entry stringlengths 6 10 | entry_name stringlengths 5 11 | protein_name stringlengths 3 2.44k | sequence stringlengths 2 35.2k | function stringlengths 7 11k |
|---|---|---|---|---|
C0HLL2 | PA2_PITAZ | Phospholipase A2 (EC 3.1.1.4) (Pa-PLA2) (Phosphatidylcholine 2-acylhydrolase) | MAFLVFAFLTLMAVETYGSLFQFRLMINYLTGKLPILSHSFYGCYCGAGGSGWPKDAIDWCCQVHDCCYGRMSASGCDPYFQPYNFSYINKNLQCVETDTSGCPRRICECDRLASICFQQHDATYNSSNIDPKRKGCGTKSPPCPN | PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. |
C0HLR3 | SCX1_CENBA | Beta-toxin Cb1 | KEGYIVNHSTGCKYECYKLGDNDYCLRECKAQYGKGAGGYCYAFGCWCTHLYEQAVVWPLPKKTCN | Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and reduces peak current and shifts the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. Has an inhibitory effect on voltage-gated sodium channel hN... |
C0HLV2 | NEPRN_NEPVE | Protein neprosin (Npr1) (EC 3.4.21.26) (Prolyl endopeptidase) | MQAKFFTFVILSSVFYFNYPLAEARSIQARLANKPKGTIKTIKGDDGEVVDCVDIYKQPAFDHPLLKNHTLQMQPSSYASKVGEYNKLEQPWHKNGECPKGSIPIRRQVITGLPVVKKQFPNLKFAPPSANTNHQYAVIAYFYGNASLQGANATINIWEPNLKNPNGDFSLTQIWISAGSGSSLNTIEAGWQVYPGRTGDSQPRFFIYWTADGYTSTGCYDLTCPGFVQTNNYYAIGMALQPSVYGGQQYELNESIQRDPATGNWWLYLWGTVVGYWPASIYNSITNGADTVEWGGEIYDSSGTGGFHTTTQMGSGHFPT... | Glutamic endopeptidase that preferentially cleaves peptide bonds on the C-terminal side of proline residues. Also cleaves peptide bonds on the C-terminal side of alanine residues but with less efficiency. In contrast to most proline-cleaving enzymes, effectively degrades proteins of any size. Found in the viscoelastic ... |
C0HLV6 | LACS_TRAHI | Laccase-S (ThLacc-S) (EC 1.10.3.2) (Benzenediol:oxygen oxidoreductase S) (Diphenol oxidase S) (Urishiol oxidase S) | FQLNVIANMNNHTMLKQTSIHWHCHFQKGTNWADGHAFVNACPIASGHSFLYDFTAPDQHGTFWYHSHLSTQYCDGLRGHFVVYDPADPHHDLYDVDDEHTIITLADWYHVAAKLGHHFQLGADSTLINGSGRFAGDPTAHLTVIYVTQGKRYRFHLVSLSCDPNHVFSIDSNHMTVIEADAVSHEHCTVDSIQIYAGQRYSFHLTVDQDVDNYWIRAHPSFGTYSFHDGINSAIARY | Lignin degradation and detoxification of lignin-derived products (By similarity). Has activity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS). |
C0HLV7 | LACF_GANAU | Laccase (Galacc-F) (EC 1.10.3.2) (Benzenediol:oxygen oxidoreductase S) (Diphenol oxidase S) (Urishiol oxidase S) | FQLNVIANNNNHTMLTQTTIHCHGFFQGTNSADGHAFVNCCPIASGHSFLYDFSHPDQHGTFCYHSHLSTQYCCGLRGHFVVYDPSDPHCGLYDVDHDSTVITLSDWYHVAAKLGHSFCLGADSTLINGSGRSTGDCAASLTVISVTQGKRYRFHLVSLSCDPNHTFSIDGHDMSVIEVDSIASQHVTVDSIQIFAGQRYSFVLTANQSINNYWIRANPSFGNIGFHDGINSAILRY | Lignin degradation and detoxification of lignin-derived products (By similarity). Multicopper oxidase that catalyzes the oxidation of a variety of substrates, including phenolic and non-phenolic compounds. Has highest activity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), also active towards hy... |
C0HLX7 | GLEC_CHOCI | Galactose-binding lectin (CCL) | TYAEVESFGVGQSATAVYTAPGDGRDLNITIDADGGYVIHMDYRFDWGGNPSTGKPWEDILILNSKPAQTWGPQQHVNNFYFTPGTHVTLGDKSNDGHFAIIADGIQVATYDHRLPVNSVKEVKFSTTAGSGTDIWDLLLLP | Galactose-binding lectin. Displays antibacterial and hemagglutinin activity. Inhibits the growth of L.infantum promastigotes by damaging their membrane integrity and inducing cell apoptosis via the production of reactive oxygen species (ROS). Inhibition of L.infantum promastigotes appears to increase with time (MIC=1.2... |
C0HLZ9 | BARA1_DROME | Baramicin A1 [Cleaved into: Immune-induced peptide 24 (DIM-24) (DIM24) (IM24); Immune-induced peptide 10 (DIM-10) (DIM10) (IM10); Immune-induced peptide 12 (DIM-12) (DIM12) (IM12); Immune-induced peptide 13 (DIM-13) (DIM13) (IM13); Immune-induced peptide 22 (DIM-22) (DIM22) (IM22); Immune-induced peptide 5 (DIM-5) (DIM... | MKSFGLIALAICGVICVAAEPQHTYDGRNGPHVFGSPGNQVYIRGQNEGTYSVPGVGGQFQNAPQRGEHVYTDEAGNTFVNRKNAGGPASHTISGPNFSAKNLGPNGAKSVGIPQRARRSPQFHVERPGRTVDVGNGGFYIQRGRRSPQLHVARPDRTVTIGNGGVYIQRSRRSPQFHVERPDRTVDFGNGGFSAQRFRRGINDARVQGENFVARDDQAGIWDNNVSVWKRPDGRTVTIDRNGHTIVSGRGRPAQHY | Secreted immune-induced peptides induced by Toll signaling. Has a significant role in resistance to infection by the entomopathogenic fungus B.bassiana R444 and weak antifungal activity against M.rileyi PHP1705. In adult males, activity appears to be important for neuromuscular processes that mediate correct wing postu... |
C0HM00 | BARA2_DROME | Baramicin A2 [Cleaved into: Immune-induced peptide 24 (DIM-24) (DIM24) (IM24); Immune-induced peptide 10 (DIM-10) (DIM10) (IM10); Immune-induced peptide 12 (DIM-12) (DIM12) (IM12); Immune-induced peptide 13 (DIM-13) (DIM13) (IM13); Immune-induced peptide 22 (DIM-22) (DIM22) (IM22); Immune-induced peptide 5 (DIM-5) (DIM... | MKSFGLIALAICGVICVAAEPQHTYDGRNGPHVFGSPGNQVYIRGQNEGTYSVPGVGGQFQNAPQRGEHVYTDEAGNTFVNRKNAGGPASHTISGPNFSAKNLGPNGAKSVGIPQRARRSPQFHVERPGRTVDVGNGGFYIQRGRRSPQLHVARPDRTVTIGNGGVYIQRSRRSPQFHVERPDRTVDFGNGGFSAQRFRRGINDARVQGENFVARDDQAGIWDNNVSVWKRPDGRTVTIDRNGHTIVSGRGRPAQHY | Secreted immune-induced peptides induced by Toll signaling. Has a significant role in resistance to infection by the entomopathogenic fungus B.bassiana R444 and weak antifungal activity against M.rileyi PHP1705. In adult males, activity appears to be important for neuromuscular processes that mediate correct wing postu... |
C0HM14 | PA2BD_CRODU | Phospholipase A2 crotoxin basic subunit CBd (CTX subunit CBd) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) | HLLQFNKMIKFETRKNAIPFYAFYGCYCGWGGRGRPKDATDRCCFVHDCCYGKLAKCNTKWDIYRYSLKSGYITCGKGTWCEEQICECDRVAAECLRRSLSTYKYGYMFYPDSRCRGPSETC | Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission. It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a small acidic, non-enzymati... |
C0HM45 | LEC_NARPS | Mannose-specific lectin (Agglutinin) (NPA) (NPL) (NPL7) (NPn) | DNILYSGETLSPGEFLNNGRYVFIMQEDCNLVLYDVDKPIWATNTGGLDRRCHLSMQSDGNLVVYSPRNNPIWASNTGGENGNYVCVLQKDRNVVIYGTARWATGTNIH | D-mannose-binding lectin which binds alpha-D-linked mannose. Displays a high affinity for alpha-(1-6)-mannose oligomers. Able to interact with both terminal and internal alpha-D-mannosyl residues. Displays antiviral activity and therefore may contribute to defense against infections. |
C0HM55 | FSX1_UNCAX | Fusexin 1 (Fsx1) | MRRAALILAFVLFIGLSSATVTSADSITYNSGTSEFFDGDVFAIEVTADQSTDEIDIYLGASELSEKTDGEVNQDLSIEFTHQDSKLKYSTSTSDELRDIVTLTTYYEDGFDTEQDAIDAIKSDCYDLNQNGNGSGRYSRYYSVTSPVYDYEIYCFQKNEKLATPAYIDNPDEIFTAKAELQAGDKTIQSATLSNGDAGDGTVTDLGDSKISWNGNLDLGASEPENSRVIALYSNDFENGWRIGNKQSYEDYKTFIGGGDAYDLLIDWQDGTYTASEVEDELVNTDANQAVEEASSSTTDLVNAKVKDSSLDTGSFVYDT... | Exhibits fusogenic activity. Mediates cell-cell fusion in mammalian cells when present in both cells (bilateral fusion). {ECO:0000255|HAMAP-Rule:MF_00869, ECO:0000269|PubMed:35794124}. |
C0KTJ6 | GATDH_CERSP | Galactitol 2-dehydrogenase (L-tagatose-forming) (EC 1.1.1.406) (Galactitol dehydrogenase) (GDH) (GatDH) (Galactitol:NAD(+) 5-oxidoreductase) | MDYRTVFRLDGACAAVTGAGSGIGLEICRAFAASGARLILIDREAAALDRAAQELGAAVAARIVADVTDAEAMTAAAAEAEAVAPVSILVNSAGIARLHDALETDDATWRQVMAVNVDGMFWASRAFGRAMVARGAGAIVNLGSMSGTIVNRPQFASSYMASKGAVHQLTRALAAEWAGRGVRVNALAPGYVATEMTLKMRERPELFETWLDMTPMGRCGEPSEIAAAALFLASPAASYVTGAILAVDGGYTVW | Catalyzes the interconversion of galactitol to the rare sugar L-tagatose. Shows activity with a wide range of substrates, and catalyzes the oxidation of a variety of polyvalent aliphatic alcohols and polyols to the corresponding ketones and ketoses, respectively, and in the reverse reaction, it reduces ketones with hig... |
