entry
stringlengths 6
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| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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C0HLL2
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PA2_PITAZ
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Phospholipase A2 (EC 3.1.1.4) (Pa-PLA2) (Phosphatidylcholine 2-acylhydrolase)
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MAFLVFAFLTLMAVETYGSLFQFRLMINYLTGKLPILSHSFYGCYCGAGGSGWPKDAIDWCCQVHDCCYGRMSASGCDPYFQPYNFSYINKNLQCVETDTSGCPRRICECDRLASICFQQHDATYNSSNIDPKRKGCGTKSPPCPN
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PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
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C0HLR3
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SCX1_CENBA
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Beta-toxin Cb1
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KEGYIVNHSTGCKYECYKLGDNDYCLRECKAQYGKGAGGYCYAFGCWCTHLYEQAVVWPLPKKTCN
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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 hNav1.6/SCN8A, affecting both the activation and inactivation processes. This toxin is active against mammals and lethal to mice.
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C0HLV2
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NEPRN_NEPVE
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Protein neprosin (Npr1) (EC 3.4.21.26) (Prolyl endopeptidase)
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MQAKFFTFVILSSVFYFNYPLAEARSIQARLANKPKGTIKTIKGDDGEVVDCVDIYKQPAFDHPLLKNHTLQMQPSSYASKVGEYNKLEQPWHKNGECPKGSIPIRRQVITGLPVVKKQFPNLKFAPPSANTNHQYAVIAYFYGNASLQGANATINIWEPNLKNPNGDFSLTQIWISAGSGSSLNTIEAGWQVYPGRTGDSQPRFFIYWTADGYTSTGCYDLTCPGFVQTNNYYAIGMALQPSVYGGQQYELNESIQRDPATGNWWLYLWGTVVGYWPASIYNSITNGADTVEWGGEIYDSSGTGGFHTTTQMGSGHFPTEGYGKASYVRDLQCVDTYGNVISPTANSFQGIAPAPNCYNYQFQQGSSELYLFYGGPGCQ
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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 fluid of the pitcher, and so likely functions in the digestion of their prey.
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C0HLV6
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LACS_TRAHI
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Laccase-S (ThLacc-S) (EC 1.10.3.2) (Benzenediol:oxygen oxidoreductase S) (Diphenol oxidase S) (Urishiol oxidase S)
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FQLNVIANMNNHTMLKQTSIHWHCHFQKGTNWADGHAFVNACPIASGHSFLYDFTAPDQHGTFWYHSHLSTQYCDGLRGHFVVYDPADPHHDLYDVDDEHTIITLADWYHVAAKLGHHFQLGADSTLINGSGRFAGDPTAHLTVIYVTQGKRYRFHLVSLSCDPNHVFSIDSNHMTVIEADAVSHEHCTVDSIQIYAGQRYSFHLTVDQDVDNYWIRAHPSFGTYSFHDGINSAIARY
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Lignin degradation and detoxification of lignin-derived products (By similarity). Has activity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS).
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C0HLV7
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LACF_GANAU
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Laccase (Galacc-F) (EC 1.10.3.2) (Benzenediol:oxygen oxidoreductase S) (Diphenol oxidase S) (Urishiol oxidase S)
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FQLNVIANNNNHTMLTQTTIHCHGFFQGTNSADGHAFVNCCPIASGHSFLYDFSHPDQHGTFCYHSHLSTQYCCGLRGHFVVYDPSDPHCGLYDVDHDSTVITLSDWYHVAAKLGHSFCLGADSTLINGSGRSTGDCAASLTVISVTQGKRYRFHLVSLSCDPNHTFSIDGHDMSVIEVDSIASQHVTVDSIQIFAGQRYSFVLTANQSINNYWIRANPSFGNIGFHDGINSAILRY
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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 hydroquinone, phenol, gallic acid, catechol, guaiacol, levodopa, 2,6-dimethoxyphenol (2,6-DMP), tyrosine, ferulic acid and veratryl alcohol.
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C0HLX7
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GLEC_CHOCI
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Galactose-binding lectin (CCL)
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TYAEVESFGVGQSATAVYTAPGDGRDLNITIDADGGYVIHMDYRFDWGGNPSTGKPWEDILILNSKPAQTWGPQQHVNNFYFTPGTHVTLGDKSNDGHFAIIADGIQVATYDHRLPVNSVKEVKFSTTAGSGTDIWDLLLLP
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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 uM/ml after 24 hours, MIC=0.9 uM/ml after 48 hours and MIC=0.6 uM/ml after 72 hours). Agglutinates Gram-negative and Gram-positive bacteria including E.coli, S.aureus and S.epidermidis, and inhibits biofilm formation by S.aureus and S.epidermidis. Displays hemagglutination activity towards all types of human erythrocytes (O, A and B) and rabbit erythrocytes.
