ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q9SZ46 | MDTSLFSLFVPILVFVFIALFKKSKKPKYVKAPAPSGAWPIIGHLHLLGGKEQLLYRTLGKMADHYGPAMSLQLGSNEAFVVSSFEVAKDCFTVNDKALASRPMTAAAKHMGYNFAVFGFAPYSAFWREMRKIATIELLSNRRLQMLKHVRVSEITMGVKDLYSLWFKNGGTKPVMVDLKSWLEDMTLNMIVRMVAGKRYFGGGGSVSSEDTEEAMQCKKAIAKFFHLIGIFTVSDAFPTLSFFDLQGHEKEMKQTGSELDVILERWIENHRQQRKFSGTKENDSDFIDVMMSLAEQGKLSHLQYDANTSIKSTCLALIL... | Function: Can hydroxylate xanthotoxin (8-methoxypsoralen) to form 5-hydroxyxanthotoxin (5-hydroxy-8-methoxypsoralen) in vivo and in vitro . Involved in the early iron deficiency response, possibly through an IDE1-like mediated pathway . Involved in the pathway of sideretin biosynthesis from feruloyl CoA, a redox-active... |
A0A0N7F297 | MDSLHCLETLLLGFFVLLPCFFYFVWKKPNNKIKEPPQPAGAWPIIGHLHLLARGDLPHKILSSFADKNGPVFKIQLGVHQALVVNNSEIAKECFTTNDRFFLNRPSGVAAKIMGYNYVMLGVAPYGPYWRDMRKIIMLEFLSNRRLQSLKHVWHSEISISSKELYKLWETQNIDFCLVDMKQWLADLTLNMSVKMVVGKRFFGSASASACEETESSNCPKTLRNMFRLMGSFVLSDYLPYLRWLDLGGHEKEMKRTVKELDILFKGWLDEHKRKRLSGGKEDDDQDFMDVMLSILEESKLGNDVDTINKTACLAIILGG... | Function: Cytochrome P450 involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family . Catalyzes the hydroxylation of deoxypodophyllotoxin to form epipodophyllotoxin .
Catalytic Activity: (-)-4'-desmethyl-deoxypodophyllotoxin + O2 + reduced [NADPH--hemoprotein reductase... |
Q38Q87 | MVFPIEAIVGLVTFTFLFFFLWTKKSQKPSKPLPPKIPGGWPVIGHLFHFNDDGDDRPLARKLGDLADKYGPVFTFRLGLPLVLVVSSYEAVKDCFSTNDAIFSNRPAFLYGDYLGYNNAMLFLANYGPYWRKNRKLVIQEVLSASRLEKFKHVRFARIQASIKNLYTRIDGNSSTINLTDWLEELNFGLIVKMIAGKNYESGKGDEQVERFKKAFKDFMILSMEFVLWDAFPIPLFKWVDFQGHVKAMKRTFKDIDSVFQNWLEEHINKREKMEVNAEGNEQDFIDVVLSKMSNEYLGEGYSRDTVIKATVFSLVLDAA... | Function: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the... |
Q9LSF8 | MTFLFSTLQLSLFSLALVIFGYIFLRKQLSRCEVDSSTIPEPLGALPLFGHLHLLRGKKLLCKKLAAMSQKHGPIFSLKLGFYRLVVASDPKTVKDCFTTNDLATATRPNIAFGRYVGYNNASLTLAPYGDYWRELRKIVTVHLFSNHSIEMLGHIRSSEVNTLIKHLYKGNGGTSIVKIDMLFEFLTFNIILRKMVGKRIGFGEVNSDEWRYKEALKHCEYLAVIPMIGDVIPWLGWLDFAKNSQMKRLFKELDSVNTKWLHEHLKKRSRNEKDQERTIMDLLLDILPEDIVISGHVRDVIVKATILALTLTGSDSTSI... | Function: Involved in the biosynthesis of homoterpenes, attractants of herbivores parasitoids and predators (e.g. predatory mites and parasitoid wasps) . Catalyzes the conversion of the C20 (E,E)-geranyllinalool to C16-homoterpene 4,8,12-trimethyltrideca-1,3,7,11-tetraene (TMTT) of the C15 (E)-nerolidol to C11-homoterp... |
I3V6B7 | MELFIKLPFIQPIPFSIILVTTVSIVLLYSVFFWVTDKKKKRKKAPNAAGAWPLIGHLRLLMNDKEPLYRALGSMADKYGPAFNIRLGNQEVLVVSNWEMVKQCFGNQNDKLFSNRQTTLAAKYMLNQTTSSGFAPYGPYWRELRKIMVQQLLSKQSLESWKHLKIKEMDASFSKLNELCNNNGTGTATLIRMDEWFAELTFNVIARNVFGYQSGGRSTALTNGDTESKGERYKKTLEEALHLMSIFAVSDIFPSLEWVDRLRGLIRNMKRFGDELNSIAGCLIEEHRQKRLQSVSKSDKGVGDEQDFVDVLLSVAEKSQ... | Function: Cytochrome P450 involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine . Converts (13S,14R)-13-O-acetyl-1-hydroxy-N-methylcanadine to (13S,14R)-13-O-acetyl-1,8-dihydroxy-N-methylcanadine .
Catalytic Activity: (13S,14R)-13-O-acetyl-1-hydroxy-N-methylcanadine + O2 + reduced [NADPH--hemoprotei... |
I3PLR1 | MAYLMIKKSIYLFFDQPTAVGTLILAFLLTLSPVIIYYEQKKRGLRRNRTAITTTPLPEASGAWPVIGHLLLFMNENDLNHVTLGHMADKYGPIFSLRFGRHRTLVVSSWEMVKECFTGTNDKLFSNRPSSLAVKLMFYDTESYGFAPYGKYWRELRKISTHKLLSNQQLEKFKHLRISEVDNSFKKLHELCSNNKQGGDTTYVASLVRMDDWFAYLTFNVIGRIVSGFQSNAVAGATNSQEKYKLAIDEVSNLMATFAVSDVVPRLGWIDRLTGLTGKMKNCGKKLDAVVGDAVEDHRQKKLKISRNNTGALTEHEEED... | Function: Cytochrome P450 involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine . Converts (S)-N-methylcanadine to (S)-1-hydroxy-N-methylcanadine .
Catalytic Activity: (S)-cis-N-methylcanadine + O2 + reduced [NADPH--hemoprotein reductase] = (S)-1-hydroxy-N-methylcanadine + H(+) + H2O + oxidized [NAD... |
O65782 | MDLLLIIAGLVAAAAFFFLRSTTKKSLRLPPGPKGLPIIGNLHQMEKFNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTARPLLKGQQTMSYQGRELGFGQYTAYYREMRKMCMVNLFSPNRVASFRPVREEECQRMMDKIYKAADQSGTVDLSELLLSFTNCVVCRQAFGKRYNEYGTEMKRFIDILYETQALLGTLFFSDLFPYFGFLDNLTGLSARLKKAFKELDTYLQELLDETLDPNRPKQETESFIDLLMQIYKDQPFSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPE... | Function: Involved in the metabolism of aromatic oximes. Catalyzes the oxime metabolizing step in indole glucosinolate biosynthesis by converting indole-3-acetaldoxime into indole-3-S-alkyl-thiohydroximate. Probably required for glucosinolate activation in response to pathogens. Functions in auxin homeostasis because i... |
Q42600 | MESSISQTLSKLSDPTTSLVIVVSLFIFISFITRRRRPPYPPGPRGWPIIGNMLMMDQLTHRGLANLAKKYGGLCHLRMGFLHMYAVSSPEVARQVLQVQDSVFSNRPATIAISYLTYDRADMAFAHYGPFWRQMRKVCVMKVFSRKRAESWASVRDEVDKMVRSVSCNVGKPINVGEQIFALTRNITYRAAFGSACEKGQDEFIRILQEFSKLFGAFNVADFIPYFGWIDPQGINKRLVKARNDLDGFIDDIIDEHMKKKENQNAVDDGDVVDTDMVDDLLAFYSEEAKLVSETADLQNSIKLTRDNIKAIIMDVMFGG... | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58721
Sequence Length: 520
Pathway: Aromatic compound metabolism; phenylpropanoid biosynthesis.
Subcellular Location: Membrane
EC: 1.14.-.-
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F4JW83 | MLTLMTLIVLVPLLLFLFPHLLLRRQMLLKPYPPGPKGLPVIGNILMMNQFNHRGLAKLSRIYGGLLHLRLGFSHIFVVSSPDIARQVLQVQDHVFSNRPTTIAIRYLTYGGSDLAFCNYGPFWRRMRKLYVMMLFSRKRAESWVSVDEEVHKSVRLVASNVGKPLNICKLAFSLSRDITFRAAFGSSSSTSDESRLDEFLEIIQEFSKLFGEFNVADYVPSWLSWIDPQGINGRVEKARKSLDGFIESVIDDHLHKKKREHDNVDEETDMVDQLLAFYEEEVKVNNSVTKINLDNIKGIIMDVMFGGTETVALAIEWVL... | Function: Cytochrome P450 involved in the production of catechol-substituted substrates needed for the arabidopyrones biosynthesis. Converts p-coumaraldehyde into caffealdehyde.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57955
Sequence Length: 512
Subcellular Location: Membrane
EC: 1.14.-.-
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P0C8V0 | MFTVFLLVVLVTTVVFSTSDHRPASNHENRRASKRISEMTWEECCTNPVCRQHYMHYC | Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them (By similarity). Has possibly a distinct nAChR binding mode from other alpha-conotoxins, due to a different three residue motif (lacks the Ser-Xaa-Pro motif) (By similarity).
Sequen... |
Q9BRK5 | MVWPWVAMASRWGPLIGLAPCCLWLLGAVLLMDASARPANHSSTRERVANREENEILPPDHLNGVKLEMDGHLNRGFHQEVFLGKDLGGFDEDAEPRRSRRKLMVIFSKVDVNTDRKISAKEMQRWIMEKTAEHFQEAMEESKTHFRAVDPDGDGHVSWDEYKVKFLASKGHSEKEVADAIRLNEELKVDEETQEVLENLKDRWYQADSPPADLLLTEEEFLSFLHPEHSRGMLRFMVKEIVRDLDQDGDKQLSVPEFISLPVGTVENQQGQDIDDNWVKDRKKEFEELIDSNHDGIVTAEELESYMDPMNEYNALNEAK... | Function: May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment.