C0L2T8 | VM2C1_CRODO | Zinc metalloproteinase/disintegrin (Metalloproteinase PII) (MPII) [Cleaved into: Snake venom metalloproteinase (SVMP) (EC 3.4.24.-); Disintegrin Cdc] | MIQVLLVTICLAAFPYQGSSIILESGNVNDYEVIYPRKVTALPKGAVQPKYEDTMQYELKVNGQPVVLHLEKNKGLFSKDYSETHYSPDGRKITTNPSVEDHCYYHGRIENDADSTASISACNGLKGHFKLQGEMYIIEPLELSDSEDHAVFKLENVEKEDEAPKMCGVTQNWESNEPIKKASHLNLNPEHQRYVEIVIVVDHGMFTKYNGDSDKIRQRVHQMVNIMKESYRYMYIDISLAGIEIWSNKDLINVQPAAPNTLKSFGEWRETDLPKRKSHDNAQLLTSIDFNGQTIGIANIGAICDPKPSTRVVQDHSKIN... | [Snake venom metalloproteinase]: Snake venom zinc metalloproteinase that causes hemorrhage by provoking the degradation of the sub-endothelial matrix proteins (fibronectin, laminin, type IV collagen, nidogen, and gelatins). [Disintegrin Cdc]: Displays low cytotoxicity. In vitro, inhibits cancer cell migration (human b... |
C0LGF4 | FEI1_ARATH | LRR receptor-like serine/threonine-protein kinase FEI 1 (EC 2.7.11.1) | MMGICEMKSCCSWLLLISLLCSLSNESQAISPDGEALLSFRNAVTRSDSFIHQWRPEDPDPCNWNGVTCDAKTKRVITLNLTYHKIMGPLPPDIGKLDHLRLLMLHNNALYGAIPTALGNCTALEEIHLQSNYFTGPIPAEMGDLPGLQKLDMSSNTLSGPIPASLGQLKKLSNFNVSNNFLVGQIPSDGVLSGFSKNSFIGNLNLCGKHVDVVCQDDSGNPSSHSQSGQNQKKNSGKLLISASATVGALLLVALMCFWGCFLYKKLGKVEIKSLAKDVGGGASIVMFHGDLPYSSKDIIKKLEMLNEEHIIGCGGFGTV... | Involved in the signaling pathway that regulates cell wall function, including cellulose biosynthesis, likely via an 1-aminocyclopropane-1-carboxylic acid (ACC)-mediated signal (a precursor of ethylene). |
C0LGF5 | RGI5_ARATH | LRR receptor-like serine/threonine-protein kinase RGI5 (EC 2.7.11.1) (Protein RECEPTOR OF RGF1 5) (Protein RGF1 INSENSITIVE 5) | MERERSNFFFLFLFCSWVSMAQPTLSLSSDGQALLSLKRPSPSLFSSWDPQDQTPCSWYGITCSADNRVISVSIPDTFLNLSSIPDLSSLSSLQFLNLSSTNLSGPIPPSFGKLTHLRLLDLSSNSLSGPIPSELGRLSTLQFLILNANKLSGSIPSQISNLFALQVLCLQDNLLNGSIPSSFGSLVSLQQFRLGGNTNLGGPIPAQLGFLKNLTTLGFAASGLSGSIPSTFGNLVNLQTLALYDTEISGTIPPQLGLCSELRNLYLHMNKLTGSIPKELGKLQKITSLLLWGNSLSGVIPPEISNCSSLVVFDVSANDL... | Together with RGI1, RGI2, RGI3 and RGI4, acts as receptor of RGF1, a peptide hormone that maintains the postembryonic root stem cell niche by regulating the expression levels and patterns of the transcription factor PLETHORA (PLT). Links RGF1 signal with its downstream components. |
C0LGL9 | FEI2_ARATH | LRR receptor-like serine/threonine-protein kinase FEI 2 (EC 2.7.11.1) | MGICLMKRCCSWFLLISFLSALTNENEAISPDGEALLSFRNGVLASDGVIGLWRPEDPDPCNWKGVTCDAKTKRVIALSLTYHKLRGPLPPELGKLDQLRLLMLHNNALYQSIPASLGNCTALEGIYLQNNYITGTIPSEIGNLSGLKNLDLSNNNLNGAIPASLGQLKRLTKFNVSNNFLVGKIPSDGLLARLSRDSFNGNRNLCGKQIDIVCNDSGNSTASGSPTGQGGNNPKRLLISASATVGGLLLVALMCFWGCFLYKKLGRVESKSLVIDVGGGASIVMFHGDLPYASKDIIKKLESLNEEHIIGCGGFGTVYK... | Involved in the signaling pathway that regulates cell wall function, including cellulose biosynthesis, likely via an 1-aminocyclopropane-1-carboxylic acid (ACC)-mediated signal (a precursor of ethylene). |
C0LGP2 | MEE39_ARATH | Probable LRR receptor-like serine/threonine-protein kinase MEE39 (EC 2.7.11.1) (Protein MATERNAL EFFECT EMBRYO ARREST 39) | MKNLCWVFLSLFWFGVFLIIRFAEGQNQEGFISLDCGLPLNEPPYIESETGIQFSSDENFIQSGKTGRIPKNLESENLKQYATLRYFPDGIRNCYDLRVEEGRNYLIRATFFYGNFDGLNVSPEFDMHIGPNKWTTIDLQIVPDGTVKEIIHIPRSNSLQICLVKTGATIPMISALELRPLANDTYIAKSGSLKYYFRMYLSNATVLLRYPKDVYDRSWVPYIQPEWNQISTTSNVSNKNHYDPPQVALKMAATPTNLDAALTMVWRLENPDDQIYLYMHFSEIQVLKANDTREFDIILNGETINTRGVTPKYLEIMTWL... | Receptor-like serine/threonine-kinase required during the endosperm development in seeds. |
C0LGP9 | IMK3_ARATH | Probable leucine-rich repeat receptor-like protein kinase IMK3 (EC 2.7.11.1) (Protein INFLORESCENCE MERISTEM RECEPTOR-LIKE KINASE 3) (Protein MERISTEMATIC RECEPTOR-LIKE KINASE) | MEFITQNQAITSLSMINTDIDQPKASLRSRFLLHLIICLLFFVPPCSSQAWDGVVITQADYQGLQAVKQELIDPRGFLRSWNGSGFSACSGGWAGIKCAQGQVIVIQLPWKSLGGRISEKIGQLQALRKLSLHDNNLGGSIPMSLGLIPNLRGVQLFNNRLTGSIPASLGVSHFLQTLDLSNNLLSEIIPPNLADSSKLLRLNLSFNSLSGQIPVSLSRSSSLQFLALDHNNLSGPILDTWGSKSLNLRVLSLDHNSLSGPFPFSLCNLTQLQDFSFSHNRIRGTLPSELSKLTKLRKMDISGNSVSGHIPETLGNISSL... | Can phosphorylate AGL24. {ECO:0000269|Ref.9}. |
C0LGQ4 | MDIS2_ARATH | Protein MALE DISCOVERER 2 (AtMDIS2) (Probable LRR receptor-like serine/threonine-protein kinase MRH1) (EC 2.7.11.1) (Protein MORPHOGENESIS OF ROOT HAIR 1) | MMGCGFHFPWFFFLIIGLQAPLSLSLTSQGSALLKFRARVNSDPHGTLANWNVSGINDLCYWSGVTCVDGKVQILDLSGYSLEGTLAPELSQLSDLRSLILSRNHFSGGIPKEYGSFENLEVLDLRENDLSGQIPPELSNGLSLKHLLLSGNKFSDDMRIKIVRLQSSYEVRLKKSPKLSPLAVLGCINRKLGHCVSRNRIIQVKKVEAIVFRIKATSRRFLKAFPSFLEETDIYKRRELLEETSNLAAEPAPSAPSPSPGIITEASPRSSGSFPAVTNAKKRRPPLVPPVPSPDKGSTSPDISKNQPQDNKQSKGSKHV... | Involved in the pollen tube perception of the female signal by binding an unidentified female attractant. May be involved in the regulation of root hairs development. |
C0LGQ5 | GSO1_ARATH | LRR receptor-like serine/threonine-protein kinase GSO1 (EC 2.7.11.1) (Protein GASSHO 1) (Protein SCHENGEN 3) | MQPLVLLLLFILCFSGLGQPGIINNDLQTLLEVKKSLVTNPQEDDPLRQWNSDNINYCSWTGVTCDNTGLFRVIALNLTGLGLTGSISPWFGRFDNLIHLDLSSNNLVGPIPTALSNLTSLESLFLFSNQLTGEIPSQLGSLVNIRSLRIGDNELVGDIPETLGNLVNLQMLALASCRLTGPIPSQLGRLVRVQSLILQDNYLEGPIPAELGNCSDLTVFTAAENMLNGTIPAELGRLENLEILNLANNSLTGEIPSQLGEMSQLQYLSLMANQLQGLIPKSLADLGNLQTLDLSANNLTGEIPEEFWNMSQLLDLVLAN... | Together with GSO2, receptor-like serine/threonine-kinase required during the development of the epidermal surface in embryos and cotyledons. In coordination with GSO2, regulates root growth through control of cell division and cell fate specification. Controls seedling root growth by modulating sucrose response after ... |
C0LGQ9 | GHR1_ARATH | LRR receptor-like serine/threonine-protein kinase GHR1 (EC 2.7.11.1) (Protein GUARD CELL HYDROGEN PEROXIDE-RESISTANT 1) (AtGHR1) (Protein RADICAL-INDUCED CELL DEATH 7) | MNLSRILLLSMFFLSAMGQLPSQDIMALLEFKKGIKHDPTGFVLNSWNDESIDFNGCPSSWNGIVCNGGNVAGVVLDNLGLTADADFSLFSNLTKLVKLSMSNNSLSGVLPNDLGSFKSLQFLDLSDNLFSSSLPKEIGRSVSLRNLSLSGNNFSGEIPESMGGLISLQSLDMSSNSLSGPLPKSLTRLNDLLYLNLSSNGFTGKMPRGFELISSLEVLDLHGNSIDGNLDGEFFLLTNASYVDISGNRLVTTSGKLLPGVSESIKHLNLSHNQLEGSLTSGFQLFQNLKVLDLSYNMLSGELPGFNYVYDLEVLKLSNN... | Receptor kinase acting as an early component in abscisic acid (ABA) signaling. Required for darkness, ABA, high CO(2) and hydrogen peroxide (H(2)O(2)) induction of S-type anion currents in guard cells leading to stomatal closure, possibly via the phosphorylation and activation of the anion channel SLAC1 and as a scaffo... |
C0LGR3 | RGI3_ARATH | LRR receptor-like serine/threonine-protein kinase RGI3 (EC 2.7.11.1) (Protein RECEPTOR OF RGF1 1) (Protein RGF1 INSENSITIVE 3) | MPPNIYRLSFFSSLLCFFFIPCFSLDQQGQALLSWKSQLNISGDAFSSWHVADTSPCNWVGVKCNRRGEVSEIQLKGMDLQGSLPVTSLRSLKSLTSLTLSSLNLTGVIPKEIGDFTELELLDLSDNSLSGDIPVEIFRLKKLKTLSLNTNNLEGHIPMEIGNLSGLVELMLFDNKLSGEIPRSIGELKNLQVLRAGGNKNLRGELPWEIGNCENLVMLGLAETSLSGKLPASIGNLKRVQTIAIYTSLLSGPIPDEIGYCTELQNLYLYQNSISGSIPTTIGGLKKLQSLLLWQNNLVGKIPTELGNCPELWLIDFSEN... | Together with RGI1, RGI2, RGI4 and RGI5, acts as receptor of RGF peptides (e.g. RGF1, GLV5/CLEL1/RGF2, GLV7/CLEL3/RGF3, GLV3/RGF4, GLV10/CLEL7/RGF5 and RGF10/CLELN), peptide hormones which maintain the postembryonic root stem cell niche by regulating the expression levels and patterns of the transcription factor PLETHO... |
C0LGT6 | EFR_ARATH | LRR receptor-like serine/threonine-protein kinase EFR (EC 2.7.11.1) (Elongation factor Tu receptor) (EF-Tu receptor) | MKLSFSLVFNALTLLLQVCIFAQARFSNETDMQALLEFKSQVSENNKREVLASWNHSSPFCNWIGVTCGRRRERVISLNLGGFKLTGVISPSIGNLSFLRLLNLADNSFGSTIPQKVGRLFRLQYLNMSYNLLEGRIPSSLSNCSRLSTVDLSSNHLGHGVPSELGSLSKLAILDLSKNNLTGNFPASLGNLTSLQKLDFAYNQMRGEIPDEVARLTQMVFFQIALNSFSGGFPPALYNISSLESLSLADNSFSGNLRADFGYLLPNLRRLLLGTNQFTGAIPKTLANISSLERFDISSNYLSGSIPLSFGKLRNLWWLG... | Constitutes the pattern-recognition receptor (PPR) that determines the specific perception of elongation factor Tu (EF-Tu), a potent elicitor of the defense response to pathogen-associated molecular patterns (PAMPs) phosphorylates BIK1 upon elicitation to regulate immune responses such as defense hormone expression (e.... |
