMGAMENKSLNIFNSKLVLASPETATDADYAAILGVIGHEYFHNWTGNRVTCRDWFQLSLKEGLTVFRDQEFSSDMGSRTVKRIADVSKLRIYQFPQDAGPMAHPVRPHSYIKMDNFYTVTVYEKGAEVVRMYKTLLGTQGFRKGIDLYFERHDEQAVTCEDFFAAMRDANNADFANFLQWYSQAGTPVVKVVSSYNADARTFSLKFSQEIPPTPGQPTKEPTFIPVVVGLLDSSGKDITLSSVHHDGTVQTISGSSTILRVTKKEEEFVFSDIPERPVPSLFRGFSAPVRVETDLSNDDLFFLLAHDSDEFNRWEAGQVLARKLMLNLVSDFQQNKPLALNPKFVQGLGSVLSDSSLDKEFIAKAITLPGEGEIMDMMAVADPDAVHAVRKFVRKQLASELKEELLKIVENNRSTEAYVFDHSNMARRALKNTALAYLASLEDPAYMELALNEYKMATNLTDQFAALAALSQNPGKTRDDILADFYNKWQDDYLVVNKWFLLQSTSDIPGNVENVKKLLDHPAFDLRNPNKVYSLIGGFCGSPVNFHAKDGSGYKFLGDIVVQLDKLNPQVASRMVSAFSRWKRYDETRQGLAKAQLEMIMSANGLSENVFEIASKSLAA | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. Plays an essential role during prophase I of meiosis. Required for correct meiotic reconbination in both male and female gametophytes.
Catalytic Activity: Release of an N-terminal amino acid, preferentially alanine, from a wide range of peptides, amides and arylamides.
Sequence Mass (Da): 99159
Sequence Length: 883
EC: 3.4.11.14
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Q4TT88 | MLGRLAVRQAVRCSKASIKPVNTHQLCLRNFSAIRRLSFVAGAQCRPYHTTANMLHRTARGEHGMAACGNPSAAVKFERLPTFAEPTHYNVRLSPCLNQFSFDGHATIDVTIKEATDVLKVHAQSLLIQSVSLITQPGDASKSLETSYDDKLNILTIKLPTTMQPQKVQLDFKFVGELNDKMRGFYRSQYKDKNGTEKFLASTQFESTYARYAFPCFDEPIYKATFDVTLEVENHLTALSNMNVISETPTADGKRKAVTFATSPKMSSYLVAFAVGELEYISAQTKSGVEMRVYTVPGKKEQGQYSLDLSVKCIDWYNEWFDIKYPLPKCDLIAIPDFSMGAMENWGLVTYREIALLVDPGVTSTRQKSRVALVVAHELAHLWFGNLVTMKWWTDLWLKEGFASFMEYMFVGANCPEFKIWLHFLNDELASGMGLDALRNSHPIEVEIDNPNELDEIYDSITYAKSNSVNRMLCYYLSEPVFQKGLRLYLKRFQYSNAVTQDLWTALSEASGQNVNELMSGWTQQMGFPVLKVSQRQDGNNRILTVEQRRFISDGGEDPKNSQWQVPITVAVGSSPSDVKARFLLKEKQQEFTIEGVAPGEWVKLNSGTTGFYRVEYSDEMLTAMLPDIASRRMPVLDRFGLINDLSALLNTGRVSIAQFVQVAASSAKEDEYVVWGAIDEGMSKLLACAREMSEDTLKSAKQLVVKMFEQTGAELGFAEQAGEDSQKMMLRSLVQARLARAGHQPTIDKFTQMFNDFLEKGTPIHPDIRLATFGVVARYGGKEGFDKLMNLRETTTFQEIERQTMVAMSQTPEESLLAQLFEYGFEKNKVRPQDQLYLFLGTGATHMGQQYAWKYFCEHIKEFLDKYGGANSSLFQRCLKFAGESFGNEKRAVEFQDFFCNCNVLSDTDRQTLARPIGQTVEAIRLNARLLESNRQIIENLLKQSNV | Cofactor: Binds 1 zinc ion per subunit. Can also use Ni(2+) and Co(2+) .
Function: Aminopeptidase . Required for the exit from meiosis, probably upstream of cyclin cyb-3 . Involved in the establishment of the anterior-posterior polarity at the embryonic 1-cell stage by regulating the dynamics of sperm-donated centrosomes . Plays a role in oocyte maturation . Required for embryonic development .
Catalytic Activity: Release of an N-terminal amino acid, preferentially alanine, from a wide range of peptides, amides and arylamides.
Sequence Mass (Da): 107150
Sequence Length: 948
Subcellular Location: Cytoplasm
EC: 3.4.11.14
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C7PVV3 | MTTPFYVSPEQIMKDRAEYARKGISRGRSVAVIFYDKGIVFVGENPSRALHKISEIYDRLAFAAAGRYNEYEQLRIAGVRHADMRGYVYDRRDVTGRALANTYAQALGTMFSEGAGKPYEVELAVAEVGEAAADDQGYRITFDGQVTDIRGFQVLGGAADAVTQVLESSYEENAALETVLNAAVDALGRDGTEPRTLAPNQLEVAVLERTRTQARKFRRISENALARLLGVAGDSAGEGEGDSEDGAKNGGGDAGQTGTTNPPAAKSVPADDGDVLGAVDDILGEDGTPEES | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Sequence Mass (Da): 31104
Sequence Length: 292
Pathway: Protein degradation; proteasomal Pup-dependent pathway.