Sequence Mass (Da): 41807
Sequence Length: 362
Domain: Binds calcium via its EF-hands (By similarity). Isoform 5 binds calcium.
Subcellular Location: Golgi apparatus lumen
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Q03941 | MLVVGLTGGIACGKSTVSRRLRDKYKLPIVDADKIARQVVEPGQNAYDQIVLYFKDKIPNLLLEDGHLNREALGKWVFSHKEDLQALNGITHPAIRYAMFKEIGYYYLKGYRMCVLDVPLLFEGNLDSICGVTVSVICTQELQLERLMTRNPELSEEDAKNRLNSQMSTEERMARSDYILQNNSTLVDLYEQIESVVKKIQPSKLRTVLEYFPPFGAVSASSIVMSRLLMKKLQNKKSSAV | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 27340
Sequence Length: 241
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q01667 | MASNSLMSCGIAAVYPSLLSSSKSKFVSAGVPLPNAGNVGRIRMAAHWMPGEPRPAYLDGSAPGDFGFDPLGLGEVPANLERYKESELIHCRWAMLAVPGILVPEALGYGNWVKAQEWAALPGGQATYLGNPVPWGTLPTILAIEFLAIAFVEHQRSMEKDPEKKKYPGGAFDPLGYSKDPKKLEELKVKEIKNGRLALLAFVGFCVQQSAYPGTGPLENLATHLADPWHNNIGDIVIPFN | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phos... |
P59807 | MPIFRFTALAMTLGLLSAPYNAMAATSNPAFDPKNLMQSEIYHFAQNNPLADFSSDKNSILTLSDKRSIMGNQSLLWKWKGGSSFTLHKKLIVPTDKEASKAWGRSSTPVFSFWLYNEKPIDGYLTIDFGEKLISTSEAQAGFKVKLDFTGWRAVGVSLNNDLENREMTLNATNTSSDGTQDSIGRSLGAKVDSIRFKAPSNVSQGEIYIDRIMFSVDDARYQWSDYQVKTRLSEPEIQFHNVKPQLPVTPENLAAIDLIRQRLINEFVGGEKETNLALEENISKLKSDFDALNIHTLANGGTQGRHLITDKQIIIYQPE... | Function: Endolytic, broad-specificity glycosaminoglycan lyase, which degrades the polysaccharides chondroitin, chondroitin-4-sulfate, chondroitin-6-sulfate, dermatan sulfate and to a lesser extent hyaluronan, by beta-elimination of 1,4-hexosaminidic bond to unsaturated tetrasaccharides and disaccharides. Is not active... |
C5G6D7 | MLILSFLCPAFLNAQIVTDERMFSFEEPQLPACITGVQSQLGISGAHYKDGKHSLEWTFEPNGRLELRKDLKFEKKDPTGKDLYLSAFIVWIYNEQPQDAAIEFEFLKDGRKCASFPFGINFKGWRAAWVCYERDMQGTPEEGMNELRIVAPDAKGRLFIDHLITATKVDARQQTADLQVPFVNAGTTNHWLVLYKHSLLKPDIELTPVSDKQRQEMKLLEKRFRDMIYTKGKVTEKEAETIRKKYDLYQITYKDGQVSGVPVFMVRASEAYERMIPDWDKDMLTKMGIEMRAYFDLMKRIAVAYNNSEAGSPIRKEMRR... | Cofactor: Divalent metal cation. Requires divalent metal cation for binding of dermatan sulfate substrate, whereas it is not necessary for the binding of chondroitin sulfate substrates. Prefers Ca(2+) or Mg(2+), binding 1 ion per subunit.
Function: Broad-specificity glycosaminoglycan lyase, which acts in an exolytic fa... |
G7IYC1 | MSSSNLGNVVCVTGASGYIASWLVRLLLHRGYTVKATVRDPNDPKKVDHLVKLDGAKERLQLFKANLLEEGAFDSVVQGCHGVFHTASPFYHDVKDPQAELIDPALKGTLNVLNSCAKSPSLKRVVLTSSIAAVAYNGKPRTPDVVVDETWFTDADFCAKSNLWYVVSKTLAEEAAWKFVKENNIDMVTINPAMVIGPLLQPVLNTSAAAILNLINGAQTFPNASFGWVNVKDVANAHILAYENASASGRHCLVERVAHYSEVVRILRELYPSLQLPEKCADDKPYVPIYQVSKEKAKSLGLEYTPLEVSIKETVESLKE... | Function: Involved in lignin biosynthesis (By similarity). Regulates the monolignol composition by catalyzing the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (By similarity). Can use coumaraldehyde and coniferaldehyde as substrates, but barely sinapaldehyde .
Catalytic Activity: (E)-cinnamalde... |
Q6ERW9 | MSRHFRTHTTSRLTFPSSSGGLAITRLPFSSTSSKLLLQQLSSTSPAAAATAVTITTSSPARNLQRARASAAEQGMEEHGKAAVGWAARDDSGVLSPYNFSRRAQKDDDVTIKVLYCGICHTDLHVVKNDWGNAMYPVVPGHEIVGVVTGVGAGVTKFKAGDTVGVGFFVGSCRTCDSCGKGYENYCPTMVITSNGKDYGGAATQGGFSDAIVVNEHYVLRVPAGLPLDGAAPLLCAGVTVYSPMVIHGLNAPGKHVGVVGLGGLGHVAVKFAKAFGMRVTVISTSPGKRREALEHLGADEFLVSRDAGQMAAAAGTMDG... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective al... |
Q6ERW7 | MSRHFRTHTTSRLTFPSSSGGLAITRLPFSSTSSKLLLQQLSSTSPAAAATAVTITTSSPARNLQRARASAAEQGMEEHGKAAVGWAARDDSGVLSPYNFSRRAQKDDDVTIKVLYCGICHTDLHIVKNDWGNAMYPVVPGHEIVGVVTGVGAGVTKFKAGDTVGVGYFVASCRGCECCGNGYENYCAKMVTTCNGVDHDHGGGAATQGGFSDAIVVNEHYVLRVPAGLPLDSAAPLLCAGVTVYSPMVIHGLNAPGKHVGVVGLGGLGHVAVKFAKAFGMRVTVISTSPGKRQEALEHLGADEFLVSRDAGQMAAAAAT... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective al... |
Q9VBW3 | MVYHHHNHESRIIHCRKQLTSWRRRSLLLTIIVVTATVVSLISQEAEAHNQNAPPILYVRERNWRISETEKVGQIIDRVRAEDPDGDDLIFGIEPRFSLPGGENDASPPEKIPFQIDRETGVVTLNESLAGRAGQNFLIYITVTDGSYTAKNEVFINILGERENSSGYRPQTSISNVVHNISQFLPRFDQLPGVQSIRNGLPNSRPGGWYPPVPQNNIFGPPPFGNNYPPPPPNIPGVRGEQSGEEEQPDEEVTPTTPVRISSTTPKSRTKLTPITANNSTRVESAIPAETTTPSGGHHNNSSSPITIFSLKSGTIPIVV... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 86220
Sequence Length: 773
Subcellular Location: Membrane
EC: 2.7.10.1
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P20021 | MSEQKVKLMEEEMNVYRVQGFTCANCAGKFEKNVKKIPGVQDAKVNFGASKIDVYGNASVEELEKAGAFENLKVSPEKLANQTIQRVKDDTKAHKEEKTPFYKKHSTLLFATLLIAFGYLSHFVNGEDNLVTSMLFVGSIVIGGYSLFKVGFQNLIRFDFDMKTLMTVAVIGATIIGKWAEASIVVILFAISEALERFSMDRSRQSIRSLMDIAPKEALVRRNGQEIIIHVDDIAVGDIMIVKPGEKIAMDGIIVNGLSAVNQAAITGESVPVSKAVDDEVFAGTLNEEGLIEVKITKYVEDTTITKIIHLVEEAQGERA... | Function: Couples the hydrolysis of ATP with the export of cadmium . Involved in cadmium resistance .
Catalytic Activity: ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 78812
Sequence Length: 727
Subcellular Location: Cell membrane
EC: 7.... |
O32219 | MRLVKQEYVLDGLDCSNCARKIENGVKGIKGINGCAVNFAASTLTVSADGKEEQWVTNKVEKKVKSIDPHVTVRQKHIKKSADDGYRNRMVNMLIRMAAAVILGAAAYLVQSGTIEFFLFLGAYLIIGGDIIIRAVKNIIRGQVFDEHFLMALATIGAFLIQQYPEGVAVMLFYQIGELFQGAAVSRSRKSISALMDIRPDYANLKTKNGIEQVSSEDVQTGDIIVVNPGESIPLDGKVVQGSAMVDTSALTGESVPRKAAEGQDVMSGFINQNGVLHIEVTKGYQESAVSKILDLVQNASSRKARTENFITKFAKYYTP... | Function: Couples the hydrolysis of ATP with the transport of cadmium, zinc and cobalt out of the cell. Does not seem to transport copper.
Catalytic Activity: ATP + H2O + Zn(2+)(in) = ADP + H(+) + phosphate + Zn(2+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75405
Sequence Length: 702
Subce... |
Q60048 | MAEKTVYRVDGLSCTNCAAKFERNVKEIEGVTEAIVNFGASKITVTGEASIQQVEQAGAFEHLKIIPEKESFTDPEHFTDHQSFIRKNWRLLLSGLFIAVGYASQIMNGEDFYLTNALFIFAIFIGGYSLFKEGFKNLLKFEFTMETLMTIAIIGAAFIGEWAEGSIVVILFAVSEALERYSMDKARQSIRSLMDIAPKEALVRRSGTDRMVHVDDIQIGDIMIIKPGQKIAMDGHVVKGYSAVNQAAITGESIPVEKNIDDSVFAGTLNEEGLLEVAVTKRVEDTTISKIIHLVEEAQGERAPAQAFVDTFAKYYTPAI... | Function: Couples the hydrolysis of ATP with the export of cadmium.