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C0HLZ9
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BARA1_DROME
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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) (DIM5) (IM5); Immune-induced peptide 6 (DIM-6) (DIM6) (IM6); Immune-induced peptide 8 (DIM-8) (DIM8) (IM8)]
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MKSFGLIALAICGVICVAAEPQHTYDGRNGPHVFGSPGNQVYIRGQNEGTYSVPGVGGQFQNAPQRGEHVYTDEAGNTFVNRKNAGGPASHTISGPNFSAKNLGPNGAKSVGIPQRARRSPQFHVERPGRTVDVGNGGFYIQRGRRSPQLHVARPDRTVTIGNGGVYIQRSRRSPQFHVERPDRTVDFGNGGFSAQRFRRGINDARVQGENFVARDDQAGIWDNNVSVWKRPDGRTVTIDRNGHTIVSGRGRPAQHY
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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 posture upon Toll activation.
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C0HM00
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BARA2_DROME
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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) (DIM5) (IM5); Immune-induced peptide 6 (DIM-6) (DIM6) (IM6); Immune-induced peptide 8 (DIM-8) (DIM8) (IM8)]
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MKSFGLIALAICGVICVAAEPQHTYDGRNGPHVFGSPGNQVYIRGQNEGTYSVPGVGGQFQNAPQRGEHVYTDEAGNTFVNRKNAGGPASHTISGPNFSAKNLGPNGAKSVGIPQRARRSPQFHVERPGRTVDVGNGGFYIQRGRRSPQLHVARPDRTVTIGNGGVYIQRSRRSPQFHVERPDRTVDFGNGGFSAQRFRRGINDARVQGENFVARDDQAGIWDNNVSVWKRPDGRTVTIDRNGHTIVSGRGRPAQHY
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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 posture upon Toll activation.
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C0HM14
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PA2BD_CRODU
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Phospholipase A2 crotoxin basic subunit CBd (CTX subunit CBd) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
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HLLQFNKMIKFETRKNAIPFYAFYGCYCGWGGRGRPKDATDRCCFVHDCCYGKLAKCNTKWDIYRYSLKSGYITCGKGTWCEEQICECDRVAAECLRRSLSTYKYGYMFYPDSRCRGPSETC
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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-enzymatic and non-toxic subunit (CA1, CA2, CA3 or CA4). The complex acts by binding to a specific 48-kDa protein (R48) receptor located on presynaptic membranes, forming a transient ternary complex CA-CB-R48, followed by dissociation of the CA-CB complex and release of the CA subunit. At equilibrium, only the CB subunits remain associated with the specific crotoxin receptor. In addition to neurotoxicity, crotoxin has been found to exert myotoxicity, nephrotoxicity, and cardiovascular toxicity (By similarity). Moreover, anti-inflammatory, immunomodulatory, anti-tumor and analgesic effects of crotoxin have also been reported (By similarity). Monomer CBd: The basic subunit of crotoxin is a snake venom phospholipase A2 (PLA2) that exhibits weak neurotoxicity (10-fold less than the heterodimer) and very strong anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (By similarity). In addition, it shows the same effects described for the heterodimer and binds the nucleotide-binding domain (NBD1) of CFTR chloride channels and increases the channel current (By similarity). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
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C0HM45
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LEC_NARPS
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Mannose-specific lectin (Agglutinin) (NPA) (NPL) (NPL7) (NPn)
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DNILYSGETLSPGEFLNNGRYVFIMQEDCNLVLYDVDKPIWATNTGGLDRRCHLSMQSDGNLVVYSPRNNPIWASNTGGENGNYVCVLQKDRNVVIYGTARWATGTNIH
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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.