C0LGU0 | PRK1_ARATH | Pollen receptor-like kinase 1 (AtPRK1) (EC 2.7.11.1) (LRR receptor-like serine/threonine-protein kinase RLK) | MPPMQARTLSVYNVMVPLVCLLLFFSTPTHGLSDSEAILKFKESLVVGQENALASWNAKSPPCTWSGVLCNGGSVWRLQMENLELSGSIDIEALSGLTSLRTLSFMNNKFEGPFPDFKKLAALKSLYLSNNQFGGDIPGDAFEGMGWLKKVHLAQNKFTGQIPSSVAKLPKLLELRLDGNQFTGEIPEFEHQLHLLNLSNNALTGPIPESLSMTDPKVFEGNKGLYGKPLETECDSPYIEHPPQSEARPKSSSRGPLVITAIVAALTILIILGVIFLLNRSYKNKKPRLAVETGPSSLQKKTGIREADQSRRDRKKADHR... | Receptor-like kinase involved in the control of pollen germination and pollen tube polar growth. |
C0LGU7 | MDIS1_ARATH | Protein MALE DISCOVERER 1 (AtMDIS1) (Probable LRR receptor-like serine/threonine-protein kinase At5g45840) (EC 2.7.11.1) | MGCRWNPIGFQFSCFMFLIITLQSRSSLSLESEGFVLLKFRARVDSDPHGTLANWNVSDHDHFCSWFGVTCVDNKVQMLNLSGCSLGGTLAPELSQLSELRSLILSKNKLSGDIPNEFASFAKLEFLDLRDNNLNGVVPPELNKVLTPENLLLSGNKFAGFMTVKFLRLQSLYKVQMNKNRELSSVSADVLDCVNRKLGYCVSRRSLITRNKAKAFVLRIRATSRHYMVRRESHGKNYVVNYHPSENETSIFKRRELLEETSNLAAMPAPDTPSPSPEIITIVFPRSSGSFPALTNAKKRIPPLIPPSSPPPLPTNNTIA... | Involved in the pollen tube perception of the female signal. |
C0LGV1 | RGI2_ARATH | LRR receptor-like serine/threonine-protein kinase RGI2 (EC 2.7.11.1) (Protein RECEPTOR OF RGF1 3) (Protein RGF1 INSENSITIVE 2) (Protein ROOT CLAVATA-HOMOLOG1 1) | MSLQMPIPRKKALTVSHFSITLSLFLAFFISSTSASTNEVSALISWLHSSNSPPPSVFSGWNPSDSDPCQWPYITCSSSDNKLVTEINVVSVQLALPFPPNISSFTSLQKLVISNTNLTGAISSEIGDCSELIVIDLSSNSLVGEIPSSLGKLKNLQELCLNSNGLTGKIPPELGDCVSLKNLEIFDNYLSENLPLELGKISTLESIRAGGNSELSGKIPEEIGNCRNLKVLGLAATKISGSLPVSLGQLSKLQSLSVYSTMLSGEIPKELGNCSELINLFLYDNDLSGTLPKELGKLQNLEKMLLWQNNLHGPIPEEIG... | Together with RGI1, RGI3, RGI4 and RGI5, acts as receptor of RGF peptides (e.g. RGF1, GLV5/CLEL1/RGF2, GLV7/CLEL3/RGF3, GLV3/RGF4, GLV10/CLEL7/RGF5 and RGF10/CLELN), peptide hormones which maintain the postembryonic root stem cell niche by regulating the expression levels and patterns of the transcription factor PLETHO... |
C0LGW2 | PAM74_ARATH | Probable LRR receptor-like serine/threonine-protein kinase PAM74 (EC 2.7.11.1) (Protein PHOTOSYNTHESIS AFFECTED MUTANT 74) | MDSPCWLLLLLLGAFAIIGCVQAQDQQEFISLDCGLPMTEPSSYTESVTGLRFSSDAEFIQTGESGKIQASMENDYLKPYTRLRYFPEERRNCYSLSVDKNRKYLIRARFIYGNYDGRNSNPIFELHLGPNLWATIDLQKFVNGTMEEILHTPTSNSLNVCLVKTGTTTPLISALELRPLGNNSYLTDGSLNLFVRIYLNKTDGFLRYPDDIYDRRWHNYFMVDDWTQIFTTLEVTNDNNYEPPKKALAAAATPSNASAPLTISWPPDNPGDQYYLYSHFSEIQDLQTNDTREFDILWDGAVVEEGFIPPKLGVTTIHNL... | Required for accurate photosynthesis. {ECO:0000269|Ref.4}. |
C0LGW6 | ERL1_ARATH | LRR receptor-like serine/threonine-protein kinase ERL1 (EC 2.7.11.1) (Protein ERECTA-like kinase 1) | MKEKMQRMVLSLAMVGFMVFGVASAMNNEGKALMAIKGSFSNLVNMLLDWDDVHNSDLCSWRGVFCDNVSYSVVSLNLSSLNLGGEISPAIGDLRNLQSIDLQGNKLAGQIPDEIGNCASLVYLDLSENLLYGDIPFSISKLKQLETLNLKNNQLTGPVPATLTQIPNLKRLDLAGNHLTGEISRLLYWNEVLQYLGLRGNMLTGTLSSDMCQLTGLWYFDVRGNNLTGTIPESIGNCTSFQILDISYNQITGEIPYNIGFLQVATLSLQGNRLTGRIPEVIGLMQALAVLDLSDNELVGPIPPILGNLSFTGKLYLHGN... | Receptor kinase that regulates inflorescence architecture and organ shape as well as stomatal patterning, including density and clustering, together with ER and ERL2. Redundantly involved with ER in procambial development regulation. Forms a functional ligand-receptor pair with EPF1 (AC Q8S8I4). Forms a constitutive co... |
C0LGX3 | HSL2_ARATH | LRR receptor-like serine/threonine-protein kinase HSL2 (EC 2.7.11.1) (Protein HAESA-LIKE2) | MLTNTNLFFFLSLLLLSCFLQVSSNGDAEILSRVKKTRLFDPDGNLQDWVITGDNRSPCNWTGITCHIRKGSSLAVTTIDLSGYNISGGFPYGFCRIRTLINITLSQNNLNGTIDSAPLSLCSKLQNLILNQNNFSGKLPEFSPEFRKLRVLELESNLFTGEIPQSYGRLTALQVLNLNGNPLSGIVPAFLGYLTELTRLDLAYISFDPSPIPSTLGNLSNLTDLRLTHSNLVGEIPDSIMNLVLLENLDLAMNSLTGEIPESIGRLESVYQIELYDNRLSGKLPESIGNLTELRNFDVSQNNLTGELPEKIAALQLISF... | Receptor-like serine/threonine-kinase acting on substrates that controls floral organ abscission. Regulated by the 'INFLORESCENCE DEFICIENT IN ABSCISSION' (IDA) family of ligands. |
C0LLJ0 | IMA8_MOUSE | Importin subunit alpha-8 (Karyopherin subunit alpha-7) | MATSKAPKERLKNYKYRGKEMSLPRQQRIASSLQLRKTRKDEQVLKRRNIDLFSSDMVSQALVKEVNFTLDDIIQAVNSSDPILHFRATRAAREMISQENTPPLNLIIEAGLIPKLVDFLKATPHPKLQFEAAWVLTNIASGTSEQTRAVVKEGAIQPLIELLCSPHLTVSEQAVWALGNIAGDCAEFRDCVISNNAIPHLINLISKGIPITFLRNISWTLSNLCRNKDPYPSESAVRQMLPPLCQLLLHRDNEILADTCWALSYLTKGGKEYIHHVVTTGILPRLVELMTSSELSISIPCLHTIGNIVAGTDEQTQMAI... | Functions in nuclear protein import. |
C0LNR0 | FABH_LISM4 | Beta-ketoacyl-[acyl-carrier-protein] synthase III (Beta-ketoacyl-ACP synthase III) (KAS III) (EC 2.3.1.180) (EC 2.3.1.300) (3-oxoacyl-[acyl-carrier-protein] synthase 3) (3-oxoacyl-[acyl-carrier-protein] synthase III) (Branched-chain beta-ketoacyl-[acyl-carrier-protein] synthase) | MNAGILGVGKYVPEKIVTNFDLEKIMDTSDEWIRTRTGIEERRIARDDEYTHDLAYEAAKVAIKNAGLTPDDIDLFIVATVTQEATFPSVANIIQDRLGAKNAAGMDVEAACAGFTFGVVTAAQFIKTGAYKNIVVVGADKLSKITNWDDRTTAVLFGDGAGAVVMGPVSDDHGLLSFDLGSDGSGGKYLNLDENKKIYMNGREVFRFAVRQMGEASLRVLERAGLEKEDLDLLIPHQANIRIMEASRERLNLPEEKLMKTVHKYGNTSSSSIALALVDAVEEGRIKDNDNVLLVGFGGGLTWGALIIRWGK | Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-A... |
C0LT23 | CERK_ORYSJ | Ceramide kinase (OsCERK) (EC 2.7.1.138) | MEGGGEALFLDGVGEVTVAVGDDGLSFQPLHQEVSSSCWSSIIMQPKLESKLKFSDVYAVELLEVGPVCEPWNARATVQGKINTEMNRFVIHTVTRPRKRPSPWVPCEYIFGHKDQQTCKTWVEHIKTCINKEQDRPKSLMVFVHPLCGKGRGCKNWETVAPLFERAKVKTKVIVTQRAGHAYDTLASLSDKDLKKFDGVIAVGGDGLFNEILNGLLSTRHTNSYPPTPEGFGYFRNNMKCQEHRNNDLSNSELTGDDANAISGSSNTPDDHEPLLSTTRSTGLDISSSDSSDEPCNGDQVPLVSFPNNWFRLGIIPSGS... | Catalyzes specifically the phosphorylation of ceramide to form ceramide 1-phosphate. Possesses activity on ceramide analog (C6 synthetic ceramide) in vitro. Ceramide is a critical sphingolipid metabolite that induces programmed cell death (PCD) in plants and ceramide-1-phosphate has a PCD suppressive effect. Thus, cera... |
C0LU16 | MED21_ARATH | Mediator of RNA polymerase II transcription subunit 21 (Mediator complex subunit 21) (RNAPII complex component SRB7) | MDIISQLQEQVNTIAAITFNAFGTLQRDAPPVQLSPNYPEPPATTTVTDDATPFPEQPKQLSAGLVKAAKQFDALVAALPLSEGGEGAQLKRIAELQVENDLVGQELQKQLEAAEKELKQVQELFGQAADNCLNMKKPE | Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters... |
C0M0V4 | AAH1_SOYBN | Allantoate deiminase 1 (EC 3.5.3.9) (Allantoate amidohydrolase 1) (GmAAH1) | MYSATASNTFFLLSCFLLFCLLSAPSCVSMFSGIETGDLEKRDDLFPQILRDEAVARLYELGKVSDASGYLERTFLSPASMKAIDLIRKWMEDAGLRTWVDQMGNVHGRVDGANENAEALLIGSHMDTVVDAGMFDGSLGIVSAISAVKAMHVNGKLQKLKRPVEVIAFSDEEGVRFQTTFLGSGAIAGILPGTTLEISDKREVMIKDFLKENSMDITEESLLKLKYDPKSVWGYVEVHIEQGPVLEQVGFPLGVVKGIAGQTRLKVTVRGSQGHAGTVPMSMRQDPMAAAAEQIVVLESLCKHPEEYLSYDGHCSDSTV... | Involved in the catabolism of purine nucleotides. Can use allantoate as substrate. The sequential activity of AAH, UGLYAH and UAH allows a complete purine breakdown without the intermediate generation of urea. |
C0MAL8 | THSA_STRE4 | NAD(+) hydrolase ThsA (NADase ThsA) (SeThsA) (EC 3.2.2.5) | MFIIKGEVSRKDLIREIEKAIKSDELGAFIGAGLSIPAGFCSWKELLREPAEEIGLDVEKESDLVNLAQYYSNSKKRTSIDDLIKGQFSQLVKPTENHKLLSQLPISTFWTTNYDKLIEKALENNMKKPYVKTKDEQLRGTNHNFDAIVYKLHGDVETPEDAVITRSDYEEFGYNKRKLFREVLEGDLLTKTFLFLGFSFEDPNFNYVIGRLRVLLDEKNTRKHYCIMKRVQDADEDYEYKKARQELQIEDLNRYGIFTYLVNKYDEITEILSTLVDRFRRKTIFISGSAYSYSAYSQKTGENFIHKLSFELSKNGYHIV... | NAD(+) hydrolyzing component (NADase) of the Thoeris antiviral defense system, composed of ThsA and ThsB (maybe SEQ_0762). Has a low NADase activity that is strongly activated by 3' cyclic ADP-D-ribose (3'cADPR) and weakly activated by 2'cADPR. Upon activation binds and hydrolyzes NAD(+), leading to cell death and inhi... |