Subcellular Location: Cytoplasm
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P12729 | MKFQHTFIALLSLLTYANAYDYFTTTLANQNPVCASVDVIQNVCTEVCGRFVRYIPDATNTNQFTFAEYTTNQCTVQVTPAVTNTFTCADQTSSHALGSDWSGVCKITATPAPTVTPTVTPTVTPTVTPTPTNTPNPTPSQTSTTTGSASTVVASLSLIIFSMILSLC | Function: May bind F-actin and nucleates actin assembly.
PTM: O-glycosylated in the repeat region. The oligosaccharides contain N-acetylglucosamine and fucose as the major constituents.
Location Topology: Lipid-anchor
Sequence Mass (Da): 17879
Sequence Length: 168
Subcellular Location: Cell membrane
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D0KTH0 | MVIMGNELQLENKILKGTTTVGIRVNDGVILAADRRASAGFFVANKMVRKVLYITDKIGITTAGSVADLQFIYDVLKNIYHYNSITKYGPISIKGIATRLANVLSATKYFPYIVQILIGGYDDQPRLFNLDYLGDITEENYVATGSGSPVAMGVLEDEYNPKMTLDEAADLAKRAVFSAIKRDSFTGTGVIVAKIHSKGHEELEFYLNKKM | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 23271
Sequence Length: 211
Subcellular Location: Cytoplasm
EC: 3.4.25.1
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Q09841 | MMGINERKGFDFEYYQRNLLLQEKGFPTPKATSTGTTIVGVIAKDCIVLGADTRATAGPIIADKNCKKLHLISPNIWCAGAGTAADTEFVTSMISSNIELHSLYTNRKPRVVTALTMLKQHLFRYQGHIGAYLVLGGYDCKGPHLFTIAAHGSSDKLPYVALGSGSLAAISVLETKYQPDLERHEAMELVKEAIEAGIFNDLGSGSNCDLVVIDEEKATPYRGYSKPNERATKQSKYTYDRGTTAVLKEDIYKFVTVQDLDEMQVDV | 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 (Potential).
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 29337
Sequence Length: 267
Subcellular Location: Cytoplasm
EC: 3.4.25.1
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Q5JHL8 | MEKKTGTTTVGIRTKEGVVLAADTQASLDHMVETLNIRKILPITDRIAITTAGSVGDVQALARMLEAEARYYQFTWGRPMTAKAMAHLLSNILNENKWFPYMVQIIIGGYVEEPTLANLDPLGGLIFDDYTATGSGSPFAIAVLEDGFRKDMSLEEAKELAVRAVRTAGKRDVYTGDRKVQVVVISKDGMKEEFVEFKE | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 21978
Sequence Length: 199
Subcellular Location: Cytoplasm
EC: 3.4.25.1
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P07753 | MTAILERRENSSLWARFCEWITSTENRLYIGWFGVIMIPCLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIITGAVIPTSNAIGLHFYPIWEAASLDEWLYNGGPYQLIVCHFLLGVYCYMGREWELSFRLGMRPWIAVAYSAPVAAASAVFLVYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVIGIWFTALGLSTMAFNLNGFNFNQSVVDSQGRVLNTWADIINRANLGMEVMHERNAHNFPLDLASTNSSSNN | 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. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids.
Function: This is one of the two reaction center proteins of photosystem II.
Catalytic Activity: 2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2
PTM: Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39042
Sequence Length: 352
Subcellular Location: Plastid
EC: 1.10.3.9
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Q9T351 | MTATLERRESASIWGRFCNWVTSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYEIIVLHFLLGVACYMGREWELSYRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANAGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAAVEAPAVNG | 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. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex 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.