Catalytic Activity: ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 77089
Sequence Length: 711
Subcellular Location: Cell membrane
EC: 7.2.2.21
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P58414 | MSKASKQTTYRVDGMSCTNCAGKFEKNVKNLEGVTDAKVNFGAGKISVYGETSISQIEKAGAFENLRVTDEKDYSSKPAKKESFLKKNWHLVVSIIFIILAFISQNISGEDSTTTIILYVIAIVVGGFNLFKEGFANLIKLDFTMESLMTIAIIGASIIGEWAEGSIVVILFAFSEVLERYSMDKARQSIRSLMDIAPKEALIRRDDVEQMIAVSDIQIGDIMIIKPGQKIAMDGVVIKGYSAINQSAITGESIPVEKKVDDEVFAGTLNEEGLLEVKVTKHVEDTTISKIIHLVEEAQGERAPAQAFVDKFAKYYTPTI... | Function: Couples the hydrolysis of ATP with the export of cadmium.
Catalytic Activity: ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76478
Sequence Length: 707
Subcellular Location: Cell membrane
EC: 7.2.2.21
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P41637 | MGSLESEKTVTGYAARDSSGHLSPYTYNLRKKGPEDVIVKVIYCGICHSDLVQMRNEMGMSHYPMVPGHEVVGIVTEIGSEVKKFKVGEHVGVGCIVGSCRSCGNCNQSMEQYCSKRIWTYNDVNHDGTPTQGGFASSMVVDQMFVVRIPENLPLEQAAPLLCAGVTVFSPMKHFAMTEPGKKCGILGLGGVGHLGVKIAKAFGLHVTVISSSDKKKEEAMEVLGADAYLVSKDTEKMMEAAESLDYIMDTIPVAHPLEPYLALLKTNGKLVMLGVVPEPLHFVTPPLILGRRSIAGSFIGGMEETQETLDFCAEKKVSS... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective al... |
Q8R5M8 | MASAVLPSGSQCAAAAAVAAAAAPPGLRLRLLLLLLSAAALIPTGDGQNLFTKDVTVIEGEVATISCQVNKSDDSVIQLLNPNRQTIYFRDFRPLKDSRFQLLNFSSSELKVSLTNVSISDEGRYFCQLYTDPPQESYTTITVLVPPRNLMIDIQKDTAVEGEEIEVNCTAMASKPATTIRWFKGNKELKGKSEVEEWSDMYTVTSQLMLKVHKEDDGVPVICQVEHPAVTGNLQTQRYLEVQYKPQVHIQMTYPLQGLTREGDAFELTCEAIGKPQPVMVTWVRVDDEMPQHAVLSGPNLFINNLNKTDNGTYRCEASN... | Function: Mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner . Also mediates heterophilic cell-cell adhesion with CADM3 and NECTIN3 in a Ca(2+)-independent manner . Interaction with CRTAM promotes natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ T-cells in vitr... |
Q8N3J6 | MIWKRSAVLRFYSVCGLLLQGSQGQFPLTQNVTVVEGGTAILTCRVDQNDNTSLQWSNPAQQTLYFDDKKALRDNRIELVRASWHELSISVSDVSLSDEGQYTCSLFTMPVKTSKAYLTVLGVPEKPQISGFSSPVMEGDLMQLTCKTSGSKPAADIRWFKNDKEIKDVKYLKEEDANRKTFTVSSTLDFRVDRSDDGVAVICRVDHESLNATPQVAMQVLEIHYTPSVKIIPSTPFPQEGQPLILTCESKGKPLPEPVLWTKDGGELPDPDRMVVSGRELNILFLNKTDNGTYRCEATNTIGQSSAEYVLIVHDVPNTL... | Function: Adhesion molecule that engages in homo- and heterophilic interactions with the other nectin-like family members, leading to cell aggregation. Important for synapse organization, providing regulated trans-synaptic adhesion. Preferentially binds to oligodendrocytes.
Location Topology: Single-pass type I membran... |
Q8BLQ9 | MIWKRSAVLRFYSVCGLLLQGSQGQFPLTQNVTVVEGGTAILTCRVDQNDNTSLQWSNPAQQTLYFDDKKALRDNRIELVRASWHELSISVSDVSLSDEGQYTCSLFTMPVKTSKAYLTVLGVPEKPQISGFSSPVMEGDLMQLTCKTSGSKPAADIRWFKNDKEIKDVKYLKEEDANRKTFTVSSTLDFRVDRSDDGVAVICRVDHESLNATPQVAMQVLEIHYTPSVKIIPSTPFPQEGQALTLTCESKGKPLPEPVLWTKDGAELPDPDRMVVSGRELNILFLNKTDNGTYRCEATNTIGQSSAEYVLIVHDVPNTL... | Function: Adhesion molecule that engages in homo- and heterophilic interactions with the other nectin-like family members, leading to cell aggregation. Important for synapse organization, providing regulated trans-synaptic adhesion. Preferentially binds to oligodendrocytes (By similarity).
PTM: Glycosylation at Asn-51 ... |
Q16790 | MAPLCPSPWLPLLIPAPAPGLTVQLLLSLLLLVPVHPQRLPRMQEDSPLGGGSSGEDDPLGEEDLPSEEDSPREEDPPGEEDLPGEEDLPGEEDLPEVKPKSEEEGSLKLEDLPTVEAPGDPQEPQNNAHRDKEGDDQSHWRYGGDPPWPRVSPACAGRFQSPVDIRPQLAAFCPALRPLELLGFQLPPLPELRLRNNGHSVQLTLPPGLEMALGPGREYRALQLHLHWGAAGRPGSEHTVEGHRFPAEIHVVHLSTAFARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLSRLEEIAEEGSETQVPGLDISALLPSD... | Function: Catalyzes the interconversion between carbon dioxide and water and the dissociated ions of carbonic acid (i.e. bicarbonate and hydrogen ions).
PTM: Asn-346 bears high-mannose type glycan structures.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O... |
Q8VHB5 | MASLGPSPWAPLSTPAPTAQLLLFLLLQVSAQPQGLSGMQGEPSLGDSSSGEDELGVDVLPSEEDAPEEADPPDGEDPPEVNSEDRMEESLGLEDLSTPEAPEHSQGSHGDEKGGGHSHWSYGGTLLWPQVSPACAGRFQSPVDIRLERTAFCRTLQPLELLGYELQPLPELSLSNNGHTVQLTLPPGLKMALGPGQEYRALQLHLHWGTSDHPGSEHTVNGHRFPAEIHVVHLSTAFSELHEALGRPGGLAVLAAFLQESPEENSAYEQLLSHLEEISEEGSKIEIPGLDVSALLPSDLSRYYRYEGSLTTPPCSQGVI... | Function: Catalyzes the interconversion between carbon dioxide and water and the dissociated ions of carbonic acid (i.e. bicarbonate and hydrogen ions).
PTM: Asn-325 bears high-mannose type glycan structures.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O... |
P40880 | MSLQIGRTERARSPVFVFAHKRQLLHGRCSTIDNANCSTCSMKINSTCTLTALPIAALPGPRTTSHYSTAAANWCYATVAPRARSSTIAASLGTPAPSSSASFRPKLIRTTPVQAAPVAPALMDAAVERLKTGFEKFKTEVYDKKPDFFEPLKAGQAPKYMVFACADSRVCPSVTLGLEPGEAFTIRNIANMVPAYCKNKYAGVGSAIEYAVCALKVEVIVVIGHSRCGGIKALLSLKDGADDSFHFVEDWVRIGFPAKKKVQTECASMPFDDQCTVLEKEAVNVSLQNLLTYPFVKEGVTNGTLKLVGGHYDFVSGKFE... | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 35074
Sequence Length: 324
Subcellular Location: Plastid
EC: 4.2.1.1
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P17067 | MSTSSINGFSLSSLSPAKTSTKRTTLRPFVSASLNTSSSSSSSTFPSLIQDKPVFASSSPIITPVLREEMGKGYDEAIEELQKLLREKTELKATAAEKVEQITAQLGTTSSSDGIPKSEASERIKTGFLHFKKEKYDKNPALYGELAKGQSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVPPYDQAKYAGTGAAIEYAVLHLKVSNIVVIGHSACGGIKGLLSFPFDGTYSTDFIEEWVKIGLPAKAKVKAQHGDAPFAELCTHCEKEAVNASLGNLLTYPFVREGLVNKTLALKGGYYDFVKGSFELWGLEF... | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 35377
Sequence Length: 328
Subcellular Location: Plastid
EC: 4.2.1.1
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P16016 | MSTINGCLTSISPSRTQLKNTSTLRPTFIANSRVNPSSSVPPSLIRNQPVFAAPAPIITPTLKEDMAYEEAIAALKKLLSEKGELENEAASKVAQITSELADGGTPSASYPVQRIKEGFIKFKKEKYEKNPALYGELSKGQAPKFMVFACSDSRVCPSHVLDFQPGEAFMVRNIANMVPVFDKDKYAGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSFPDAGPTTTDFIEDWVKICLPAKHKVLAEHGNATFAEQCTHCEKEAVNVSLGNLLTYPFVRDGLVKKTLALQGGYYDFVNGSFELWGLEYGLSPSQSV | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 34570
Sequence Length: 319
Subcellular Location: Plastid
EC: 4.2.1.1
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A0A1L4BJ42 | MRASLFIVIFVVSFITISCLSTDDEEARWIEKRGDCLPHLKLCKADKDCCSKKCKRRGTNPEKRCR | Function: This toxin stabilizes ryanodine receptor 1 (RyR1) opening in a long-lasting subconductance state (20% and 38% of the full conductance state have been found) . It promotes an increase in the opening probability at intermediate concentration . Furthermore, it triggers calcium release from sarcoplasmic vesicles ... |
P04195 | MPQQLSPINIETKKAISNARLKPLDIHYNESKPTTIQNTGKLVRINFKGGYISGGFLPNEYVLSSLHIYWGKEDDYGSNHLIDVYKYSGEINLVHWNKKKYSSYEEAKKHDDGLIIISIFLQVLDHKNVYFQKIVNQLDSIRSANTSAPFDSVFYLDNLLPSKLDYFTYLGTTINHSADAVWIIFPTPINIHSDQLSKFRTLLSSSNHDGKPHYITENYRNPYKLNDDTQVYYSGEIIRAATTSPARENYFMRWLSDLRETCFSYYQKYIEENKTFAIIAIVFVFILTAILFFMSRRYSREKQN | Function: Binds to chondroitin sulfate on the cell surface to provide virion attachment to target cell.
