ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P00634 | MKQSTIALALLPLLFTPVTKARTPEMPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIGDGMGDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQDATPAALVAHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVTLGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPT... | 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
|
P83456 | AGFPEQEPEPKFWNDWAQKTLDKALSLQTLNKNKAQNLILFLGDGMGVPTVTAARILKGQLRGQPGEEGQLEMDKFPFVALSKTYNTNAQVADSAGTATAYLCGVKANEGTVGVSAAAVRSQANTTQGNEVTSILRWAKDAGKSIGIVTTTRVNHATPSAAYAHCVDRDWYSDNEMPADAVEAGCKDIARQLFENIPDIDVIMGGGRKYMYPKNTTDVEYPGQPKHSGTRKDGRNLVKEWVDRNTEKKGHYVWNKKDLLSLNPTKVDYLLGLFEPADLPYDLERNKETDPSLSEMVEVAIKILRRNPNGFYLLVEGGRID... | 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 | MNLSPSRTPICAALAAALLGAAALAPAHAAQRILQLSEDTTHSKPVSAASALRGTPLAKAGAADRVCEAGAKWLRVGFKQLKLAGYDSLVLTSSGGDKLVFEGQHWNQRSFTTRPLRGECVDIQPYFSQPDSAFQLDRYDYSTVALDKATVVVAGAGDICDTSGNACQGTSDLIVSINPTAVFTAGDNAYNSGTLSEYNSRYAPTWGRFKALTSPSPGNHDYSTTGAKGYFDYFNGSGNQTGPAGDRSKGYYSWDVGDWHFVSLNTMSGGTVAQAQIDWLKADLAANTKPCTAAYFHHPLLSRGSYSGYSQVKPFWDALY... | 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 | MASERDPLLPVHGEGPESPSRRNWKTWIKHGILLILVLSTVIFFYFFSSHKSKGTNEKPKFVIMMVSDGMGPGSLSMTRSFVETLNDKEGYRLPLDEHLIGSSRTRSSSSLITDSAAGATAFSCANKTYNGAVGVLDNEKPCGTILEAAKEAGYLTGIVVTSRVTDATPASFSAHAANRFMQDLIAEYQVGMGPLGRSVDLLFGGGLCSFLPKSTYRSCRSDNLDLLKYARKKEGFQILLNRTDFDELSNAQLPLLGLFSDYHLSYDIDYQPEVQPKLSEMVETALDVLLNATNEDTSKGFFLLIEGSRIDMASHNNDPI... | 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 | MQPAVSLIAGAVLSALLCSSAIAAETSANADGLTDRAARGNLVEPGGARRLAGDQTTALKASLSDKTAKNVILLIGDGMGDSEITAARNYAEGAGGYFKGIDALPLTGQYTHYSLDRKTHKPDYVTDSAASATAWATGVKTYNGALGVDVNGKDQPTLLEIAKAAGKATGNVSTAELQDATPAALVSHVISRKCYGPEETSEKCAANALENGGRGSITEQLLKTRADVTLGGGAKSFNQLAKSGEWQGKSLKDQAAAQGYQWVSNADELQAVTLANQQKPLLGLFADGNMPVRWLGPKASYHGNLDKPAVTCENNPARTA... | 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 | MMTHTLPSEQTRLVPGSDSSSRPKKRRISKRSKIIVSTVVCIGLLLVLVQLAFPSSFALRSASHKKKNVIFFVTDGMGPASLSMARSFNQHVNDLPIDDILTLDEHFIGSSRTRSSDSLVTDSAAGATAFACALKSYNGAIGVDPHHRPCGTVLEAAKLAGYLTGLVVTTRITDATPASFSSHVDYRWQEDLIATHQLGEYPLGRVVDLLMGGGRSHFYPQGEKASPYGHHGARKDGRDLIDEAQSNGWQYVGDRKNFDSLLKSHGENVTLPFLGLFADNDIPFEIDRDEKEYPSLKEQVKVALGALEKASNEDKDSNGF... | 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... |
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 Loca... |
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 Loca... |
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
... |
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 (... |
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
... |
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: Viri... |
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 (... |
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: Endo... |
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: Endoplasmi... |
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: Endoplasmi... |
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
... |
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
... |
