ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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P00634 | MKQSTIALALLPLLFTPVTKARTPEMPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIGDGMGDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQDATPAALVAHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVTLGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLAQMTDKAIELLSKNEKGFFLQVEGASIDKQDHAANPCGQIGETVDLDEAVQRALEFAKKEGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYGNSEEDSQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTMKAALGLK | Cofactor: Binds 1 Mg(2+) ion.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 49439
Sequence Length: 471
Subcellular Location: Periplasm
EC: 3.1.3.1
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P83456 | AGFPEQEPEPKFWNDWAQKTLDKALSLQTLNKNKAQNLILFLGDGMGVPTVTAARILKGQLRGQPGEEGQLEMDKFPFVALSKTYNTNAQVADSAGTATAYLCGVKANEGTVGVSAAAVRSQANTTQGNEVTSILRWAKDAGKSIGIVTTTRVNHATPSAAYAHCVDRDWYSDNEMPADAVEAGCKDIARQLFENIPDIDVIMGGGRKYMYPKNTTDVEYPGQPKHSGTRKDGRNLVKEWVDRNTEKKGHYVWNKKDLLSLNPTKVDYLLGLFEPADLPYDLERNKETDPSLSEMVEVAIKILRRNPNGFYLLVEGGRIDHGHHEGKDKQAIHEAVEMDRAIGRADLMTSTSDTLTVVTADHSHLFSFGGYTPRGNEIFGLAAFISDVDQKPFTAILYGNGPGYKLVNGARENVSTVDYQDNSYLAQAAVPLSSETHGGEDVAVFAKGPMAHLLHGVHEQNYIPHAMAYAACIGQNR | Cofactor: Binds 1 Mg(2+) ion.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 52198
Sequence Length: 477
Subcellular Location: Cell membrane
EC: 3.1.3.1
|
Q05205 | MNLSPSRTPICAALAAALLGAAALAPAHAAQRILQLSEDTTHSKPVSAASALRGTPLAKAGAADRVCEAGAKWLRVGFKQLKLAGYDSLVLTSSGGDKLVFEGQHWNQRSFTTRPLRGECVDIQPYFSQPDSAFQLDRYDYSTVALDKATVVVAGAGDICDTSGNACQGTSDLIVSINPTAVFTAGDNAYNSGTLSEYNSRYAPTWGRFKALTSPSPGNHDYSTTGAKGYFDYFNGSGNQTGPAGDRSKGYYSWDVGDWHFVSLNTMSGGTVAQAQIDWLKADLAANTKPCTAAYFHHPLLSRGSYSGYSQVKPFWDALYAAKADLVLVGHDHNYQRYGKMNPDKAAASDGIRQVLVGTGGRAFYGISGSHALLEASNDSTFGVLKLTLSATGYTGDFVPRAGSSYTDHFTGTCNKGSGNPPTQTLTLNSVRDVTVKSGGSRDNGATLYADGSDGGQVLRGLMAWNVSSAAGKTLTGAQVKLQVSDRSTGTYDLYRAGAAWTEANASYSGVSLGSKIGSVVPSATGAQSIALNAAGFSW | PTM: The C-terminal Pro-sequence may be required for translocation of the phosphatase across the outer membrane.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 56490
Sequence Length: 539
Subcellular Location: Secreted
EC: 3.1.3.1
|
O60109 | MASERDPLLPVHGEGPESPSRRNWKTWIKHGILLILVLSTVIFFYFFSSHKSKGTNEKPKFVIMMVSDGMGPGSLSMTRSFVETLNDKEGYRLPLDEHLIGSSRTRSSSSLITDSAAGATAFSCANKTYNGAVGVLDNEKPCGTILEAAKEAGYLTGIVVTSRVTDATPASFSAHAANRFMQDLIAEYQVGMGPLGRSVDLLFGGGLCSFLPKSTYRSCRSDNLDLLKYARKKEGFQILLNRTDFDELSNAQLPLLGLFSDYHLSYDIDYQPEVQPKLSEMVETALDVLLNATNEDTSKGFFLLIEGSRIDMASHNNDPIAHVYEVMEYNRAFEIASAFVEKNGGSLISTSDHETGGLTVGRQVSKKYPEYLWKPQVLSLALHSIEYLASAIVNHNQNTLLPYIEQFVLPAIGIPDPNPKQIHDIYVARHNIFNLINVLSDIVSVEAQIGWTTHGHTAVDVNVYGVGEVTEHLRGNMENIEIGQFMEIYLNVSLSDVTEKLKDAPIHGAPDRPSLVETSFSDRLVGFGADLF | Cofactor: Binds 1 Mg(2+) ion.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 58666
Sequence Length: 532
Subcellular Location: Membrane
EC: 3.1.3.1
|
P19147 | MQPAVSLIAGAVLSALLCSSAIAAETSANADGLTDRAARGNLVEPGGARRLAGDQTTALKASLSDKTAKNVILLIGDGMGDSEITAARNYAEGAGGYFKGIDALPLTGQYTHYSLDRKTHKPDYVTDSAASATAWATGVKTYNGALGVDVNGKDQPTLLEIAKAAGKATGNVSTAELQDATPAALVSHVISRKCYGPEETSEKCAANALENGGRGSITEQLLKTRADVTLGGGAKSFNQLAKSGEWQGKSLKDQAAAQGYQWVSNADELQAVTLANQQKPLLGLFADGNMPVRWLGPKASYHGNLDKPAVTCENNPARTAATPTLAAMTEKAIALLKDNPNGFFLQVEGASIDKQDHAANPCGQIGETVDLDEAVQKALAFARADGNTLVIVTADHAHASQIVSADAKAPGLTQKLTTKDGAPMTLSYGNSEEESQGHTGTQLRVAAYGPHAANVVGLTDQTDLFFTMRDAMGIK | Cofactor: Binds 1 Mg(2+) ion.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 49265
Sequence Length: 475
Subcellular Location: Periplasm
EC: 3.1.3.1
|
P11491 | MMTHTLPSEQTRLVPGSDSSSRPKKRRISKRSKIIVSTVVCIGLLLVLVQLAFPSSFALRSASHKKKNVIFFVTDGMGPASLSMARSFNQHVNDLPIDDILTLDEHFIGSSRTRSSDSLVTDSAAGATAFACALKSYNGAIGVDPHHRPCGTVLEAAKLAGYLTGLVVTTRITDATPASFSSHVDYRWQEDLIATHQLGEYPLGRVVDLLMGGGRSHFYPQGEKASPYGHHGARKDGRDLIDEAQSNGWQYVGDRKNFDSLLKSHGENVTLPFLGLFADNDIPFEIDRDEKEYPSLKEQVKVALGALEKASNEDKDSNGFFLMVEGSRIDHAGHQNDPASQVREVLAFDEAFQYVLEFAENSDTETVLVSTSDHETGGLVTSRQVTASYPQYVWYPQVLANATHSGEFLKRKLVDFVHEHKGASSKIENFIKHEILEKDLGIYDYTDSDLETLIHLDDNANAIQDKLNDMVSFRAQIGWTTHGHSAVDVNIYAYANKKATWSYVLNNLQGNHENTEVGQFLENFLELNLNEVTDLIRDTKHTSDFDATEIASEVQHYDEYYHELTN | Cofactor: Binds 1 Mg(2+) ion.
Function: Phosphatase with broad substrate specificity. A truncated (soluble) version of the protein is responsible for the production of (E,E)-farnesol from (E,E)-farnesyl diphosphate. Acts as a fructose-2,6-bisphosphate 6-phosphatase .
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 63004
Sequence Length: 566
Subcellular Location: Vacuole membrane
EC: 3.1.3.1
|
P0CP79 | MNTSHPIPTTMASKSFLSLLVALFVAICFVLSPGVDAAKGPVITNKVYFDIEHGGKPLGRIVMGLYGKTVPKTAENFRALATGKNSDGEDLGYGYEGSSFHRIIKNFMIQGGDFTKGDGTGGKSIYGSKFPDENFKLKHTGPGVLSMANAGRDTNGSQFFICTVKTAWLDNRHVVFGHVLEGMDVVYAMENVKTSRGDKPVEPITIAASGELPIEHEVDEQGNQVPFRIEL | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 24958
Sequence Length: 231
Subcellular Location: Endoplasmic reticulum lumen
EC: 5.2.1.8
|
Q9TW32 | MKVIFVVLAIVLVTLWAMPSEAGKDPKITNKVFFDIEIDNKPAGRIVFGLYGKTVPKTVENFRALCTGEKGLGTSGKPLHYKDSKFHRIIPNFMIQGGDFTRGDGTGGESIYGKKFNDENFKIKHSKPGLLSMANAGPNTNGSQFFITTVVTSWLDGRHTVFGEVIEGMDIVKLLESIGSQSGTPSKIAKISNSGEL | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 21399
Sequence Length: 197
Subcellular Location: Microsome
EC: 5.2.1.8
|
P23869 | MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEPIKNEANNGLKNTRGTLAMARTQAPHSATAQFFINVVDNDFLNFSGESLQGWGYCVFAEVVDGMDVVDKIKGVATGRSGMHQDVPKEDVIIESVTVSE | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 18153
Sequence Length: 164
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
Q4I5R9 | MFNLRRLFASALFLGLGLLFLAQTAEAAKGPKITHKVYFDITQGDQPLGRVVMGLYGKTVPETTENFRALATGEKGFGYEGSAFHRVIKNFMIQGGDFTKGDGTGGKSIYGDRFKDENFKLKHTKKGLLSMANAGRDTNGSQFFITTVVTSWLDGKHVVFGEVLEGYEIIEKIENSKTGAADRPVEAVKIAKSGELDVPPEGLVGTSEFAAEEVASAGWSPMQKAGLFAIFAGVLFVGLRSARQHSRF | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26883
Sequence Length: 248
Subcellular Location: Membrane
EC: 5.2.1.8
|
P44499 | MVTLHTNFGDIKIKLDFDKAPVTAENFLNYCKDGFYNNTIFHRVIDGFMIQGGGMESGMREKATKAPIQNEANNRLSNKRGTIAMARTSDPHSATAQFFINVADNDFLNYRSKEMFGREVVQEWGYAVFGEVVEGMDVVDKIKKVKTGNKGFHQDVPTEDVVITSVSIE | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 18965
Sequence Length: 169
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
P23284 | MLRLSERNMKVLLAAALIAGSVFFLLLPGPSAADEKKKGPKVTVKVYFDLRIGDEDVGRVIFGLFGKTVPKTVDNFVALATGEKGFGYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSIYGERFPDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSRDKPLKDVIIADCGKIEVEKPFAIAKE | Function: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 23743
Sequence Length: 216
Subcellular Location: Virion
EC: 5.2.1.8
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P46697 | MPTNEQRRATAKRKLKRQLERRAKQARWRRVLLISGGVVVAVAVIITVVATVVISKLGHKHDTASSTASNSLTATKTPAVTPSVLPLPSFQPSTNLGVNCQYPPSADKAAKPVKPPRAGKVPTDPATVSASMATNQGNIGLLLNNAESPCTVNSFASLTGQGFFNNTKCHRLTTSLMLGVLQCGDPKVDGTGGPGYKFANEYPTDQYPPNDPKLKQPVLYPRGTLAMANSGPNTNGSQFFLVYHDSQLPPEYTVFGTIQADGLATLDKIAKGGIASGGDDGPPATEVTIESLRLD | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 31178
Sequence Length: 295
EC: 5.2.1.8
|
P9WHW0 | MGHLTPVAAPRLACAFVPTNAQRRATAKRKLERQLERRAKQAKRRRILTIVGGSLAAVAVIVAVVVTVVVNKDDHQSTTSATPTDSASTSPPQAATAPPLPPFKPSANLGANCQYPPSPDKAVKPVKLPRTGKVPTDPAQVSVSMVTNQGNIGLMLANNESPCTVNSFVSLAQQGFFKGTTCHRLTTSPMLAVLQCGDPKGDGTGGPGYQFANEYPTDQYSANDPKLNEPVIYPRGTLAMANAGPNTNSSQFFMVYRDSKLPPQYTVFGTIQADGLTTLDKIAKAGVAGGGEDGKPATEVTITSVLLD | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 32371
Sequence Length: 308
EC: 5.2.1.8
|
Q7S7Z6 | MFSLRRLLLAATLFLGAMLLFAQSAEAAKGPKITHKVYFDIEQGDKPLGRIVMGLYGKTVPKTAENFRALATGEKGFGYEGSTFHRVIKQFMIQGGDFTKGDGTGGKSIYGDKFPDENFKLKHSKKGLLSMANAGKDTNGSQFFITTVITSWLDGKHVVFGEVLEGYDVVEKIENTKTGPRDAPAEPIKIAKSGELEVPPEGLEGQSEWASPAYANEDEKPAAPVPVTDAKPPAHDSIPAATADDDDTGAPLFAKVLFFGVLVLGLVLYIRLRRAPKGTYGKGME | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 30743
Sequence Length: 285
Subcellular Location: Membrane
EC: 5.2.1.8
|
P24368 | MLRLSERNMKVLFAAALIVGSVVFLLLPGPSVANDKKKGPKVTVKVYFDFQIGDEPVGRVTFGLFGKTVPKTVDNFVALATGEKGFGYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSIYGERFPDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTSWLDGKHVVFGKVLEGMDVVRKVENTKTDSRDKPLKDVIIVDCGKIEVEKPFAIAKE | Function: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 23803
Sequence Length: 216
Subcellular Location: Endoplasmic reticulum lumen
EC: 5.2.1.8
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Q27774 | MAVLRVLCGLLLVSILFLGFVLSEGNGPKVTEKVFFDIEVDEQPLGRIIIGLFGKTVPKTVENFKQLSIGTTLKDGRTAAYKGSTFHRVIKSFMIQGGDFTNHDGTGGFSIYGERFPDENFKLKHVGAGWLSMANAGPNTNGAQFFITTTQNPWLDGKHVVFGKVVEGMSVVRQIENMQTDSRDRPVKSVKIANCGHIPVDVPFSVSNTDAAE | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 23238
Sequence Length: 213
Subcellular Location: Endoplasmic reticulum lumen
EC: 5.2.1.8
|
Q26551 | MAVLKPLCPLLLLSIICFGLIRSEANGPKVTDKVFFDIEVDGKPLARIIIGLFGKTVPKTVENFKQLSIGTQLKDGRTASYKGSTFHRVIKSFMIQGGDFTNHDGTGGFSIYGDRFPDENFKLRHVGAGWLSMANAGPDTNGSQFFITTVKTSWLDGKHVVFGKVVEGMNIVRQIESETTDSRDRPVKSIKIASCGHIPVEIPFSVTNSDAVE | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 23294
Sequence Length: 213
Subcellular Location: Endoplasmic reticulum lumen
EC: 5.2.1.8
|
P77949 | MAEQLYATLKTNRGDIEIRLLPNHAPKTVRNFVELATGQREWVNPETGEKSTDRLYDGTVFHRVISGFMIQGGDPLGNGTGGPGYKFADEFHPELGFTQPYLLAMANAGPGTNGSQFFLTVSPTAWLTGKHTIFGEVSGEAGRKVVDAIAATPTNPRTDRPLEDVVIESVVVETR | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 19017