Catalytic Activity: 2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2
PTM: Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38764
Sequence Length: 353
Subcellular Location: Plastid
EC: 1.10.3.9
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P09193 | MVTLSNTSMVGGRDLPSTGFAWWSGNARLINLSGKLLGAHVAHAGLIVFWAGAMTLFEVAHFIPEKPMYEQGLILLPHIATLGWGVGPAGEVTDIFPFFVVGVLHLISSAVLGLGGIYHALRGPEVLEEYSSFFGYDWKDKNQMTNIIGYHLILLGCGALLLVFKAMFFGGVYDTWAPGGGDVRVITNPTLNPAIIFGYLLKAPFGGEGWIISVNNMEDIIGGHIWIGLICISGGIWHILTKPFGWARRALIWSGEAYLSYSLGALSLMGFIASVFVWFNNTAYPSEFYGPTGMEASQSQAFTFLVRDQRLGANIASAQGPTGLGKYLMRSPSGEIIFGGETMRFWDFRGPWLEPLRGPNGLDLDKLRNDIQPWQVRRAAEYMTHAPLGSLNSVGGVITDVNSFNYVSPRAWLATSHFVLGFFFLVGHLWHAGRARAAAAGFEKGIDRETEPTLFMPDLD | 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 (By similarity). Required for correct assembly of PSII .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50303
Sequence Length: 460
Subcellular Location: Cellular thylakoid membrane
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Q8DIF8 | MVTLSSNSIFATNRDQESSGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMTLFELAHFIPEKPMYEQGLILIPHIATLGWGVGPGGEVVDTFPFFVVGVVHLISSAVLGFGGVYHAIRGPETLEEYSSFFGYDWKDKNKMTTILGFHLIVLGIGALLLVAKAMFFGGLYDTWAPGGGDVRVITNPTLDPRVIFGYLLKSPFGGEGWIVSVNNLEDVVGGHIWIGLICIAGGIWHILTTPFGWARRAFIWSGEAYLSYSLGALSMMGFIATCFVWFNNTVYPSEFYGPTGPEASQAQAMTFLIRDQKLGANVGSAQGPTGLGKYLMRSPTGEIIFGGETMRFWDFRGPWLEPLRGPNGLDLNKIKNDIQPWQERRAAEYMTHAPLGSLNSVGGVATEINSVNFVSPRSWLATSHFVLAFFFLVGHLWHAGRARAAAAGFEKGIDRESEPVLSMPSLD | 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.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50245
Sequence Length: 461
Subcellular Location: Cellular thylakoid membrane
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Q0ZJ24 | MKTLYSLRRFYPVETLFNGTLALAGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGPGGEVIDTFPYFVSGVLHLISSAVLGFGGIYHALLGPETLEESFPFFGYVWKDRNKMTTILGIHLILLGIGAFLLVFKALYFGGVYDTWAPGGGDVRKITNLTLSPSVIFGYLLKSPFGGEGWIVSVDDLEDIIGGHVWLGSICIFGGIWHILTKPFAWARRALVWSGEAYLSYSLGALAVFGFIACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVGSAQGPTGLGKYLMRSPTGEVIFGGETMRFWDLRAPWLEPLRGPNGLDLSRLKKDIQPWQERRSAEYMTHAPLGSLNSVGGVATEINAVNYVSPRSWLATSHFVLGFFLFVGHLWHAGRARAAAAGFEKGIDRDFEPVLSMTPLN | 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.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51840
Sequence Length: 473
Subcellular Location: Plastid
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B0C1V6 | MTIAVGRAQERGWFDVLDDWLKRDRFVFIGWSGILLFPCAFLSIGGWFTGTTFVTSWYTHGLASSYLEGANFLTVAVSTPADSLGHSLLLLWGPEAQGDFTRWCQLGGLWNFTTLHGVFGLIGFMLRQFEIARLVGVRPYNAVAFSGPIAVYVSVFLMYPLGQSSWFFAPSWGVTSIFRFLLFAQGFHNLTLNPFHMMGVAGILGGALLCAIHGATVENTLFEDGQDANTFAAFTPTQAEETYSMVTANRFWSQIFGIAFSNKRWLHFFMLFVPVTGLWASAIGLVGIALNMRAYDFVSQEIRAAEDPEFETFYTKNILLNEGLRAWMAPQDQIHENFIFPEEVLPRGNAL | 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. The PSII complex 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): 39266
Sequence Length: 351
Subcellular Location: Cellular thylakoid membrane
EC: 1.10.3.9
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Q8YQI2 | MSGTTGERPFSDIVTSIRYWVIHSITIPALFIAGWLFVSTGLAYDVFGTPRPDEYYTQARQELPIVNNRFEAKKQVEQLIQK | 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): 9408
Sequence Length: 82
Subcellular Location: Cellular thylakoid membrane
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P60128 | MTIDRTYPIFTVRWLAIHGLAVPTVFFLGSISAMQFIQR | Cofactor: With its partner (PsbE) 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.
PTM: The N-terminus is blocked.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4498
Sequence Length: 39
Subcellular Location: Plastid
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B0JX58 | MLTLKIAVYIVVSFFVLLFIFGFLSGDPTRNPGRKDFE | 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): 4352
Sequence Length: 38
Subcellular Location: Cellular thylakoid membrane
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B0C6Z7 | MEAVLLLAKLPEAFSVFSPIVDVMPVIPLFFLALAFVWQAAVGFK | 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): 4937
Sequence Length: 45
Subcellular Location: Cellular thylakoid membrane
|
P56782 | MLNIFNLICIFFNSTLFSSTFLVAKLPEAYAFLNPIVDVMPVIPLFFLLLAFVWQAAVSFR | 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): 6975
Sequence Length: 61
Subcellular Location: Plastid
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Q7NMA8 | MSKDPKNPGVELNRTSLYMGLVLVLVIILLFSNYFIN | 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): 4213
Sequence Length: 37
Subcellular Location: Cell inner membrane
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Q6B8K6 | MSGPNPNKEPVELNRTSLFWGLLLIFVLAVLFSSYFFN | 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): 4362
Sequence Length: 38
Subcellular Location: Plastid
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