C0MHL9 | POLG_SAFV | Genome polyprotein [Cleaved into: Leader protein (L); Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Rho) (Virion protein 4); Capsid protein VP2 (Beta) (P1B) (Virion protein 2); Capsid protein VP3 (Gamma) (P1C) (Virion protein 3); Capsid protein VP1 (Alpha) (P1D) (Virion protein 1); Protein 2A (P2A); Protein 2... | MACKHGYPLLCPLCTALDITPDGSFTLLFDNEWYPTDLLTVNLDDDVFYPLDTNMDWTDLPLIQDIVMEPQGNSNSSDKNNSQSSGNEGVIINNYYSNQYQNSIDLSANANGVGKENSKPQGQLMNILGSAADAFKNIAPLLMDQNTEEMTNLSDRVSSDTAGNTATNTQSTVGRLFGFGQRHKGKHPASCADTATDKVLAAERYYTIKLASWTKTQESFDHIRVPLPHALAGENGGVFSSTLRRHYLCKCGWRIQVQCNASQFHAGSLLVFMAPEFDTSNHSTEVEPRADTAFKVDANWQKHAQILTGHAYVNTTTKVN... | [Leader protein]: Forms a complex with host RAN and probably binds to exportins carrying activated MAPK in order to mediate the hyperphosphorylation of host Phe/Gly containing nuclear pore proteins (Nups) resulting in cessation of active nucleocytoplasmic transport (Probable). Proteins with NLS signals fail to import, ... |
C0NL63 | ARO1_AJECG | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10);... | MGVPTKISILGRESIVADFGIWRNYVAKDLLSSCSSSTYILISDTNLTPLYLEGFQRSFEDAATNVSPKPRLLTYEIPPGESSKSRETKADIEDWMLARQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSDEKFAALERDAETILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVSIGMVKEAELARHLGILNNVSVSRISKCL... | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
C0P9J6 | ADH1A_MAIZE | Aminoaldehyde dehydrogenase 1a (ZmAMADH1a) (EC 1.2.1.-) (4-trimethylammoniobutyraldehyde dehydrogenase AMADH1a) (EC 1.2.1.47) (Aminobutyraldehyde dehydrogenase AMADH1a) (EC 1.2.1.19) (Betaine aldehyde dehydrogenase AMADH1a) (EC 1.2.1.8) (Gamma-guanidinobutyraldehyde dehydrogenase AMADH1a) (EC 1.2.1.54) | MASPAMVPLRQLFVDGEWRPPAQGRRLPVVNPTTEAHIGEIPAGTAEDVDAAVAAARAALKRNRGRDWARAPGAVRAKYLRAIAAKVIERKPELAKLEALDCGKPYDEAAWDMDDVAGCFEYFADQAEALDKRQNSPVSLPMETFKCHLRREPIGVVGLITPWNYPLLMATWKIAPALAAGCTAVLKPSELASVTCLELADICKEVGLPSGVLNIVTGLGPDAGAPLSAHPDVDKVAFTGSFETGKKIMASAAPMVKPVTLELGGKSPIVVFDDVDIDKAVEWTLFGCFWTNGQICSATSRLLIHTKIAKKFNERMVAWA... | Dehydrogenase that catalyzes the oxidation of several aminoaldehydes. Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively. Catalyzes the oxidation of 4-... |
C0QRP9 | GPMPP_PERMH | Glucosyl-3-phosphoglycerate/mannosyl-3-phosphoglycerate phosphatase (GpgP) (MpgP) (EC 3.1.3.70) (EC 3.1.3.85) | MVIFTDLDGTLLNHEDYSFKDAIPSLERIKKKGIPLVIVTSKTKKEVELIQKELGIEEPFIVENGAAVFFPKGYRGFNIRCDQENRYCIIKLGRDYREIRDFIEKIKDKFKIKGFGDMTVEEIVRLTDLPYDRAELAKERDFTEPFIIEDEKDIKDLEEIAEKEGFKITKGGRFYHLIGKGQDKGRAVQIVKKVFEENYGEVPLTVGLGDSRNDIPMLREVDIPILIPHINKKYESVNLPGIIKAEYPGSKGWNESIWRILNEIERGCC | Involved in the biosynthesis of glucosylglycerate. Catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) and mannosyl-3-phosphoglycerate (MPG) to glucosylglycerate (GG) and mannosylglycerate (MG), respectively. |
C0QRQ2 | GPGS_PERMH | Glucosyl-3-phosphoglycerate synthase (GpgS) (EC 2.4.1.266) | MADFFQNGVITTLQNFRNRSLEELEYELELFSKRRNMVLLLPALYSEFEGPAMPKIIQELKDIRYLYKIVLSLDRATEEEFKKVKKIMSEINTEVKVIWHDGPRMQRLYRELEEAGFNVSIPGKGRSVWMSLGYILSDADAYAIALHDCDIVNYSRELPARLLYPVVHPALDFEFSKGYYARVTHKLYGRVTRIFYTPLIRALIRILGCNRFLVYLDSFRYALSGEFAFIRTLARGIRISPTWGLEVSMLSEVYQNTSFNRICQVEVMDTYEHKHQKLVKSTSEGLVKMASDIAKTLFRVLAHDGFVFSEAFFRTLLTTY... | Involved in the biosynthesis of 6-O-methylglucose lipopolysaccarides (MGLPs). Catalyzes the transfer of a glucose (Glc) moiety from uridine diphosphate (UDP-Glc) to the position 2 of 3-phospho-D-glycerate (3-PGA) to form glucosyl-3-phosphoglycerate (GPG). GpgS is most active with UDP-glucose, followed by GDP-glucose, A... |
C0RGW8 | TCPB_BRUMB | Probable 2' cyclic ADP-D-ribose synthase TcpB (2'cADPR synthase TcpB) (EC 3.2.2.-) (Brucella TIR-containing protein 1) (Btp1) (NAD(+) hydrolase TcpB) (EC 3.2.2.6) (TIR domain-containing protein in Brucella) (TcpB) | MSSYSSNIDRLQREIARLKADDSREMSKEKQAQSKAHKAQQAISSAKSLSTQKSKMSELERATRDGAAIGKKRADIAKKIADKAKQLSSYQAKQFKADEQAVKKVAQEQKRLSDERTKHEAFIKQSLSSMRTTASATMEAEEEYDFFISHASEDKEAFVQDLVAALRDLGAKIFYDAYTLKVGDSLRRKIDQGLANSKFGIVVLSEHFFSKQWPARELDGLTAMEIGGQTRILPIWHKVSYDEVRRFSPSLADKVALNTSLKSVEEIAKELHSLI | Virulence factor that interferes with host Toll-like receptor 2 (TLR2) and TLR4 signaling, resulting in the reduction of dendritic cell maturation, inhibition of pro-inflammatory cytokine secretion and impaired NF-kappa-B activation in macrophages. Binds host lipids. Has NAD(+) hydrolase (NADase) activity, catalyzes cl... |
C0S433 | ARO1_PARBP | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10);... | MGVPTKISILGRESIVADFGIWRNYVAKDLLSNCASSTYILISDTNLTPLYLAGFQQSFENAAAGLSPKPRLLTYEIPPGESSKSRETKAEIEDWMLTRQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALENDADVILAAVKSKNTPDRLRFSSIQETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVSIGMVKEAELARHLGILNNVSVARIAKCL... | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
C0SP85 | YUKE_BACSU | Protein YukE | MAGLIRVTPEELRAMAKQYGVESQEVLNQVDRLNRMISDLKSMWEGASSEAFADQYEQLKPSFIKMSDLLQDVNQQLDQTANTLESTDQDIANQIRG | Required to deliver LXG toxins to target cells. |
C0SPC1 | CCRZ_BACSU | Cell cycle regulator CcrZ (EC 2.7.1.15) (EC 2.7.1.229) (Cell cycle regulator protein interacting with FtsZ) | MNIDMNWLGQLLGSDWEIFPAGGATGDAYYAKHNGQQLFLKRNSSPFLAVLSAEGIVPKLVWTKRMENGDVITAQHWMTGRELKPKDMSGRPVAELLRKIHTSKALLDMLKRLGKEPLNPGALLSQLKQAVFAVQQSSPLIQEGIKYLEEHLHEVHFGEKVVCHCDVNHNNWLLSEDNQLYLIDWDGAMIADPAMDLGPLLYHYVEKPAWESWLSMYGIELTESLRLRMAWYVLSETITFIAWHKAKGNDKEFHDAMEELHILMKRIVD | Plays a role in cell cycle regulation and chromosome integrity. Activates DnaA-dependent chromosomal DNA replication initiation ensuring that the chromosome is replicated at the right time during the cell cycle (By similarity). May regulate replication initiation through phosphorylation of a possible second messenger o... |
C0SUT9 | JMJ16_ARATH | Putative lysine-specific demethylase JMJ16 (EC 1.14.11.-) (Jumonji domain-containing protein 16) (AtJMJ16) (Protein JUMONJI 16) (Lysine-specific histone demethylase JMJ16) ([histone H3]-trimethyl-L-lysine(4) monodemethylase JMJ16) | MGTELMRICVKEDSDDLPSVPPGFESYATFTLKRVVPATTSDKAKTPAIESVSATEQAKMEVESDEAKAARALRRRPWINHSGCDDDGDCAANNDNAASQNPDQNCDVKPALPKGVVRGCEECKDCQKVTARWHPDEARRPDLEDAPVFYPSEEEFEDTLNYIAKIRPEAEKYGICRIVPPPSWKPPCPLKEKQVWEGSKFTTRVQRVDKLQNRSSMKKISKLPNQMRKKKRKCMKMGMDSVTNGMGDPCSASTGMNELETFGFEPGPGFTLKDFQKYADEFKAQYFKKSETSTDDKCKVDNSIDCWEPALEDVEGEYWR... | Functions as histone H3 'Lys-4' (H3K4me) demethylase involved in the negative regulation of gene expression. Active on H3K4me1, H3K4me2 and H3K4me3. Not active on mono-, di- and trimethylated H3K9, H3K27 and H3K36 in somatic cells. However, also active on H3K9 when in complex with MMD1, a meiocyte-specific histone read... |
C0SV12 | JMJ29_ARATH | Lysine-specific demethylase JMJ29 (EC 1.14.11.-) (Jumonji domain-containing protein 29) (AtJMJ29) (Protein JUMONJI 29) (Lysine-specific histone demethylase JMJ29) ([histone H3]-trimethyl-L-lysine monodemethylase JMJ29) | MDSGVKLEHMNCFQLSYQYSWTTRKKRTLKPFMSKGSSPSSSSDSRKRKLSRAEDSDDSAVKRNAKRRRKICKVEEYYEDDDCILSDWVQRNTAKRIDKRNEEVEVMVKIESGDDCTIGKWFSDVSSKRKDKRQVEVDEDEEWEEEVTLCSKIKATSSRSRTHSLSANSPENVTDVISPCRSRSPASNVSDSIQKNDCTSSRKQSGPICHQCLKGERITLLICSECEKTMFCLQCIRKWYPNLSEDDVVEKCPLCRQNCNCSKCLHLNGLIETSKRELAKSERRHHLQYLITLMLPFLNKLSIFQKLEIEFEATVQGKLP... | May function as histone H3 lysine demethylase and be involved in regulation of gene expression. |
C0VHC9 | CAP4_ACIS2 | CD-NTase-associated protein 4 (Cap4) (EC 3.1.-.-) (Endodeoxyribonuclease Cap4) | MSASLLEKQSTGGAIARVGFGYQDAFVLRSLPLWLSQSAFSHIVSEALSDIEVCYFSSEKSLHVMYEAKNHSLTATEFWDEIRRFKSLFDTHPKNFIWFNLVCPSYNTAISPLISKIDRLRGVGSSYDDDSSVSVNGRSEYLDWCVGKKIDFSLAEFALDYVGFITFNSENSESIFLSEIQDTINIELLRSQVKQLKDQFKNLISRSSFGPIYRKDFENFICHALEEDRSQWLLDPIKINLSASSSQYQDLNLDISDFNGPDRAQKTSSDWNSLIKKAVSIGDFIHNSGDRRTLLIDGKQRMSTACMLGYVFSATRNFLL... | 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 death and t... |