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C0HM55
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FSX1_UNCAX
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Fusexin 1 (Fsx1)
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MRRAALILAFVLFIGLSSATVTSADSITYNSGTSEFFDGDVFAIEVTADQSTDEIDIYLGASELSEKTDGEVNQDLSIEFTHQDSKLKYSTSTSDELRDIVTLTTYYEDGFDTEQDAIDAIKSDCYDLNQNGNGSGRYSRYYSVTSPVYDYEIYCFQKNEKLATPAYIDNPDEIFTAKAELQAGDKTIQSATLSNGDAGDGTVTDLGDSKISWNGNLDLGASEPENSRVIALYSNDFENGWRIGNKQSYEDYKTFIGGGDAYDLLIDWQDGTYTASEVEDELVNTDANQAVEEASSSTTDLVNAKVKDSSLDTGSFVYDTPELLSYPSFTVYVDAGENGYIEVTKPTGDPDIISTSSTEIKEGDEGTVTATVENVGDGEGEFSGRLSSCGEGFSIVDDQNTKNVGAGESVTYSFDVAFSSVSSESKEISGSCTFEVNGVESSDSTSVSVTGIQQSECNPGDQRREKNENDRWEIYTCQDNGLTYEYDVTCAEDEKAVAQGDNQFSCEKQDDDSGGGDNTGSDSGLFSNLFGGSGSGDLLTQVHTALSILAGLVAGFFGYRGARWIHGETDIKGGFKLESRNVSRVKRGSPVAGIVGAVLGFVVGYGVASVFHPVVQIIVVLGIAVGLYYFR
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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}.
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C0KTJ6
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GATDH_CERSP
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Galactitol 2-dehydrogenase (L-tagatose-forming) (EC 1.1.1.406) (Galactitol dehydrogenase) (GDH) (GatDH) (Galactitol:NAD(+) 5-oxidoreductase)
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MDYRTVFRLDGACAAVTGAGSGIGLEICRAFAASGARLILIDREAAALDRAAQELGAAVAARIVADVTDAEAMTAAAAEAEAVAPVSILVNSAGIARLHDALETDDATWRQVMAVNVDGMFWASRAFGRAMVARGAGAIVNLGSMSGTIVNRPQFASSYMASKGAVHQLTRALAAEWAGRGVRVNALAPGYVATEMTLKMRERPELFETWLDMTPMGRCGEPSEIAAAALFLASPAASYVTGAILAVDGGYTVW
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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 high stereoselectivity yielding the corresponding S-configurated alcohols. Shows high activity with D-threitol, xylitol, 1,2-hexanediol, 1,2-pentanediol, 2-hexanol, L-erythrulose, D-ribulose and acetoin. Specific for NAD(+).
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C0L2T8
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VM2C1_CRODO
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Zinc metalloproteinase/disintegrin (Metalloproteinase PII) (MPII) [Cleaved into: Snake venom metalloproteinase (SVMP) (EC 3.4.24.-); Disintegrin Cdc]
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MIQVLLVTICLAAFPYQGSSIILESGNVNDYEVIYPRKVTALPKGAVQPKYEDTMQYELKVNGQPVVLHLEKNKGLFSKDYSETHYSPDGRKITTNPSVEDHCYYHGRIENDADSTASISACNGLKGHFKLQGEMYIIEPLELSDSEDHAVFKLENVEKEDEAPKMCGVTQNWESNEPIKKASHLNLNPEHQRYVEIVIVVDHGMFTKYNGDSDKIRQRVHQMVNIMKESYRYMYIDISLAGIEIWSNKDLINVQPAAPNTLKSFGEWRETDLPKRKSHDNAQLLTSIDFNGQTIGIANIGAICDPKPSTRVVQDHSKINLRVALTMTHELSHNLGIHHDTGSCSCSGYSCIMSPVISDEPSKYFSDCSYIQCWNFIMNQKPQCILKKPLRTDTVSTPVSGNELLEARIECDCGSIENPCCYATTCKLRPGSQCAEGMCCDQCRFMKKGTVCRVSLVNKNDDTCTGQSADCPRNVLYG
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[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 breast cancer cell line MDA-MB-231) with a significant rate after 24 hours of incubation.