Sequence Length: 175
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
P83221 | MSTVELNTSAGRIVLELNDAEAPKTVENFLAYVRSGHYDGTIFHRVISDFMIQGGGFTPDMQQKSTLAPIQNEADNGLRNDNYTVAMARTNDPHSATAQFFINVKDNAFLNHTSKTPNGWGYAVFGRVTEGQDVVDAIKGVKTGSSRGHQDVPVQPVVIESAKILG | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 18025
Sequence Length: 166
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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B9KCQ6 | MQIQPSMYINRELSWLAFNSRVLDQCSKDLPLLEKLKFIAIYCTNLDEFYMIRVAGLKQLFIAGISTASNDEMTPLTQLKAIRNYLHEEKYVVEQYFTKITQDLEKENLFIRSYEELDEDLKQQCNDHFFSNIFPVIVPIAVDATHPFPHLNNLSFSLVVKLCDPMHPELLKFGMVRIPRVLPRFYQVSSNIYVPIESIVRHHTEHIFPGYKLLSSAAFRVTRNADMEIEEEEADDFMMILEQGLKLRRKGAFIRLQIEKGADEQLIEFLSSHMNIFHKDIYEYSILLNLPSLWQIISNKEFTHLLNPVYTPKILPPFGDNVSIFSAIDKQDILAIQPYESFEPVYQFIKEASKDPKVVSIRMTLYRVEKNSNIVQALIDAASDGKQVTVMVELKARFDEENNLHWAKSLENAGAHVVYGITGFKVHAKVAQVIRKEGDKLKIYNHLSTGNYNASSAKIYTDVSYFTSKEEYSQDTTTFFHILSGYSKSRRLKTLSMSPKQIKERILDMIATEASHGKDGVIIAKMNALVDGDVIKALYEASNKGVKIDLIVRGICCLRPGVKGYSENIKVRSIVGKYLEHARILYFKHTEPNYFISSADWMPRNLERRLELMTPIFDEHSRAKLAQILKLQLSDNDLAYELDSEGRYRKIALNEAEKINNSQQILEEYISRIFNTLKKDTDHSRAAHLATKLFRDS | Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Mass (Da): 80404
Sequence Length: 697
EC: 2.7.4.1
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Q8FF70 | MGQEKLYIEKELSWLSFNERVLQEAADKSNPLIERMRFLGIYSNNLDEFYKVRFAELKRRIIISEEQGSNSHSRHLLGKIQSRVLKADQEFDGLYNELLLEMARNQIFLINERQLSVNQQNWLRHYFKQYLRQHITPILINPDTDLVQFLKDDYTYLAVEIIRGDTIRYALLEIPSDKVPRFVNLPPEAPRRRKPMILLDNILRYCLDDIFKGFFDYDALNAYSMKMTRDAEYDLVHEMEASLMELMSSSLKQRLTAEPVRFVYQRDMPNALVEVLREKLTISRYDSIVPGGRYHNFKDFINFPNVGKANLVNKPLPRLRHIWFDKAQFRNGFDAIRERDVLLYYPYHTFEHVLELLRQASFDPSVLAIKINIYRVAKDSRIIDSMIHAAHNGKKVTVVVELQARFDEEANIHWAKRLTEAGVHVIFSAPGLKIHAKLFLISRKENGEVVRYAHIGTGNFNEKTARLYTDYSLLTADARITNEVRRVFNFIENPYRPVTFDYLMVSPQNSRRLLYEMVDREIANAQQGLPSGITLKLNNLVDKGLVDRLYAASSSGVPVNLLVRGMCSLIPNLEGISDNIRAISIVDRYLEHDRVYIFENGGDKKVYLSSADWMTRNIDYRIEVATPLLDPRLKQRVLDIIDILFSDTVKARYIDKELSNRYVPRGNRRKVRAQLAIYDYIKSLEQSE | Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Mass (Da): 80421
Sequence Length: 688
EC: 2.7.4.1
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Q2NC49 | MGSHPITQDNDLDPPTEPGERYFNRELSWLAFNDRVLAEACNDSYPLLERLRFLSISGSNLDEFVMIRVAGLVGQVQRGIDEVSDDGRSPREQLNAVVARLEELSERQQDIWRNLRVQLADAGVHVADEERVNAEAYGWLKQHFFESILPLLTPQALDPAHPFPFISNEGLGLLFTLRRGGEELVEMVLIPSALPRFIRVPGEDALYISIESLITRFAKELFPGFEIVGDGTFRVLRDSDIEIQEEAEDLVRTFRSAIQRRRRGQVIQLEIEEEFDPTAEALLREKLDTPGATFVKTDGMLGIAGLADIVDEDRPDLKFDSYSPRYPERVLEHDGDIFAAIREKDIVIHHPYESFNVVVDFIRRAAIDPDVVAIKQALYRAGTQSEVVDALVEAAENGKSVTAVVELKARFDEEQNLYWANKLERAGVQVIYGFVDWKTHAKVAMVVRREEEGFRTYCHFGTGNYHPITAKIYTDLSYFTADPRLGRDAAKLFNFVTGYVEPRELEMLAVSPIDLRETIYAAIDNEMVNAQAGKPAAIWMKMNQITDVDMIDRLYEASQAGVEIQLVVRGICNLRPGVPGMSDNIRVKSIIGRFLEHSRIYAFANGEPMPGTSSTVYISSADLMVRNLDRRVEQLVPIDNQTVHDQVLQQVLLANLLDNEQSWELQPDGSYFRVEVGEKSFNCHRYFMTNPSLSGRGGALEAGAVPKLALRKGAV | Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Mass (Da): 80561
Sequence Length: 715
EC: 2.7.4.1
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B1YL94 | MKIDSPEFFNNREISWLQFNERVLGEVTDTRNPLMERFKFLGIFSSNLDEFYMVRVGGLKDEVLAGFNKPENKQQLTPKQQLRAIATKTKELVDQQYEAFKDVTQALKAEGISFLKHDELNEMQSEYVKTFFREQVFPVLTPVAVDAYRPFPMLSSKSLNIATALEAEDGSKRNLALVQVPAVLPRFVDLPVDDEETTAVILLEDVIISFIDSLFKGYHVLSAMPFRITRNADLPFHEEGTHDLLKLIEKELKKRRWGVGIRLEIQKNAINTNLLNMLRDVLDLQDRDIYAVDGPIDLTFAFAFYSQIGVEYDHLIYQTIMPVEPPALEKSKKLFDQILQQDYLLHHPYHTFDPIVRLIVQAANDPNVLAIKQTLYRVSGDSPIIKALKTAAENGKQVTVLVELKARFDEAKNIEWAKQLEKAGAHVIYGYSDLKTHSKITLIVRLQEGRIQRFVHLGTGNYNDSTAKLYTDIGLLTAKEQIAEDATNFFNWLSGYGEQPEWNALHTSPNSMLEKFLSLIDEEIKYHKKHGNGRIVAKMNSLTEKDIIVKLYQASRAGVRIELIVRGVCCLRPQIKGVSENIRVTSVVDRYLEHSRIFYFHHNGDDLIYCSSADWMTRNMRKRIEILFPIADEEQKNYIKDCLALTMADNVKAREQDDSGNYHYVTKGKQECESQILIQLYTNGKLKAKPSFEHPLEQKWTPVERAEEKITFDPTTSKK | Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Mass (Da): 82631
Sequence Length: 719
EC: 2.7.4.1
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A8AK73 | MLQSNEYFSGKVKSIGFTSSSTGRASVGVMAEGEYAFSTAAPEEMTVVSGALNVLLPGETEWKVYAAGEVFNVPGQSEFHLQVAEPTSYLCRYL | Function: Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
Catalytic Activity: a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 10107
Sequence Length: 94
EC: 2.4.2.1
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Q186L5 | MSEFKNVTAVKKANVYFDGKVSSRVIILPNGERKTLGLMLPGEYTFSTREEEIMEMLAGSMDVKLPGSNEFVTYKEGQKFNVPSDSSFDLKVNEVVDYCCSYIAD | Function: Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
Catalytic Activity: a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 11779
Sequence Length: 105
EC: 2.4.2.1
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Q0K784 | MEVSQFDNVSVVKKANLYFDGKCVSHTVLFPDGTRKTLGVIFPAALTFNTGAPEIMEINAGTCRVRLAGSEDWQTYGAGQQFSVPGNSSFDIEVQETLDYVCHFA | Function: Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
Catalytic Activity: a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 11486
Sequence Length: 105
EC: 2.4.2.1
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Q9AR38 | MAAAAAAMATATSATAAPPLRIRDAARRTRRRGHVRCAVASGAAEAPAAPGARVSADCVVVGGGISGLCTAQALATKHGVGDVLVTEARARPGGNITTAERAGEGYLWEEGPNSFQPSDPVLTMAVDSGLKDDLVFGDPNAPRFVLWEGKLRPVPSKPGDLPFFDLMSIPGKLRAGLGALGVRAPPPGREESVEDFVRRNLGAEVFERLIEPFCSGVYAGDPSKLSMKAAFGKVWRLEDTGGSIIGGTIKTIQERGKNPKPPRDPRLPTPKGQTVASFRKGLTMLPDAITSRLGSKVKLSWKLTSITKSDNKGYALVYETPEGVVSVQAKTVVMTIPSYVASDILRPLSSDAADALSIFYYPPVAAVTVSYPKEAIRKECLIDGELQGFGQLHPRSQGVETLGTIYSSSLFPNRAPAGRVLLLNYIGGSTNTGIVSKTESELVEAVDRDLRKMLINPKAVDPLVLGVRVWPQAIPQFLIGHLDHLEAAKSALGKGGYDGLFLGGNYVAGVALGRCVEGAYESASQISDYLTKYAYK | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Catalytic Activity: 3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX
Sequence Mass (Da): 56727
Sequence Length: 536
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Subcellular Location: Plastid
EC: 1.3.3.4
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Q9LRI8 | MSAMALSSTMALSLPQSSMSLSHCRHNRITILIPSSSLRRRGGSSIRCSTISTSNSAAAANYQNKNIGTNGVDGGGGGGGVLDCVIVGGGISGLCIAQALSTKYSNLSTNFIVTEAKDRVGGNITTMEADGYLWEEGPNSFQPSDAVLTMAVDSGLKEELVLGDPNSPRFVLWNGKLRPVPSKLTDLPFFDLMSFPGKIRAGLGALGLRPSPPAHEESVEQFVRRNLGDEVFERLIEPFCSGVYAGDPSKLSMKAAFGRVWVLEQKGGSIIGGTLKTIQERKDNPKPPRDPRLPKPKGQTVGSFRKGLSMLPTAISERLGNKVKVSWTLSGIAKSSNGEYNLTYETPDGLVSVRTKSVVMTVPSYVASSLLRPLSDVAAESLSKFHYPPVAAVSLSYPKEAIRSECLIDGELKGFGQLHSRSQGVETLGTIYSSSLFPGRAPPGRTLILNYIGGDTNPGILDKTKDELAEAVDRDLRRILINPNAKAPRVLGVRVWPQAIPQFLIGHFDLLDAAKAALTDGGHKGLFLGGNYVSGVALGRCIEGAYESAAEVVDFLSQYSDK | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Catalytic Activity: 3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 59929
Sequence Length: 562
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Subcellular Location: Plastid
EC: 1.3.3.4
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O24163 | MTTTPIANHPNIFTHQSSSSPLAFLNRTSFIPFSSISKRNSVNCNGWRTRCSVAKDYTVPSSAVDGGPAAELDCVIVGAGISGLCIAQVMSANYPNLMVTEARDRAGGNITTVERDGYLWEEGPNSFQPSDPMLTMAVDCGLKDDLVLGDPNAPRFVLWKGKLRPVPSKLTDLAFFDLMSIPGKLRAGFGAIGLRPSPPGHEESVEQFVRRNLGGEVFERLIEPFCSGVYAGDPSKLSMKAAFGKVWKLEETGGSIIGGTFKAIKERSSTPKAPRDPRLPKPKGQTVGSFRKGLRMLPDAISARLGSKLKLSWKLSSITKSEKGGYHLTYETPEGVVSLQSRSIVMTVPSYVASNILRPLSVAAADALSNFYYPPVGAVTITYPQEAIRDERLVDGELKGFGQLHPRTQGVETLGTIYSSSLFPNRAPKGRVLLLNYIGGAKNPEILSKTESQLVEVVDRDLRKMLIKPKAQDPLVVGVRVWPQAIPQFLVGHLDTLSTAKAAMNDNGLEGLFLGGNYVSGVALGRCVEGAYEVASEVTGFLSRYAYK | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Catalytic Activity: 3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX
Sequence Mass (Da): 59230
Sequence Length: 548
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Subcellular Location: Plastid
EC: 1.3.3.4
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O24164 | MAPSAGEDKHSSAKRVAVIGAGVSGLAAAYKLKIHGLNVTVFEAEGKAGGKLRSVSQDGLIWDEGANTMTESEGDVTFLIDSLGLREKQQFPLSQNKRYIARNGTPVLLPSNPIDLIKSNFLSTGSKLQMLLEPILWKNKKLSQVSDSHESVSGFFQRHFGKEVVDYLIDPFVAGTCGGDPDSLSMHHSFPELWNLEKRFGSVILGAIRSKLSPKNEKKQGPPKTSANKKRQRGSFSFLGGMQTLTDAICKDLREDELRLNSRVLELSCSCTEDSAIDSWSIISASPHKRQSEEESFDAVIMTAPLCDVKSMKIAKRGNPFLLNFIPEVDYVPLSVVITTFKRENVKYPLEGFGVLVPSKEQQHGLKTLGTLFSSMMFPDRAPNNVYLYTTFVGGSRNRELAKASRTELKEIVTSDLKQLLGAEGEPTYVNHLYWSKAFPLYGHNYDSVLDAIDKMEKNLPGLFYAGNHRGGLSVGKALSSGCNAADLVISYLESVSTDSKRHC | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Catalytic Activity: 3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX
Sequence Mass (Da): 55407
Sequence Length: 504
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Subcellular Location: Mitochondrion
EC: 1.3.3.4
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Q9LTX3 | MRNVIRRVTTMTFTFLLQSPPLPISPSPPQFSLSSSPLSKTQRFITPSQGSRLRTLCTKVIIPNMQDSGSPPLSYLTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYKPEEYSRVLAICGPGNNGGDGLVAARHLHHFGYKPFICYPKRTAKPLYTGLVTQLDSLSVPFVSVEDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYEQTLQKHPVIVSVDIPSGWHVEEGDHEDGGIKPDMLVSLTAPKLCAKRFRGPHHFLGGRFVPPSVAEKYKLELPSYPGTSMCVRIGKPPKVDISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQYSDGSVIPKPKNWGGFRLKPNLFEFWQGQPSRLHDRLQYSLQDVNGNPAWKIHRLAP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). Involved in the PLP salvage pathway. Has a higher preference for PNP over PMP. May also catalyze the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 59376
Sequence Length: 530
Domain: Most plant PPOX proteins have both a pyridoxamine 5'-phosphate oxidase domain and an extra YjeF N-terminal domain.