B9KCQ6 | MQIQPSMYINRELSWLAFNSRVLDQCSKDLPLLEKLKFIAIYCTNLDEFYMIRVAGLKQLFIAGISTASNDEMTPLTQLKAIRNYLHEEKYVVEQYFTKITQDLEKENLFIRSYEELDEDLKQQCNDHFFSNIFPVIVPIAVDATHPFPHLNNLSFSLVVKLCDPMHPELLKFGMVRIPRVLPRFYQVSSNIYVPIESIVRHHTEHIFPGYKLLSSAAFRVTRNADMEIEEEEADDFMMILEQGLKLRRKGAFIRLQIEKGADEQLIEFLSSHMNIFHKDIYEYSILLNLPSLWQIISNKEFTHLLNPVYTPKILPPFGD... | 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 = [ph... |
Q8FF70 | MGQEKLYIEKELSWLSFNERVLQEAADKSNPLIERMRFLGIYSNNLDEFYKVRFAELKRRIIISEEQGSNSHSRHLLGKIQSRVLKADQEFDGLYNELLLEMARNQIFLINERQLSVNQQNWLRHYFKQYLRQHITPILINPDTDLVQFLKDDYTYLAVEIIRGDTIRYALLEIPSDKVPRFVNLPPEAPRRRKPMILLDNILRYCLDDIFKGFFDYDALNAYSMKMTRDAEYDLVHEMEASLMELMSSSLKQRLTAEPVRFVYQRDMPNALVEVLREKLTISRYDSIVPGGRYHNFKDFINFPNVGKANLVNKPLPRLR... | 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 = [ph... |
Q2NC49 | MGSHPITQDNDLDPPTEPGERYFNRELSWLAFNDRVLAEACNDSYPLLERLRFLSISGSNLDEFVMIRVAGLVGQVQRGIDEVSDDGRSPREQLNAVVARLEELSERQQDIWRNLRVQLADAGVHVADEERVNAEAYGWLKQHFFESILPLLTPQALDPAHPFPFISNEGLGLLFTLRRGGEELVEMVLIPSALPRFIRVPGEDALYISIESLITRFAKELFPGFEIVGDGTFRVLRDSDIEIQEEAEDLVRTFRSAIQRRRRGQVIQLEIEEEFDPTAEALLREKLDTPGATFVKTDGMLGIAGLADIVDEDRPDLKFD... | 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 = [ph... |
B1YL94 | MKIDSPEFFNNREISWLQFNERVLGEVTDTRNPLMERFKFLGIFSSNLDEFYMVRVGGLKDEVLAGFNKPENKQQLTPKQQLRAIATKTKELVDQQYEAFKDVTQALKAEGISFLKHDELNEMQSEYVKTFFREQVFPVLTPVAVDAYRPFPMLSSKSLNIATALEAEDGSKRNLALVQVPAVLPRFVDLPVDDEETTAVILLEDVIISFIDSLFKGYHVLSAMPFRITRNADLPFHEEGTHDLLKLIEKELKKRRWGVGIRLEIQKNAINTNLLNMLRDVLDLQDRDIYAVDGPIDLTFAFAFYSQIGVEYDHLIYQTI... | 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 = [ph... |
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 = ... |
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 = ... |
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 = ... |
Q9AR38 | MAAAAAAMATATSATAAPPLRIRDAARRTRRRGHVRCAVASGAAEAPAAPGARVSADCVVVGGGISGLCTAQALATKHGVGDVLVTEARARPGGNITTAERAGEGYLWEEGPNSFQPSDPVLTMAVDSGLKDDLVFGDPNAPRFVLWEGKLRPVPSKPGDLPFFDLMSIPGKLRAGLGALGVRAPPPGREESVEDFVRRNLGAEVFERLIEPFCSGVYAGDPSKLSMKAAFGKVWRLEDTGGSIIGGTIKTIQERGKNPKPPRDPRLPTPKGQTVASFRKGLTMLPDAITSRLGSKVKLSWKLTSITKSDNKGYALVYET... | 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; protoporphyr... |
Q9LRI8 | MSAMALSSTMALSLPQSSMSLSHCRHNRITILIPSSSLRRRGGSSIRCSTISTSNSAAAANYQNKNIGTNGVDGGGGGGGVLDCVIVGGGISGLCIAQALSTKYSNLSTNFIVTEAKDRVGGNITTMEADGYLWEEGPNSFQPSDAVLTMAVDSGLKEELVLGDPNSPRFVLWNGKLRPVPSKLTDLPFFDLMSFPGKIRAGLGALGLRPSPPAHEESVEQFVRRNLGDEVFERLIEPFCSGVYAGDPSKLSMKAAFGRVWVLEQKGGSIIGGTLKTIQERKDNPKPPRDPRLPKPKGQTVGSFRKGLSMLPTAISERLG... | 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: Porphyr... |
O24163 | MTTTPIANHPNIFTHQSSSSPLAFLNRTSFIPFSSISKRNSVNCNGWRTRCSVAKDYTVPSSAVDGGPAAELDCVIVGAGISGLCIAQVMSANYPNLMVTEARDRAGGNITTVERDGYLWEEGPNSFQPSDPMLTMAVDCGLKDDLVLGDPNAPRFVLWKGKLRPVPSKLTDLAFFDLMSIPGKLRAGFGAIGLRPSPPGHEESVEQFVRRNLGGEVFERLIEPFCSGVYAGDPSKLSMKAAFGKVWKLEETGGSIIGGTFKAIKERSSTPKAPRDPRLPKPKGQTVGSFRKGLRMLPDAISARLGSKLKLSWKLSSITK... | 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; protoporphyr... |