C0Z2L5 | BZP44_ARATH | bZIP transcription factor 44 (AtbZIP44) | MNNKTEMGSSTSGNCSSVSTTGLANSGSESDLRQRDLIDERKRKRKQSNRESARRSRMRKQKHLDDLTAQVTHLRKENAQIVAGIAVTTQHYVTIEAENDILRAQVLELNHRLQSLNEIVDFVESSSSGFGMETGQGLFDGGLFDGVMNPMNLGFYNQPIMASASTAGDVFNC | Transcription factor that binds to the DNA G-box motif 5'-CACGTG-3' of MAN7 promoter. Involved in the positive regulation of seed germination through MAN7 gene activation. MAN7 is required for both, loosening of the micropylar endosperm, and rupture of the seed coat in germinating seeds. |
C1CZ84 | IRRE_DEIDV | Radiation response metalloprotease IrrE (EC 3.4.24.-) (DNA repair regulatory protein IrrE) | MTDPAPPPTALAAAKARMRELAASYGAGLPGRDTHSLMHGLDGITLTFMPMGQRDGAYDPEHHVILINSQVRPERQRFTLAHEISHALLLGDDDLLSDLHDEYEGDRLEQVIETLCNVGAAALLMPAELIDDLLTRFGPTGRALAELARRADVSATSALYALAERTAPPVIYAVCALSRQEDEGEGGGAKELTVRASSASAGVKYSLSAGTPVPDDHPAALALDTRLPLAQDSYVPFRSGRRMPAYVDAFPERQRVLVSFALPAGRSEPDADKPEAPGDQS | Plays a central regulatory role in DNA repair and protection pathways in response to radiation stress. Acts as a site-specific metalloprotease that cleaves and inactivates the repressor proteins DdrOC and DdrOP3, resulting in induced expression of genes required for DNA repair and cell survival after exposure to radiat... |
C1FYJ9 | ARO1_PARBD | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10);... | MGVPTKISILGRESIVADFGIWRNYVAKDLLSNCASSTYILISDTNLTPLYLAGFQQSFENAAAGLSPKPRLLTYEIPPGESSKSRETKAEIEDWMLARQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALENDADVILAAVKSKNTPDRLRFSSIQETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVSIGMVKEAELARHLGILNNVSVARIAKCL... | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
C1H8L1 | ARO1_PARBA | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10);... | MGVPTKISILGRESIVADFGIWRNYVAKDLLSSCASSTYILISDTNLTPLYLAGFQQSFENAAAGLSPKPRLLTYEIPPGESSKSRETKADIEDWMLTRQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALENDADVILAAVKSKNTPERLRFSNIQETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVSIGMVKEAELARHLGILNNVSVARIVKCL... | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
C1I202 | PNPB_PSEWB | p-benzoquinone reductase (EC 1.6.5.6) (NAD(P)H dehydrogenase (quinone)) | MPTKIQIVFYSSYGHIYKMAEAIAAGAREVGDVEVTLLQVPELMPEEVQVKSGIKGYRAAFGSIPYATPEVLAEADAIIFGTPTRFGNMCSQMRNFLDQTGGLWMSGGLIGKVGSVFTSTASQHGGQETTITSFHTTLLHHGMVIVGVPYSEPGLTNMTEISGGTPYGASTLAGADGSRQPSENELQIARFQGKHVATIAKRLANNK | Involved in the degradation of para-nitrophenol (PNP). Catalyzes the reduction of p-benzoquinone to hydroquinone. |
C1ITJ8 | HMR1_BOVIN | Major histocompatibility complex class I-related gene protein (MHC class I-related gene protein) (Class I histocompatibility antigen-like protein) | MMLLLPLIIVLMMKLSDARTHSLRYFRLGISEPGYGIPEFISAGYVDSHPITMYNSVSQLKEPRALWMEENLAPDHWERYTQLLRGWQQAFKVELKQLQHHYNHSGFHTYQRMIGCELLEDGSITGFLQYAYDGQDFLIFNKDTLSWMAMDNVADIIRRVWEANRHELQYQKNWLEEECIAWLKRFLEYGKDALQRTEPPKVRVNHKETFPGITTLYCRAYGFYPPEISINWMKNGEEIFQDTDYGGILPSGDGTYQTWVSVELDPQNGDIYSCHVEHGGVHMVLQGFQESETILLVVKAVGFIVLAIALAGVGILAWRK... | Antigen-presenting molecule specialized in displaying microbial pyrimidine-based metabolites to alpha-beta T cell receptors (TCR) on innate-type mucosal-associated invariant T (MAIT) cells. In complex with B2M preferentially presents riboflavin-derived metabolites to semi-invariant TCRs on MAIT cells, guiding immune su... |
C1JCT1 | POL_SINV3 | Polyprotein [Cleaved into: Helicase (EC 3.6.4.13); 3C-like protease (3CL-PRO) (EC 3.4.22.-); RNA-directed RNA polymerase (EC 2.7.7.48); Capsid protein VP1] | MSEKTQTFVQNETHVLDMTSDFKSDLSLEKVTSSVEQTDDLVSKIINNNDLDIKDLSFLRNLLLSTLQYLGIAKFVAINITLSILSILMLLINSCAKFTRIVNLSSHILNIITTLGLYFQVSSMEIEEITQTFENEFGTYDDDKILSHYIKICNLPNRKDVYEYISLNDLKYKIKLPDISFYELKNDILSKNKNLHLWIFQKFTDEFLAMWFGVQPYRISNLREMLVISRQGFIPKDLFNEIRKLCNMGVSVIISFIQSKLFDEPFKKRDCTQALKDASVISSPFDTLWNLISKQVCDNSAEERFTQTILDFTSEFDNFL... | [Capsid protein VP1]: Assembles with VP1-FSD and VP2 to form an icosahedral capsid. VP1 is about 5 time more abundant than VP1-FSD in the virion. |
C1JCT2 | POLFS_SINV3 | Polyprotein-FSD [Cleaved into: Helicase (EC 3.6.4.13); 3C-like protease (3CL-PRO) (EC 3.4.22.-); RNA-directed RNA polymerase (EC 2.7.7.48); Capsid protein VP1-FSD; Capsid protein VP2] | MSEKTQTFVQNETHVLDMTSDFKSDLSLEKVTSSVEQTDDLVSKIINNNDLDIKDLSFLRNLLLSTLQYLGIAKFVAINITLSILSILMLLINSCAKFTRIVNLSSHILNIITTLGLYFQVSSMEIEEITQTFENEFGTYDDDKILSHYIKICNLPNRKDVYEYISLNDLKYKIKLPDISFYELKNDILSKNKNLHLWIFQKFTDEFLAMWFGVQPYRISNLREMLVISRQGFIPKDLFNEIRKLCNMGVSVIISFIQSKLFDEPFKKRDCTQALKDASVISSPFDTLWNLISKQVCDNSAEERFTQTILDFTSEFDNFL... | [Capsid protein VP1-FSD]: Assembles with VP1 and VP2 to form an icosahedral capsid. VP1 is about 5 time more abundant than VP1-FSD in the virion. |
C1K5M2 | CPT1_SOLLC | Dimethylallylcistransferase CPT1, chloroplastic (EC 2.5.1.28) (Cis-prenyltransferase 1) (SlCPT1) (Neryl-diphosphate synthase 1) | MSSLVLQCWKLSSPSLILQQNTSISMGAFKGIHKLQIPNSPLTVSARGLNKISCSLNLQTEKLCYEDNDNDLDEELMPKHIALIMDGNRRWAKDKGLEVYEGHKHIIPKLKEICDISSKLGIQIITAFAFSTENWKRSKEEVDFLLQMFEEIYDEFSRSGVRVSIIGCKSDLPMTLQKCIALTEETTKGNKGLHLVIALNYGGYYDILQATKSIVNKAMNGLLDVEDINKNLFDQELESKCPNPDLLIRTGGEQRVSNFLLWQLAYTEFYFTNTLFPDFGEEDLKEAIMNFQQRHRRFGGHTY | Uses dimethylallyl diphosphate and isopentenyl diphosphate to catalyze the cis-prenyl chain elongation and produce the 10 carbon product neryl diphosphate. |
C1PGW1 | TED7_ZINVI | Protein TRACHEARY ELEMENT DIFFERENTIATION-RELATED 7A (TED7-1) | MASPLSQSVFPHFPPPSPAATPPPAPTTPSTPPPHFISPPPHSVPPPSPPHSVPPPLHPVPPPSPPHPVSPPPHTVPPPSPPHPVSPPPHTVPPPSPPHPVFPPPHTVPPPSPHFVPPPPNMVPPPSPPHANPPPPPPPHSVPPPPHTVPPPPPPPHIIPPPAHALSPPPPHIIPPPPPSPSNHSTTIVVIFVSCGGVFFLAFAMAALWCFLKKKKKKMVQKAENIHFDEHRKVTERIEQGPHGTETAILSVEDDIHIEEDIKKSELENFRKGLHLNYGNTYNIDTGKPSSSFGHHYLHG | Involved in the secondary cell wall (SCW) formation of vessel elements (e.g. protoxylem and metaxylem), thus promoting tracheary element (TE) differentiation. |
C3K613 | FADB_PSEFS | Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)] | MIYEGKAITVKALESGIVELKFDLKGESVNKFNRLTLNELRQAVDTIKADASIKGVIVSSGKDVFIVGADITEFVDNFKLPDAELVAGNLEANKIFSDFEDLNVPTVAAINGIALGGGLEMCLAADFRVMSATAKIGLPEVKLGIYPGFGGTVRLPRLIGADNAIEWIAAGKENRAEDALKVGAVDAVVAPDKLAEAALNLIKGAISGEFDYKAKRQPKLEKLKLNAIEQMMSFETAKGFVAGQAGPNYPAPVEAIKTIQKAANFGRDKALEVEAAGFVKLAKTSAAQSLIGLFLNDQELKKKAKAYDEIARDVKQAAVL... | Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. |
C3SBW0 | PNMT_THLFG | Pavine N-methyltransferase (TfPavNMT) (EC 2.1.1.300) | METKQTKKEAVANLIKRIEHGEVSDEEIRGMMKIQVQKRLKWGYKPTHEQQLAQLVTFAQSLKGMEMAEEVDTLDAELYEIPLPFLHIMCGKTLKFSPGYFKDESTTLDESEVYMMDLYCERAQIKDGQSILDLGCGHGSLTLHVAQKYRGCKVTGITNSVSQKEFIMDQCKKLDLSNVEIILEDVTKFETEITYDRIFAVALIEHMKNYELFLKKVSTWIAQYGLLFVEHHCHKVFAYQYEPLDEDDWYTEYIFPSGTLVMSSSSILLYFQEDVSVVNHWTLSGKHPSLGFKQWLKRLDDNIDEVKEIFESFYGSKEKA... | N-methyltransferase with a substrate preference for (+-)-pavine and (S)-reticuline, but also active with the protoberberines scoulerine and stylopine and, to a lesser extent, tetrahydropapaverine (THP) and tetrahydropalmatine. Is not active on (R)-reticuline, cryptopine, glaucine, codeine, canadaline, noscapine and ber... |
C3UVB0 | ACD_DESML | Glutaryl-CoA dehydrogenase (GDH(Des)) (EC 1.3.99.32) | MDFNLSKELQMLQKEVRNFVNKKIVPFADQWDNENHFPYEEAVRPMGELGFFGTVIPEEYGGEGMDQGWLAAMIVTEEIARGSSALRVQLNMEVLGCAYTILTYGSEALKKKYVPKLSSAEFLGGFGITEPDAGSDVMAMSSTAEDKGDHWLLNGSKTWISNAAQADVLIYYAYTDKAAGSRGLSAFVIEPRNFPGIKTSNLEKLGSHASPTGELFLDNVKVPKENILGKPGDGARIVFGSLNHTRLSAAAGGVGLAQACLDAAIKYCNERRQFGKPIGDFQMNQDMIAQMAVEVEAARLLAYKAAAAKDEGRLNNGLDV... | Catalyzes the dehydrogenation of Glutaryl-CoA to glutaconyl-CoA. |