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
Subcellular Location: Plastid
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Q9ZPY1 | MGTHVAPWKQLLFGAIEANSHLSHSSYVQLATIGLNGRPSNRTVVFRGFEENSDRIQINTDLRSRKIEELKHCPFSEMCWYFSDTWEQFRINGRIEVIDASNPDQTKLQQREKAWFANSLRSRLIYVCPTPGSPCNSEQSSQQVKLDPSSGPVPEYCLLLLEPEKVDYLNLKTNQRLFFSSMATGTGEKCWTSEKVNP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). Has an in vitro catalytic efficiency for PNP approximately 300-fold lower than that of PPOX1.
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 22620
Sequence Length: 198
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
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Q54DT8 | MIQKVGIIGSGISGLSSYYYLRNGINLTSKFSKNNLKINIFEKSNKVGGNIQTRIIQGKNKDEKIIVEEGPRSLRALGRGLNTLEFIKRLGISNDIIFSSANSNGKFVLLDGKPKEIPMTSLFDIIKFSFKHSIVSSILKEPFKKVPSQVKEMDPNWDESVHDFFSRRLGKTMTKTFIEPTILGIYGGDYTNLSIKSTFKRAALLEPFGGLILGSLFKSKKQKQFELDLDKNEKRLLPSKNELTELFDKDTDKTNVFSFKENGLSRMIQKLKSLIESDSLTKLYLSTSIVEIEKDVTNGTLKVTDNKGNQYQYDQLISTIPLNQLAPMFKKSDSKLYQLLQSVNYTSIAVINLIYKSNKNVVKIISDKGFGYLVPSKENQSVIGVCFDSNTFPEFVNNNNNNNNDNDNGNEKDQSIITVMIGGNNGIKDRNDNWIDVTNTSKDKLLDIALKHLDKVLDIESSPDFTNVSIYDNGIPHYNIGHQNLINEIQNHITKNYGTTLLLGGNSIDGVGINDSIHKSKQLINSLKLSNN | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Catalytic Activity: 3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX
Sequence Mass (Da): 59681
Sequence Length: 532
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Subcellular Location: Mitochondrion
EC: 1.3.3.4
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P50336 | MGRTVVVLGGGISGLAASYHLSRAPCPPKVVLVESSERLGGWIRSVRGPNGAIFELGPRGIRPAGALGARTLLLVSELGLDSEVLPVRGDHPAAQNRFLYVGGALHALPTGLRGLLRPSPPFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLGAGRTPQPDSALIRQALAERWSQWSLRGGLEMLPQALETHLTSRGVSVLRGQPVCGLSLQAEGRWKVSLRDSSLEADHVISAIPASVLSELLPAEAAPLARALSAITAVSVAVVNLQYQGAHLPVQGFGHLVPSSEDPGVLGIVYDSVAFPEQDGSPPGLRVTVMLGGSWLQTLEASGCVLSQELFQQRAQEAAATQLGLKEMPSHCLVHLHKNCIPQYTLGHWQKLESARQFLTAHRLPLTLAGASYEGVAVNDCIESGRQAAVSVLGTEPNS | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Catalytic Activity: 3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 50765
Sequence Length: 477
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Subcellular Location: Mitochondrion inner membrane
EC: 1.3.3.4
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Q10062 | MSIAICGGGIAGLSTAFYLARLIPKCTIDLYEKGPRLGGWLQSVKIPCADSPTGTVLFEQGPRTLRPAGVAGLANLDLISKLGIEDKLLRISSNSPSAKNRYIYYPDRLNEIPSSILGSIKSIMQPALRPMPLAMMLEPFRKSKRDSTDESVGSFMRRRFGKNVTDRVMSAMINGIYAGDLNDLSMHSSMFGFLAKIEKKYGNITLGLIRALLAREILSPAEKALKAALLAEPKTAELSNSMKSTSMFAFKEGIETITLSIADELKKMPNVKIHLNKPAKTLVPHKTQSLVDVNGQAYEYVVFANSSRNLENLISCPKMETPTSSVYVVNVYYKDPNVLPIRGFGLLIPSCTPNNPNHVLGIVFDSEQNNPENGSKVTVMMGGSAYTKNTSLIPTNPEEAVNNALKALQHTLKISSKPTLTNATLQQNCIPQYRVGHQDNLNSLKSWIEKNMGGRILLTGSWYNGVSIGDCIMNGHSTARKLASLMNSSS | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Catalytic Activity: 3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX
Sequence Mass (Da): 53462
Sequence Length: 490
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Subcellular Location: Mitochondrion
EC: 1.3.3.4
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P40012 | MLLPLTKLKPRAKVAVVGGGVSGLCFTYFLSKLRPDVEITLFESQNRTGGWIYSCNTRDMSGNPIMLEKGPRTLRGVSDGTVLIMDTLKDLGKEAVIQSIDKGCIADKKFLLDPSDKLVQVPNSISTTVKFLLNPLGKGLITGMMGEWFRKKSPHPGQDESVESICDRRFGNNYISNNMISALLRGIYGDDVSLLSAKRTFKKIYYNELKHGSNTQAMIDNMRGKSRSKKTENLHQSLTGCLNDYSNAFGKDRSKLLDLSNTLKKYPMLGLAGGLETFPKIVRNALNEFKNVKIVTGNPVTQIMKRPANETTIGLKAKSGDQYETFDHLRLTITPPKIAKLLPKDQNSLSKLLDEIQSNTIILVNYYLPNKDVIDADLQGFGYLVPKSNKNPGKLLGVIFDSVIERNFKPLFDKLSTNPNALNKYTKVTAMIGGCMLNEHGVPVVPSREVTINAVKDALNNHLGISNKDLEAGQWEFTIADRCLPRFHVGYDAWQERAERKLQESYGQTVSVGGMGFSRSPGVPDVIVDGFNDALQLSK | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Catalytic Activity: 3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX
Sequence Mass (Da): 59703
Sequence Length: 539
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Subcellular Location: Mitochondrion inner membrane
EC: 1.3.3.4
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P43309 | MTSLSPPVVTTPTVPNPATKPLSPFSQNNSQVSLLTKPKRSFARKVSCKATNNDQNDQAQSKLDRRNVLLGLGGLYGVAGMGTDPFAFAKPIAPPDVSKCGPADLPQGAVPTNCCPPPSTKIIDFKLPAPAKLRIRPPAHAVDQAYRDKYYKAMELMKALPDDDPRSFKQQAAVHCAYCDGAYDQVGFPELELQIHNSWLFFPFHRYYLYFFEKILGKLINDPTFALPFWNWDSPAGMPLPAIYADPKSPLYDKLRSANHQPPTLVDLDYNGTEDNVSKETTINANLKIMYRQMVSNSKNAKLFFGNPYRAGDEPDPGGGSIEGTPHAPVHLWTGDNTQPNFEDMGNFYSAGRDPIFFAHHSNVDRMWSIWKTLGGKRTDLTDSDWLDSGFLFYNENAELVRVKVRDCLETKNLGYVYQDVDIPWLSSKPTPRRAKVALSKVAKKLGVAHAAVASSSKVVAGTEFPISLGSKISTVVKRPKQKKRSKKAKEDEEEILVIEGIEFDRDVAVKFDVYVNDVDDLPSGPDKTEFAGSFVSVPHSHKHKKKMNTILRLGLTDLLEEIEAEDDDSVVVTLVPKFGAVKIGGIKIEFAS | Cofactor: Binds 2 copper ions per subunit.
Function: Catalyzes the oxidation of mono- and o-diphenols to o-diquinones.
Catalytic Activity: 2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O
Sequence Mass (Da): 65721
Sequence Length: 593
Subcellular Location: Plastid
EC: 1.10.3.1
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O81103 | MATAPSPTTMGTYSSLISTNSFSTFLPNKSQLSLSGKSKHYVARRSSISCKATNNNNSNNQNEQQEESSRLLGKLDRRNILIGLGGLYGATTLDRKPFAFADPIAPPDLTTCKPAEITPGGSETVPCCPPVTTKIKTFKPDLSIPLRTSPAAHQVTDEYLAKFKKAQAAMRALPDDDPRSMVQQAKVHCAYCNGAYPQVGFTDNDIQVHFSWLFFPFHRMYLYFYERILGKLIDDPTFALPYWNWDSPVGFPIPDIYTDTSSPLYDQYRNADHQPPVLVDLSYGGKDDDVDEQTRIDENLAIMYRQMVSGAKTPDLFFGHAYRAGNLNTGKYPGTIENMPHNNIHIWVGDPSQTHQEDMGNFYSAGRDPLFYAHHANVDRMWNIWKTLGGKRKDITDTDWLDAEFLFYDENAELVRVKVRDSLEPEKQLRYNYEPVSLPWLFTKPTARKTKNKTKAKVAATQLTSKFPATLVEVTTVEVARPKPRKRSKKEKVDEEELLIIKDIEFEGTEAVKFDVFINDDAESLSRRDKSEFAGSFVHVPQGKTTKAKTKTNLKLGITDLLEDLGAEDDSSVLVTLVPRVSNSPITIGGFKIEYSS | Cofactor: Binds 2 copper ions per subunit.
Function: Catalyzes the oxidation of mono- and o-diphenols to o-diquinones. Uses preferentially 4-methylcatechol and chlorogenic acid as substrates, followed by caffeic acid, pyrogallol, and catechol, but barely active toward dopamine and L-dopa. No activity detected with monophenols (e.g. phenol and tyramine).
Catalytic Activity: 2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O
Sequence Mass (Da): 67133
Sequence Length: 597
Subcellular Location: Plastid
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P43310 | MATLSSPTIITTTSILLNNPFLPKTPQLSAHHHRGVRSVNGKVSCQTKNNNGNDENNQFQLIQNPNTNTPYLLDRRNILLGLGGMYAALGSEGANYYNTLAAPILPDVEKCTLSDALWDGSVGDHCCPPPFDLNITKDFEFKNYHNHVKKVRRPAHKAYEDQEWLNDYKRAIAIMKSLPMSDPRSHMQQARVHCAYCDGSYPVLGHNDTRLEVHASWLFPSFHRWYLYFYERILGKLINKPDFALPYWNWDHRDGMRIPEIFKEMDSPLFDPNRNTNHLDKMMNLSFVSDEEGSDVNEDDQYEENILLMRKAMVYPSVSDDPNKAELFLGSPYRAGDKMEGDVSGAGILERMPHNSVHVWTRSNTIKGNQDMGAFWSAGRDPLFYCHHSNVDRMWSLWTDVLHGGNFPKTPEYDDYRNAYFYFYDENANPVRVYVRDSFDTERLGYKYEDQELPWMSITQQQQQQQRQQQRQPLLGGRLKTRTFSLVKKVLTELKVMLPLPLKYSVIKTKVDRPKKSRTKEDKLEHEEVLVINFKLGKSKDFIKFDVYINDGTDYKPEDKTKINLEYAGSFTSLTHGGGGGGGDMSHMAEEDMGKNTVLKLALNQLLEDLDATDDDSIQVTIVPKSGTDSIVITGIDIE | Cofactor: Binds 2 copper ions per subunit.
Function: Catalyzes the oxidation of mono- and o-diphenols to o-diquinones.
Catalytic Activity: 2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O
Sequence Mass (Da): 73237
Sequence Length: 639
Subcellular Location: Plastid
EC: 1.10.3.1
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A0A166YZR3 | MNDFVFSDIPDNVKPMASVEFDDPLTIATGDVLNWTLWLTRNFPALSSIIMRLPSSLVSMVTSSFEGANQMVQVKTSTHNLYSLSLPTHARKQIISQLVEHEKNHIGPKSKDCVMQRLLNAHRDSESKISIPTPDATLRSEAVGFTLAGTADPPNILALGTFMAARDSEMQKGLYKELKAIWPDLRSPAPSYNLLHQLPLLRGIIKESIRFTHGVATGPARLVGAGGARIGGYNVPAKASSFSAAATSDCS | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity . The single multifunctional NRPS ppzA is responsible for the biosynthesis of peramine . The condensation domain of ppzA is proposed to catalyze formation of a peptide bond between 1-pyrroline-5-carboxylate and arginine (By similarity). The methylation domain of ppzA would catalyze the N-methylation of the alpha-amino group of arginine (By similarity). The reductase domain is proposed to be responsible for reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase (By similarity). Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine (By similarity). This final oxidation to give the pyrrole functionality may be spontaneous (By similarity). In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium rileyi that contains additionnal pyrrolopyrazine biosynthesis genes (Probable). The 2-oxoglutarate-Fe(II) type oxidoreductases ppzC and ppzD could be candidates for conversion of proline into an oxidized derivative to be used by the ppzA A1-domain as substrate (Probable). The other ppz genes encode proteins predicted to derivatize peramine into more complex pyrrolopyrazine metabolites (Probable).
Sequence Mass (Da): 27201
Sequence Length: 251
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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C4PWA1 | MSESAELTELYSAIEETTRVVGAPCRRDTVRPILTAYEDVIAQSVISFRVQTGTSDAGDLDCRFTLLPKDMDPYATALSNGLTAKTDHPVGSLLEEVHRQFPVDCYGIDFGAVGGFKKAWSFFRPDSLQSASDLAALPSMPSGVSENLGLFDRYGMTDTVSVVGFDYAKRSVNLYFTGASPESFEPRGIQAILRECGLPEPSDELLRFGEEAFAIYVTLSWDSQKIERVTYSVNTPDPMALPVRIDTRIEQLVKDAPLGSAGHRYVYGVTATPKGEYHKIQKYFQWQSRVEKMLTADAG | Function: Involved in the biosynthesis of prenylated phenazines. Catalyzes the transfer of a dimethylallyl moiety to C-9 of 5,10-dihydrophenazine 1-carboxylate (dihydro-PCA). Specific for both dimethylallyl diphosphate and dihydro-PCA.
Catalytic Activity: 5,10-dihydrophenazine 1-carboxylate + dimethylallyl diphosphate = 5,10-dihydro-9-dimethylallylphenazine 1-carboxylate + diphosphate
Sequence Mass (Da): 33012
Sequence Length: 299
Pathway: Antibiotic biosynthesis; phenazine biosynthesis.