O24164 | MAPSAGEDKHSSAKRVAVIGAGVSGLAAAYKLKIHGLNVTVFEAEGKAGGKLRSVSQDGLIWDEGANTMTESEGDVTFLIDSLGLREKQQFPLSQNKRYIARNGTPVLLPSNPIDLIKSNFLSTGSKLQMLLEPILWKNKKLSQVSDSHESVSGFFQRHFGKEVVDYLIDPFVAGTCGGDPDSLSMHHSFPELWNLEKRFGSVILGAIRSKLSPKNEKKQGPPKTSANKKRQRGSFSFLGGMQTLTDAICKDLREDELRLNSRVLELSCSCTEDSAIDSWSIISASPHKRQSEEESFDAVIMTAPLCDVKSMKIAKRGNP... | 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; protoporphyr... |
Q9LTX3 | MRNVIRRVTTMTFTFLLQSPPLPISPSPPQFSLSSSPLSKTQRFITPSQGSRLRTLCTKVIIPNMQDSGSPPLSYLTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYKPEEYSRVLAICGPGNNGGDGLVAARHLHHFGYKPFICYPKRTAKPLYTGLVTQLDSLSVPFVSVEDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYEQTLQKHPVIVSVDIPSGWHVEEGDHEDGGIKPDMLVSLTAPKLCAKRFRGPHHFLGGRFVPPSVAEKYKLELPSYPGTSMCVRIGKPPKVDISAM... | 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 N... |
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'-... |
Q54DT8 | MIQKVGIIGSGISGLSSYYYLRNGINLTSKFSKNNLKINIFEKSNKVGGNIQTRIIQGKNKDEKIIVEEGPRSLRALGRGLNTLEFIKRLGISNDIIFSSANSNGKFVLLDGKPKEIPMTSLFDIIKFSFKHSIVSSILKEPFKKVPSQVKEMDPNWDESVHDFFSRRLGKTMTKTFIEPTILGIYGGDYTNLSIKSTFKRAALLEPFGGLILGSLFKSKKQKQFELDLDKNEKRLLPSKNELTELFDKDTDKTNVFSFKENGLSRMIQKLKSLIESDSLTKLYLSTSIVEIEKDVTNGTLKVTDNKGNQYQYDQLISTI... | 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; protoporphyr... |
P50336 | MGRTVVVLGGGISGLAASYHLSRAPCPPKVVLVESSERLGGWIRSVRGPNGAIFELGPRGIRPAGALGARTLLLVSELGLDSEVLPVRGDHPAAQNRFLYVGGALHALPTGLRGLLRPSPPFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLGAGRTPQPDSALIRQALAERWSQWSLRGGLEMLPQALETHLTSRGVSVLRGQPVCGLSLQAEGRWKVSLRDSSLEADHVISAIPASVLSELLPAEAAPLARALSAITAVSVAVVNLQ... | 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: Porphyr... |
Q10062 | MSIAICGGGIAGLSTAFYLARLIPKCTIDLYEKGPRLGGWLQSVKIPCADSPTGTVLFEQGPRTLRPAGVAGLANLDLISKLGIEDKLLRISSNSPSAKNRYIYYPDRLNEIPSSILGSIKSIMQPALRPMPLAMMLEPFRKSKRDSTDESVGSFMRRRFGKNVTDRVMSAMINGIYAGDLNDLSMHSSMFGFLAKIEKKYGNITLGLIRALLAREILSPAEKALKAALLAEPKTAELSNSMKSTSMFAFKEGIETITLSIADELKKMPNVKIHLNKPAKTLVPHKTQSLVDVNGQAYEYVVFANSSRNLENLISCPKME... | 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; protoporphyr... |
P40012 | MLLPLTKLKPRAKVAVVGGGVSGLCFTYFLSKLRPDVEITLFESQNRTGGWIYSCNTRDMSGNPIMLEKGPRTLRGVSDGTVLIMDTLKDLGKEAVIQSIDKGCIADKKFLLDPSDKLVQVPNSISTTVKFLLNPLGKGLITGMMGEWFRKKSPHPGQDESVESICDRRFGNNYISNNMISALLRGIYGDDVSLLSAKRTFKKIYYNELKHGSNTQAMIDNMRGKSRSKKTENLHQSLTGCLNDYSNAFGKDRSKLLDLSNTLKKYPMLGLAGGLETFPKIVRNALNEFKNVKIVTGNPVTQIMKRPANETTIGLKAKSG... | 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; protoporphyr... |
P43309 | MTSLSPPVVTTPTVPNPATKPLSPFSQNNSQVSLLTKPKRSFARKVSCKATNNDQNDQAQSKLDRRNVLLGLGGLYGVAGMGTDPFAFAKPIAPPDVSKCGPADLPQGAVPTNCCPPPSTKIIDFKLPAPAKLRIRPPAHAVDQAYRDKYYKAMELMKALPDDDPRSFKQQAAVHCAYCDGAYDQVGFPELELQIHNSWLFFPFHRYYLYFFEKILGKLINDPTFALPFWNWDSPAGMPLPAIYADPKSPLYDKLRSANHQPPTLVDLDYNGTEDNVSKETTINANLKIMYRQMVSNSKNAKLFFGNPYRAGDEPDPGGG... | 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 | MATAPSPTTMGTYSSLISTNSFSTFLPNKSQLSLSGKSKHYVARRSSISCKATNNNNSNNQNEQQEESSRLLGKLDRRNILIGLGGLYGATTLDRKPFAFADPIAPPDLTTCKPAEITPGGSETVPCCPPVTTKIKTFKPDLSIPLRTSPAAHQVTDEYLAKFKKAQAAMRALPDDDPRSMVQQAKVHCAYCNGAYPQVGFTDNDIQVHFSWLFFPFHRMYLYFYERILGKLIDDPTFALPYWNWDSPVGFPIPDIYTDTSSPLYDQYRNADHQPPVLVDLSYGGKDDDVDEQTRIDENLAIMYRQMVSGAKTPDLFFGH... | 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 mono... |