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C0LGF4
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FEI1_ARATH
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LRR receptor-like serine/threonine-protein kinase FEI 1 (EC 2.7.11.1)
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MMGICEMKSCCSWLLLISLLCSLSNESQAISPDGEALLSFRNAVTRSDSFIHQWRPEDPDPCNWNGVTCDAKTKRVITLNLTYHKIMGPLPPDIGKLDHLRLLMLHNNALYGAIPTALGNCTALEEIHLQSNYFTGPIPAEMGDLPGLQKLDMSSNTLSGPIPASLGQLKKLSNFNVSNNFLVGQIPSDGVLSGFSKNSFIGNLNLCGKHVDVVCQDDSGNPSSHSQSGQNQKKNSGKLLISASATVGALLLVALMCFWGCFLYKKLGKVEIKSLAKDVGGGASIVMFHGDLPYSSKDIIKKLEMLNEEHIIGCGGFGTVYKLAMDDGKVFALKRILKLNEGFDRFFERELEILGSIKHRYLVNLRGYCNSPTSKLLLYDYLPGGSLDEALHERGEQLDWDSRVNIIIGAAKGLSYLHHDCSPRIIHRDIKSSNILLDGNLEARVSDFGLAKLLEDEESHITTIVAGTFGYLAPEYMQSGRATEKTDVYSFGVLVLEVLSGKRPTDASFIEKGLNVVGWLKFLISEKRPRDIVDPNCEGMQMESLDALLSIATQCVSPSPEERPTMHRVVQLLESEVMTPCPSEFYDSSSD
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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).
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C0LGF5
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RGI5_ARATH
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LRR receptor-like serine/threonine-protein kinase RGI5 (EC 2.7.11.1) (Protein RECEPTOR OF RGF1 5) (Protein RGF1 INSENSITIVE 5)
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MERERSNFFFLFLFCSWVSMAQPTLSLSSDGQALLSLKRPSPSLFSSWDPQDQTPCSWYGITCSADNRVISVSIPDTFLNLSSIPDLSSLSSLQFLNLSSTNLSGPIPPSFGKLTHLRLLDLSSNSLSGPIPSELGRLSTLQFLILNANKLSGSIPSQISNLFALQVLCLQDNLLNGSIPSSFGSLVSLQQFRLGGNTNLGGPIPAQLGFLKNLTTLGFAASGLSGSIPSTFGNLVNLQTLALYDTEISGTIPPQLGLCSELRNLYLHMNKLTGSIPKELGKLQKITSLLLWGNSLSGVIPPEISNCSSLVVFDVSANDLTGDIPGDLGKLVWLEQLQLSDNMFTGQIPWELSNCSSLIALQLDKNKLSGSIPSQIGNLKSLQSFFLWENSISGTIPSSFGNCTDLVALDLSRNKLTGRIPEELFSLKRLSKLLLLGNSLSGGLPKSVAKCQSLVRLRVGENQLSGQIPKEIGELQNLVFLDLYMNHFSGGLPYEISNITVLELLDVHNNYITGDIPAQLGNLVNLEQLDLSRNSFTGNIPLSFGNLSYLNKLILNNNLLTGQIPKSIKNLQKLTLLDLSYNSLSGEIPQELGQVTSLTINLDLSYNTFTGNIPETFSDLTQLQSLDLSSNSLHGDIKVLGSLTSLASLNISCNNFSGPIPSTPFFKTISTTSYLQNTNLCHSLDGITCSSHTGQNNGVKSPKIVALTAVILASITIAILAAWLLILRNNHLYKTSQNSSSSPSTAEDFSYPWTFIPFQKLGITVNNIVTSLTDENVIGKGCSGIVYKAEIPNGDIVAVKKLWKTKDNNEEGESTIDSFAAEIQILGNIRHRNIVKLLGYCSNKSVKLLLYNYFPNGNLQQLLQGNRNLDWETRYKIAIGAAQGLAYLHHDCVPAILHRDVKCNNILLDSKYEAILADFGLAKLMMNSPNYHNAMSRVAGSYGYIAPEYGYTMNITEKSDVYSYGVVLLEILSGRSAVEPQIGDGLHIVEWVKKKMGTFEPALSVLDVKLQGLPDQIVQEMLQTLGIAMFCVNPSPVERPTMKEVVTLLMEVKCSPEEWGKTSQPLIKPSSS
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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.