PTM: Apparently non-glycosylated.
Sequence Mass (Da): 35446
Sequence Length: 304
Subcellular Location: Virion membrane
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A0A1V6PBE7 | MSDSTMDTQLALLVWGIAVCVTLAIVVPRWIGNNSKEPPSLGGSMLSNTYQYMTDMHGFLQRVASAQRSSKIIKFRLGPKKIYMVSGEKNIQAINRPSHSISPDVFFLEVMANVWGASKEEVGKFKQDQSGRSKNPVPGHDVKPGQPRLWHGQHRVYSEYLQRTDHANALSNKYFQLFSERLTKQPLGDWTELRLSHFFESDMAEAALVALMGPRIVELNPGFWPTMWEFARLAPRLMWGLPRWVNPKPWEIRELFHGMCRRYVDAAKREFDWNGPDVDAGWEPHYGSRMARELISWAEKNLSPETTAGMVATFIFGTNA... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of calbistrin A and related compounds. Calbistrin A is a secondary metabolite with an interesting structure that was recently found to have bioactivity against leukemia cells. It consists of two polyketides linked by an est... |
P0DP23 | MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK | Function: Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding . Calcium-binding is required for the activation of calmodulin . Among the enzymes to be stimulated by the calmodulin-calc... |
P49913 | MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQVLSYKEAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPDTPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKRCMGTVTLNQARGSFDISCDKDNKRFALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES | Function: Antimicrobial protein that is an integral component of the innate immune system . Binds to bacterial lipopolysaccharides (LPS) . Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2 . Postsecretory processing generates multiple cathelicidin antimicrobial peptides with various lengths... |
P51437 | MQFQRDVPSLWLWRSLSLLLLLGLGFSQTPSYRDAVLRAVDDFNQQSLDTNLYRLLDLDPEPQGDEDPDTPKSVRFRVKETVCGKAERQLPEQCAFKEQGVVKQCMGAVTLNPAADSFDISCNEPGAQPFRFKKISRLAGLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPE | Function: Antimicrobial protein that is an integral component of the innate immune system (By similarity). Binds to bacterial lipopolysaccharides (LPS) (By similarity).
PTM: Proteolytically cleaved by cathepsin CTSG.
Sequence Mass (Da): 19453
Sequence Length: 172
Subcellular Location: Secreted
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B8G5D6 | MQPHLFTPLTIGSVTLRNRIGMSPMCQYSAVDGFPTDWHLMHLGARAAGGVGLIILEATAVSPEGRISPFDLGIWSDDHIAALSRIVKLIESLGAVAGIQLAHAGRKASVGRPWEGGKPIAPANGGWPVVGPTAEPFAPGYPTPIPLDAAGIARVVADFATATKRARAAGFRWIEIHAAHGYLLHNFLSPLGNDRNDEYGGDLRGRVRLLSEVTAAVRAEWPSDLPLAVRLSCSDWTPEGLTIADTVEVARMLREQGVDLIDCSSGGIAPGITIPVGEGYQVPFAAQVRREANIATAAVGLITRPEHADAIVRNGDADLV... | Function: Ene-reductase that catalyzes the stereoselective reduction of activated C-C double bonds . Shows very good activity with 4-ketoisophorone, 2-cyclohexen-1-one and 1-octen-3-one, and low activity with maleimide, 2-methyl-pentenal, 2-methyl-cyclohexen-1-one, 2-cyclopenten-1-one and trans-2-hexen-1-al . Shows the... |
Q9MBA1 | MNAAVFSPSALSLPISFSKTRSSFLSRKKGVKGEFRVFAVFGDESGLVEKKSQWRPLFDVEDPRSKAPPYKGKFLDVNQAIEVARFDIQYLDWRARQDLLTIMILHDKVVDVLNPLAREYKSIGTVKKELAGLQEELSKAHQQVHISEARVSTALDKLAHMEELVNDRLLPGRVVTELDKPSSSTTASAVELDREKTNTGAKSLNVSGPVPPYSPHLKNFWYPVAFTADLKHDTMVPIECFEQPWVIFRGEDGKPGCVRNTCAHRACPLDLGTVNEGRIQCPYHGWEYSTDGECKKMPSTKLLKVKIKSLPCLEQEGMIW... | Function: Catalyzes a two-step oxygenase reaction involved in the synthesis of chlorophyll b. Acts specifically on the non-esterified chlorophyllide a and not on chlorophyll a.
Catalytic Activity: chlorophyllide a + 2 H(+) + 2 NADPH + 2 O2 = chlorophyllide b + 3 H2O + 2 NADP(+)
Location Topology: Peripheral membrane pr... |
Q9ZWM5 | MLPASLQRKAAAVGGRGPTNQSRVAVRVSAQPKEAPPASTPIVEDPESKFRRYGKHFGGIHKLSMDWLDSVPRVRVRTKDSRQLDDMLELAVLNERLAGRLEPWQARQKLEYLRKRRKNWERIFEYVTRQDAAATLAMIEEANRKVEESLSEEAREKTAVGDLRDQLESLRAQVAQAQERLAMTQSRVEQNLQRVNELKAEATTLERMRKASDLDIKERERIAISTVAAKGPASSSSSAAAVSAPATSATLTVERPAATTVTQEVPSTSYGTPVDRAPRRSKAAIRRSRGLESSMEIEEGLRNFWYPAEFSARLPKDTLV... | Function: Catalyzes a two-step oxygenase reaction involved in the synthesis of chlorophyll b. Acts specifically on the non-esterified chlorophyllide a and not on chlorophyll a.
Catalytic Activity: chlorophyllide a + 2 H(+) + 2 NADPH + 2 O2 = chlorophyllide b + 3 H2O + 2 NADP(+)
Location Topology: Peripheral membrane pr... |
Q9XJ38 | MQSKLLGLQDEISEARDKLRTSEARVAQNLKRVDELKAEAASLERMRLASSSSTDSTVSIASRGGAAVAATTSVPDHVEREGIQSRVRGSGMASTSYPSHVPQPSQAVRRGPKPKDSRRLRSSLELEDGLRNFWYPTEFAKKLEPGMMVPFDLFGVPWVLFRDEHSAPTCIKDSCAHRACPLSLGKVINGHVQCPYHGWEFDGSGACTKMPSTRMCHGVGVAALPCVEKDGFVWVWPGDGPPPDLPPDFTAPPAGYDVHAEIMVDVPVEHGLLMENLLDLAHAPFTHTTTFARGWPIPEAVRFHATKMLAGDWDPYPISM... | Function: Catalyzes a two-step oxygenase reaction involved in the synthesis of chlorophyll b. Acts specifically on the non-esterified chlorophyllide a and not on chlorophyll a.
Catalytic Activity: chlorophyllide a + 2 H(+) + 2 NADPH + 2 O2 = chlorophyllide b + 3 H2O + 2 NADP(+)
Location Topology: Peripheral membrane pr... |
A0A5D0EMF2 | MKKKIFIGSSSEELRIAEKVKKILEQDNEFEVTIWNDNSIWDNSVFKLNHNFLTDLLNSSLSSDFGILIGTCDDKVIVRGTERLQPRDNVLFELGFFIGKLGLDNCAFLIDKNIHILSDVQGITLARANMGDPDELKRAVNCIKEHFKHQPNSGINFFPSSTLASVYHENFIKPTCQTIIEDNGILDTAGKKHTNCLVKIIIPNKINIDVNSQFQILKNKISTNTLSFNYKGRPRNISIEIVESSEENTTIIDFPTIISGIYYAISNLLPQDSETDSITYRNILARELDRFVNTLYKFIKRDGYDEIVKIVYEDKLY | Function: CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell ... |
A0A381HAP5 | MRGKRIFIGSSSEELRLAEQAKKILEKNTNYQVTIWNENMWDKAVFRLNNSYLNDLIRATLHFDFGILIGTKDDKVIFRGSEEIQPRDNVLFELGLFIGRLGLNNCAFLVDEEIKILSDVKGISLARFKEKDSDSFNNAVLSIRESFDRQNDSDINFFPSSTLAAVYYENFIKPTCSHIINNGGLLDKNGYIYKKCTIKIIIPKKLTSDVNSQFQRIKAKIETKELSFEYLGRPRNINVEIIAEDGEVMIIDFPTILSGINYAISNLLPQDFNSMSVDYEAILSRELERFVYTLKKIALRDGFDDLIKIVDEDN | Function: CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell ... |
P0DUD9 | MKTRIFIGSSKEGLEIAEYIKLQLGTKYECYLWTDDIFKFNESFLYTLLKEASLFDFGILVATKDDLSTIRDKSFDTPRDNVIFEFGLFLGRLGPSRAFVIQESGAKLPTDLLGITVPQFEKTIPLANSTSLNNEIERISKTIDEKITLGELGLLPSTVLAIGYFYNFVSIVCESIHTKSDIKVDDAIFKKFELNIVIPKDLDADIKKRATVYFKSKTLKEIQFETSSRNFPVFVTYDNQSKDVLKLYDMPTTLGGIDKAIEMFMRKGHIGKTSQQKLLEERELRNFQTTLQNLIDNDAFCRNIVKIIQEE | Function: CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell ... |
P0DUE0 | MKTRIFIGSSSEGIDVAKRIKTFFAPEYDCFLWTDDIFRNNESFLETLVKSASLFDFGFMVFSADDKTTIRDQHFESPRDNVLFEYGLFLGRVGLDRAFVIAETDAKIPTDMLGITQTRYETIVNSKGIKVATDSLESSLQKLKKQIDENVQLGHLGLLPSTVIAISYFEGFVKLAAEWLVENTPELMINNHKFNKASLKIVMPESLDTDIKRSAMMYYKRHGLEEARIDTKHRNYPIHFASKTEDGILEVYDMPTILTGIDKAIDMYFRVGHIGKTNEQKLAEDHEMNNFKRVLQLLINEDAFCRECVEIIEPQP | Function: CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell ... |
A0A2T5Y4G4 | MKKRIFIGSSSEQLTILNEIVDLLGDDVECIPWTDAFALNKSGLDSLIKQTRLADYSILIATKDDLTKQRGESLTKPRDNVVFEFGLFLGAAGPEKCYLIAEEDTDLPTDLDGITVAKFTRNSGQYNSLDKIVESIRTHLVKIAEMSQLGLLPSTALAIGYYNSFIKRVCEEIHGSECVELEGKKIKVKSFRVDVVIPETLDDNGVGNFTTLYNKRYGLSKATTCTNPALLGTRGFPFHFKVDPPDANQESPVDIHLLDIPSTLSTIVESLKLYLPSNQVGQDFDMDYLEMRELENFAKVLKYLIGRNAATKGYVNVLTN... | Function: CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell ... |
P0DUD7 | MEKIYTWLKTNSYIVHHVSTSLNIISFIIVLIWIFESTIKEKLNIIFTVNLEAIVVFISILIVGLNQLLQKLLIEAEYSPAFALAVGYFKNFIFPAITQIKENGEVNPKICIYKPKHFDELTSTNIDMIKAELTNKKYNLSEINLSLKGARARDILTLNKKSKIHSYFDFPNTLLSLYSYVDFKIASSNNNSSELKKKKFVELLIEQFYLKLNELIQENNLTNNITFCDKNLQGL | Function: CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell ... |
A0A150XSR0 | MKYGLLQENGKVAEFIQIKTIMKNVIANVSTAITLALMILWIKYPNRIEWEAIIGILLVIKEVTIRWQIGKIESLEFSPAISLAHGYVNNFLEPAINELLMKASNNINFSIYIPHDLEELSDQQIDRMKLQIEANGYRLKEIKLKKKTGRPHDLLLVEKQEGTLSYFDFPRTLLSLQSYIDYKVDSTKNEFSEEKKIAMGAKLVDAFHNEVDRLIKKKNLEGIVTFVSKDLELY | Function: CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell ... |
P39850 | MESTIDLSELLGRVRKNMKLLIILPLLGLLISAIISFFFLDVKYQASTQILVNQKGNDSQIMAQEVQSNIQLVNTYSEIVKSPRILDKVSKELDDKYSRSEISSMLTVTNQAESQVLNIDVESKSGSNSEKIANKIAEVFSDEVPDIMNVDNVSVLSTADNTGKQVAPKPMVNLVVGLVIGLVIALLIIFIKEVFDKRIKTEEEVENELVIPVLGSIQKFD | Function: Required for the biosynthesis of type 1 capsular polysaccharide.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24496
Sequence Length: 221
Pathway: Capsule biogenesis; capsule polysaccharide biosynthesis.