P43310 | MATLSSPTIITTTSILLNNPFLPKTPQLSAHHHRGVRSVNGKVSCQTKNNNGNDENNQFQLIQNPNTNTPYLLDRRNILLGLGGMYAALGSEGANYYNTLAAPILPDVEKCTLSDALWDGSVGDHCCPPPFDLNITKDFEFKNYHNHVKKVRRPAHKAYEDQEWLNDYKRAIAIMKSLPMSDPRSHMQQARVHCAYCDGSYPVLGHNDTRLEVHASWLFPSFHRWYLYFYERILGKLINKPDFALPYWNWDHRDGMRIPEIFKEMDSPLFDPNRNTNHLDKMMNLSFVSDEEGSDVNEDDQYEENILLMRKAMVYPSVSD... | 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 forma... |
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 ... |
P78968 | MGQGSSKHADSKLDSYPSFSRSDTQGSIKSLKSLKTVLGKGKDSNHDRRTSTDTTHSRHRYPETPPSLPPPPSPGILATSPAVLQKHQQEDSGNSSQSPTSPHPSNQPAMLSPSTAASQHHHHHSSSSSYAVSPTSPTSPTSSGPIGSNFDSASEHNGPVYPQDQQGPVIIPNSAISSTDPDDPETVVSLNVDEMIQRLIHVGYSRKSSKSVCLKNAEITSICMAVREIFLSQPTLLELTPPVKIVGDVHGQYSDLIRLFEMCGFPPSSNYLFLGDYVDRGKQSLETILLLFLYKIRYPENFFLLRGNHECANITRVYGF... | 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
|
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 splici... |
P0AFM0 | MCEHHHAAKHILCSQCDMLVALPRLEHGQKAACPRCGTTLTVAWDAPRQRPTAYALAALFMLLLSNLFPFVNMNVAGVTSEITLLEIPGVLFSEDYASLGTFFLLFVQLVPAFCLITILLLVNRAELPVRLKEQLARVLFQLKTWGMAEIFLAGVLVSFVKLMAYGSIGVGSSFLPWCLFCVLQLRAFQCVDRRWLWDDIAPMPELRQPLKPGVTGIRQGLRSCSCCTAILPADEPVCPRCSTKGYVRRRNSLQWTLALLVTSIMLYLPANILPIMVTDLLGSKMPSTILAGVILLWSEGSYPVAAVIFLASIMVPTLKM... | 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 | MESNNGEAKIQKVKNWSPVWIFPIVTALIGAWVLFYHYSHQGPEVTLITANAEGIEGGKTTIKSRSVDVGVVESATLADDLTHVEIKARLNSGMEKLLHKDTVFWVVKPQIGREGISGLGTLLSGVYIELQPGAKGSKMDKYDLLDSPPLAPPDAKGIRVILDSKKAGQLSPGDPVLFRGYRVGSVETSTFDTQKRNISYQLFINAPYDRLVTNNVRFWKDSGIAVDLTSAGMRVEMGSLTTLLSGGVSFDVPEGLDLGQPVAPKTAFVLYDDQKSIQDSLYTDHIDYLMFFKDSVRGLQPGAPVEFRGIRLGTVSKVPF... | 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: Ce... |
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 | MAIYYKFKSARDYDTISMDGPFITVGLLKEKIYETKHLGSGKDLDIVISNAQTNEEYLDEAMLIPKNTSVLIRRVPGRPRIRIITREEPRVEDKVENVQADMNNVITADASPVEDEFDEFGNDLYSIPDAPAVHSNNLCHDSAPADDEETKLKALIDTPALDWHQQGADSFGPGRGYGRGMAGRMGGRGFGMERTTPPPGYVCHRCNVSGHFIQHCSTNGNPNFDVKRVKPPTGIPKSMLMATPNGSYSLPSGAVAVLKPNEDAFEKEMEGLTSTTRSVGEFPPELKCPLCKEVMRDAALASKCCLKSYCDKCIRDHIIA... | 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... |
Q2KI51 | MAPGQMPHQPAPWRGTHPLFLLSPLMGLLSRAWSLLRAPGPPEPWLVEAVTEADQGGAGLEDEAKASLATYHALWGRHPQEETKDSGAAEEDREASPGACPNLEAKHSLPEAWGLSDDDDEKYGGEEATGVPREQKEFMDGQPAPLPLSLLIRSLPDLPGEEESKEEAVTGGGGNEVTAFSFPLSHWECCPGEEEEEEEENGEAVRVCRPVNGATEERTQTEAATKTSMSPSSVGSHLRAWECCSGKESEEEEKDKQAEKGDADPGPHFTSLAQRPSLRTWQHPSSAITEEEEDRDSEEMGASSSVPLTSAFLSDWVYQP... | 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-be... |
O75807 | MAPGQAPHQATPWRDAHPFFLLSPVMGLLSRAWSRLRGLGPLEPWLVEAVKGAALVEAGLEGEARTPLAIPHTPWGRRPEEEAEDSGGPGEDRETLGLKTSSSLPEAWGLLDDDDGMYGEREATSVPRGQGSQFADGQRAPLSPSLLIRTLQGSDKNPGEEKAEEEGVAEEEGVNKFSYPPSHRECCPAVEEEDDEEAVKKEAHRTSTSALSPGSKPSTWVSCPGEEENQATEDKRTERSKGARKTSVSPRSSGSDPRSWEYRSGEASEEKEEKAHKETGKGEAAPGPQSSAPAQRPQLKSWWCQPSDEEEGEVKALGAA... | 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-b... |