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C0LGL9
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FEI2_ARATH
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LRR receptor-like serine/threonine-protein kinase FEI 2 (EC 2.7.11.1)
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MGICLMKRCCSWFLLISFLSALTNENEAISPDGEALLSFRNGVLASDGVIGLWRPEDPDPCNWKGVTCDAKTKRVIALSLTYHKLRGPLPPELGKLDQLRLLMLHNNALYQSIPASLGNCTALEGIYLQNNYITGTIPSEIGNLSGLKNLDLSNNNLNGAIPASLGQLKRLTKFNVSNNFLVGKIPSDGLLARLSRDSFNGNRNLCGKQIDIVCNDSGNSTASGSPTGQGGNNPKRLLISASATVGGLLLVALMCFWGCFLYKKLGRVESKSLVIDVGGGASIVMFHGDLPYASKDIIKKLESLNEEHIIGCGGFGTVYKLSMDDGNVFALKRIVKLNEGFDRFFERELEILGSIKHRYLVNLRGYCNSPTSKLLLYDYLPGGSLDEALHKRGEQLDWDSRVNIIIGAAKGLAYLHHDCSPRIIHRDIKSSNILLDGNLEARVSDFGLAKLLEDEESHITTIVAGTFGYLAPEYMQSGRATEKTDVYSFGVLVLEVLSGKLPTDASFIEKGFNIVGWLNFLISENRAKEIVDLSCEGVERESLDALLSIATKCVSSSPDERPTMHRVVQLLESEVMTPCPSDFYDSSSD
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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).
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C0LGP2
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MEE39_ARATH
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Probable LRR receptor-like serine/threonine-protein kinase MEE39 (EC 2.7.11.1) (Protein MATERNAL EFFECT EMBRYO ARREST 39)
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MKNLCWVFLSLFWFGVFLIIRFAEGQNQEGFISLDCGLPLNEPPYIESETGIQFSSDENFIQSGKTGRIPKNLESENLKQYATLRYFPDGIRNCYDLRVEEGRNYLIRATFFYGNFDGLNVSPEFDMHIGPNKWTTIDLQIVPDGTVKEIIHIPRSNSLQICLVKTGATIPMISALELRPLANDTYIAKSGSLKYYFRMYLSNATVLLRYPKDVYDRSWVPYIQPEWNQISTTSNVSNKNHYDPPQVALKMAATPTNLDAALTMVWRLENPDDQIYLYMHFSEIQVLKANDTREFDIILNGETINTRGVTPKYLEIMTWLTTNPRQCNGGICRMQLTKTQKSTLPPLLNAFEVYSVLQLPQSQTNEIEVVAIKNIRTTYGLSRISWQGDPCVPKQFLWDGLNCNITDISAPPRIISLNLSSSGLSGTIVSNFQNLAHLESLDLSNNSLSGIVPEFLATMKSLLVINLSGNKLSGAIPQALRDREREGLKLNVLGNKELCLSSTCIDKPKKKVAVKVVAPVASIAAIVVVILLFVFKKKMSSRNKPEPWIKTKKKRFTYSEVMEMTKNLQRPLGEGGFGVVYHGDLNGSEQVAVKLLSQTSAQGYKEFKAEVELLLRVHHINLVNLVGYCDEQDHFALIYEYMSNGDLHQHLSGKHGGSVLNWGTRLQIAIEAALGLEYLHTGCKPAMVHRDVKSTNILLDEEFKAKIADFGLSRSFQVGGDQSQVSTVVAGTLGYLDPEYYLTSELSEKSDVYSFGILLLEIITNQRVIDQTRENPNIAEWVTFVIKKGDTSQIVDPKLHGNYDTHSVWRALEVAMSCANPSSVKRPNMSQVIINLKECLASENTRISRNNQNMDSGHSSDQLNVTVTFDTDVKPKAR
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Receptor-like serine/threonine-kinase required during the endosperm development in seeds.
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C0LGP9
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IMK3_ARATH
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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)
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MEFITQNQAITSLSMINTDIDQPKASLRSRFLLHLIICLLFFVPPCSSQAWDGVVITQADYQGLQAVKQELIDPRGFLRSWNGSGFSACSGGWAGIKCAQGQVIVIQLPWKSLGGRISEKIGQLQALRKLSLHDNNLGGSIPMSLGLIPNLRGVQLFNNRLTGSIPASLGVSHFLQTLDLSNNLLSEIIPPNLADSSKLLRLNLSFNSLSGQIPVSLSRSSSLQFLALDHNNLSGPILDTWGSKSLNLRVLSLDHNSLSGPFPFSLCNLTQLQDFSFSHNRIRGTLPSELSKLTKLRKMDISGNSVSGHIPETLGNISSLIHLDLSQNKLTGEIPISISDLESLNFFNVSYNNLSGPVPTLLSQKFNSSSFVGNSLLCGYSVSTPCPTLPSPSPEKERKPSHRNLSTKDIILIASGALLIVMLILVCVLCCLLRKKANETKAKGGEAGPGAVAAKTEKGGEAEAGGETGGKLVHFDGPMAFTADDLLCATAEIMGKSTYGTVYKATLEDGSQVAVKRLREKITKSQKEFENEINVLGRIRHPNLLALRAYYLGPKGEKLVVFDYMSRGSLATFLHARGPDVHINWPTRMSLIKGMARGLFYLHTHANIIHGNLTSSNVLLDENITAKISDYGLSRLMTAAAGSSVIATAGALGYRAPELSKLKKANTKTDVYSLGVIILELLTGKSPSEALNGVDLPQWVATAVKEEWTNEVFDLELLNDVNTMGDEILNTLKLALHCVDATPSTRPEAQQVMTQLGEIRPEETTATTSEPLIDVPEASASTSQ
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Can phosphorylate AGL24. {ECO:0000269|Ref.9}.