EC: 2.5.1.121
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P78968 | MGQGSSKHADSKLDSYPSFSRSDTQGSIKSLKSLKTVLGKGKDSNHDRRTSTDTTHSRHRYPETPPSLPPPPSPGILATSPAVLQKHQQEDSGNSSQSPTSPHPSNQPAMLSPSTAASQHHHHHSSSSSYAVSPTSPTSPTSSGPIGSNFDSASEHNGPVYPQDQQGPVIIPNSAISSTDPDDPETVVSLNVDEMIQRLIHVGYSRKSSKSVCLKNAEITSICMAVREIFLSQPTLLELTPPVKIVGDVHGQYSDLIRLFEMCGFPPSSNYLFLGDYVDRGKQSLETILLLFLYKIRYPENFFLLRGNHECANITRVYGFYDECKRRCNIKIWKTFINTFNCLPIASVVAGKIFCVHGGLSPSLSHMDDIREIPRPTDVPDYGLLNDLLWSDPADTENDWEDNERGVSFVFNKNVIRQFLAKHDFDLICRAHMVVEDGYEFFNDRTLCTVFSAPNYCGEFDNWGAVMSVNSELLCSFELIKPLDQAAIRRELKKSKRSGMAIYQSPPAEQVTQSV | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 57131
Sequence Length: 515
Subcellular Location: Cytoplasm
EC: 3.1.3.16
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P03772 | MRYYEKIDGSKYRNIWVVGDLHGCYTNLMNKLDTIGFDNKKDLLISVGDLVDRGAENVECLELITFPWFRAVRGNHEQMMIDGLSERGNVNHWLLNGGGWFFNLDYDKEILAKALAHKADELPLIIELVSKDKKYVICHADYPFDEYEFGKPVDHQQVIWNRERISNSQNGIVKEIKGADTFIFGHTPAVKPLKFANQMYIDTGAVFCGNLTLIQVQGEGA | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 25219
Sequence Length: 221
EC: 3.1.3.16
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O60828 | MPLPVALQTRLAKRGILKHLEPEPEEEIIAEDYDDDPVDYEATRLEGLPPSWYKVFDPSCGLPYYWNADTDLVSWLSPHDPNSVVTKSAKKLRSSNADAEEKLDRSHDKSDRGHDKSDRSHEKLDRGHDKSDRGHDKSDRDRERGYDKVDRERERDRERDRDRGYDKADREEGKERRHHRREELAPYPKSKKAVSRKDEELDPMDPSSYSDAPRGTWSTGLPKRNEAKTGADTTAAGPLFQQRPYPSPGAVLRANAEASRTKQQD | Function: Intrinsically disordered protein that acts as a scaffold, and which is involved in different processes, such as pre-mRNA splicing, transcription regulation, innate immunity and neuron development . Interacts with splicing-related factors via the intrinsically disordered region and regulates alternative splicing of target pre-mRNA species . May suppress the ability of POU3F2 to transactivate the DRD1 gene in a POU3F2 dependent manner. Can activate transcription directly or via association with the transcription machinery . May be involved in ATXN1 mutant-induced cell death . The interaction with ATXN1 mutant reduces levels of phosphorylated RNA polymerase II large subunit . Involved in the assembly of cytoplasmic stress granule, possibly by participating in the transport of neuronal RNA granules . Also acts as an innate immune sensor of infection by retroviruses, such as HIV, by detecting the presence of reverse-transcribed DNA in the cytosol . Directly binds retroviral reverse-transcribed DNA in the cytosol and interacts with CGAS, leading to activate the cGAS-STING signaling pathway, triggering type-I interferon production .
Sequence Mass (Da): 30472
Sequence Length: 265
Domain: The WW domain may play a role as a transcriptional activator directly or via association with the transcription machinery. The WW domain mediates interaction with WBP11, ATN1, SF3B1 and the C-terminal domain of the RNA polymerase II large subunit.
Subcellular Location: Nucleus
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P0AFM0 | MCEHHHAAKHILCSQCDMLVALPRLEHGQKAACPRCGTTLTVAWDAPRQRPTAYALAALFMLLLSNLFPFVNMNVAGVTSEITLLEIPGVLFSEDYASLGTFFLLFVQLVPAFCLITILLLVNRAELPVRLKEQLARVLFQLKTWGMAEIFLAGVLVSFVKLMAYGSIGVGSSFLPWCLFCVLQLRAFQCVDRRWLWDDIAPMPELRQPLKPGVTGIRQGLRSCSCCTAILPADEPVCPRCSTKGYVRRRNSLQWTLALLVTSIMLYLPANILPIMVTDLLGSKMPSTILAGVILLWSEGSYPVAAVIFLASIMVPTLKMIAIAWLCWDAKGHGKRDSERMHLIYEVVEFVGRWSMIDVFVIAVLSALVRMGGLMSIYPAMGALMFALVVIMTMFSAMTFDPRLSWDRQPESEHEES | Function: Component of a transport pathway that contributes to membrane integrity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46463
Sequence Length: 417
Subcellular Location: Cell inner membrane
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P43671 | MESNNGEAKIQKVKNWSPVWIFPIVTALIGAWVLFYHYSHQGPEVTLITANAEGIEGGKTTIKSRSVDVGVVESATLADDLTHVEIKARLNSGMEKLLHKDTVFWVVKPQIGREGISGLGTLLSGVYIELQPGAKGSKMDKYDLLDSPPLAPPDAKGIRVILDSKKAGQLSPGDPVLFRGYRVGSVETSTFDTQKRNISYQLFINAPYDRLVTNNVRFWKDSGIAVDLTSAGMRVEMGSLTTLLSGGVSFDVPEGLDLGQPVAPKTAFVLYDDQKSIQDSLYTDHIDYLMFFKDSVRGLQPGAPVEFRGIRLGTVSKVPFFAPNMRQTFNDDYRIPVLIRIEPERLKMQLGENADVVEHLGELLKRGLRGSLKTGNLVTGALYVDLDFYPNTPAITGIREFNGYQIIPTVSGGLAQIQQRLMEALDKINKLPLNPMIEQATSTLSESQRTMKNLQTTLDSMNKILASQSMQQLPTDMQSTLRELNRSMQGFQPGSAAYNKMVADMQRLDQVLRELQPVLKTLNEKSNALVFEAKDKKDPEPKRAKQ | Function: Component of a transport pathway that contributes to membrane integrity . May directly span the intermembrane space, facilitating the transport of substrates across the periplasm (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 60520
Sequence Length: 546
Subcellular Location: Cell inner membrane
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P0AB10 | MKKWLVTIAALWLAGCSSGEINKNYYQLPVVQSGTQSTASQGNRLLWVEQVTVPDYLAGNGVVYQTSDVKYVIANNNLWASPLDQQLRNTLVANLSTQLPGWVVASQPLGSAQDTLNVTVTEFNGRYDGKVIVSGEWLLNHQGQLIKRPFRLEGVQTQDGYDEMVKVLAGVWSQEAASIAQEIKRLP | Function: Component of a transport pathway that contributes to membrane integrity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 20634
Sequence Length: 187
Subcellular Location: Cell outer membrane
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Q2V4B2 | MAISKPPPLHFTFFHNQDSSIDTSDSNLALSIDTSRRRRDVLLTISGTLIPQLFFFDRKRSSSANAADFFNFGAPPPEPERTVELAQEGLRKNAENIKRIKEIMIEKKLWKEGGKELRRSASNMKQDFYLIIQAKPPKDRPLFRSLYSSLFNSITKMDYAARDGDETKVLEYYINIVAILDDIFPRI | Function: Required for both formation and activity of the chloroplast NAD(P)H dehydrogenase (NDH) complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21534
Sequence Length: 187
Subcellular Location: Plastid
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F4JP52 | MAIYYKFKSARDYDTISMDGPFITVGLLKEKIYETKHLGSGKDLDIVISNAQTNEEYLDEAMLIPKNTSVLIRRVPGRPRIRIITREEPRVEDKVENVQADMNNVITADASPVEDEFDEFGNDLYSIPDAPAVHSNNLCHDSAPADDEETKLKALIDTPALDWHQQGADSFGPGRGYGRGMAGRMGGRGFGMERTTPPPGYVCHRCNVSGHFIQHCSTNGNPNFDVKRVKPPTGIPKSMLMATPNGSYSLPSGAVAVLKPNEDAFEKEMEGLTSTTRSVGEFPPELKCPLCKEVMRDAALASKCCLKSYCDKCIRDHIIAKSMCVCGATHVLADDLLPNKTLRDTINRILESGNSSAENAGSMCQVQDMESVRCPPPKALSPTTSAASGGEKKPAPSNNNETSTLKPSIEIAEITSAWASAEIVKVEKPVDASANIQGSSNGKEAAVSQLNTQPPKEEMPQQVASGEQGKRKKKKPRMSGTDLAGPDYMMPMGPGPGNQYFNGFQPGFNGVQHGFNGVQPGFNGFHHGFNGFPGPFPGAMPPFVGYGFGGVIHPDPFAAQGFGFPNIPPPYRDLAEMGNRMNLQHPIMGREEFEAKKTEMKRKRENEIRRSEGGNVVRDSEKSRIMNNSAVTSSPVKPKSRQGPPPPISSDYDRRRRSDRSSPERQSSRRFTSPPRSSSRKSERDRHHDLDSEHDRRRDRPRETDRKHRKRSEKSSSDPTVEIDDNNKSNVFTRISFPEESSGKQRKTSKSSPAPPESSVAPVSSGRRHHSRREREMVEYDSSDDEDRHFKRKPSRYKRSPSVAPSDAGDEHFRHSKRSKGERARA | Function: E3 ubiquitin ligase acting as a negative regulator of oxidative stress tolerance, probably by mediating 26S proteasome-mediated degradation of PRMT13/PRMT4B, thus preventing APX1 and GPX1 accumulation via the reduction of histone H3 methylation (H3R17me2a). Confers sensitivity to cadmium CdCl(2) and salt NaCl stresses.
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): 91306
Sequence Length: 826
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q2KI51 | MAPGQMPHQPAPWRGTHPLFLLSPLMGLLSRAWSLLRAPGPPEPWLVEAVTEADQGGAGLEDEAKASLATYHALWGRHPQEETKDSGAAEEDREASPGACPNLEAKHSLPEAWGLSDDDDEKYGGEEATGVPREQKEFMDGQPAPLPLSLLIRSLPDLPGEEESKEEAVTGGGGNEVTAFSFPLSHWECCPGEEEEEEEENGEAVRVCRPVNGATEERTQTEAATKTSMSPSSVGSHLRAWECCSGKESEEEEKDKQAEKGDADPGPHFTSLAQRPSLRTWQHPSSAITEEEEDRDSEEMGASSSVPLTSAFLSDWVYQPEDTEEEDEEEEDCDSEATEDEGEAEVSSATPPPSAFLSAWVYRPGEDTEEEEDCDSEATEDEGEAEVSSATPPTSAFLSAWVYQPGDTEEEEDCDSEATEDEGEAEVSSATPPPSAFLSAWVYRPGEDTEEEDEYEDEDNESGAADLGPSPSLQTQSALLRDQIYQPGEKTDGGEAAEKWGEAESCPFRVAIYLPGEKPPPPWDPPRLPLRLQRRLKSAQTPTRHQDLERLLKTRKVRFSEKVSIHPLVVWAGPAQAARRGPWEQFARDRSRFARRIAQVQEELGPYLTPAARARAWARLGNPPTSLATVPAPTQTSPMTPIQATPLSHALASPSPPCVSPSLDLSGRRG | Function: Recruits the serine/threonine-protein phosphatase PPP1CA to prevents excessive phosphorylation of the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress. Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1. May promote apoptosis by inducing TP53 phosphorylation on 'Ser-15'. Plays an essential role in autophagy by tuning translation during starvation, thus enabling lysosomal biogenesis and a sustained autophagic flux.
PTM: Phosphorylated on tyrosine by LYN; which impairs its antiproliferative activity.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 73053
Sequence Length: 670
Subcellular Location: Endoplasmic reticulum membrane
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O75807 | MAPGQAPHQATPWRDAHPFFLLSPVMGLLSRAWSRLRGLGPLEPWLVEAVKGAALVEAGLEGEARTPLAIPHTPWGRRPEEEAEDSGGPGEDRETLGLKTSSSLPEAWGLLDDDDGMYGEREATSVPRGQGSQFADGQRAPLSPSLLIRTLQGSDKNPGEEKAEEEGVAEEEGVNKFSYPPSHRECCPAVEEEDDEEAVKKEAHRTSTSALSPGSKPSTWVSCPGEEENQATEDKRTERSKGARKTSVSPRSSGSDPRSWEYRSGEASEEKEEKAHKETGKGEAAPGPQSSAPAQRPQLKSWWCQPSDEEEGEVKALGAAEKDGEAECPPCIPPPSAFLKAWVYWPGEDTEEEEDEEEDEDSDSGSDEEEGEAEASSSTPATGVFLKSWVYQPGEDTEEEEDEDSDTGSAEDEREAETSASTPPASAFLKAWVYRPGEDTEEEEDEDVDSEDKEDDSEAALGEAESDPHPSHPDQRAHFRGWGYRPGKETEEEEAAEDWGEAEPCPFRVAIYVPGEKPPPPWAPPRLPLRLQRRLKRPETPTHDPDPETPLKARKVRFSEKVTVHFLAVWAGPAQAARQGPWEQLARDRSRFARRITQAQEELSPCLTPAARARAWARLRNPPLAPIPALTQTLPSSSVPSSPVQTTPLSQAVATPSRSSAAAAAALDLSGRRG | Function: Recruits the serine/threonine-protein phosphatase PPP1CA to prevents excessive phosphorylation of the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress . Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1 . May promote apoptosis by inducing p53/TP53 phosphorylation on 'Ser-15' . Plays an essential role in autophagy by tuning translation during starvation, thus enabling lysosomal biogenesis and a sustained autophagic flux . Acts also a viral restriction factor by attenuating HIV-1 replication . Mechanistically, mediates the inhibition of HIV-1 TAR RNA-mediated translation .
PTM: Phosphorylated at multiple Ser/Thr residues. Phosphorylated on tyrosine by LYN; which impairs its antiproliferative activity. Phosphorylation at Tyr-262 enhances proteasomal degradation, this position is dephosphorylated by PTPN2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 73478
Sequence Length: 674
Subcellular Location: Endoplasmic reticulum membrane
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Q6IN02 | MAPSPRPQHVLHWKEAHSFYLLSPLMGFLSRAWSRLRGPEVSEAWLAETVAGANQIEADALLTPPPVSENHLPLRETEGNGTPEWSKAAQRLCLDVEAQSSPPKTWGLSDIDEHNGKPGQDGLREQEVEHTAGLPTLQPLHLQGADKKVGEVVAREEGVSELAYPTSHWEGGPAEDEEDTETVKKAHQASAASIAPGYKPSTSVYCPGEAEHRATEEKGTDNKAEPSGSHSRVWEYHTRERPKQEGETKPEQHRAGQSHPCQNAEAEEGGPETSVCSGSAFLKAWVYRPGEDTEEEEDSDLDSAEEDTAHTCTTPHTSAFLKAWVYRPGEDTEEEDDGDWDSAEEDASQSCTTPHTSAFLKAWVYRPGEDTEEEDDSENVAPVDSETVDSCQSTQHCLPVEKTKGCGEAEPPPFQVAFYLPGQKPAPPWAAPKLPLRLQKRLRSFKAPARNQDPEIPLKGRKVHFSEKVTVHFLAVWAGPAQAARRGPWEQFARDRSRFARRIAQAEEQLGPYLTPAFRARAWTRLRNLPLPLSSSSLPLPEPCSSTEATPLSQDVTTPSPLPSEIPPPSLDLGGRRG | Function: Recruits the serine/threonine-protein phosphatase PPP1CA to prevents excessive phosphorylation of the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress. Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1. May promote apoptosis by inducing TP53 phosphorylation on 'Ser-15'. Plays an essential role in autophagy by tuning translation during starvation, thus enabling lysosomal biogenesis and a sustained autophagic flux.