C3VD30 | ZAR1L_MOUSE | Protein ZAR1-like (Zygote arrest protein 1-like) (Zygote arrest protein 2) | MERLFCVPCGYGTTDPLTYPGPWRHCQQQNWPQNMGAPIFLARLRVPANVSQSCMNPYNRAQLQAVSTQMDPNLSLWLRSVHTTEVGVQVSLRVDKSVQCSQGSQTLHSSSLSDRTSSRKPTEAWEVGRRALIRRPQDGEDEESQEELTGPTEASQLLLPTWSRDREEQFPRLKELGEEYAHSPQDRKGKQFLELKYGYFHCKDCKRRWESAYVWCISGTNKVYFKQLCNKCQKSFNPYRVEEIQCQTCLRVCCSCSPKKRHIDVRRPHRQELCGHCKDKKFSCSVFFSLK | mRNA-binding protein required for maternal mRNA storage, translation and degradation during oocyte maturation. Probably promotes formation of some phase-separated membraneless compartment that stores maternal mRNAs in oocytes: acts by undergoing liquid-liquid phase separation upon binding to maternal mRNAs (By similari... |
C3VPR6 | NLRC5_MOUSE | Protein NLRC5 | MDAESIRLNNENLWAWLVRLLSKNPEWLSAKLRSFLPTMDLDCSYEPSNPEVIHRQLNRLFAQGMATWKSFINDLCFELDVPLDMEIPLVSIWGPRDEFSKQLGAGEESCPGPQLYHGAKRPFQSYGSSPRRKNSKKQQLELAKKYLKLLKTSAQQWHGGVCPGAWLTPHSPQTYIPPVLQWSRATAPLDAQEGATLGDPEAADNIDVSIQDLFSFKAHKGPRVTVLLGKAGMGKTTLAYRLRWRWAQGQLDRFQALFLFEFRQLNMITQLPTLPQLLFDLYLMPESEPDAVFQYLKENAQEVLLIFDGLDEALHADSVG... | Probable regulator of the NF-kappa-B and type I interferon signaling pathways. May also regulate the type II interferon signaling pathway. Plays a role in homeostatic control of innate immunity and in antiviral defense mechanisms. |
C3W4R6 | PA2A1_MACLB | Acidic phospholipase A2 1 (Vl-PLA2-1) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) | MRTLWIVAVWLMGVEGDLSQFGDMINKKTGTFGLFSYIYYGCYCGWGGKGKPQDATDRCCFVHDCCYGSVNGCDPKLSTYSYSFQNGDIVCGDDDPCLRAVCECDRVAAICFGENMNTYDKKYMLYSLFDCKEESEKC | Snake venom phospholipase that inhibits ADP- and collagen-induced human platelet aggregation. This inhibition is completely inhibited by abolition of catalytic activity in case of collagen as inducer and partially inhibited in case of ADP as inducer. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups ... |
C3W947 | CTSR_GEOSE | Transcriptional regulator CtsR (Class three stress gene repressor) | MPNISDIIEQYLKQVLNMSDQDIVEIKRSEIANKFRCVPSQINYVINTRFTLERGYIVESKRGGGGYIRIMKVKTKSEAQLIDQLLELIDHRISQSSAEDVIKRLMEEKVISEREAKMMLSVMDRSVLYIDLPERDELRARMLKAMLTSLKYK | Controls the expression of the cellular protein quality control genes clpC, clpE and clpP, as well as mcsA and mcsB, by acting as a repressor of these class III stress genes. After heat shock, CtsR is degraded by the ClpCP and ClpEP proteolytic systems, ensuring the derepression of clpE, clpP and the clpC operon. CtsR ... |
C4AMC7 | WASH3_HUMAN | Putative WAS protein family homolog 3 (Protein FAM39DP) | MTPVRMQHSLAGQTYAVPLIQPDLRREEAVQQMADALQYLQKVSGDIFSRISQQVEQSRSQVQAIGEKVSLAQAKIEKIKGSKKAIKVFSSAKYPAPERLQEYGSIFTGAQDPGLQRRPRHRIQSKHRPLDERALQEKDFPVCVSTKPEPEDDAEEGLGGLPSNISSVSSLLLFNTTENLGKKYVFLDPLAGAVTKTHVMLGAETEEKLFDAPLSISKREQLEQQVPENYFYVPDLGQVPEIDVPSYLPDLPGITNDLMYIADLGPGIAPSAPGTIPELPTFHTEVAEPLKVDLQDGVLTPPPPPPPPPPAPEVLASAPP... | Acts as a nucleation-promoting factor at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. Involved in endocytic trafficking of EGF. Involved in transfer... |
C4B644 | CPVDH_PSEAH | Vitamin D(3) 25-hydroxylase (EC 1.14.15.15) (Cytochrome P450) | MALTTTGTEQHDLFSGTFWQNPHPAYAALRAEDPVRKLALPDGPVWLLTRYADVREAFVDPRLSKDWRHTLPEDQRADMPATPTPMMILMDPPDHTRLRKLVGRSFTVRRMNELEPRITEIADGLLAGLPTDGPVDLMREYAFQIPVQVICELLGVPAEDRDDFSAWSSVLVDDSPADDKNAAMGKLHGYLSDLLERKRTEPDDALLSSLLAVSDEDGDRLSQEELVAMAMLLLIAGHETTVNLIGNGVLALLTHPDQRKLLAEDPSLISSAVEEFLRFDSPVSQAPIRFTAEDVTYSGVTIPAGEMVMLGLAAANRDAD... | Hydroxylates vitamin D(3) into 25-hydroxyvitamin D(3) and 1-alpha,25-dihydroxyvitamin D(3), its physiologically active forms. It first hydroxylates the C-25 position of vitamin D(3) to form 25-hydroxyvitamin D(3), then subsequently hydroxylates the C-1-alpha position to form 1-alpha,25-dihydroxyvitamin D(3). Also displ... |
C4JYG6 | ARO1_UNCRE | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10);... | MATPTVIKILGRDSIVADPGIWKRHVAQDLLTNCPSSTYILISDTTLTPLYVPSFQQAFEAAASSVTPKPRLLTYAIPPGEVSKSRQTKAEIEDWMLSRQPPCGRDTVIIALGGGVIGDLIGYVSATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTTHGKNLIGAIWQPEKIYLDMEFLNTLPEREFINGMAETAAISSEEDFAALERNADAILAAVKSENTTERPRFSGIQEILKLTILASARFKADVVSKDEREGGLRNLLNFGHSIGHAIEGILAPQILHGECVAIGMVKEAELARHLGILKSVAVSRLVKCLASY... | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
C4LSS0 | ARGI_ENTH1 | Arginase (EhArg) (EC 3.5.3.1) | MQFEKVTYIAVPQKYGQKKVGVEEGPKFLEKLGFMNVLEQVAKSVNKKTITEPKTPQELGVTNARNLNEVESVNIELRDTIAKEYDVNNLLINIGGDHSIGLGTIAGVVKAMKPNARVGVVWFDAHPDMNTPENSPSGNIHGMPLACAVGLGPQRLTSIMPHYITPKDIMYVGIRSIDVGEQFEIQDKHIDHFTAEDVKRVGMKEVIEAINKKFVDYDVIHLSFDIDGIDPEFILGTGTPVPKGISLEDSLYFMSEMGKMKKLHSVDIVEYNPKIEEEITGKNVLKCISSLFGIKC | Catalyzes the hydrolysis of L-arginine into urea and L-ornithine, which is a precursor for polyamine biosynthesis. By depleting host L-arginine, a substrate for nitric oxide synthase (NOS), prevents the production of nitric oxide (NO) by host activated macrophages, and thus allows the parasite to evade host immune resp... |
C4LVG4 | ACTP_ENTH1 | Actophorin (EhActo) | MAGIQLADEVTSVYNDFKLSHKYRYIVFKMNDGMTEVVVEKTAEKNATYDDFLKDLPEKSARYAVYDLEYDTPEGLRQKIIFYLWTPEGCKIREKMLYSATKATIKQALVGLSAEIQATDAGELNLDEVIAKVKTISK | Actin-binding protein that severs actin filaments. |
C4LZC2 | PFP_ENTH1 | Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (EC 2.7.1.90) (6-phosphofructokinase, pyrophosphate dependent) (PPi-dependent phosphofructokinase) (PPi-PFK) (Pyrophosphate-dependent 6-phosphofructose-1-kinase) | MSLSALHKYRLQYKPVLPKHIADIDNITIEEGAKTQSAVNQKELSELFKHTYGLPICNIVAGKNADIHRVIRCGFILSGGPAAGGHNVVAGLFDGLMKGNKENKLYGFRCGAGGILSNDYIEITAELVDKHRNTGGFDLVGSGRTKIETEEQFATAFKHITALKLNAMVVVGGDDSNTNAALLAEYFAAHGSDCVFVGVPKTIDGDLKNQYIETSFGFDTACKTYSELIGNIQRDAISSRKYWHFIKVMGRSASHIALEAALETQPTYCIISEEVEDKKMTVSQIASEIADIVIERHKKGLNFGVVLIPEGLVEFIPEVK... | Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenes... |
C4M1P9 | DBR1_ENTH1 | Lariat debranching enzyme (EC 3.1.4.-) (Intron debranching enzyme) (RNA lariat debranching enzyme) | MATEQIQHIAIVGCVHGKYREMYRQLSEYEKSTGKEISFVICTGDMQTLRYEADLVYLKVPPKYKQMGDFHLYYEGKEKAPYLTLFIGGNHESSNVLLHLYNGGFVCFNMYYLGVCSCININGLRIVGVSGIYKSFDEKKPYTYPPSPNDVVSLFHTRNYVIQMLSNLSQSSQIDISLSHDWPQGIVMKGNYKQLYRFQPGFKKDGASLGSPINKVILNTLKPKYWISGHMHCEYHAEEGPTHFIALGKIGYKNAISYLDLPLKQKTDLEYDKDWVCNLIMTWPAFSNKAQFPDLSYSISELLSKRTKELDKKIIELWEK... | Cleaves the 2'-5' phosphodiester linkage at the branch point of excised lariat intron RNA and converts them into linear molecules that can be subsequently degraded, thereby facilitating ribonucleotide turnover. |
C4M4P4 | COAA_ENTH1 | Coactosin | MSGFDLSEVAGPVAEVIDDKNEEVEFVVFGVQTQPNKLVVDAKGKGGLEEVKAALKEDALQFAYYRTISGDEESKRVKFVFISWAGEGIKKPKLRAVMSILKGDVKNVINNFHIELHATSLDDLVEDEIAAKIKKAGGADYSFNTTSN | Actin-binding protein which is involved in F-actin stabilization. May play a role during phagocytosis and pseudopod formation by contributing to the maintenance of F-actin. |
C4M4T9 | DPNP_ENTH1 | 3'(2'),5'-bisphosphate nucleotidase (EC 3.1.3.7) (3'-phosphoadenosine 5'-phosphatase-1) (PAP phosphatase-1) (Inositol-1,4-bisphosphate 1-phosphatase) (EC 3.1.3.57) | MSFDKELALALEIVQVSCKITTSVAEHTLTDQTQIKNDKSPVTVGDYSVQAYVNKKIHETFPEDQIVAEEDTKTIPEDIFAKVCKHVQIYSDMKDDEIRKSIDLGNSTGGKGRHWVLDPIDGTLGFLRREQYAVCLAFMIDGDIKVGVLGCPNFEGGLIVAAQKGCGAKMFSVNDIKNGKDIHVSTTPKTSDMCFCESVEVSHTDQSRSKTITERLQVTKPPVRMDSQCKYMAIASGRADVYLRLPRNLSYQEKIWDHAAGYLIVKEAGGKVTDIYGNDLDFSLGRTLCNNHGIVASNGILHEETVNVVKDVLSDLK | Converts 3'(2')-phosphoadenosine 5'-phosphate (PAP) to AMP. Is also able to hydrolyze inositol 1,4-bisphosphate but with less efficiency. |
C4M633 | INPP_ENTH1 | Inositol polyphosphate 1-phosphatase (EhIPPase) (EC 3.1.3.57) (3'(2'),5'-bisphosphate nucleotidase) (EC 3.1.3.7) | MQTSLFEFANVLITAVKEASYSISKFKEEVEIKYKSDGSEVTQVDTQSQQIIFSIIKNKYPTINIIGEEDVENGIPDNQLPTITQLSFGSLENKIININDIIIYVDPLDGTDCYTHKQYDSVCVLVGVTYKGKPMIGIVSKPFYNNEITFAIENYISSISLQPLNDKIIFVCSKKNDIQHLIKSFPDPYEVKYKGGSGAKMMAIIHQEADIYYHPLIQSCTWDTLAAQVILEAQGGIVCDIYGNPLCYPSSKKESMRHKKGVLCLSPRAKKYLPYMLSISKTILL | Catalyzes the hydrolysis of the 1-position phosphate from inositol 1,4-bisphosphate. Is also able to convert 3'(2')-phosphoadenosine 5'-phosphate (PAP) to AMP but with less efficiency. |