Subcellular Location: Cell membrane
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P39851 | MAKKKSTISPLYVHDKPKSTISEKFRGIRSNIMFSNAENEIKSLLITSEKSASGKSILSANIAVTYAQAGYKTLIIDGDMRKPTQHYIFDLPNNSGLSNLIINKTTYSDSIKETRVENLNVLTAGPTPPNPSELIASSKFATIFNELLNHYDFIVIDTPPINTVTDAQVYARIVKNCVLVIDAEKNNKSEVKKAKGLLTKAGGKVLGAVLNKMPIDKNSSYYYYYGED | Function: Required for the biosynthesis of type 1 capsular polysaccharide.
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 25176
Sequence Length: 228
Pathway: Capsule biogenesis; capsule polysaccharide biosynthesis.
EC: 2.7.10.2
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P39852 | MVDIHNHILVDVDDGPKSINEAIELLKQAQSENVTDIVATPHHLHKRYSNDIEKVKIKLNELKNNSEIKKLGLNLYVGQEIRITDQIIEGIKNKEIEGINESRYLLIEFPSNEIPYYTNQLFYELQTMGYIPIIAHPERNKAIVQNLDLLFELINGGALSQITASSLLGDFGNNIRKLSLKMIDSNLAHFIASDAHSITNRPFMLKQLFNDRKLKAYYEELESYLKNGKLVLTNERISKQIPTQDYKQKKWFGLL | Function: Required for the biosynthesis of type 1 capsular polysaccharide.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 29377
Sequence Length: 255
Pathway: Capsule biogenesis; capsule polysaccharide biosynthesis.
EC: 3.1.3.48
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Q51693 | MNSFKWGKKIILFCLIVSLMGGIGVSCSFNKIKDSVKQKIDSMGDKGTYGVSASHPLAVEEGMKVLKNGGSAVDAAIVVSYVLGVVELHASGIGGGGGMLIISKDKETFIDYRETTPYFTGNQKPHIGVPGFVAGMEYIHDNYGSLPMGELLQPAINYAEKGFKVDDSLTMRLDLAKPRIYSDKLSIFYPNGEPIETGETLIQTDLARTLKKIQKEGAKGFYEGGVARAISKTAKISLEDIKGYKVEVRKPVKGNYMGYDVYTAPPPFSGVTLLQMLKLAEKKEVYKDVDHTATYMSKMEEISRIAYQDRKKNLGDPNYV... | Function: Transpeptidase that cleaves the poly-gamma-D-glutamate capsule and catalyzes the formation of an amide bond with the side-chain amino group of meso-diaminopimelic acid (m-DAP) in the peptidoglycan scaffold . Degradation of the high-molecular weight capsule (H-capsule) to the lower-molecular weight capsule (L-... |
Q70LC6 | MAKLNRKLRQDSTDRYKTKLYLWRNLGGLIPEDMAISVTESITADWKQYNDMMSKVRNETLDILKTNKVATEDYIGYIAFAEELAHQVWKNKNSSPDPNTANEASKTDLESKYSDVYGLDVTVLDAIYNAVIPIIMGGGS | Function: Self-assembles to form a helical, filamentous nucleocapsid mesuring 900 nm in length and 24 nm in width (Probable) . Together with capsid protein 2, wraps arounds the DNA and maintains it in an A-form (Probable). Capsid proteins probably maintain the DNA in A-form by non-specific desolvation and specific coor... |
Q914J4 | MAGRQSHKKIDVRNDTSTRYKGKLYGIFVNYMGEKYAQQLVENMYSNYNDVFVEIYNKMHNALRPTLVKLAGAGATFPLWQLVNEAIYAVYLTHKETASFLVTKYVARGVPAMTVKTLLAEVGNQLKELVPAVAEQIGSVTLDHTNVVSTVDNIVTSMPALPNSYAGVLMKTKVPTVTPHYAGTGTFSSMESAYKALEDIERGL | Function: Self-assembles to form a helical, filamentous nucleocapsid mesuring 1980 nm in length and 24 nm in width. Together with capsid protein 2, wraps arounds the DNA and maintains it in an A-form. Capsid proteins probably maintain the DNA in A-form by non-specific desolvation and specific coordination of the DNA ph... |
A0A346LU62 | MPSRRTGITTEDAITKYSVKAKTEQTAYKNATKDMVVQAQNIMNFYSVVNQALIPWLNAHGVGGNLRILYRQLANEYVKVLNTKQSGEVIKRLKIALRHKYWLRGLDEAMLDEFMDYIDSLKSTTTNYIIFNMQSSK | Function: Self-assembles to form a helical, filamentous nucleocapsid (Probable) . Together with capsid protein 2, wraps arounds the DNA and maintains it in an A-form (Probable) . Capsid proteins probably maintain the DNA in A-form by non-specific desolvation and specific coordination of the DNA phosphate groups by posi... |
Q70LC7 | MVNKKYRQDSKDRYQYKQYIYRSIGGIVPPEMAETVTANQTAQWEAGFTPYHKLRLAIKEICKTDGIPNIKWGMYIAFGEKLLKSYLKMKAGSASSDMIAEYINNAISAFSSRTGISQETAQKIADFITSNY | Function: Self-assembles to form a helical, filamentous nucleocapsid mesuring 900 nm in length and 24 nm in width (Probable). Together with capsid protein 1, wraps arounds the DNA and maintains it in an A-form (Probable). Capsid proteins probably maintain the DNA in A-form by non-specific desolvation and specific coor... |
Q914J5 | MARRNRRLSSASVYRYYLKRISMNIGTTGHVNGLSIAGNPEIMRAIARLSEQETYNWVTDYAPSHLAKEVVKQISGKYNIPGAYQGLLMAFAEKVLANYILDYKGEPLVEIHHNFLWELMQRQSGAGLGVTSGFIYTFVRKDGKPVTVDMSKVLTEIEDALFKLVKK | Function: Self-assembles to form a helical, filamentous nucleocapsid mesuring 1980 nm in length and 24 nm in width. Together with capsid protein 1, wraps arounds the DNA and maintains it in an A-form. Capsid proteins probably maintain the DNA in A-form by non-specific desolvation and specific coordination of the DNA ph... |
P0C6H6 | MDIDPYKEFGASVELLSFLPSDFFPSIRDLLDTASALYREALESPEHCSPHHTALRQAILCWGELMNLATWVGSNLEDPASRELVVSYVNVNMGLKIRQLLWFHISCLTFGRETVLEYLVSFGVWIRTPPAYRPPNAPILSTLPETTVVRRRGRSPRRRTPSPRRRRSESPRRRRSQSRESQC | Function: Self assembles to form an icosahedral capsid. Most capsids appear to be large particles with an icosahedral symmetry of T=4 and consist of 240 copies of capsid protein, though a fraction forms smaller T=3 particles consisting of 180 capsid proteins. Entering capsids are transported along microtubules to the n... |
P36285 | MATTHTLLSFDDLEFLLHRKDLTDLYGERCGTLNLVINPYELFLPDELDDDCCDDPFNCCFPDVYASIGTEYSYIDPPELIHEEHCATNGTWPNGDPCEPILPPFTITGTHHYYATKPGEVVSGILSKLGSSWDPSLRSTADVSNSFTFRAESDGPGSAEIVTEEQGTVVQQQPAPAPTALATLATASTGKSVEQEWMTFFSYHTSINWSTVESQGKILYSQALNPSINPYLDHIAKLYSTWSGGIDVRFTVSGSGVFGGKLAALLVPPGVEPIESVSMLQYPHVLFDARQTEPVIFTIPDIRKTLFHSMDETDTTKLVI... | Function: Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2... |
Q76TT7 | MIKLVLLVAAIAIFGTGFITVIINQFTSAKNIIMDLYNSDTWLIWLFGRMAVLFSHPLMLTISSLYIVGFIVSKTLYS | Function: May self assemble to form a helical capsid wrapping up the viral genomic DNA. The virion assembly and budding take place at the host inner membrane (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8761
Sequence Length: 78
Subcellular Location: Virion
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P25993 | MKRRLVLENGAVFEGEAFGSLEHNMGEVVFNTGMTGYQEILSDPSYCGQIVTLTYPLIGNYGINRDDFESITPFVKGLIIKELCELPSNWRSAYTLDEYLKMKNIPGLQGIDTRKLTRMIRTAGALKGTFASSDEDIEAVLKRLNETELPRNQVSQVSAKTAYPSPGRGKRIVLVDFGMKHGILRELNKRKCDVIVVPYNITAEEVLQLKPDGIMLSNGPGDPKDVPEAIEMIKGVLGKVPLFGICLGHQLFALACGANTEKMKFGHRGSNHPVKELATGKVALTSQNHGYTVSSISKTELEVTHIAINDDTIEGLKHKT... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 40119
Sequence Length: 364
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
EC: 6.3.5.5
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A1UTE8 | MTKTTLSSDPWSIKKPTALLVLADGTVIEGEGIGAIGIVEAEVCFNTAITGYEEILTDPSYTGQIINFTFPHIGNVGTNSEDIEDLTPLHHYGAVGAIFKAHSSPSNYRANENLNQWLKKHQIIALCGIDTRALTALIREKGAQNAVIAHDPNGNFDINALKERAQKWSGLLNLDLAKEVTSKQSIEWNEKPWIWNKGYTINNEYNFHIVAIDYGIKRNILRLMAAQGARITVVPAHTSVQEILAMKPDGIFLSNGPGDPNATAEYAVPMIKTFIECNIPLFGICLGHQLLALAVGAKTIKMHQGHHGANHPVKNLITEK... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 43998