PTM: Phosphorylated at multiple Ser/Thr residues. Phosphorylated on tyrosine by LYN; which impairs its antiproliferative activity. Phosphorylation at Tyr-236 enhances proteasomal degradation, this position is dephosphorylated by PTPN2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 63570
Sequence Length: 578
Subcellular Location: Endoplasmic reticulum membrane
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P23865 | MNMFFRLTALAGLLAIAGQTFAVEDITRADQIPVLKEETQHATVSERVTSRFTRSHYRQFDLDQAFSAKIFDRYLNLLDYSHNVLLASDVEQFAKKKTELGDELRSGKLDVFYDLYNLAQKRRFERYQYALSVLEKPMDFTGNDTYNLDRSKAPWPKNEAELNALWDSKVKFDELSLKLTGKTDKEIRETLTRRYKFAIRRLAQTNSEDVFSLAMTAFAREIDPHTNYLSPRNTEQFNTEMSLSLEGIGAVLQMDDDYTVINSMVAGGPAAKSKAISVGDKIVGVGQTGKPMVDVIGWRLDDVVALIKGPKGSKVRLEILPAGKGTKTRTVTLTRERIRLEDRAVKMSVKTVGKEKVGVLDIPGFYVGLTDDVKVQLQKLEKQNVSSVIIDLRSNGGGALTEAVSLSGLFIPAGPIVQVRDNNGKVREDSDTDGQVFYKGPLVVLVDRFSASASEIFAAAMQDYGRALVVGEPTFGKGTVQQYRSLNRIYDQMLRPEWPALGSVQYTIQKFYRVNGGSTQRKGVTPDIIMPTGNEETETGEKFEDNALPWDSIDAATYVKSGDLTAFEPELLKEHNARIAKDPEFQNIMKDIARFNAMKDKRNIVSLNYAVREKENNEDDATRLARLNERFKREGKPELKKLDDLPKDYQEPDPYLDETVNIALDLAKLEKARPAEQPAPVK | Function: Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses.
Catalytic Activity: The enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 76663
Sequence Length: 682
Subcellular Location: Cell inner membrane
EC: 3.4.21.102
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P45306 | MVMKFKMSKNVICYTWLSVCLSSAIPAFAVQPTLKPSDISIPAISEESQLATKRATTRLTQSHYRKIKLDDDFSEKIFDRYIKNLDFNHNTFLQSDIDELRQKYGTKLDEQLNQGDLSAAFDIYDVMMKRRYERYTYALSLLDKEPDLNGQDQIEIDREKAAAPQTEADANKLWDARVKNDIINLKLKDKKWSEIKAKLTKRYNLAIRRLTQTKADDIVQIYLNAFAREIDPHTSYLSPRTAKSFNESINLSLEGIGTTLQSEDDEISIKSLVPGAPAERSKKLHPGDKIIGVGQATGDIEDVVGWRLEDLVEKIKGKKGTKVRLEIEPAKGGKSRIITLVRDKVRIEDQAAKLTFEKVSGKNIAVIKIPSFYIGLTEDVKKLLVKLENQKAEALIVDLRENGGGALTEAVALSGLFITDGPVVQVRDAYQRIRVHEDDDATQQYKGLLFVMINRYSASASEIFAAAMQDYRRGIIIGQNTFGKGTVQQSRSLNFIYDLDQSPLGVLQYTIQKFYRVNGGSTQLKGVAADINFPEIIDAKEYGEDKEDNALAWDKIPSASYMEVGNINYIDNAVNILNEKHLARIAKDPEFVALNEELKVRNERRDRKFLSLNYKMRKAENDKDDARRLKDLNERFKREGKKALKDIDDLPKDYEAPDFFLKEAEKIAADFVIFNSDQKINQANGLSEAKTESKK | Function: Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses (By similarity).
Catalytic Activity: The enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 78870
Sequence Length: 695
Subcellular Location: Cell inner membrane
EC: 3.4.21.102
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Q9NQV5 | MLKMAEPIASLMIVECRACLRCSPLFLYQREKDRMTENMKECLAQTNAAVGDMVTVVKTEVCSPLRDQEYGQPCSRRPDSSAMEVEPKKLKGKRDLIVPKSFQQVDFWFCESCQEYFVDECPNHGPPVFVSDTPVPVGIPDRAALTIPQGMEVVKDTSGESDVRCVNEVIPKGHIFGPYEGQISTQDKSAGFFSWLIVDKNNRYKSIDGSDETKANWMRYVVISREEREQNLLAFQHSERIYFRACRDIRPGEWLRVWYSEDYMKRLHSMSQETIHRNLARGEKRLQREKSEQVLDNPEDLRGPIHLSVLRQGKSPYKRGFDEGDVHPQAKKKKIDLIFKDVLEASLESAKVEAHQLALSTSLVIRKVPKYQDDAYSQCATTMTHGVQNIGQTQGEGDWKVPQGVSKEPGQLEDEEEEPSSFKADSPAEASLASDPHELPTTSFCPNCIRLKKKVRELQAELDMLKSGKLPEPPVLPPQVLELPEFSDPAGKLVWMRLLSEGRVRSGLCGG | Function: May be involved in transcription regulation.
Sequence Mass (Da): 57863
Sequence Length: 511
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q9H4Q4 | MMGSVLPAEALVLKTGLKAPGLALAEVITSDILHSFLYGRWRNVLGEQLFEDKSHHASPKTAFTAEVLAQSFSGEVQKLSSLVLPAEVIIAQSSIPGEGLGIFSKTWIKAGTEMGPFTGRVIAPEHVDICKNNNLMWEVFNEDGTVRYFIDASQEDHRSWMTYIKCARNEQEQNLEVVQIGTSIFYKAIEMIPPDQELLVWYGNSHNTFLGIPGVPGLEEDQKKNKHEDFHPADSAAGPAGRMRCVICHRGFNSRSNLRSHMRIHTLDKPFVCRFCNRRFSQSSTLRNHVRLHTGERPYKCQVCQSAYSQLAGLRAHQKSARHRPPSTALQAHSPALPAPHAHAPALAAAAAAAAAAAAHHLPAMVL | Function: Involved in the positive regulation of histone H3-K9 dimethylation.
Sequence Mass (Da): 40403
Sequence Length: 367
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q9H4Q3 | MHGAARAPATSVSADCCIPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGELVDESGGSPLEWIGLIRAARNSQEQTLEAIADLPGGQIFYRALRDVQPGEELTVWYSNSLAQWFDIPTTATPTHDEKGEERYICWYCWRTFRYPNSLKAHLRFHCVFSGGGGGAFLHHEHAARQGAVPAADGLGLSPKPPAPDFAAPSQAGTLRPHPLGPPPVQACGAREGIKREASSAPSATSPTPGKWGQPKKGKEQLDRALDMSGAARGQGHFLGIVGGSSAGVGSLAFYPGVRSAFKPAGLARAAAAAHGDPYREESSSKQGAGLALGRLLGGGRACGRPGSGENSAAGGAGHHHHHHAHHHHHPKCLLAGDPPPPPPPGLPCSGALRGFPLLSVPPEEASAFKHVERAPPAAAALPGARYAQLPPAPGLPLERCALPPLDPGGLKAYPGGECSHLPAVMPAFTVYNGELLYGSPATTAYYPLKLHFGGLLKYPESISYFSGPAAAALSPAELGSLASIDREIAMHNQQLSEMAAGKGRGRLDSGTLPPAVAAAGGTGGGGSGGSGAGKPKTGHLCLYCGKLYSRKYGLKIHMRTHTGYKPLKCKVCLRPFGDPSNLNKHIRLHAEGNTPYRCEFCGKVLVRRRDLERHVKSRHPGQSLLAKAGDGPGAEPGYPPEPGDPKSDDSDVDVCFTDDQSDPEVGGGGERDL | Function: May be involved in transcriptional regulation. Is required for the differentiation of KISS1-expressing neurons in the arcuate (Arc) nucleus of the hypothalamus. Is a critical regulator of GABAergic cell fate in the cerebellum, required for normal postnatal cerebellar development (By similarity).
Sequence Mass (Da): 73981
Sequence Length: 707
Subcellular Location: Nucleus
EC: 2.1.1.-
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E9PZZ1 | MPAHVTPRTEDARRGAGPSSACGCSWFCHLRPVEDPASPSVCLAAVATMHGTSRTSATSVNADCCIPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGELVDESGGSPLEWIGLIRAARNPQEQTLEAIADLPGGQIFYRALRDVQPGEELTVWYSNSLAQWFDIPTTATPTHDEKGEERYICWYCWRTFRYPNSLKAHLRFHCVLSGGGGRAFLPQEHAARPGASPVAEGLGLPPKPTVPDLTAPVQAIALRPQAPAAQLAQACGARESIKREASLAPLATSPPPGKWGTPKKGKEQPDRAHSQFLGIVGGSSGGGGGLPFYPGVRSAFKPAGLARAAAQSDPYREEGGGKGPGLALGRLLGGGRAGGRPGSGESPAGHHHHHHHAHHHHHHHPKCLLAGEPPPAGLPCPGALRAFPLLAGHPEEASAFKHVERAPPAAATTSLPSARYAALPAPGLPVERCALQPLDGGSLKAYPGGGGGGECSPLPAVMPAFTVYSGDLLYGPPAAYYPLKLHLGGLLKYPESISYLSGPAAAAAAAAAAAAAAAAIGPAELGSLASIDREIAMHTQQLSEMAAGKSRARLDSGTLPPAVVAATGPGGGGGGGSAAGKPKTGHLCLYCGKLYSRKYGLKIHMRTHTGYKPLKCKVCLRPFGDPSNLNKHIRLHAEGNTPYRCEFCGKVLVRRRDLERHVKSRHPGQSLMAKAGDGPGPEPSYALEPGDPKSEDSDVDVCFTDDQSDPEAGGRGEHDS | Function: May be involved in transcriptional regulation. Is required for the differentiation of Kiss1-expressing neurons in the arcuate (Arc) nucleus of the hypothalamus. Is a critical regulator of GABAergic cell fate in the cerebellum, required for normal postnatal cerebellar development .
Sequence Mass (Da): 78705
Sequence Length: 754
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q9GZV8 | MALPRPSEAVPQDKVCYPPESSPQNLAAYYTPFPSYGHYRNSLATVEEDFQPFRQLEAAASAAPAMPPFPFRMAPPLLSPGLGLQREPLYDLPWYSKLPPWYPIPHVPREVPPFLSSSHEYAGASSEDLGHQIIGGDNESGPCCGPDTLIPPPPADASLLPEGLRTSQLLPCSPSKQSEDGPKPSNQEGKSPARFQFTEEDLHFVLYGVTPSLEHPASLHHAISGLLVPPDSSGSDSLPQTLDKDSLQLPEGLCLMQTVFGEVPHFGVFCSSFIAKGVRFGPFQGKVVNASEVKTYGDNSVMWEIFEDGHLSHFIDGKGGTGNWMSYVNCARFPKEQNLVAVQCQGHIFYESCKEIHQNQELLVWYGDCYEKFLDIPVSLQVTEPGKQPSGPSEESAEGYRCERCGKVFTYKYYRDKHLKYTPCVDKGDRKFPCSLCKRSFEKRDRLRIHILHVHEKHRPHKCSTCGKCFSQSSSLNKHMRVHSGDRPYQCVYCTKRFTASSILRTHIRQHSGEKPFKCKYCGKSFASHAAHDSHVRRSHKEDDGCSCSICGKIFSDQETFYSHMKFHEDY | Function: Transcription factor that has both positive and negative roles on transcription. Required for the maintenance of embryonic stem cell identity and the reacquisition of pluripotency in somatic cells. May play an essential role in germ cell development at 2 levels: the reacquisition of potential pluripotency, including SOX2 up-regulation, and successful epigenetic reprogramming, characterized by EHMT1 repression. Its association with CBFA2T2 is required for the functions in pluripotency and germ cell formation (By similarity). Directly up-regulates the expression of pluripotency gene POU5F1 through its proximal enhancer. Binds to the DNA consensus sequence 5'-GGTC[TC]CTAA-3'.
Sequence Mass (Da): 64062
Sequence Length: 571
Domain: The first 5 zinc fingers, but not the last one, are required for DNA-binding and transcriptional activity.
Subcellular Location: Nucleus
EC: 2.1.1.-
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E9Q3T6 | MALPPSGETQSQDKANYLPQSNPHHLTTYYAHAPGYSHFRNLATTEEEFQPWKLAAAVLESQAMAPLDAFRMTAPLLNPGLAVQSEPLYNLPWYKLSPWNRIPQFTPEVPRFLDSTEHRSSGSSNQNLVLGGGGGQISGQRWEAENLLLPSPVIASLLPDGIKSSQSISVPQTLNQEGKLPFCGFNFTEEELSFVLYGAIASPEHPTDLQHAISGILVPTESSGSNHLHKTLDKDSLQLPEGLCLMQTSFGDVPHFGVFCSDFIAKGVRFGPFRGRVVNASEVKAHRDNSRMWEIFEDGHLSHFIDGKGSGNWMSYVNCARFPKEQNLLAVQHQGQIFYESCRDIQRNQELLVWYGNGYEKFLGVPMNLRVTEQGGQQLSESSEESAEGYRCERCGKVFTYKYYRDKHLKYTPCVDKGDRKFPCSLCQRSFEKRDRLRIHILHVHERHRPYLCSTCGKSFSQSSSLNKHMRVHSGDRPYQCVYCTKKFTASSILRTHIRQHSGEKPFKCKHCGKAFASHAAHDSHVRRSHKDNGRSSCDICGKGFLDQEAFYAHMRLHKTC | Function: Transcription factor that has both positive and negative roles on transcription (By similarity). Plays a role in cellular pluripotency. Essential for germ cell development at 2 levels: the reacquisition of potential pluripotency, including SOX2 up-regulation, and successful epigenetic reprogramming, characterized by EHMT1 repression. Its association with CBFA2T2 is required for the functions in pluripotency and germ cell formation.
Sequence Mass (Da): 63374
Sequence Length: 561
Subcellular Location: Nucleus
EC: 2.1.1.-
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P13727 | MKLPLLLALLFGAVSALHLRSETSTFETPLGAKTLPEDEETPEQEMEETPCRELEEEEEWGSGSEDASKKDGAVESISVPDMVDKNLTCPEEEDTVKVVGIPGCQTCRYLLVRSLQTFSQAWFTCRRCYRGNLVSIHNFNINYRIQCSVSALNQGQVWIGGRITGSGRCRRFQWVDGSRWNFAYWAAHQPWSRGGHCVALCTRGGHWRRAHCLRRLPFICSY | Function: Cytotoxin and helminthotoxin. Also induces non-cytolytic histamine release from human basophils. Involved in antiparasitic defense mechanisms and immune hypersensitivity reactions. The proform acts as a proteinase inhibitor, reducing the activity of PAPPA.
PTM: Nitrated.
Sequence Mass (Da): 25206
Sequence Length: 222
Subcellular Location: Secreted
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Q61878 | MKFPLLLALLVGGASALHLSSETSDSKSPLMDENLPRDAEISGPEGEECPPGEELMPLEGEKEEGSGSEGVPGDEGAVSGQDVTDVDLQCPKEEDTTSLMGDSGCKTCRYLLVRRAECFDKAQSVCRRCYRGTLASIHSFSVNFGIQSAVRGINQGQVWIGGRIKGWGRCKRFRWVDGSSWNFAYWAAGQPCPGGGRCVTLCTQGGHWRLSHCVKRRPFICSY | Function: Cytotoxin and helminthotoxin. MBP also induces non-cytolytic histamine release from basophils. It is involved in antiparasitic defense mechanisms and immune hypersensitivity reactions (By similarity).