Q6IN02 | MAPSPRPQHVLHWKEAHSFYLLSPLMGFLSRAWSRLRGPEVSEAWLAETVAGANQIEADALLTPPPVSENHLPLRETEGNGTPEWSKAAQRLCLDVEAQSSPPKTWGLSDIDEHNGKPGQDGLREQEVEHTAGLPTLQPLHLQGADKKVGEVVAREEGVSELAYPTSHWEGGPAEDEEDTETVKKAHQASAASIAPGYKPSTSVYCPGEAEHRATEEKGTDNKAEPSGSHSRVWEYHTRERPKQEGETKPEQHRAGQSHPCQNAEAEEGGPETSVCSGSAFLKAWVYRPGEDTEEEEDSDLDSAEEDTAHTCTTPHTSAF... | 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-be... |
P23865 | MNMFFRLTALAGLLAIAGQTFAVEDITRADQIPVLKEETQHATVSERVTSRFTRSHYRQFDLDQAFSAKIFDRYLNLLDYSHNVLLASDVEQFAKKKTELGDELRSGKLDVFYDLYNLAQKRRFERYQYALSVLEKPMDFTGNDTYNLDRSKAPWPKNEAELNALWDSKVKFDELSLKLTGKTDKEIRETLTRRYKFAIRRLAQTNSEDVFSLAMTAFAREIDPHTNYLSPRNTEQFNTEMSLSLEGIGAVLQMDDDYTVINSMVAGGPAAKSKAISVGDKIVGVGQTGKPMVDVIGWRLDDVVALIKGPKGSKVRLEIL... | 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, i... |
P45306 | MVMKFKMSKNVICYTWLSVCLSSAIPAFAVQPTLKPSDISIPAISEESQLATKRATTRLTQSHYRKIKLDDDFSEKIFDRYIKNLDFNHNTFLQSDIDELRQKYGTKLDEQLNQGDLSAAFDIYDVMMKRRYERYTYALSLLDKEPDLNGQDQIEIDREKAAAPQTEADANKLWDARVKNDIINLKLKDKKWSEIKAKLTKRYNLAIRRLTQTKADDIVQIYLNAFAREIDPHTSYLSPRTAKSFNESINLSLEGIGTTLQSEDDEISIKSLVPGAPAERSKKLHPGDKIIGVGQATGDIEDVVGWRLEDLVEKIKGKKG... | 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... |
Q9NQV5 | MLKMAEPIASLMIVECRACLRCSPLFLYQREKDRMTENMKECLAQTNAAVGDMVTVVKTEVCSPLRDQEYGQPCSRRPDSSAMEVEPKKLKGKRDLIVPKSFQQVDFWFCESCQEYFVDECPNHGPPVFVSDTPVPVGIPDRAALTIPQGMEVVKDTSGESDVRCVNEVIPKGHIFGPYEGQISTQDKSAGFFSWLIVDKNNRYKSIDGSDETKANWMRYVVISREEREQNLLAFQHSERIYFRACRDIRPGEWLRVWYSEDYMKRLHSMSQETIHRNLARGEKRLQREKSEQVLDNPEDLRGPIHLSVLRQGKSPYKRG... | 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 | MMGSVLPAEALVLKTGLKAPGLALAEVITSDILHSFLYGRWRNVLGEQLFEDKSHHASPKTAFTAEVLAQSFSGEVQKLSSLVLPAEVIIAQSSIPGEGLGIFSKTWIKAGTEMGPFTGRVIAPEHVDICKNNNLMWEVFNEDGTVRYFIDASQEDHRSWMTYIKCARNEQEQNLEVVQIGTSIFYKAIEMIPPDQELLVWYGNSHNTFLGIPGVPGLEEDQKKNKHEDFHPADSAAGPAGRMRCVICHRGFNSRSNLRSHMRIHTLDKPFVCRFCNRRFSQSSTLRNHVRLHTGERPYKCQVCQSAYSQLAGLRAHQKS... | 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 | MHGAARAPATSVSADCCIPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGELVDESGGSPLEWIGLIRAARNSQEQTLEAIADLPGGQIFYRALRDVQPGEELTVWYSNSLAQWFDIPTTATPTHDEKGEERYICWYCWRTFRYPNSLKAHLRFHCVFSGGGGGAFLHHEHAARQGAVPAADGLGLSPKPPAPDFAAPSQAGTLRPHPLGPPPVQACGAREGIKREASSAPSATSPTPGKWGQPKKGKEQLDRALDMSGAARGQGHFLGIVGGSSAGVGSLAFYPGVRSAFKPAGLARAAAAAHGDPYREESSSKQ... | 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... |
E9PZZ1 | MPAHVTPRTEDARRGAGPSSACGCSWFCHLRPVEDPASPSVCLAAVATMHGTSRTSATSVNADCCIPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGELVDESGGSPLEWIGLIRAARNPQEQTLEAIADLPGGQIFYRALRDVQPGEELTVWYSNSLAQWFDIPTTATPTHDEKGEERYICWYCWRTFRYPNSLKAHLRFHCVLSGGGGRAFLPQEHAARPGASPVAEGLGLPPKPTVPDLTAPVQAIALRPQAPAAQLAQACGARESIKREASLAPLATSPPPGKWGTPKKGKEQPDRAHSQFLGIVGGSSGG... | 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
Se... |
Q9GZV8 | MALPRPSEAVPQDKVCYPPESSPQNLAAYYTPFPSYGHYRNSLATVEEDFQPFRQLEAAASAAPAMPPFPFRMAPPLLSPGLGLQREPLYDLPWYSKLPPWYPIPHVPREVPPFLSSSHEYAGASSEDLGHQIIGGDNESGPCCGPDTLIPPPPADASLLPEGLRTSQLLPCSPSKQSEDGPKPSNQEGKSPARFQFTEEDLHFVLYGVTPSLEHPASLHHAISGLLVPPDSSGSDSLPQTLDKDSLQLPEGLCLMQTVFGEVPHFGVFCSSFIAKGVRFGPFQGKVVNASEVKTYGDNSVMWEIFEDGHLSHFIDGKGG... | 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, in... |