Sequence Length: 399
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
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Q8G816 | MSQNESGTIAIPMYDKDDAVLVLEDGQVYVGKPYGALGETTGEIVFATGMTGYQETLTDPSYDRQIVVQTFPHIGDTGVNSEDPESSRIWVAGYIVRDPSPNVSNWRAEGSLDDDLAKNGIVGLSHIDTRKLVRHLRSAGVMRAGIFSGDALTDQATGALKTIEQLLEDVKNTPQMQGLSLYDEVSTKETYTIEPCGEYEGKEPLYTVAAVDLGIKGMTPHRMAERGCRVHVVPSTITFAEIENLNPDGVFFSNGPGDPEQAGPEIELLRQVLDAGYPFFGICFGNQLLGRALGFGTYKLKFGHRGINQPVKDLTTGKVE... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 44265
Sequence Length: 407
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
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Q89DR8 | MTQHDNDPAWPDHKPTALLVLADGTVLEGFGLGAEGHAVGEVCFNTAMTGYEEILTDPSYAGQLITFTFPHIGNVGTNEEDIETVNMAATPGARGVILRTAITDPSNYRATKHLDAWLKARGIIGLSGIDTRALTALIRSKGMPNAVIAHARNGEFDLHGLKEEAREWPGLEGMDLVPMVTSGQRFTWDETPWLWDKGFGQQDKTEFNVVAIDYGIKRNILRLLAGVGCKVTVVPATTSAEDILAMKPDGVFLSNGPGDPAATGKYAVPVIRDVIKSGTPTFGICLGHQMLGLAVGAKTKKMHQGHHGANHPVKDETTGK... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 42714
Sequence Length: 396
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
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Q7U7F9 | MPHPSSRQAHLVLADGTVLTGDAFGHRGSVVGEVVFNTGMTGYQEVLTDPSYAGQLVTFTYPELGNTGVNGDDQEADHPHARGVIARQLAPCASNWRCSESLDNWMERHGLVGICGVDTRALVRRLRDGGAINGVISSDGRSPADLLAEVRHAPSMEGLNLASQVSTTEPYEWSSPCRVGFDQRLKQHPDLPYRVVAIDFGIKRAILDRLVAHGCAVTVLPSDADLDTVMSHQPEGVFLSNGPGDPAAVDSGIDLARSLLERANLPLFGICLGHQILGLALGGKTFKLGYGHRGLNHPCGTSGQVEITSQNHGFAISADS... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 41105
Sequence Length: 383
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
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Q9XB61 | MSNSFCVVYKGSDTDINNIQRDFDGKGEALSNGYLFIEQNGHYQKCEMERGTAYLIGSLYNRTFLIGLAGVWEGEAYLANDAELLALLFTRLGANALALAEGDFCFFIDEPNGELTVITESRGFSPVHVVQGKKAWMTNSLKLVTAAEGEGALWFEEEALVCQSLMRADTYTPVKNAQRLKPGAVHVLTHDSEGYSFVESRTLTTPASNQLLALPREPLLALIDRYLNAPLEDLAPRFDTVGIPLSGGLDSSLVTALASRHFKKLNTYSIGTELSNEFEFSQQVADALGTHHQMKILSETEVINGIIESIYYNEIFDGLS... | Function: Involved in the biosynthesis of carbapenam-3-carboxylate, a beta-lactam antibiotic of the carbapenem class. Catalyzes the ATP-dependent formation of (3S,5S)-carbapenam-3-carboxylate from (2S,5S)-5-carboxymethylproline.
Catalytic Activity: (2S,5S)-5-carboxymethylproline + ATP = (3S,5S)-carbapenam-3-caboxylate ... |
P51201 | MIKKIPAILVLEDGTYYKGWSFQADQSIVTIGEVVFNTGMTGYQEIITDPSYFQQIVTFTYPEIGNTGINSEDIESQTISIKGLVAKNICKISSSWRQQESLVQYLNRYKIPFIFGIDTRSLTQYLRRSGTMNGCISNKNLNHAYLQRKISEVPHMTGLDLIPNVTTNIMYDWDEKSLPSWYLADRNREKIYSQLKVIVIDFGVKLNILRRLATLGCQITVMPASTPTQDILSCKPDGILLSNGPGDPSAVNYGIKTVKELLNQNIPIFGICMGHQILNLALEAKTFKLKFGHRGINHPSGLKQQVEITSQNHGFAVDLQ... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 43296
Sequence Length: 384
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
Subcellular Location: Plastid
EC: 6... |
B4S5S1 | MQQTPAKLVLENGSVYTGYAFGHIGETGGEVVFNTALTGYQEIVTDPSYAGQMVVMTYPLIGNYGVNQSDAESQKIWASALIVREMSNIHSNFAATGSLDQYLKEAKVMGLAGIDTRKLVREIRQKGAMRGVISAIDPDEKRLEEKALKIPEMTGLDLVKKVSTSQTYTIDCDDAEYHVVAYDYGIKQNILRMLQNAKCKVTVLNANTPIEEALKLDPDGIFLSNGPGDPFAVTYAIDNIKKLAEHNTQQKPVPLFGICLGHQLMSLAFGAKTYKLKFGHHGSNHPVKNLKSSSIEITSQNHGFAVAMESLPESLEMTHL... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 40956
Sequence Length: 371
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
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P38098 | MTKPAILALADGSIFRGEAIGADGQTVGEVVFNTAMTGYQEILTDPSYAQQIVTLTYPHIGNTGTTPEDAEANRVWAAGLIIRDLPLIASNWRSKQSLPDYLKANGTVAIAGIDTRRLTRILREKGSQNGCILAGADATEERALELARAFPGLKGMDLAKEVTTAERYEWRSSVWNLESDSHPEIPAGELPYHVVAYDYGVKLNILRMLVARGCRLTVVPAQTPASEVLALNPDGIFLSNGPGDPEPCDYAIQAIREFLDTEIPVFGICLGHQLLALASGAKTLKMGHGHHGANHPVQDLDSGVVMITSQNHGFAVDEST... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 40828
Sequence Length: 378
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
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Q8ZY49 | MEDGSVFAGRLIGAEKIAVGEVVFTTSVVGYPQTLTDPSYKGQIITFTMPLIGNYGVSEDQLESDGIKAEGVVLFEATFPSHYKSVMSLEEWLASSGVPGVARVDTRALVQMLREHGVMMGAIGPEDPAVLMEALRKSPHYEDVVYVDMVSVKEPVLLGEGRLCIGVVDCGVKRSIVREFLKRGVRVKLVPCRRTELAFDCDALFISNGPGNPKLLDFLSAKVSEYVEYKKPLMGICLGHQVIAMALGAGIYKLKFGHRASNKPVRDIRFTGRTYITTHNHGYAVDPRGTDLKVWAVQPDDGTVEGLYHERLPILTTQWH... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 38228
Sequence Length: 346
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
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Q8U086 | MGVHKKGYLVLEDGSVIEGKAFGAETIRYGEVVFTTAMVGYPESLTDPSYKGQILIATNPLMGTYGVSSKSLKEHGLPLHYESDSIKVEGFVISFLMRPNHWSSEMTLDEWLRREGVPGLYGVDTRALVKKIREEGVMRGAIVTTETDLEEILENIRKISYESTNFVELVSPKNPIVHTPKNVKFRVVVLDLGVKFGILRELLKRGIEVVRIPWNWDILEAYYSYNADGIFISNGPGNPTLLKEVAKRIRKAFNEEIPMMGICLGQQLLALADGAEIYKLKYGHRGINKPVKDLESGKAFVTTQNHGYAIVPESLNEFKV... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 41714
Sequence Length: 371
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
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Q8XZ85 | MLPSFPPAILALADGTVFRGYSIGAAGHTIGEVVFNTAITGYQEILTDPSYSRQIVTLTYPHIGNVGVNREDVEATKVHAAGLIIKDLPILASNFRQEHSLSHYLKGEKVVAIAGIDTRKLTRILREKGAQNGCVLAGEDNPQKAIDLARSFPGLSGMDLAKVVSVTQPYEWNQTEWALGRGYGVQDKPQFHVVAYDFGVKYNILRMLAERGCRVTVVPAQTSAADALAYNPDGVFLSNGPGDPQPCDYAIAATKDFIERRIPTFGICLGHQIMGLAVGGKTLKMKTGHHGANHPVKDLQDGRVIITSQNHGFAVDPESL... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 40946
Sequence Length: 378
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
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P13258 | KLGVPQPEGGYATSQKEAIEVAKRIGFPVLVRPSYVLGGRAMEIVYDEMDLERYMKEAVRVSHEHPILIDDFLEAASEIDVDAVCDQKDVIIGAIMEHIEEAGVHSGDSACVIPPQSLSPEVLDQVRDYTRKIALALRVKGLINIQMAEKGGKVYVLEANPRSSRTIPFVSKAVGIPLAKIAAKVIVGHSLKSLGYMDEPKPKHVSIKEVLLPFDKLPGADPVLGPEMKSTGEVMGIDYDFGRAYYKAELAADNVLPLTGKVFLSIRNADKTELVDVAKKLQAAGLELMGTEGTVNYLAQHGVFMDVVKKVHDGSPNVID... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 43692
Sequence Length: 398
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from... |
Q9FK63 | MFLKLFLLLSLVSFSHSDSSSTVSCPNGTDFHQLTTVFRYVSGFNSSWFSSNCSAVITHVVLPSRKLNGTVSWNPIRNLTRLRVLDLSNNSLDGSLPTWLWSMPGLVSVNLSRNRFGGSIRVIPVNGSVLSAVKELNLSFNRFKHAVNFTGFTNLTTLDLSHNSLGVLPLGLGSLSGLRHLDISRCKINGSVKPISGLKSLDYLDLSENSMNGSFPVDFPNLNHLQFLNLSANRFSGSVGFDKYRKFGKSAFLHGGDFVFNDSKIPYHHRIHRLPHRHPPPVRQRNVKTHRTNHTPLVIGLSSSLGALIIVIFAAAIILI... | Cofactor: Uses manganese ion preferentially to magnesium ion.