PTM: Nitrated.
Sequence Mass (Da): 24255
Sequence Length: 223
Subcellular Location: Secreted
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Q63189 | MKFPLLLALLVGGAFALHLSSEASDSKSPLVDESLPREAEISRPEVEESPPGEQLMSLEEEEEEEEEEGSGSEGALGNEGAVSGQDVTDENLQSPKEEDTTSLMGDSGFKTGRYLLVRRPECFNKAQLVCRSCYRGTLASIHSFSVNFRIQSFVRGINQGQVWIGGRIVGWGRCKRFRWIDGSSWNFAYWAAGQPRRGGGRCVTLCTRGGHWRRSGCGKRRPFICAY | Function: Cytotoxin and helminthotoxin. MBP also induces non-cytolytic histamine release from basophils. It is involved in antiparasitic defense mechanisms and immune hypersensitivity reactions (By similarity).
PTM: Nitrated.
Sequence Mass (Da): 25129
Sequence Length: 227
Subcellular Location: Secreted
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Q865B6 | MAWDMCNQDSVWTDIECAALVGEDQPLCPDLPELDLSELDVNDLDTDSFLGGLKWCSDQSEIISNQYNNEPSNIFEKIDEENEANLLAVLTETLDSLPVDEDGLPSFDALTDGDVTTENEASPSSMPDGTPPPQEAEEPSLLKKLLLAPANTQLSYNECSGLSTQNHANHNHRIRTNPAVVKTENSWSNKAKSICQQQKPQRRPCSELLKYLTTNDDPPHTKPTETRNSSRDKCTSKKKAHTQSQSQHLQAKPTSLSLPLTPESPNDPKGSPFENKTIERTLSVELSGTAGLTPPTTPPHKANQDNPFRASPKLKPPCKTVVPPPSKKTRYSESSGTHGNNSTKKGPEQSELYAQLSKTSALGGGHEERKARRPSLRLFGDHDYCQSINSKAEILINISQELHDSRQLDSKDAASDWQRQMCSSTDSDQCYLTETSEASRQVSPGSARKQLQDQEIRAELNKHFGHPSQAVFDDEADKTSELRDSDFSNEQFSKLPMFINSGLAMDGLFDDSEDESDKLNSPWDGTQSYSLFDVSPSCSSFNSPCRDSVSPPKSLFSQRPQRMRSRSRSFSQHRSCSRSPYSRSRSRSPGSRSSSRSCYYSESGHCRHRTHRNSPLCARSRSRSPYSRRPRYDSYEEYQHERLKREEYRREYEKRESERAKQRERQRQKAIEERRVIYVGKIRPDTTRTELRDRFEVFGEIEECTVNLRDDGDSYGFITYRYTCDAFAALENGYTLRRSNETDFELYFCGRKQFFKSNYADLDSNSDDFDPASTKSKYDSLDFDSLLKEAQRSLRR | Function: Transcriptional coactivator for steroid receptors and nuclear receptors. Greatly increases the transcriptional activity of PPARG and thyroid hormone receptor on the uncoupling protein promoter. Can regulate key mitochondrial genes that contribute to the program of adaptive thermogenesis. Plays an essential role in metabolic reprogramming in response to dietary availability through coordination of the expression of a wide array of genes involved in glucose and fatty acid metabolism. Acts as a key regulator of gluconeogenesis: stimulates hepatic gluconeogenesis by increasing the expression of gluconeogenic enzymes, and acting together with FOXO1 to promote the fasting gluconeogenic program (By similarity). Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner. Also involved in the integration of the circadian rhythms and energy metabolism. Required for oscillatory expression of clock genes, such as BMAL1 and NR1D1, through the coactivation of RORA and RORC, and metabolic genes, such as PDK4 and PEPCK (By similarity).
PTM: Phosphorylation by AMPK in skeletal muscle increases activation of its own promoter. Phosphorylated by CLK2.
Sequence Mass (Da): 90336
Sequence Length: 796
Subcellular Location: Nucleus
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Q9QYK2 | MAWDMCSQDSVWSDIECAALVGEDQPLCPDLPELDLSELDVNDLDTDSFLGGLKWCSDQSEIISNQYNNEPANIFEKIDEENEANLLAVLTETLDSLPVDEDGLPSFDALTDGDVTTDNEASPSSMPDGTPPPQEAEEPSLLKKLLLAPANTQLSYNECSGLSTQNHANHTHRIRTNPAIVKTENSWSNKAKSICQQQKPQRRPCSELLKYLTTNDDPPHTKPTENRNSSRDKCASKKKSHTQPQSQHAQAKPTTLSLPLTPESPNDPKGSPFENKTIERTLSVELSGTAGLTPPTTPPHKANQDNPFKASPKLKPSCKTVVPPPTKRARYSECSGTQGSHSTKKGPEQSELYAQLSKSSVLSRGHEERKTKRPSLRLFGDHDYCQSVNSKTDILINISQELQDSRQLDFKDASCDWQGHICSSTDSSQCYLRETLEASKQVSPCSTRKQLQDQEIRAELNKHFGHPSQAVFDDKVDKTSELRDGNFSNEQFSKLPVFINSGLAMDGLFDDSEDENDKLSYPWDGTQSYSLFDVSPSCSSFNSPCRDSVSPPKSLFSQRPQRMRSRSRSFSRHRSCSRSPYSRSRSRSPGSRSSSRSCYYYESSHYRHRTHRNSPLYVRSRSRSPYSRRPRYDSYEANEHERLKRDEYRREYEKRESERAKQRERQKQKAIEERRVIYVGKIRPDTTRTELRDRFEVFGEIEECTVNLRDDGDSYGFITYRYTCDAFAALENGYTLRRSNETDFELYFCGRKQFFKSNYADLDSNSDDFDPASTKSKYDSLDFDSLLKEAQRSLRR | Function: Transcriptional coactivator for steroid receptors and nuclear receptors. Greatly increases the transcriptional activity of PPARG and thyroid hormone receptor on the uncoupling protein promoter. Can regulate key mitochondrial genes that contribute to the program of adaptive thermogenesis. Plays an essential role in metabolic reprogramming in response to dietary availability through coordination of the expression of a wide array of genes involved in glucose and fatty acid metabolism. Acts as a key regulator of gluconeogenesis: stimulates hepatic gluconeogenesis by increasing the expression of gluconeogenic enzymes, and acting together with FOXO1 to promote the fasting gluconeogenic program (By similarity). Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner. Also involved in the integration of the circadian rhythms and energy metabolism. Required for oscillatory expression of clock genes, such as BMAL1 and NR1D1, through the coactivation of RORA and RORC, and metabolic genes, such as PDK4 and PEPCK (By similarity).
PTM: Phosphorylation by AMPK in skeletal muscle increases activation of its own promoter. Phosphorylated by CLK2.
Sequence Mass (Da): 90622
Sequence Length: 796
Subcellular Location: Nucleus
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Q86YN6 | MAGNDCGALLDEELSSFFLNYLADTQGGGSGEEQLYADFPELDLSQLDASDFDSATCFGELQWCPENSETEPNQYSPDDSELFQIDSENEALLAELTKTLDDIPEDDVGLAAFPALDGGDALSCTSASPAPSSAPPSPAPEKPSAPAPEVDELSLLQKLLLATSYPTSSSDTQKEGTAWRQAGLRSKSQRPCVKADSTQDKKAPMMQSQSRSCTELHKHLTSAQCCLQDRGLQPPCLQSPRLPAKEDKEPGEDCPSPQPAPASPRDSLALGRADPGAPVSQEDMQAMVQLIRYMHTYCLPQRKLPPQTPEPLPKACSNPSQQVRSRPWSRHHSKASWAEFSILRELLAQDVLCDVSKPYRLATPVYASLTPRSRPRPPKDSQASPGRPSSVEEVRIAASPKSTGPRPSLRPLRLEVKREVRRPARLQQQEEEDEEEEEEEEEEEKEEEEEWGRKRPGRGLPWTKLGRKLESSVCPVRRSRRLNPELGPWLTFADEPLVPSEPQGALPSLCLAPKAYDVERELGSPTDEDSGQDQQLLRGPQIPALESPCESGCGDMDEDPSCPQLPPRDSPRCLMLALSQSDPTFGKKSFEQTLTVELCGTAGLTPPTTPPYKPTEEDPFKPDIKHSLGKEIALSLPSPEGLSLKATPGAAHKLPKKHPERSELLSHLRHATAQPASQAGQKRPFSCSFGDHDYCQVLRPEGVLQRKVLRSWEPSGVHLEDWPQQGAPWAEAQAPGREEDRSCDAGAPPKDSTLLRDHEIRASLTKHFGLLETALEEEDLASCKSPEYDTVFEDSSSSSGESSFLPEEEEEEGEEEEEDDEEEDSGVSPTCSDHCPYQSPPSKANRQLCSRSRSSSGSSPCHSWSPATRRNFRCESRGPCSDRTPSIRHARKRREKAIGEGRVVYIQNLSSDMSSRELKRRFEVFGEIEECEVLTRNRRGEKYGFITYRCSEHAALSLTKGAALRKRNEPSFQLSYGGLRHFCWPRYTDYDSNSEEALPASGKSKYEAMDFDSLLKEAQQSLH | Function: Plays a role of stimulator of transcription factors and nuclear receptors activities. Activates transcriptional activity of estrogen receptor alpha, nuclear respiratory factor 1 (NRF1) and glucocorticoid receptor in the presence of glucocorticoids. May play a role in constitutive non-adrenergic-mediated mitochondrial biogenesis as suggested by increased basal oxygen consumption and mitochondrial number when overexpressed. May be involved in fat oxidation and non-oxidative glucose metabolism and in the regulation of energy expenditure. Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner.
Sequence Mass (Da): 113222
Sequence Length: 1023
Domain: Contains 2 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, which are usually required for the association with nuclear receptors.
Subcellular Location: Nucleus
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P41783 | METSKEKTITSPGPYIVRLLNSSLNGCEFPLLTGRTLFVVGQSDALTASGQLPDIPADSFFIPLDHGGVNFEIQVDTDATEIILHELKEGNSESRSVQLNTPIQVGELLILIRPESEPWVPEQPEKLETSAKKNEPRFKNGIVAALAGFFILGIGTVGTLWILNSPQRQAAELDSLLGQEKERFQVLPGRDKMLYVAAQNERDTLWARQVLARGDYDKNARVINENEENKRISIWLDTYYPQLAYYRIHFDEPRKPVFWLSRQRNTMSKKELEVLSQKLRALMPYADSVNITLMDDVTAAGQAEAGLKQQALPYSRRNHKGGVTFVIQGALDDVEILRARQFVDSYYRTWGGRYVQFAIELKDDWLKGRSFQYGAEGYIKMSPGHWYFPSPL | Function: Required for invasion of epithelial cells.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 44460
Sequence Length: 392
Subcellular Location: Cell membrane
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P41786 | MIRRYLYTFLLVMTLAGCKDKDLLKGLDQEQANEVIAVLQMHNIEANKIDSGKLGYSITVAEPDFTAAVYWIKTYQLPPRPRVEIAQMFPADSLVSSPRAEKARLYSAIEQRLEQSLQTMEGVLSARVHISYDIDAGENGRPPKPVHLSALAVYERGSPLAHQISDIKRFLKNSFADVDYDNISVVLSERSDAQLQAPGTPVKRNSFATSWIVLIILLSVMSAGFGVWYYKNHYARNKKGITADDKAKSSNE | Function: Required for invasion of epithelial cells. Could be involved in protein secretion.
Location Topology: Lipid-anchor
Sequence Mass (Da): 28210
Sequence Length: 252
Subcellular Location: Cell outer membrane
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Q84JQ4 | MESKCLMFVSIVSVFFMVVNGVSETETLLKFKNSLVIGRANALESWNRRNPPCKWTGVLCDRGFVWGLRLENLELSGSIDIEALMGLNSLRSLSFINNKFKGPFPEFKKLVALKSLYLSNNQFDLEIPKDAFDGMGWLKKLHLEQNNFIGEIPTSLVKSPKLIELRLDGNRFTGQIPEFRHHPNMLNLSNNALAGQIPNSFSTMDPKLFEGNKGLCGKPLDTKCSSPYNHSSEPKSSTKKTSSKFLYIVAAAVAALAASLIIIGVVIFLIRRRKKKQPLLSAEPGPSSLQMRAGIQESERGQGSYHSQNRAAKKMIHTTKLSFLRDDKGKFELQDLLKASAEILGSGCFGASYKTLLSNGSVMVVKRFKHMNSAGIDEFQEHMKRLGRLNHENLLPIVAYYYKKEEKLFVSDFVANGSLAAHLHGHKSLGQPSLDWPTRFNIVKGVGRGLLYLHKNLPSLMAPHGHLKSSNVLLSEKFEPLLMDYGLIPMINEESAQELMVAYKSPEYVKQSRVTKKTDVWGLGVLILEILTGKLLESFSQVDKESEEDLASWVRSSFKGEWTQELFDQEMGKTSNCEAHILNLMRIGLSCCEVDVEKRLDIREAVEKMEDLMKEREQGDDDFYSTYASEADGRSSRGLSSEGINLS | Function: Receptor-like kinase involved in the control of pollen germination and pollen tube polar growth . Phosphorylates ROPGEF1 in its C-terminal region, releasing its auto-inhibition, and thereby activating the ROP1 signaling pathway . May act as a scaffolding protein, recruiting ROPGEF12 to the plasma membrane by binding to its C-terminal domain . Phosphorylates ROPGEF12, releasing its auto-inhibition .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 72522
Sequence Length: 647
Domain: The protein kinase domain may be catalytically impaired due to the lack of the conserved Asp active site at position 466, which is replaced by a His residue.
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q20443 | MKKLASLQFFNLKLLLNGESSRGFSKFKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLIVMERPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVLRRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQQTLSWDALTKNKVQKKTSESSDDHHSETLGDHSETEEDRSPPTSSVSQQPGSADEGVGLSASSSNTHNQKKPNHKEFRMAKTSLLAPPTSIEMKAAVQASKTPTQFNVHTALKNQRQIKKHHSPQPPNSTVLTALRRAMSREAQNRISGVFSQD | Function: Involved in the negative regulation of synaptic differentiation in PLM neurons.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 49769
Sequence Length: 441
EC: 2.7.11.1
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Q9LPT1 | MRNWEDPFTLACNTALKKNLPSCIFIIIFISVLCPVAMSQVVVPDSDADCLLRFKDTLANGSEFRSWDPLSSPCQGNTANWFGVLCSNYVWGLQLEGMGLTGKLNLDPLVPMKNLRTISFMNNNFNGPMPQVKRFTSLKSLYLSNNRFSGEIPADAFLGMPLLKKILLANNAFRGTIPSSLASLPMLLELRLNGNQFQGQIPSFQQKDLKLASFENNDLDGPIPESLRNMDPGSFAGNKGLCDAPLSPCSSSSPGVPVVPVSPVDPKSTSPPTGKKAGSFYTLAIILIVIGIILVIIALVFCFVQSRRRNFLSAYPSSAGKERIESYNYHQSTNKNNKPAESVNHTRRGSMPDPGGRLLFVRDDIQRFDLQDLLRASAEVLGSGTFGASYKAAISSGQTLVVKRYKHMNNVGRDEFHEHMRRLGRLNHPNILPLVAYYYRREEKLLVTEFMPNSSLASHLHANNSAGLDWITRLKIIKGVAKGLSYLFDELPTLTIPHGHMKSSNIVLDDSFEPLLTDYALRPMMSSEHAHNFMTAYKSPEYRPSKGQIITKKTDVWCFGVLILEVLTGRFPENYLTQGYDSNMSLVTWVNDMVKEKKTGDVFDKEMKGKKNCKAEMINLLKIGLRCCEEEEERRMDMREVVEMVEMLREGESEDDFGSMDHRGTHNNVYSSMLLDDDDFGFSMNR | Function: Receptor-like kinase involved in the control of pollen germination and pollen tube polar growth . The extracellular domain serves as a sensor for peptides derived from GRI . May act as a downstream element for ROS-dependent cell death induced by GRI .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 76861
Sequence Length: 686
Domain: The protein kinase domain may be catalytically impaired due to the lack of the conserved Asp active site at position 500, which is replaced by a His residue.