E9Q3T6 | MALPPSGETQSQDKANYLPQSNPHHLTTYYAHAPGYSHFRNLATTEEEFQPWKLAAAVLESQAMAPLDAFRMTAPLLNPGLAVQSEPLYNLPWYKLSPWNRIPQFTPEVPRFLDSTEHRSSGSSNQNLVLGGGGGQISGQRWEAENLLLPSPVIASLLPDGIKSSQSISVPQTLNQEGKLPFCGFNFTEEELSFVLYGAIASPEHPTDLQHAISGILVPTESSGSNHLHKTLDKDSLQLPEGLCLMQTSFGDVPHFGVFCSDFIAKGVRFGPFRGRVVNASEVKAHRDNSRMWEIFEDGHLSHFIDGKGSGNWMSYVNCA... | 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, character... |
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 Len... |
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 | MAWDMCNQDSVWTDIECAALVGEDQPLCPDLPELDLSELDVNDLDTDSFLGGLKWCSDQSEIISNQYNNEPSNIFEKIDEENEANLLAVLTETLDSLPVDEDGLPSFDALTDGDVTTENEASPSSMPDGTPPPQEAEEPSLLKKLLLAPANTQLSYNECSGLSTQNHANHNHRIRTNPAVVKTENSWSNKAKSICQQQKPQRRPCSELLKYLTTNDDPPHTKPTETRNSSRDKCTSKKKAHTQSQSQHLQAKPTSLSLPLTPESPNDPKGSPFENKTIERTLSVELSGTAGLTPPTTPPHKANQDNPFRASPKLKPPCKT... | 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 ro... |
Q9QYK2 | MAWDMCSQDSVWSDIECAALVGEDQPLCPDLPELDLSELDVNDLDTDSFLGGLKWCSDQSEIISNQYNNEPANIFEKIDEENEANLLAVLTETLDSLPVDEDGLPSFDALTDGDVTTDNEASPSSMPDGTPPPQEAEEPSLLKKLLLAPANTQLSYNECSGLSTQNHANHTHRIRTNPAIVKTENSWSNKAKSICQQQKPQRRPCSELLKYLTTNDDPPHTKPTENRNSSRDKCASKKKSHTQPQSQHAQAKPTTLSLPLTPESPNDPKGSPFENKTIERTLSVELSGTAGLTPPTTPPHKANQDNPFKASPKLKPSCKT... | 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 ro... |
Q86YN6 | MAGNDCGALLDEELSSFFLNYLADTQGGGSGEEQLYADFPELDLSQLDASDFDSATCFGELQWCPENSETEPNQYSPDDSELFQIDSENEALLAELTKTLDDIPEDDVGLAAFPALDGGDALSCTSASPAPSSAPPSPAPEKPSAPAPEVDELSLLQKLLLATSYPTSSSDTQKEGTAWRQAGLRSKSQRPCVKADSTQDKKAPMMQSQSRSCTELHKHLTSAQCCLQDRGLQPPCLQSPRLPAKEDKEPGEDCPSPQPAPASPRDSLALGRADPGAPVSQEDMQAMVQLIRYMHTYCLPQRKLPPQTPEPLPKACSNPS... | 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 mitoc... |
P41783 | METSKEKTITSPGPYIVRLLNSSLNGCEFPLLTGRTLFVVGQSDALTASGQLPDIPADSFFIPLDHGGVNFEIQVDTDATEIILHELKEGNSESRSVQLNTPIQVGELLILIRPESEPWVPEQPEKLETSAKKNEPRFKNGIVAALAGFFILGIGTVGTLWILNSPQRQAAELDSLLGQEKERFQVLPGRDKMLYVAAQNERDTLWARQVLARGDYDKNARVINENEENKRISIWLDTYYPQLAYYRIHFDEPRKPVFWLSRQRNTMSKKELEVLSQKLRALMPYADSVNITLMDDVTAAGQAEAGLKQQALPYSRRNHK... | 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 | MESKCLMFVSIVSVFFMVVNGVSETETLLKFKNSLVIGRANALESWNRRNPPCKWTGVLCDRGFVWGLRLENLELSGSIDIEALMGLNSLRSLSFINNKFKGPFPEFKKLVALKSLYLSNNQFDLEIPKDAFDGMGWLKKLHLEQNNFIGEIPTSLVKSPKLIELRLDGNRFTGQIPEFRHHPNMLNLSNNALAGQIPNSFSTMDPKLFEGNKGLCGKPLDTKCSSPYNHSSEPKSSTKKTSSKFLYIVAAAVAALAASLIIIGVVIFLIRRRKKKQPLLSAEPGPSSLQMRAGIQESERGQGSYHSQNRAAKKMIHTTK... | 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 ... |
Q20443 | MKKLASLQFFNLKLLLNGESSRGFSKFKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLIVMERPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVLRRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQQTLSWDALTKNKVQKKTSESSDDHHSETLGDHS... | 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 | MRNWEDPFTLACNTALKKNLPSCIFIIIFISVLCPVAMSQVVVPDSDADCLLRFKDTLANGSEFRSWDPLSSPCQGNTANWFGVLCSNYVWGLQLEGMGLTGKLNLDPLVPMKNLRTISFMNNNFNGPMPQVKRFTSLKSLYLSNNRFSGEIPADAFLGMPLLKKILLANNAFRGTIPSSLASLPMLLELRLNGNQFQGQIPSFQQKDLKLASFENNDLDGPIPESLRNMDPGSFAGNKGLCDAPLSPCSSSSPGVPVVPVSPVDPKSTSPPTGKKAGSFYTLAIILIVIGIILVIIALVFCFVQSRRRNFLSAYPSSAG... | 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(+) +... |