Function: Can phosphorylate the myelin basic protein in vitro . Required for endosperm development in embryos . Maybe involved in auxin and osmotic stress responses .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
PTM:... |
Q174R2 | MFENQQQLLRLHGCKLFIIGENDNLVNKYGHSVAIACCYDPQGMSVRVFREGSQQQLEEYPVSVKTTHLNHGITSHILIVGGEMIYVKFASEEDCQSFRMLLQNMSGKVNSVFNLRTEDSSASQYFQFYGYLSQQQNMMQDFVRTSTYQRAIYSNSQDFHNKIVLDVGAGSGILSFFAVQAGAAKVYAVEASNMAQYAQQLVLSNNLDGKIIVIAGKIEEIELPEMVDIIISEPMGYMLYNERMLETYLHGKKWLRPEGKMFPSRGDLHVAPFTDEALYMEQYNKANFWMQTEFHGVNLVALRDAAMKEYFRQPIVDTFD... | Function: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins. May methylate histone H3 at 'Arg-17' and activate transcription via chromatin remodeling.
PTM: The dimethylated protein is the major form.
Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionin... |
Q7Q2B7 | MARMQGCSVLVLDDSDKLVNKYDHKVTVVCSYDPQGMAVRLLQEGATPPKQLEEYLVSGAGTTHLSRGHTSHMLVVGGELVLFRFASRGDCQQFRSLLHKLSGKVNSVFNLRTEDSSASQYFQFYGYLSQQQNMMQDFVRTSTYQRAIYNNAQDFQNKIVLDVGAGSGILSFFAVQAGAAKVYAVEASNMAQYAQQLVSSNNLTDRIIVIAGKIEEIDLPERVDVIISEPMGYMLYNERMLETYLHGKKWLKPDGKMYPSRGDLHVAPFTDEALYMEQYNKANFWMQTEFHGVNLVALRDAAMKEYFRQPIVDTFDIRIC... | Function: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins. May methylate histone H3 at 'Arg-17' and activate transcription via chromatin remodeling.
PTM: The dimethylated protein is the major form.
Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionin... |
Q6DC04 | MAVSVFSGVRLLSIGDANGDIQRHSEQQPLRLEIKMNQDAAQIILSNNEETCVFKCTVLRETECSRVGKQSFIITLGCNSVLLQFASPADFSSFYNLLKICRGQKGDRSVFSDRTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMAQHAEVLVNSNRLSERVVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKFLKPSGKMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPIVDTFDIR... | Function: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p... |
Q9VH48 | MSSLRPEEARKLATAASVSPLSNCQFCGVVISSIADEQKLEFTNKYKGSCTLLCSYDSQGVVLRVVSDDDRSHVLKEYMIAADTDAAQMGRRSYAVSLDADNLVLRFASEQDQQLFRKVVENVKHLRPKSVFSQRTEESSASQYFQFYGYLSQQQNMMQDYVRTSTYQRAILGNAVDFQDKIVLDVGAGSGILSFFAVQAGAAKVYAIEASNMAQYAQQLVESNNVQHKISVIPGKIEEIELPEKVDVIISEPMGYMLYNERMLETYLHARKWLKPQGKMYPTHGDLHIAPFSDESLYSEQYNKANFWYQSAFHGVDLTT... | Function: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins. May methylate histone H3 at 'Arg-17' and activate transcription via chromatin remodeling. Coordinates ecdysone-mediated expression of cell death genes.
PTM: The dimethylated protein is the major form.
Cata... |
P0CM57 | MPNSSKPRSQASAAKLNPLWYTYACATLVAAVVLGNILRWAFLELPDSYHCSALLNTGKWLDPGTWTNWQPEGCFQLPLSAQSWQKCLASPTVNTHQALHSSYYDKRTALFVGDSTVRQLYFAAARKVGKTSKAWELEGEKHTDRSLLVSDPLGGPSLELEFWWDPYLNSSKTIGLLSGQSSVPSSLLVMGSGLWYLRNPSSGGLASWGAMIYDTFELVKKNQGSPQTALINPWDNMLLGPGITLPGLLPNQPPKFVDHSREVEARSLFSRASSISHRPTDFSISDAIVFLPISTPVREKLSPSRAETIFHTDVEAMNAD... | Function: Probable O-acetyltransferase required for the O-acetylation of the capsular glucoronoxylmannans (GXM) involved in virulence.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 107504
Sequence Length: 960
Subcellular Location: Membrane
EC: 2.3.1.-
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Q6BE25 | MWQLKIGADTVPSDPSNAGGWLSTLNNHVGRQVWHFHPELGSPEDLQQIQQARQHFSDHRFEKKHSADLLMRMQFAKENSSFVNLPQVKVKDKEDVTEEAVTRTLRRAINFYSTIQADDGHWPGDYGGPMFLIPGLVITLSITGALNAVLSTEHQREICRYLYNHQNKDGGWGLHIEGPSTMFGSVLNYVTLRLLGEEAEDGQGAVDKARKWILDHGGAAAITSWGKMWLSVLGVYEWAGNNPLPPELWLLPYLLPCHPGRMWCHCRMVYLPMCYLYGKRFVGPITPIIRSLRKELYLVPYHEVDWNKARNQCAKEDLYY... | Function: Oxidosqualene cyclase involved in the biosynthesis of cycloartenol.
Catalytic Activity: (S)-2,3-epoxysqualene = cycloartenol
Sequence Mass (Da): 87364
Sequence Length: 766
EC: 5.4.99.8
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Q55D85 | MTTTNWSLKVDRGRQTWEYSQEKKEATDVDIHLLRLKEPGTHCPEGCDLNRAKTPQQAIKKAFQYFSKVQTEDGHWAGDYGGPMFLLPGLVITCYVTGYQLPESTQREIIRYLFNRQNPVDGGWGLHIEAHSDIFGTTLQYVSLRLLGVPADHPSVVKARTFLLQNGGATGIPSWGKFWLATLNAYDWNGLNPIPIEFWLLPYNLPIAPGRWWCHCRMVYLPMSYIYAKKTTGPLTDLVKDLRREIYCQEYEKINWSEQRNNISKLDMYYEHTSLLNVINGSLNAYEKVHSKWLRDKAIDYTFDHIRYEDEQTKYIDIGP... | Function: Converts oxidosqualene to cycloartenol (in vitro).
Catalytic Activity: (S)-2,3-epoxysqualene = cycloartenol
Sequence Mass (Da): 80763
Sequence Length: 703
EC: 5.4.99.8
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Q46896 | MTWLPLNPIPLKDRVSMIFLQYGQIDVIDGAFVLIDKTGIRTHIPVGSVACIMLEPGTRVSHAAVRLAAQVGTLLVWVGEAGVRVYASGQPGGARSDKLLYQAKLALDEDLRLKVVRKMFELRFGEPAPARRSVEQLRGIEGSRVRATYALLAKQYGVTWNGRRYDPKDWEKGDTINQCISAATSCLYGVTEAAILAAGYAPAIGFVHTGKPLSFVYDIADIIKFDTVVPKAFEIARRNPGEPDREVRLACRDIFRSSKTLAKLIPLIEDVLAAGEIQPPAPPEDAQPVAIPLPVSLGDAGHRSS | Cofactor: Protospacer integration in vitro also occurs with Mn(2+) and also requires low concentrations of KCl . The transesterification function works equally well with Mg(2+), Mn(2+) or Co(2+) in vitro .
Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that pro... |
P07498 | MKSFLLVVNALALTLPFLAVEVQNQKQPACHENDERPFYQKTAPYVPMYYVPNSYPYYGTNLYQRRPAIAINNPYVPRTYYANPAVVRPHAQIPQRQYLPNSHPPTVVRRPNLHPSFIAIPPKKIQDKIIIPTINTIATVEPTPAPATEPTVDSVVTPEAFSESIITSTPETTTVAVTPPTA | Function: Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk.
PTM: The N-terminus is blocked.