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q3E991 | MAAAVLNPGFFLLILLLSFSISPSLQYVSESEPLVRFKNSVKITKGDLNSWREGTDPCSGKWFGIYCQKGLTVSGIHVTRLGLSGTITVDDLKDLPNLKTIRLDNNLLSGPLPHFFKLRGLKSLMLSNNSFSGEIRDDFFKDMSKLKRLFLDHNKFEGSIPSSITQLPQLEELHMQSNNLTGEIPPEFGSMKNLKVLDLSTNSLDGIVPQSIADKKNLAVNLTENEYLCGPVVDVGCENIELNDPQEGQPPSKPSSSVPETSNKAAINAIMVSISLLLLFFIIVGVIKRRNKKKNPDFRMLANNRENDVVEVRISESSSTTAKRSTDSSRKRGGHSDDGSTKKGVSNIGKGGNGGGGGALGGGMGDIIMVNTDKGSFGLPDLMKAAAEVLGNGSLGSAYKAVMTTGLSVVVKRIRDMNQLAREPFDVEMRRFGKLRHPNILTPLAYHYRREEKLVVSEYMPKSSLLYVLHGDRGIYHSELTWATRLKIIQGVAHGMKFLHEEFASYDLPHGNLKSSNVLLSETYEPLISDYAFLPLLQPSNASQALFAFKTPEFAQTQQVSHKSDVYCLGIIILEILTGKFPSQYLNNGKGGTDIVQWVQSSVAEQKEEELIDPEIVNNTESMRQMVELLRVGAACIASNPDERLDMREAVRRIEQVKT | Function: Key receptor for sensing species-specific attractants in cooperation with other pollen receptor-like kinases . Essential for pollen tube reorientation toward attractant peptides .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 72637
Sequence Length: 659
Domain: The juxtamembrane domain (288-383) is required for interactions with ROPGEFs, while the kinase domain (384-659) is required for pollen tube growth.
Subcellular Location: Cell membrane
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Q81WH6 | MLIGKRLNDRYKLLKMIGGGGMANVYLAHDDILGRDVAVKILRLDYSNNEEFIKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVMEYVPGQTLKQYIIERGMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGVIKVTDFGIATATSATTITHTNSVLGSVHYLSPEQARGGIANKQSDIYSLGIVMFELLTGRQPFSGESAVAIALKHLQSEIPSPKRWNENIPQSVENIILKATAKDPFHRYQSANAMKRDIETALYPERINEQPFYIPEDMEATKAIPIIQQEQLFENVTDETIVLKGSKVDEQIRKEETDLSKKKKRSNKWLKILITTFLLLAIGITLALTVIPGFFIPKDVKVPDVAGMKYTTAVNTLVEKGFEVTEPNIVYTDDVETGDVIKTDPVAGRVVKENSKITIYQSGGKKKSKMIDFTGKDLESIRTELEEKYKQVTVYYIEDDRPKGAIVEQIPTSDQMVVEAEQELKIWVSKGPYQIRPGDFSRWTENSVTGYLNERKLTPDIKREYSDTVDKGLVISQSPKPGTPLKEGDKVTIIISEGPKPKVTKTVKVDNISIPYESSIIGEKKPQTIEIYKEDMQQKMDRPIETRTISESATISLEFVIQEDTKGRYKIVRDGVTIIDKEVPYPTQ | Function: Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Probably autophosphorylates and phosphorylates FusA (EF-G, elongation factor G); the latter modification is likely necessary for germination in response to peptidoglycan.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 74153
Sequence Length: 657
Domain: The C-terminal extracellular domain containing the PASTA repeats binds peptidoglycan.
Subcellular Location: Spore membrane
EC: 2.7.11.1
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O34507 | MLIGKRISGRYQILRVIGGGGMANVYLAEDIILDREVAIKILRFDYANDNEFIRRFRREAQSASSLDHPNIVSIYDLGEEDDIYYIVMEYVEGMTLKEYITANGPLHPKEALNIMEQIVSAIAHAHQNQIVHRDIKPHNILIDHMGNIKVTDFGIATALSSTTITHTNSVLGSVHYLSPEQARGGLATKKSDIYALGIVLFELLTGRIPFDGESAVSIALKHLQAETPSAKRWNPSVPQSVENIILKATAKDPFHRYETAEDMEADIKTAFDADRLNEKRFTIQEDEEMTKAIPIIKDEELAKAAGEKEAEVTTAQENKTKKNGKRKKWPWVLLTICLVFITAGILAVTVFPSLFMPKDVKIPDVSGMEYEKAAGLLEKEGLQVDSEVLEISDEKIEEGLMVKTDPKADTTVKEGATVTLYKSTGKAKTEIGDVTGQTVDQAKKALKDQGFNHVTVNEVNDEKNAGTVIDQNPSAGTELVPSEDQVKLTVSIGPEDITLRDLKTYSKEAASGYLEDNGLKLVEKEAYSDDVPEGQVVKQKPAAGTAVKPGNEVEVTFSLGPEKKPAKTVKEKVKIPYEPENEGDELQVQIAVDDADHSISDTYEEFKIKEPTERTIELKIEPGQKGYYQVMVNNKVVSYKTIEYPKDE | Function: Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan . Another group did not detect phosphorylation of EF-G . PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests that they form a functional couple in vivo. Might also be involved in sporulation and biofilm formation. Does not seem to be involved in stress response.
PTM: Autophosphorylation on threonine residue(s) and serine residue considerably increases the kinase activity of the protein. Dephosphorylated in vitro by PrpC.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 71866
Sequence Length: 648
Domain: The cytoplasmic domain has Ser/Thr kinase activity . The C-terminal extracellular domain containing the PASTA repeats binds peptidoglycan.
Subcellular Location: Spore membrane
EC: 2.7.11.1
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A6QGC0 | MIGKIINERYKIVDKLGGGGMSTVYLAEDTILNIKVAIKAIFIPPREKEETLKRFEREVHNSSQLSHQNIVSMIDVDEEDDCYYLVMEYIEGPTLSEYIESHGPLSVDTAINFTNQILDGIKHAHDMRIVHRDIKPQNILIDSNKTLKIFDFGIAKALSETSLTQTNHVLGTVQYFSPEQAKGEATDECTDIYSIGIVLYEMLVGEPPFNGETAVSIAIKHIQDSVPNVTTDVRKDIPQSLSNVILRATEKDKANRYKTIQEMKDDLSSVLHENRANEDVYELDKMKTIAVPLKKEDLAKHISEHKSNQPKRETTQVPIVNGPAHHQQFQKPEGTVYEPKPKKKSTRKIVLLSLIFSLLMIALVSFVAMAMFGNKYEETPDVIGKSVKEAEQIFNKNNLKLGKISRSYSDKYPENEIIKTTPNTGERVERGDSVDVVISKGPEKVKMPNVIGLPKEEALQKLKSLGLKDVTIEKVYNNQAPKGYIANQSVTANTEIAIHDSNIKLYESLGIKQVYVEDFEHKSFSKAKKALEEKGFKVESKEEYSDDIDEGDVISQSPKGKSVDEGSTISFVVSKGKKSDSSDVKTTTESVDVPYTGKNDKSQKVKVYIKDKDNDGSTEKGSFDITSDQRIDIPLRIEKGKTASYIVKVDGKTVAEKEVSYDDV | Function: Probable protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing either m-Dpm (meso-diaminopimelate) or L-lys, which act as spore germinants. Probably autophosphorylates and phosphorylates FusA (EF-G, elongation factor G); the latter modification is likely necessary for germination in response to peptidoglycan.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 74363
Sequence Length: 664
Domain: The C-terminal extracellular domain containing the PASTA repeats binds peptidoglycan.
Subcellular Location: Spore membrane
EC: 2.7.11.1
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Q7KTX7 | MSFIFKFIATFVRKMLELLQFGGKTLTHTLSIYVKTNTGKTLTVNLEPQWDIKNVKELVAPQLGLQPDDLKIIFAGKELSDATTIEQCDLGQQSVLHAIRLRPPVQRQKIQSATLEEEEPSLSDEASKPLNETLLDLQLESEERLNITDEERVRAKAHFFVHCSQCDKLCNGKLRVRCALCKGGAFTVHRDPECWDDVLKSRRIPGHCESLEVACVDNAAGDPPFAEFFFKCAEHVSGGEKDFAAPLNLIKNNIKNVPCLACTDVSDTVLVFPCASQHVTCIDCFRHYCRSRLGERQFMPHPDFGYTLPCPAGCEHSFIEEIHHFKLLTREEYDRYQRFATEEYVLQAGGVLCPQPGCGMGLLVEPDCRKVTCQNGCGYVFCRNCLQGYHIGECLPEGTGASATNSCEYTVDPNRAAEARWDEASNVTIKVSTKPCPKCRTPTERDGGCMHMVCTRAGCGFEWCWVCQTEWTRDCMGAHWFG | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as Paris, Marf, Opa1, Miro, pnut, Septin1, Tom20 and porin . Mediates monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates, depending on the context . Protects against mitochondrial dysfunction during cellular stress, by acting downstream of Pink1, to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components . Depending on the severity of mitochondrial damage and/or dysfunction, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to regulating mitochondrial dynamics and eliminating severely damaged mitochondria via mitophagy . Appears to be particularly important in maintaining the physiology and function of cells with high energy demands that are undergoing stress or altered metabolic environment, including spermatids, muscle cells and neurons such as the dopaminergic (DA) neurons . Activation and recruitment onto the outer membrane of damaged/dysfunctional mitochondria (OMM) requires Pink1-mediated phosphorylation of both park and ubiquitin . In depolarized mitochondria, mediates the decision between mitophagy or preventing apoptosis by inducing either the poly- or monoubiquitination of porin/VDAC; polyubiquitination of porin promotes mitophagy, while monoubiquitination of porin decreases mitochondrial calcium influx which ultimately inhibits apoptosis . When cellular stress results in irreversible mitochondrial damage, promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by promoting the ubiquitination of mitochondrial proteins . Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains following mitochondrial damage, leading to mitophagy . In developing tissues, inhibits JNK-mediated apoptosis by negatively regulating bsk transcription . The Pink1-park pathway also promotes fission and/or inhibits fusion of damaged mitochondria by mediating the ubiquitination and subsequent degradation of proteins involved in mitochondrial fusion/fission such as Marf, Opa1 and fzo . This prevents the refusion of unhealthy mitochondria with the healthy mitochondrial network and/or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes . Regulates motility of damaged mitochondria by phosphorylating Miro which likely promotes its park-dependent degradation by the proteasome; in motor neurons, this inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria being eliminated in the soma . The Pink1-park pathway is also involved in mitochondrial regeneration processes such as promoting mitochondrial biogenesis, activating localized mitochondrial repair, promoting selective turnover of mitochondrial proteins and initiating the mitochondrial import of endogenous proteins . Involved in mitochondrial biogenesis via the ubiquitination of transcriptional repressor Paris which leads to its subsequent proteasomal degradation and allows activation of the transcription factor srl . Promotes localized mitochondrial repair by activating the translation of specific nuclear-encoded mitochondrial RNAs (nc-mtRNAs) on the mitochondrial surface, including several key electron transport chain component nc-mtRNAs .
PTM: Auto-ubiquitinates in an E2-dependent manner leading to its own degradation.