Q3E991 | MAAAVLNPGFFLLILLLSFSISPSLQYVSESEPLVRFKNSVKITKGDLNSWREGTDPCSGKWFGIYCQKGLTVSGIHVTRLGLSGTITVDDLKDLPNLKTIRLDNNLLSGPLPHFFKLRGLKSLMLSNNSFSGEIRDDFFKDMSKLKRLFLDHNKFEGSIPSSITQLPQLEELHMQSNNLTGEIPPEFGSMKNLKVLDLSTNSLDGIVPQSIADKKNLAVNLTENEYLCGPVVDVGCENIELNDPQEGQPPSKPSSSVPETSNKAAINAIMVSISLLLLFFIIVGVIKRRNKKKNPDFRMLANNRENDVVEVRISESSST... | 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 do... |
Q81WH6 | MLIGKRLNDRYKLLKMIGGGGMANVYLAHDDILGRDVAVKILRLDYSNNEEFIKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVMEYVPGQTLKQYIIERGMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGVIKVTDFGIATATSATTITHTNSVLGSVHYLSPEQARGGIANKQSDIYSLGIVMFELLTGRQPFSGESAVAIALKHLQSEIPSPKRWNENIPQSVENIILKATAKDPFHRYQSANAMKRDIETALYPERINEQPFYIPEDMEATKAIPIIQQEQLFENVTDETIVLKGSKVDEQ... | 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 p... |
O34507 | MLIGKRISGRYQILRVIGGGGMANVYLAEDIILDREVAIKILRFDYANDNEFIRRFRREAQSASSLDHPNIVSIYDLGEEDDIYYIVMEYVEGMTLKEYITANGPLHPKEALNIMEQIVSAIAHAHQNQIVHRDIKPHNILIDHMGNIKVTDFGIATALSSTTITHTNSVLGSVHYLSPEQARGGLATKKSDIYALGIVLFELLTGRIPFDGESAVSIALKHLQAETPSAKRWNPSVPQSVENIILKATAKDPFHRYETAEDMEADIKTAFDADRLNEKRFTIQEDEEMTKAIPIIKDEELAKAAGEKEAEVTTAQENKT... | 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 phosphoryl... |
A6QGC0 | MIGKIINERYKIVDKLGGGGMSTVYLAEDTILNIKVAIKAIFIPPREKEETLKRFEREVHNSSQLSHQNIVSMIDVDEEDDCYYLVMEYIEGPTLSEYIESHGPLSVDTAINFTNQILDGIKHAHDMRIVHRDIKPQNILIDSNKTLKIFDFGIAKALSETSLTQTNHVLGTVQYFSPEQAKGEATDECTDIYSIGIVLYEMLVGEPPFNGETAVSIAIKHIQDSVPNVTTDVRKDIPQSLSNVILRATEKDKANRYKTIQEMKDDLSSVLHENRANEDVYELDKMKTIAVPLKKEDLAKHISEHKSNQPKRETTQVPIV... | 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... |
Q7KTX7 | MSFIFKFIATFVRKMLELLQFGGKTLTHTLSIYVKTNTGKTLTVNLEPQWDIKNVKELVAPQLGLQPDDLKIIFAGKELSDATTIEQCDLGQQSVLHAIRLRPPVQRQKIQSATLEEEEPSLSDEASKPLNETLLDLQLESEERLNITDEERVRAKAHFFVHCSQCDKLCNGKLRVRCALCKGGAFTVHRDPECWDDVLKSRRIPGHCESLEVACVDNAAGDPPFAEFFFKCAEHVSGGEKDFAAPLNLIKNNIKNVPCLACTDVSDTVLVFPCASQHVTCIDCFRHYCRSRLGERQFMPHPDFGYTLPCPAGCEHSFIE... | 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', 'Ly... |
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.-
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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.-
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A9KKT8 | MKWKKLSLETTTEAVDLVCDMLLSLGIEGIEVVDKVPITEEEKKRMFIDILPELGEDDGIATINFYLENEEDLPSLKVSIQEGLDELRDFVEVGSGKLSLSETEDKDWINNWKEFFKPFRVDDTIVIKPTWEKLEERKETDLVIEIDPGTAFGTGAHETTKLCILNIKKYMQPGATLLDVGCGSGILTIIGRKLGAKTAVAIDIDENAVSASKENCDVNQLEAVLCQSSDSSTRTEGRIELFDGNVIEDRGLRERIGLNSYDFVVANILADIIIPLSAVVGEFMKPGAYFISSGIIDMKAEEVKEAILRNGFIIEEITTM... | 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.-
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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.-
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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.-
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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.-
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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.-
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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.-