Sequence Mass (Da): 20305
Sequence Length: 182
Subcellular Location: Secreted
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Q9ZQI2 | MDIEKAGSRREEEEPIVQRPKLDKGKGKAHVFAPPMNYNRIMDKHKQEKMSPAGWKRGVAIFDFVLRLIAAITAMAAAAKMATTEETLPFFTQFLQFQADYTDLPTMSSFVIVNSIVGGYLTLSLPFSIVCILRPLAVPPRLFLILCDTVMMGLTLMAASASAAIVYLAHNGNSSSNWLPVCQQFGDFCQGTSGAVVASFIAATLLMFLVILSAFALKRTT | Function: Regulates membrane-cell wall junctions and localized cell wall deposition. Required for establishment of the Casparian strip membrane domain (CSD) and the subsequent formation of Casparian strips, a cell wall modification of the root endodermis that determines an apoplastic barrier between the intraorganismal... |
Q08DY9 | MENTENSVDSKSIKTSETKILHGSKSMDSGISLEESYKMDYPEMGLCIIINNKNFHENTGMACRSGTDVDAANLRETFMNLKYEVRIKNDLTCKEMLELMSNVSKEDHSKRSSFICVLLSHGEEGIIFGTNGPVNLKKLASFFRGDYCRSLTGKPKLFIIQACRGTELDCGIETDSGAEDDMACQKIPVEADFLYAYSTAPGYFSWRNAKNGSWFIQALCEMLKKHAHRLELMHILTRVNRKVAIEYESFSTDSAFHAKKQIPCIMSMLTKELYF | Function: Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-heli... |
P0DI36 | MEGSGEHGETSKGPLSKGVSRGLCILDLIFRVIAVIGTLASAIAMGTTNQTMPFFTQFVQFKERYSDLPTLTFFVVANSIASAYLIISLPLSIVHIIRSRAKYSRLILIFFDVAMLALVTAAASAGAAIVYLAHNGNVSANWFAICQQFDSFCERISGSLIGSFAAMVVLILLILLSAVALARR | Function: Regulates membrane-cell wall junctions and localized cell wall deposition. Required for establishment of the Casparian strip membrane domain (CSD) and the subsequent formation of Casparian strips, a cell wall modification of the root endodermis that determines an apoplastic barrier between the intraorganismal... |
P42574 | MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIIINNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDDDMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVNRKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYH | Function: Thiol protease that acts as a major effector caspase involved in the execution phase of apoptosis . Following cleavage and activation by initiator caspases (CASP8, CASP9 and/or CASP10), mediates execution of apoptosis by catalyzing cleavage of many proteins . At the onset of apoptosis, it proteolytically clea... |
Q42547 | MDPYKYRPSSAYNAPFYTTNGGAPVSNNISSLTIGERGPVLLEDYHLIEKVANFTRERIPERVVHARGISAKGFFEVTHDISNLTCADFLRAPGVQTPVIVRFSTVVHERASPETMRDIRGFAVKFYTREGNFDLVGNNTPVFFIRDGIQFPDVVHALKPNPKTNIQEYWRILDYMSHLPESLLTWCWMFDDVGIPQDYRHMEGFGVHTYTLIAKSGKVLFVKFHWKPTCGIKNLTDEEAKVVGGANHSHATKDLHDAIASGNYPEWKLFIQTMDPADEDKFDFDPLDVTKIWPEDILPLQPVGRLVLNRTIDNFFNETE... | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 56695
Sequence Length: 492
Subcellular Location: Peroxisome
EC: 1.11.1.6
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P18123 | MTMDPTKFRPSSSHDTTVTTTNAGAPVWNDNEALTVGPRGPILLEDYHLIEKVAHFARERIPERVVHARGASAKGFFECTHDVTSLTCADFLRAPGVRTPVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLGNNFPVFFIRDGIKFPDVIHAFKPNPRSHVQEYWRVFDFLSHLPESLHTFFFLFDDVGVPSDYRHMEGFGVNTYTFVSAAGKAQYVKFHWKPTCGVRCILTDEEAALVGGRNHSHATQDLYDSIAAGSFPEWTLYVQVMDPDTEEQYDFDPLDDTKTWPEDLLPLRPVGRLVLDRNVDNFFN... | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Its levels are highest in the light period and are lowest in the dark period, hence it may be important for scavenging hydrogen peroxide at night, rather than during the day.
Catalytic... |
Q86UT8 | MAPAQRCPLCRQTFFCGRGHVYSRKHQRQLKEALERLLPQVEAARKAIRAAQVERYVPEHERCCWCLCCGCEVREHLSHGNLTVLYGGLLEHLASPEHKKATNKFWWENKAEVQMKEKFLVTPQDYARFKKSMVKGLDSYEEKEDKVIKEMAAQIREVEQSRQEVVRSVLEPQAVPDPEEGSSAPRSWKGMNSQVASSLQQPSNLDLPPAPELDWMETGPSLTFIGHQDIPGVGNIHSGATPPWMIQDEEYIAGNQEIGPSYEEFLKEKEKQKLKKLPPDRVGANFDHSSRTSAGWLPSFGRVWNNGRRWQSRHQFKTEA... | Function: Component of the minor spliceosome that promotes splicing of a specific, rare minor intron subtype . Negative regulator of centrosome duplication . Constrains centriole number by modulating the degradation of the centrosome-duplication-associated protein SASS6 in an acetylation-dependent manner. SIRT1 deacety... |
P07773 | MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV | Cofactor: Binds 1 Fe(3+) ion per subunit.
Catalytic Activity: catechol + O2 = cis,cis-muconate + 2 H(+)
Sequence Mass (Da): 34347
Sequence Length: 311
Domain: Contains an helical zipper domain, consisting of five N-terminal helices from each subunit, which forms the molecular dimer axis.
Pathway: Aromatic compound meta... |
P83715 | MNXQQIDMLVKQLN | Cofactor: Binds 1 Fe(3+) ion per subunit.
Catalytic Activity: catechol + O2 = cis,cis-muconate + 2 H(+)
Sequence Mass (Da): 1686
Sequence Length: 14
Pathway: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-4,5-dihydro-2-furylacetate from catechol: step 1/3.
EC: 1.13.11.1
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P90682 | MPQTKGKPHEEQLEQYKNSQTKPFVLTTSNGAPIFNKKASLTVGPRGPLLLQDVVFLDEMAHFDRERIPERVVHAKGGGAHGFFEVTDDITKYCKADVFSTIGKRTPIFIRFSTVGGELGSADTQRDPRGFAIKFYTEEGNWDLVGNNTPIFFIRDPIFFPNFIHTQKRNPVTHLKDPNMMWDFFSLRPETTHQVMILFGDRGIPDGFRHMDGFGSHTFKLVNKDGNAVYCKFHIKTAQGIRNLPPDVAIKLAGEDPDYSIRDLYDSIENGNYPVWRLMIQVMTFEEAANYRFNPFDITKVWSHKEFPLILVGKIVLNKN... | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 61962
Sequence Length: 541
Subcellular Location: Peroxisome
EC: 1.11.1.6
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P53634 | MGAGPSLLLAALLLLLSGDGAVRCDTPANCTYLDLLGTWVFQVGSSGSQRDVNCSVMGPQEKKVVVYLQKLDTAYDDLGNSGHFTIIYNQGFEIVLNDYKWFAFFKYKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKKVGTASENVYVNIAHLKNSQEKYSNRLYKYDHNFVKAINAIQKSWTATTYMEYETLTLGDMIRRSGGHSRKIPRPKPAPLTAEIQQKILHLPTSWDWRNVHGINFVSPVRNQASCGSCYSFASMGMLEARIRILTNNSQTPILSPQEVVSCSQYAQGCEGGFPYLIAGKYAQDFGLVEEA... | Cofactor: Binds 1 Cl(-) ion per heavy chain.
Function: Thiol protease . Has dipeptidylpeptidase activity . Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids . Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate . Can act... |
P00948 | MLFHVKMTVKLPVDMDPAKATQLKADEKELAQRLQREGTWRHLWRIAGHYANYSVFDVSSVEACNDTLMQLPLFPYMDIEVDGLCRHPSSIHSDDR | Catalytic Activity: (S)-muconolactone = (4,5-dihydro-5-oxofuran-2-yl)-acetate
Sequence Mass (Da): 11116
Sequence Length: 96
Pathway: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-4,5-dihydro-2-furylacetate from catechol: step 3/3.
EC: 5.3.3.4
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P80067 | MGPWTHSLRAALLLVLLGVCTVSSDTPANCTYPDLLGTWVFQVGPRHPRSHINCSVMEPTEEKVVIHLKKLDTAYDEVGNSGYFTLIYNQGFEIVLNDYKWFAFFKYEVKGSRAISYCHETMTGWVHDVLGRNWACFVGKKMANHSEKVYVNVAHLGGLQEKYSERLYSHNHNFVKAINSVQKSWTATTYEEYEKLSIRDLIRRSGHSGRILRPKPAPITDEIQQQILSLPESWDWRNVRGINFVSPVRNQESCGSCYSFASLGMLEARIRILTNNSQTPILSPQEVVSCSPYAQGCDGGFPYLIAGKYAQDFGVVEENC... | Cofactor: Binds 1 Cl(-) ion per heavy chain.
Function: Thiol protease . Has dipeptidylpeptidase activity . Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate . Can act ... |
P95609 | MALFHVRMDVAIPRDLDPKVRDETIAKEKAYSQELQRSGKWPEIWRIVGQYSNISIFDVESADELHEILWNLPLFPYMNIEIMPLTKHGSDVK | Catalytic Activity: (S)-muconolactone = (4,5-dihydro-5-oxofuran-2-yl)-acetate
Sequence Mass (Da): 10912
Sequence Length: 93
Pathway: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-4,5-dihydro-2-furylacetate from catechol: step 3/3.
EC: 5.3.3.4
|
Q26563 | MHWVFHCILIILACLRFTCADTPANCTYEDAHGRWKFHIGDYQSKCPEKLNSKQSVVISLLYPDIAIDEFGNRGHWTLIYNQGFEVTINHRKWLVIFAYKSNGEFNCHKSMPMWTHDTLIDSGSVCSGKIGVHDKFHINKLFGSKSFGRTLYHINPSFVGKINAHQKSWRGEIYPELSKYTIDELRNRAGGVKSMVTRPSVLNRKTPSKELISLTGNLPLEFDWTSPPDGSRSPVTPIRNQGICGSCYASPSAAALEARIRLVSNFSEQPILSPQTVVDCSPYSEGCNGGFPFLIAGKYGEDFGLPQKIVIPYTGEDTGK... | Cofactor: Binds 1 Cl(-) ion per heavy chain.
Function: Thiol protease. Has a role as a digestive enzyme.
Sequence Mass (Da): 51281
Sequence Length: 454
Subcellular Location: Lysosome
EC: 3.4.22.-
|
P54720 | MNKSFEIGTLLLRVITGIIFFVHGLSKFQGMEGTIQFFGSIGLPSFMAYVIAAIELIGGVLVFFGLATRIVGVLFALTLIGAIITVKLKAPFMGNAEFDYLLLLTSIHLALTGSRFLALDPFVFKGKKNGNVSA | Function: Essential for growth and viability in the presence of catechol and probably involved in the detoxification of catechol.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14419
Sequence Length: 134
Subcellular Location: Cell membrane
EC: 1.-.-.-
|
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