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
Sequence Mass (Da): 54105
Sequence Length: 482
Domain: The RING-type 1 zinc finger domain is required for ubiquitination activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Mitochondrion
EC: 2.3.2.31
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Q04AV7 | MKLLEIKIESSYDVEDALAYFATEDLKALGTEARRRSDFEQAGWLHDSTVVDMDDIPNLPDELEFIAYFDEETDPEEMVKCFKDKLAELAGYGLKTAPGEISVDYVADQDWNTVWKKYYHVINLSRHLAIVPEWEDYQPVFKDQEIIRLDPGLAFGTGNHQTTQLAMLGIERAMVKPLTVADVGTGSGILAIAAHKLGAKSVLATDISDESMTAAEENAALNGIYDIALQKTSLLADVDGKFDLIVANILAEILLDLIPQLDSHLNEDGQVIFSGIDYLQLPKIEQALAENSFQIDLKMRAGRWIGLAISRKHD | 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): 34931
Sequence Length: 314
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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C4Z0Q0 | MKWNKYSIQTTTDAVDMISSALNDIGIEGIEIEDNVQLTKEEAKSMFVDFIPDLPPDDGRAKVNFYIDSEEDDGSMLEKVKAELEDLRMFIDIGEGTITESETEDKDWINNWKQYWHTFTIGDLFIKPTWEPETEEMKGHAVLSIDPGTAFGTGSHETTRMVIKQLQKYVKDGDEVLDVGCGSGILSVVALKYGAKHAFGTDLDPNAIIASEENAEQNNIDKKQLEVIEGNIIDDKAVKDACGYECYDIVCANILADVLEPLSTCIHEHMKHGAYFITSGIIDTKENEVAEAFKKNPELEIVEINHDGEWVNITARRK | 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): 35659
Sequence Length: 318
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q038Q5 | MNDWTALTVTTTTEAIEAVSNILMEAGAVGIQIKDAADFKKETVDAHGTWFDPKTVPHLASGAQVIGYFDPATSLVEQRDHIATRVRGLAQFGLDPGAATVTLADVRQADWANVWKQYYHPLRVSRFLTIVPKWEHYTPQQAGELQLTLDPGMAFGTGTHPTTQLMLSLLESVIRGGETMIDVGTGSGILAIAAERLGVGDILATDVDEIAVRNAEANIKLNPVSHITVIANDLLKGITLSADLIVANILAEVLVPLIPQVRPRLKAHGHFLLAGIIANKATLIIRTLEDNGFSIAQRREAGGWVALDAVIKETA | 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): 33871
Sequence Length: 315
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
A9KKT8 | MKWKKLSLETTTEAVDLVCDMLLSLGIEGIEVVDKVPITEEEKKRMFIDILPELGEDDGIATINFYLENEEDLPSLKVSIQEGLDELRDFVEVGSGKLSLSETEDKDWINNWKEFFKPFRVDDTIVIKPTWEKLEERKETDLVIEIDPGTAFGTGAHETTKLCILNIKKYMQPGATLLDVGCGSGILTIIGRKLGAKTAVAIDIDENAVSASKENCDVNQLEAVLCQSSDSSTRTEGRIELFDGNVIEDRGLRERIGLNSYDFVVANILADIIIPLSAVVGEFMKPGAYFISSGIIDMKAEEVKEAILRNGFIIEEITTMGDWTSIVAKKPNK | 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): 36958
Sequence Length: 333
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q88VP9 | MKWTEVTVSTSNEAVEAVANILMEAGASGVKIDDALDYQNLKPDRYGEIIDLATIPHVTSGAKISAYYPETVFVPEVIPTIKQRVSQLTDFGLNPAPNEVSMTALSDEDWATAWKKYYHPVRVTRYLTIVPSWEQYQPVQSGELVLRLDPGQAFGTGTHPTTKLCLQALETVINGGEHLIDVGTGSGVLSIAAKAMGVGAVEAYDLDDVAVASAQTNLDLNPVAKDVHVAANDLLAGIDTQADIIVANILAEIIIPLVPQARQNLKRGGYFIASGIIDDKFQVVMTTIKEAGFQITQHTQMGDWHGIVAYLPTAED | 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): 34101
Sequence Length: 316
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
C1DCV9 | MSWQQVAIDADSRIAERFADTLMELGALSTAIEDAAAGTEFEQPIFGEPGEPVDRLWEQSRIIVLFAADADVAMLIAAAAGEAGMPTPVYTVEAVESQDWVRLTQSQFDPIRISGRLWITPTWHDAPDANAINLALDPGLAFGTGSHPTTRLCLQWLDANICGGESVLDYGCGSGILAIAAIKLGATDVTGIDIDPQAVQASRDNAVQNQVTAAFGLPDTLEDGRQFDVLVANILANPLRMLGDLLASHVRAGGRIVLSGILEEQAQELSELYSAWFEMDPPVFDEGWTRLSGVRRA | 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): 31890
Sequence Length: 297
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q5ZYB1 | MWFQLKIEHCPNDKIEEITEELEECGALSITLTDKNDNPVLEPEPGTTPLWPEVIIHALFAQAEEAQYAREQLVAKRPSLHCSLELLADKNWERAWMDDFRPQRFGNRLWVCPTWLPPPEPDAVNLILDPGLAFGTGTHATTSLCLTWLEQADLKNKSIIDYGCGSGILSLAAIKLGAKHVYAVDIDNQALQATQSNAHANHITESQLSISFPEALQNPVHLVIANILLAPLISLKERFHQLLPSGAHLVTSGILEEQAPLLIDAYDSAFTHIATEYCEGWSLLVFTSK | 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): 32117
Sequence Length: 289
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
A6QBN7 | MQDKYYELTITLDDQYVDLISDYIMNIHDEGLEFATGKIVMRSESDLTFVKDALVALQDELESDIHMDFNLEEKENIDWIKSYQESIQPIEAGKFYIFPSWYEPKEGYINIKIDPALAFGSGHHATTFSCLEAISKTVKAGDRVVDVGCGSGILGLAAKKLGATVELCDTDPLSVESCKENFKLNEAQYDELWEGSIDKAVGTYDVVIANIIADVLRFISRDLKAAVQEGGYLILSGILDKKEELVKASFQDLTLEKRTLKDEWVTLVYKKEKING | 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): 31034
Sequence Length: 276
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q67S51 | MRYLEIRIRCQRAAADAVGNLLLTLTGAGYAVDDPLIVEQNRSRWDMTDLPPGDPEWVTVSGWLPEAGDVEQQRLRLETGLDEIRSLGLGAVDPARFRWVEEEDWAHAWKAYFRPTRVGDRLVVVPAWEEYAPQEGELPIRIDPGMAFGTGTHATTALCMRWLEELVTPGSRVIDVGTGSGILAVAAKHLGAAEVVAIDVDPVAVDAARENAGRNGVEIDVRLATLDQVAEGEADLIVANIIASVIVDILPDVASRLKPGGRFLASGIIAARKEAVTEAMTDAWLLPVGAREQDGWVAILAMKP | 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): 32911
Sequence Length: 304
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q39ZZ2 | MNEFWLQINIIVPAAGIDLVCHEMTELGSAGITVEERALDTFVVPDPDADIPETLILKVYFPPEIEPEQLARQVAERLAWLAPLIPGLEVVTPEISRVRAEDWAENWKQHFGIQRIGSRLVIRPTWEAFSPDPQDAVLTLDPGMAFGTGSHATTRLCLEALAELYETPPGPQRVLDVGTGSGILAVAAALLGAGQVLGCDIDETACQVALDNARQNGVIEQIAVTLDPLETLGGDFDVVLANILAEENARLAPELVHRLAPGGVLILSGILNEKEQLVIDAFAGRGLTGPDIRRQDEWSCLCYIKEA | 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): 33234
Sequence Length: 307
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q31N39 | MPVSQSWWQVEVHCDPLLEDLLYWRLSEAGGRGFVCESKAQGLQVHSYFPAELWEETIRDRLLQEINADAADLGLPTPSLSWQTLDEEDWSESWKRHWQPQELGDRFLIQPAWLEPEPSDRLLLQLDPGTAFGTGAHPTTQLCLEGLETVPVADKVIADVGCGSGILAIGALLLGAKQVYAVDTDPLAVGATQANAALNDLEGDRFWTAIGSADQLQPLHAQGVRFDGFLCNILAHIIQALTPTLSELASPGSWAIFSGLLTSQADTVSVTLEEYGWVIRDRASQGDWCRLVADFRPER | 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): 32930
Sequence Length: 299
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
A0LQ64 | MNGEWIGIDVACGPDVADDVAAELAGTFGVSVEFRSTGIRFYLDAGSAPHDWRTTLEGILREMGTRRFPGASFPYSVSTLAGDDWADGWKAYFKPLRVGKHLVVCPTWEEFAPDAGDRIIRMDPGRAFGTGQHETTRLCLEWLEDRALQALPSAPGSLLDVGTGSGILAVAAALLGFHPVQAVDDDPEAVEVAAENIALNGMESAIELLAGTARQASGAFDVVIANIQAIPLVGMASELVRLTAPAGLAALSGILVEQGEVVKSAYRDLGLLPRKMRTAGEWCLLEFKKP | 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): 30848
Sequence Length: 290
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
B0U111 | MSIVEMGKNAKQAAKELAQANTELKNNVLHELEKSLLDNAEYILQQNQKDLDNAKKNNLSKAFVDRLTLTPARIESMAQGVRQIADFADPIGKIEKGFKHPKGMTISQIRVPLGVIAMIFESRPNVTIDAGALALKSGNAIILRGGSDALHTNIALKNIFQEVCEKHGLSKNIVQLVEDIARERVTELVTLDKYIDVIIPRGGKSLKKAIQQQATISMIETGAGICHTYIDEFADLDKAIKIVINAKTQRPGVCNALESLLVHQNIAEKFLPKLEIELAKYNVELRADNESLKYLGNAILATPEDWDTEYLDLVLSIKTVANINEAIEHINTHGSMHSECIVTESYTNTEIFLNEVDAAAVYANASTRFTDGSEFGFGGEIGISTQKLHARGPMGINELTTLKYIIRGNGQVRG | 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): 45516
Sequence Length: 414
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
|
Q6NDE4 | MTASLKAIDGSAELTTLMTDLGRQARAAARTLALAPPEQKNRALEAMERAIRAGADKILAANAEDVADAKAAGTTSAFLDRLTLTPARVEAMAEGIAVVRGIADPVGTVTESWQRPNGMTIERVRVPLGVVAVIFESRPNVAADAGVLCLKSGNAVILRGGSESFRSCRAIHDRLVQGLREAGLPDAAITLVPTRDRAAVGLLLAGLDGSVDVIVPRGGKSLVARVESEARVPVFAHLEGVNHVYVDRSADLEMAKSIVLNAKMRRTGVCGAAETLLIDRAAATTHLAPLVTMLIDSGCEVRGDQTVQQVDPRVKPASDEDWDTEYLDAVIAAKLVDGVDGAIVHIHNHGSHHTDAIVAEDAQAAAKFLGEVDSAIVLHNASTQFADGGEFGFGAEIGIATGKFHARGPVGAEQLTTFKYRIHGSGQTRP | 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): 45120
Sequence Length: 430
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
|
Q3IEY8 | MNKLNWRRIVLKVGSALIAPDQDGCRSRYILTIAQFIVRCRARGIEVILVSSGSVAAGAHLFPSDTARSVVMKKAMAAAGQTEMIAMWDRFFDFPSAQLLLTHGDLRDHERYQSIRETVFTLLEHGVLPIINENDAVTTDDLKVGDNDNLSAMVAAAADADALLIFSDVDGLYDKNPNLHDDAILLPEIKSIDDSIYAMAGCATSAVGTGGMKTKIEAAEKATSHGISTYIINGFKEETFTRLLAGENPGTIFLPYEKPMQDSVHWMTHTANEQGEVVVDGSFDKSLEGETGCIRGDEIMAVHGEFAIGDTILVRSEDGTRLAKATANYSSCLLSFIADNEQSEFSEKMQDSIGPVISEKHIALLEKS | 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): 40037
Sequence Length: 368
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
|
Q989S7 | MQEKIRETCLATKTVKLLSARRLIVKIGSAVVADAETGEIRGPWLETLIKDVVRFFARGQQVIIVTSGAVAAGSRHFKQLDRSLRIEEKQAAAAIGQIRLMIAYEQSLKRHGFGLGQVLLTSADVDNQRCRLNARSAFQQLLNVGAVPVINENDATATPEVCLGDNDRLAARVAQIAKADLLILLSDVDGLFTEDPHDNPLARMIPEVRRITPEIEIMASLSPARHGSGGMVTKLMAARIAMEAGCNVVIAKGSKSYPLAAIENGAPSTWFIPPARETATRGGR | 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): 30683
Sequence Length: 284
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
|
Q92LF7 | MEDKFDLSSARLVVVKIGSTLVLDRETSGIRSSWLESLTEDVSRLLTRGQQVVLVSSGAVAIGSTIVDRLATYSQVSHKQAAAALGQVQLTHAYSESLKRHGLQVAQLLMGRGDLVDPAHRLNTRAVLLRLIDLGAVPLVNENDTTATCGTRVGDNDRLAAWIAEIINADLLILLSNVDGLFMKDPRNNPLTPMLTEVESITREIEAMATQSVDPYSSGGMISKIEAGKIAMNAGCRMIIANGTRSHPLYAIESGGPSTHFIPVARDRV | 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): 28953
Sequence Length: 269
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
|
Q747Q3 | MRSGILSKVKRIVIKIGSGVLTCGDNGLNKPLMGSIAAQVAELRASGRQVIIVSSGAVAAGRKELGIDGRPRSIPQKQAAAAIGQSRLMHAYEEAFEPFGHKVAQILLTRDDLAHRGRFLNARATLDTLLSFGVIPIINENDTVVFDEIKFGDNDSLSALVTNLAEANLLVILTDIDGFYEANPRTNPDARLIPLVRQITREMERAAGGSGSTVGTGGMVTKLAAAKKAGQFGVPTLMLNGRNPSLLAEAFAGREVGTLFLPGKESLNRRKHWIAHTLRPSGKIIVDDGARTVLARQGKSLLPSGVVRVEGKFDRGACVRVCGTDGTEIARGLVDYSHDEITRILGHRSGEIEAILGYKYGDEIIHRDNLVVL | 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): 39997
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
|
A4W027 | MTEKTIVFKVGTSSLTQENGSLDRIKIARITNQLAQLHQKGYQIVLVTSGSIAAGFRRLGFDKRPTKIAEKQASAAVGQGLLIEEYTQNLMKDGIVSAQILLTQDDFADARRYQNASQALQVLLKQRAIPIINENDTIAIEEIKVGDNDTLSAQVASLLKADLLVLLTDVDGLYTANPNSDPTAQHLPQIKEITEDLFAMAAGAGSSNGTGGMTTKLQAAQIATKSGVPVFICSSKEDTALLQAVTQANRGTLFLADDHAMNQRKQWMAFYARTDAAVEVDAGAVDAMLHQGRSLLATGVKALEGDFEVGQVVEVYSQADHRLIGKGRVKLSSKDLQDQLANGRAEGVLIHRNDWVSL | 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): 38616
Sequence Length: 358
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
|
Q67LC1 | MRERLRHCKRVIIKVGTSTLTHPGGHLHLGRMEALVRQIADLHFEGRQVILVTSGAVGAGLGRLGLAERPAEVAAKQALAAVGQGLLMQRYEGLFSEYGLVVGQVLLTREDLEDPDRRASSAQVMERLLAWGVIPIVNENDTVTSEEIRVGDNDTLSARVAALVRADLLILLSDVDGLYPADPHLHPGLSPIPWVSPDDDLDRFAGGPGSANGTGGMVTKVAAARICAEHGIPMVLACGERPDVLRQILAGEEIGTLFSREG | 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): 28006
Sequence Length: 262
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
|
Q2LR78 | MNENREQVLKNVKRVLIKIGSAVLTGDNGLDLERIQHLVDQMAALTHRGYQVVMVTSGAIASGKHRLGITTALKSIPQKQAAAAIGQGRLMRIYSNSFGKHGLYVGQILLTMSDLTDRRRFLNIRNTLSTLMEWGIIAIINENDTVAIDEIKFGDNDNLAAMIANIIEAHLVINLTSTPGLYDRNPASSRNARLIPLVREITEDIEAAASEEGTSVGTGGMKSKVMAAKKVTAFGIPYIIAPGKQKDVLLDIFDGNELGTLFLPMREHLSSRKYWIAFTLRSRGVLSIDAGARTAILEEGKSLLPSGIVGVEGDFIVGDPVTCVDRDGVPLAKGLVNYSAPDIRKIMGLKTSRIEQVLGHKDYDEIIHRDNLAVIRRSRRHREAG | 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): 42139
Sequence Length: 385
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
|
Q9IIH4 | MGTSGADLENIVLSLGLHSGFLGIFDKHFPGFLNVNKPSFAIVNTGDIIQGGLHWIAFAFDNVTSTFFMFDPFGWSDMELYRKYEFQYHRILKSTALTKPSRCIKLVKSKEAVQCTCSAACGLFCCLFLASFYHYPTFPMRGNPIIDLVDGIPPTKLHSSYGIYLTHCNQKKLIAWLLSNSAYFRKNAMLMIHNTRLYYLYTHL | 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): 23222
Sequence Length: 204
Subcellular Location: Virion
EC: 3.4.22.39
|
P42672 | MSGTTETQLRDLLSSMHLRHRFLGVFDKSFPGFLDPHVPASAIVNTGSRASGGMHWIGFAFDPAAGRCYMFDPFGWSDQKLWELYRVKYNAFMRRTGLRQPDRCFTLVRSTEAVQCPCSAACGLFSALFIVSFDRYRSKPMDGNPVIDTVVGVKHENMNSPPYRDILHRNQERTYYWWTKNSAYFRAHQEELRRETALNALPENHV | 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): 23764
Sequence Length: 206
Subcellular Location: Virion
EC: 3.4.22.39
|
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