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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.-
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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.-
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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.-
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B0U111 | MSIVEMGKNAKQAAKELAQANTELKNNVLHELEKSLLDNAEYILQQNQKDLDNAKKNNLSKAFVDRLTLTPARIESMAQGVRQIADFADPIGKIEKGFKHPKGMTISQIRVPLGVIAMIFESRPNVTIDAGALALKSGNAIILRGGSDALHTNIALKNIFQEVCEKHGLSKNIVQLVEDIARERVTELVTLDKYIDVIIPRGGKSLKKAIQQQATISMIETGAGICHTYIDEFADLDKAIKIVINAKTQRPGVCNALESLLVHQNIAEKFLPKLEIELAKYNVELRADNESLKYLGNAILATPEDWDTEYLDLVLSIKTV... | 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
Sequ... |
Q6NDE4 | MTASLKAIDGSAELTTLMTDLGRQARAAARTLALAPPEQKNRALEAMERAIRAGADKILAANAEDVADAKAAGTTSAFLDRLTLTPARVEAMAEGIAVVRGIADPVGTVTESWQRPNGMTIERVRVPLGVVAVIFESRPNVAADAGVLCLKSGNAVILRGGSESFRSCRAIHDRLVQGLREAGLPDAAITLVPTRDRAAVGLLLAGLDGSVDVIVPRGGKSLVARVESEARVPVFAHLEGVNHVYVDRSADLEMAKSIVLNAKMRRTGVCGAAETLLIDRAAATTHLAPLVTMLIDSGCEVRGDQTVQQVDPRVKPASDE... | 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
Sequ... |
Q3IEY8 | MNKLNWRRIVLKVGSALIAPDQDGCRSRYILTIAQFIVRCRARGIEVILVSSGSVAAGAHLFPSDTARSVVMKKAMAAAGQTEMIAMWDRFFDFPSAQLLLTHGDLRDHERYQSIRETVFTLLEHGVLPIINENDAVTTDDLKVGDNDNLSAMVAAAADADALLIFSDVDGLYDKNPNLHDDAILLPEIKSIDDSIYAMAGCATSAVGTGGMKTKIEAAEKATSHGISTYIINGFKEETFTRLLAGENPGTIFLPYEKPMQDSVHWMTHTANEQGEVVVDGSFDKSLEGETGCIRGDEIMAVHGEFAIGDTILVRSEDGT... | 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: s... |
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: s... |
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: s... |
Q747Q3 | MRSGILSKVKRIVIKIGSGVLTCGDNGLNKPLMGSIAAQVAELRASGRQVIIVSSGAVAAGRKELGIDGRPRSIPQKQAAAAIGQSRLMHAYEEAFEPFGHKVAQILLTRDDLAHRGRFLNARATLDTLLSFGVIPIINENDTVVFDEIKFGDNDSLSALVTNLAEANLLVILTDIDGFYEANPRTNPDARLIPLVRQITREMERAAGGSGSTVGTGGMVTKLAAAKKAGQFGVPTLMLNGRNPSLLAEAFAGREVGTLFLPGKESLNRRKHWIAHTLRPSGKIIVDDGARTVLARQGKSLLPSGVVRVEGKFDRGACVR... | 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: s... |
A4W027 | MTEKTIVFKVGTSSLTQENGSLDRIKIARITNQLAQLHQKGYQIVLVTSGSIAAGFRRLGFDKRPTKIAEKQASAAVGQGLLIEEYTQNLMKDGIVSAQILLTQDDFADARRYQNASQALQVLLKQRAIPIINENDTIAIEEIKVGDNDTLSAQVASLLKADLLVLLTDVDGLYTANPNSDPTAQHLPQIKEITEDLFAMAAGAGSSNGTGGMTTKLQAAQIATKSGVPVFICSSKEDTALLQAVTQANRGTLFLADDHAMNQRKQWMAFYARTDAAVEVDAGAVDAMLHQGRSLLATGVKALEGDFEVGQVVEVYSQAD... | 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: s... |
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: s... |
Q2LR78 | MNENREQVLKNVKRVLIKIGSAVLTGDNGLDLERIQHLVDQMAALTHRGYQVVMVTSGAIASGKHRLGITTALKSIPQKQAAAAIGQGRLMRIYSNSFGKHGLYVGQILLTMSDLTDRRRFLNIRNTLSTLMEWGIIAIINENDTVAIDEIKFGDNDNLAAMIANIIEAHLVINLTSTPGLYDRNPASSRNARLIPLVREITEDIEAAASEEGTSVGTGGMKSKVMAAKKVTAFGIPYIIAPGKQKDVLLDIFDGNELGTLFLPMREHLSSRKYWIAFTLRSRGVLSIDAGARTAILEEGKSLLPSGIVGVEGDFIVGDP... | 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: s... |
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 ... |
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 ... |
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