C4N147 | FABP1_DORPE | Sodium/calcium exchanger regulatory protein 1 (ReP1-NCXSQ) (Fatty acid-binding protein 1) (Na(+)/Ca(2+) exchanger regulatory protein 1) | MAADLAGKWILESSENFDDYMKAVGVGMVMRKMANAATPTQEIKIDGDSWSIKTSTTFKTTDISFTIGQEFDETTGDGRKIKTTCKIDGNAMIQDQKGSPDSILSREVKDGKMHMILKVNDVVCTRIYKRVD | Binds and may transport fatty acids such as palmitoleate. Also binds poly-phosphoinositides including phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), and phosphatidic acid. When phosphorylated, stimulate... |
C4QX80 | PSD1_KOMPG | Phosphatidylserine decarboxylase proenzyme 1, mitochondrial (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase 1 beta chain; Phosphatidylserine decarboxylase 1 alpha chain] | MPNRSFGVFPSVIYETRLGLSHQMRRPIGQPLSKLSQVSQPNQILQRNYQYKFPRIPRPKRNVLYYTFKRPQLSSATILRTVPSKIRNFSSRAKSKVKSSGRRRKFMSRWLALSSISVVLYGVVNKIKHKGIQRNSSLEPDENHSVKPNSWTLYAYSTLPLKAISRVWGQFNSFELPIWLRSPSYKFYAYVFGVNLDEVAEPDLSKFRNLGEFFYRTIKPETRPIDIDAEMVSPCDGKVLKFGIIENGEIEQVKGMTYSINALLGQQKLAAPVHRINYQLDDDDVVRRHEEFARLNGISYTIDDIIGGRGENIHHSYMNQ... | Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:19656201}. |
C4R4R8 | ARO1_KOMPG | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10);... | MSGLIEKVSILRNDSIHVGYNMSSHIVDEILTKKASSTYVLITDSNIVKMGHLQTFVDEFNRLIPSKRPGSRILTYVVPPGEANKNRATKAAIEDYLLEKGCTRDTFILAIGGGVIGDMIGYVAATFMRGVRFVQIPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPDYVFVDVAFLETLPEREFINGMAEVVKTAAIWNEQEFSRLETYSKRFLKVIRDRRVDDSVDLTSLKEHIIKLVLESIKVKAEVVTLDEREGGLRNLLNFGHSIGHAIEAILTPQALHGECVSIGAVLEAELSRYLGILSPVAVSRLYKCFA... | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
C4Y9D5 | ARO1_CLAL4 | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10);... | MSQVEKVSILGSDSIHVGYGIQDHIVEETLTNLKSSTYVIITDSNMEATAPYQTLSSKFEAGLKEFRPESRLFYYAVSPGENNKSRETKAQVEDFLLQKGCTRDTVIIAVGGGVVGDMIGFVAATFMRGVRVVQVPTTLLAMVDSSIGGKTAVDTPLGKNFVGAFHQPKYVFVDVSFLTTLPTRQFINGMAEVVKTAAIWNEEEFTRLENFAKTFIAVVTSDNIDLATIKDDLVKTVLESIRVKADVVSADEKESSLRNLLNFGHTIGHAIEAIVTPQALHGECVAVGMVKEAELARYWGVLSPVAVARLVNCIAAYNLP... | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
C4YMW2 | THI5_CANAW | 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase (HMP-P synthase) (Hydroxymethylpyrimidine phosphate synthase) (EC 2.-.-.-) (Thiamine biosynthesis protein 5) (Thiamine pyrimidine synthase) | MSTNKITFLLNWEAAPYHIPVYLANIKGYFKDENLDIAILEPSNPSDVTELVGSGKVDMGLKAMVHTLAAKARGFPVTSIGSLLDEPFTGICYLEGSGITSDFQSLKGKRIGYVGEFGKIQVDELTKHYGMTPDDYVAVRCGMNVAKYILEGTIDCGIGIECIQQVELEEALKEQGKDSNDAKMLRIDKLAELGCCCFCTILYIANDKFIAENPQAVKKFLKAIKRATDYMLAHPREAWAEYGNFKPTMQTDLNTKKFQRCYAYFSESLYNVHRDWRKVNNYGKRLDILPENYVPNYTNEYLSWPEPKEVDDPEKAQDLM... | Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. The enzyme... |
C4ZQN7 | HCHA_ECOBW | Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase) | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKLLTGDSPFAANALGKLAAQEMLAAYAG | Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and la... |
C5C7X8 | GYRB_MICLC | DNA gyrase subunit B (EC 5.6.2.2) | MVDAMPENPAEEPTAASAAPNPEAVPDAVGQPEAPVKDRKVPGEYGASAITVLEGLEAVRKRPGMYIGSTGPRGLHHLVYEVVDNSVDEALAGYATGIDVTLQADGGVRVADDGRGIPVDLHPTEGRPTVEVVMTILHAGGKFGGGGYAVSGGLHGVGISVVNALSRRVDTEVRRQGHVWRMSFADGGVPQGELVKGEATDATGTVQTFYPDAEIFDSIEFDYETLRARFQQMAFLNKGLRITLTDERVQESNEVVDDEIAGEGAAGEDVAENGLAEDAEQEPQRRSVTYLYENGLLDYVQHLNSAKKVEYVHDDVIAFE... | A type II topoisomerase that negatively supercoils DNA in an ATP-dependent manner. About 140 bp of DNA wraps around gyrase in the presence or absence of ATP, when ATP is added negative supercoils are made. A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent m... |
C5C7X9 | GYRA_MICLC | DNA gyrase subunit A (EC 5.6.2.2) | MSDETTPQTPDEPVEGAPIPGTPQTGLDIEVEHYVLPEGAADKVEPVDLESEMKRSYLDYAMAVIVGRALPDVRDGLKPVHRRVLYAMYDGGYRPDRAFNKSARVVGDVMGNYHPHGDTAIYDALVRLIQDWVQRYPLALGQGNFGSPGNDGAAAQRYTETKMAPLAMEMVRDIDEDTVDMQDNYDGKQQEPVVLPARYPNLLVNGSSGIAVGMATNIPPHNMREVAAGVQWYLEHPEATREELLEALLARVHGPDFPTGAQILGRKGIEEVYRTGRGPITMRAVVNVEEIQGRTCLVVTELPYMTNPDNLAAKIAEMVR... | A type II topoisomerase that negatively supercoils DNA in an ATP-dependent manner. About 140 bp of DNA wraps around gyrase in the presence or absence of ATP, when ATP is added negative supercoils are made. A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent m... |
C5DN02 | ARO1_LACTC | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10);... | MKVELSKVPILGKDVVHVGFDIADHIVDTIFQSCPSSTYVVINDTNVEKIPHYVDLCGELQAKLKSGSRILQYSVKPGEAHKTREQKAAIEDYLLSEGCTRDTVIIAVGGGVIGDMIGYVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAVDTPLGKNFIGAFWQPQFVFVDIKWLETLPKREFINGIAEVIKTACIWNAEEFARLEENADLFLQVVNGSKTTQVSVQGQVHELSLTNIDAMLEHVYRLVLESIKVKTHVVSSDEREAGLRNLLNFGHTIGHAYEAILTPQALHGECVSIGMIKEAELSRYLNILSPTQV... | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
C5DRQ1 | MMM1_ZYGRC | Maintenance of mitochondrial morphology protein 1 | MESNYTGMDGNWALNGTVSVGNGTLISVDEFLHNALPMHLQALFQDGNSQGPLLTMEDLEKAIEFKRASQELVNDNVLAPDGLFVELLRQQEKTLPRLISATSNTQGSFSSWSFAQGLIVGQVSVVLVLIFFIKFFIFSDSSTKTNPNPAKNSSSTNSLSGLSSESRSFISPHFFTSIMNRKGNEQAESNDDENERSRQIDDILEKTYYNVDTHPAESLDWFNVLIGQTIQQLREEAWKKDNIVYSLNAFIERKAQELPSYLDSIKITELDIGHDFPIFSNCRIQYSPNSNGRKLEAKIDIDLNDRLAVGIETRLLLNYP... | Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria (By simi... |
C5DVG6 | ARO1_ZYGRC | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10);... | MVKFEKVPILGKESIHVGYDIHTDMVQTIINDCRSSTYVVVNDTNLSKVPYCQDFVQELRSSLPEGSRLLQYAVKPGEANKTRSTKADIEDYLLSKGCTRDTVIIAIGGGIIGDMVGFVAATFMRGVRVVQVPTSLLAMVDSSIGGKTAVDTPLGKNFIGAFWQPQFVLVDVKWLETLPRREFINGMAEVIKTACIWNGLEFERLESNAELFLRVVNGSKVIKVNGLSTGEVNDIHYTNIEAMLEHTFKLVLESIKVKAEVVSSDERESSLRNLLNFGHSVGHAYEAILTPQALHGECVSIGMIKEAELSRYLGILSPTQ... | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
C5FQ73 | ARO1_ARTOC | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10);... | MEQPTTIQILGRDSIVADFGIWRRHVARDLLETLSSSTYILISDTNIAPLYVPEFERAFEEAAAEKSPKPRLLTYKIAPGESSKGRETKAEIEDWMLSCQPPCGRDTVLIALGGGVIGDLAGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPEKIYLDMEFLNTLPQREFTNGMAEVIKTAAISSETTFAELEQNADAIAAALKTENTPERSRFSGIQEILKRTILASARFKADVVSKDEREGGLRNLLNFGHSIGHAIEAILAPQILHGECVAIGMIKEVELARYLGILKGAAVARLAKCL... | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
C5G6D7 | CABC2_BACT4 | Chondroitin sulfate ABC exolyase (EC 4.2.2.21) (Chondroitin ABC exoeliminase) (Chondroitin ABC lyase II) (Chondroitin sulfate ABC lyase II) (ChS ABC lyase II) (Chondroitinase ABC II) (cABC II) (Exochondroitinase ABC) | MLILSFLCPAFLNAQIVTDERMFSFEEPQLPACITGVQSQLGISGAHYKDGKHSLEWTFEPNGRLELRKDLKFEKKDPTGKDLYLSAFIVWIYNEQPQDAAIEFEFLKDGRKCASFPFGINFKGWRAAWVCYERDMQGTPEEGMNELRIVAPDAKGRLFIDHLITATKVDARQQTADLQVPFVNAGTTNHWLVLYKHSLLKPDIELTPVSDKQRQEMKLLEKRFRDMIYTKGKVTEKEAETIRKKYDLYQITYKDGQVSGVPVFMVRASEAYERMIPDWDKDMLTKMGIEMRAYFDLMKRIAVAYNNSEAGSPIRKEMRR... | Broad-specificity glycosaminoglycan lyase, which acts in an exolytic fashion degrading chondroitin sulfates and dermatan sulfate to yield only disaccharide products. Has a preference for chondroitin 4-sulfate over chondroitin 6-sulfate. Has extremely low activity against hyaluronic acid. Is not active against acharan s... |
C5G8R4 | ARO1_AJEDR | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10);... | MGVPTKISILGRESIVADFGIWRNYVAKDLLNSCSSSTYILISDTNITPLYLDGFQKSFDDAAANLSPKPRLLTYEIPPGESSKSRETKAGIEDWMLTRQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALEDDAEIILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVAIGMVKEAELARHLGILNNVSVSRISKCL... | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
C5H429 | DBR2_ARTAN | Artemisinic aldehyde Delta(11(13)) reductase (EC 1.3.1.92) | MSENPPTLFSAYKMGNFNLSHRVVLAPMTRCRAINAIPNEALVEYYRQRSTAGGFLITEGTMISPSSAGFPHVPGIFTKEQVEGWKKVVDAAHKEGAVIFCQLWHVGRASHQVYQPGGAAPISSTSKPISKKWEILLPDATYGTYPEPRPLAANEILEVVEDYRVAAINAIEAGFDGIEIHGAHGYLLDQFMKDGINDRTDEYGGSLENRCKFILQVVQAVSAAIATDRVLIRISPAIDHTDAMDSDPRSLGLAVIERLNKLQFKLGSRLAYLHVTQPRYTADGHGQTEAGANGSEEEVAQLMKTWRGAYVGTFICCGGY... | Involved in the biosynthesis of the antimalarial endoperoxide artemisinin. Catalyzes the double bond reduction of artemisinic aldehyde to produce (11R)-dihydroartemisinic aldehyde. Also able to reduce 2-cyclohexen-1-one into cyclohexanone to a lesser extent. |
C5H431 | POLG_WSLV | Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2... | MATKGMNKSRARSRGVNMVAARVKNLAVKVKNKTKQSARGLRGFLLFLVAQIFWARKLTPQVKRLWRMVDKVQGLRILKNIRNIVTNLMKGLAGRKKKRSLTVPLVLLLIPLIAYSATVTRQRGLGLLLNVTFADVGKTYEVEGGNCSVNTLDAGKWCEDYVEYECVTLSEGEEPDDLDCWCYGVDNVRVTYGRCKSGGSRRSRRSAVITPHVDKGLTTRQEKWLPTKIGEQQLQKVEKWIMRNPLYALGAVALAYFVGTSNVQRVVIAILLLGIGPAYSTHCLGIPKRDFIRGLDGNTWVSVVLEQGSCVTLIADNKPS... | [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the... |
C5H8J1 | EME1B_ARATH | Crossover junction endonuclease EME1B (EC 3.1.22.-) (Essential meiotic endonuclease 1B) (AtEME1B) | MNDHILISDGEDQTTPLPSLSKRARKYPISAILISDSDPTPQKQPPESSFTPIFVPETPLSDDFSVVKCSFGSRALASNREDKFSGKRIISLDSEFEDSPRPETSKKNESVLAGLREPRFGLEAETSEAYYKNTRIPETNLDDDTSWMHEVSFRSSPTNDTIEVVSDQEKEDISVEKIGRKKKIRTTTLPVPGEALPKKRQSKEDKTSAMEEKKLRKEQERLEKAASKAEEAERKRLEKEKKKWEKGKLALKSIVAEIDTKVLEGSIGGLLLSRFSEKGITIHVGPNPIERSIVWTMTIPEDIAPLFPQGPKIPYLLLVY... | Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks, nicked Holliday junctions and also intact Holliday junctions with a reduced efficiency. Ma... |
C5I9X1 | ALDH1_ARTAN | Aldehyde dehydrogenase 1 (EC 1.2.1.-) (Artemisinic aldehyde oxidase) (Artemisinate synthase) (Dihydroartemisinic aldehyde oxidase) | MSSGANGSSKSASHKIKFTKLFINGEFVDSISGNTFDTINPATEEVLATVAEGRKEDIDLAVKAAREAFDNGPWPRMSGEARRKIMLKFADLIDENADELTTLEVIDGGKLFGPVRHFEVPVSSDTFRYFAGAADKIRGATLKMSSNIQAYTLREPIGVVGHIIPWNGPAFMFATKVAPALAAGCTMVIKPAEHTPLTVLFLAHLSKLAGVPDGVINVVNGFGKTAGAAVSSHMDIDMVTFTGSTEVGRTVMQAAALSNLKPVSLELGGKSPLIVFDDADVDKAAEFAILGNFTNKGEMCVAGSRVFVQEGIHDVFVKKL... | Involved in the biosynthesis of the antimalarial endoperoxide artemisinin (Ref.1, PubMed:27488942). Catalyzes the NAD(P)-dependent oxidation of artemisinin precursors, artemisinic and dihydroartemisinic aldehydes, thus producing artemisinic and dihydroartemisinic acids, respectively (Ref.1). Can use both NAD and NADP a... |
C5JKE6 | ARO1_BLAGS | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10);... | MGVPTKISILGRESIVADFGIWRNYVAKDLLNSCSSSTYILISDTNITPLYLDGFQKSFDDAAANLSPKPRLLTYEIPPGESSKSRETKAGIEDWMLTRQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALEDDAEIILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVAIGMVKEAELARHLGILNNVSVSRISKCL... | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
C5M1X2 | ARO1_CANTT | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10);... | MSIEKVPILGKETIHVGYGIQDHIVTEVVDNLASSTYVIVTDTNVEKTPQFSKLTNDFTKVLNEKRPDSRVLTYSVPPGENNKNRATKAAVEDFLLQQGCTRDTVIIAVGGGVIGDMIGFVAATFMRGVRVVQVPTTLLAMVDSSVGGKTAIDTPLGKNFIGAFHQPQYVFIDVSYLESLPTRQFINGMAEVVKTAAIWNEEEFTRLENFSKQFLSVVTAKNPDLLSIKEELVKTVLESVRVKAEVVSSDEKESSLRNLLNFGHTIGHAIEAIVTPEALHGECVSIGMIKEAELARYLGILPPVAVARLSKCLVAYGLPV... | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
C5MSH2 | POLG_SALVA | Genome polyprotein [Cleaved into: Leader protein (L); Capsid protein VP0; Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protein 2A (P2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.4.13); Protein 3A (P3A); VPg (P3B) (Protein 3B); Protein 3CD (EC 3.4.22.28); Protease 3C (EC 3.... | MEGSNGFSSSLAGLSSSRSSLRLLTHFLSLPTLPVNIYLNARRHSGWYRSPPTLPVNIYLNEQFDNLCLAALRYPGHKLYPSVHTLFPDVSPLKIPHSVPAFAHLVQRQGLRRQGNSITNIYGNGNDVTTDVGANGMSLPIAVGDMPTASTSEAPLGSNKGGSSTSPKSTSNGNVVRGSRYSKWWEPAAARALDRALDHAVDATDAVAGAASKGIKAGAAKLSNKLSGSQTTALLALPGNIAGGAPSATVNANNTSISSQALLPSVNPYPSTPAVSLPNPDAPTQVGPAADRQWLVDTLSWSETIAPLTVFSGPKALTPG... | [Leader protein]: Required for viral RNA replication and viral RNA encapsidation (By similarity). Does not have any proteolytic activity (By similarity). [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP3 (By similarity). Together they form an icosahedral capsid c... |
C5PA86 | ARO1_COCP7 | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10);... | MAAPTTIKILGRDSIVADFGIWKRHVADDLLTNCSSSTYILISDTTLTPLYVPSFQAAFENAASGLTPKPRLLTYAIPPGELSKSRQTKADIEDWMLSRQPPCGRDTVIIALGGGVIGDLIGYVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPHGKNLIGAIWQPQKIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEDFAALEKNADAILSAVKSENTPERPRFGGIQEILKLTILASARFKADVVSKDEREGGLRNLLNFGHSIGHAIEGILAPQILHGECVAIGMVKEAELARHLGLLKNVAVPRLVKCL... | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
C6HCG7 | ARO1_AJECH | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10);... | MGVPTKISILGRESIVADFGIWRNYVAKDLLSSCSSSTYILISDTNLTPLYLEGFQRSFEDAATNVSPKPRLLTYEIPPGESSKSRETKADIEDWMLARQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALERDAETILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVTADEREGGLRNLLNFGHSIGHSIEAILAPQVLHGECVSIGMVKEAELARHLGILNNVSVSRISKCL... | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
C6K2K4 | NETO2_RAT | Neuropilin and tolloid-like protein 2 (Brain-specific transmembrane protein containing 2 CUB and 1 LDL-receptor class A domains protein 2) | MALEQLCAVLKVLLITVLVVEGIAVAQKTQDGQNIGIKHVPATQCGIWVRTSNGGHFASPNYPDSYPPNKECIYILEAAPRQRIELTFDERYYIEPSFECRFDHLEVRDGPFGFSPLIDRYCGMKSPALIRSTGRFMWIKFSSDEELEGLGFRAKYSFIPDPDFTYLGGILNPIPDCQFELSGADGIVRSSQVEQEEKTKPGQAVDCIWTIKATPKAKIYLRFLDYQMEHSNECKRNFVAVYDGSSAIENLKAKFCSTVANDVMLKTGVGVIRMWADEGSRLSRFRMLFTSFVEPPCTSSTFFCHSNMCINNSLVCNGVQ... | Accessory subunit of neuronal kainate-sensitive glutamate receptors, GRIK2 and GRIK3. Increases kainate-receptor channel activity, slowing the decay kinetics of the receptors, without affecting their expression at the cell surface, and increasing the open probability of the receptor channels. Modulates the agonist sens... |
C6KEF6 | POLG_HKV1 | Genome polyprotein [Cleaved into: Leader protein (L); Capsid protein VP0; Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protein 2A (P2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.4.13); Protein 3A (P3A); VPg (P3B) (Protein 3B); Protein 3CD (EC 3.4.22.28); Protease 3C (EC 3.... | MMEGSNGFSSSLAGLSSSRSSLRLLTHLLSLPPPNRDARRHSGWYRSPPTLPVNVYLNEQFDNLCLAALRYPGCKLYPSVYTLFPDVSPFKIPQSIPAFAHLVQRQGLRRQGNPTTNIYGNGNEVTTDVGANGMSLPIAVGDMPTASSSEAPLGSNKGGSSTSPKSTSNGNVVRGSRYSKWWEPAAARALDRALDHAVDATDAVAGAASKGIKAGATKLSNKLAGSQTTALLALPGNIAGGAPSATVNANNTSISSQALLPSVNPYPSTPAVSLPNPDAPTQVGPAADRQWLVDTIPWSETTPPLTVFSGPKALTPGTYP... | [Leader protein]: Required for viral RNA replication and viral RNA encapsidation (By similarity). Does not have any proteolytic activity (By similarity). [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP3 (By similarity). Together they form an icosahedral capsid c... |
C6KEM4 | AADH2_MAIZE | Aminoaldehyde dehydrogenase 2 (ZmAMADH2) (EC 1.2.1.-) (4-trimethylammoniobutyraldehyde dehydrogenase AMADH2) (EC 1.2.1.47) (Aminobutyraldehyde dehydrogenase AMADH2) (EC 1.2.1.19) (Gamma-guanidinobutyraldehyde dehydrogenase AMADH2) (EC 1.2.1.54) | MAPPQTIPRRGLFIGGAWREPCLGRRLPVVNPATEATIGDIPAGTAEDVEIAVAAARDAFSRDGGRHWSRAPGAVRANFLRAIAAKIKDRKSELALLETLDSGKPLDEASGDMDDVAACFEYYADLAEALDGKQQSPISLPMENFKSYVLKEPIGVVGLITPWNYPLLMATWKVAPALAAGCTTILKPSELASVSCLELGAICMEIGLPPGVLNIITGLGPEAGAPLSSHSHVDKVAFTGSTETGKRIMISAAQMVKPVSLELGGKSPLIVFDDIGDIDKAVEWTMFGIFANAGQVCSATSRLLLHEKIAKKFLDRLVAW... | Dehydrogenase that catalyzes the oxidation of several aminoaldehydes. Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively. Catalyzes the oxidation of 4-... |
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