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C0LGQ4
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MDIS2_ARATH
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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)
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MMGCGFHFPWFFFLIIGLQAPLSLSLTSQGSALLKFRARVNSDPHGTLANWNVSGINDLCYWSGVTCVDGKVQILDLSGYSLEGTLAPELSQLSDLRSLILSRNHFSGGIPKEYGSFENLEVLDLRENDLSGQIPPELSNGLSLKHLLLSGNKFSDDMRIKIVRLQSSYEVRLKKSPKLSPLAVLGCINRKLGHCVSRNRIIQVKKVEAIVFRIKATSRRFLKAFPSFLEETDIYKRRELLEETSNLAAEPAPSAPSPSPGIITEASPRSSGSFPAVTNAKKRRPPLVPPVPSPDKGSTSPDISKNQPQDNKQSKGSKHVWLYVVIAVASFVGLLIIVAVIFFCRKRAVKSIGPWKTGLSGQLQKAFVTGVPKLNRSELETACEDFSNIIETFDGYTVYKGTLSSGVEIAVASTAIAESKEWTRAMEMAYRRKIDTLSRINHKNFVNLIGYCEEDDPFNRMMVFEYAPNGTLFEHLHDKETEHLDWSARMRIIMGTAYCLQHMHGMNPPMAHTDFNSSEIYLTDDYAAKVSEIPFNLEARLNPKKHVSGDLEQTSLLLPPEPEANVHSFGVLMLEIISGKLSFSDEYGSIEQWASKYLEKDDLGEMIDPSLKTFKEEELEVICDVIRECLKTEQRQRPSMKDVAEQLKQVINITPEKATPRSSPLWWAELEILSSEAT
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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.
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C0LGQ5
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GSO1_ARATH
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LRR receptor-like serine/threonine-protein kinase GSO1 (EC 2.7.11.1) (Protein GASSHO 1) (Protein SCHENGEN 3)
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MQPLVLLLLFILCFSGLGQPGIINNDLQTLLEVKKSLVTNPQEDDPLRQWNSDNINYCSWTGVTCDNTGLFRVIALNLTGLGLTGSISPWFGRFDNLIHLDLSSNNLVGPIPTALSNLTSLESLFLFSNQLTGEIPSQLGSLVNIRSLRIGDNELVGDIPETLGNLVNLQMLALASCRLTGPIPSQLGRLVRVQSLILQDNYLEGPIPAELGNCSDLTVFTAAENMLNGTIPAELGRLENLEILNLANNSLTGEIPSQLGEMSQLQYLSLMANQLQGLIPKSLADLGNLQTLDLSANNLTGEIPEEFWNMSQLLDLVLANNHLSGSLPKSICSNNTNLEQLVLSGTQLSGEIPVELSKCQSLKQLDLSNNSLAGSIPEALFELVELTDLYLHNNTLEGTLSPSISNLTNLQWLVLYHNNLEGKLPKEISALRKLEVLFLYENRFSGEIPQEIGNCTSLKMIDMFGNHFEGEIPPSIGRLKELNLLHLRQNELVGGLPASLGNCHQLNILDLADNQLSGSIPSSFGFLKGLEQLMLYNNSLQGNLPDSLISLRNLTRINLSHNRLNGTIHPLCGSSSYLSFDVTNNGFEDEIPLELGNSQNLDRLRLGKNQLTGKIPWTLGKIRELSLLDMSSNALTGTIPLQLVLCKKLTHIDLNNNFLSGPIPPWLGKLSQLGELKLSSNQFVESLPTELFNCTKLLVLSLDGNSLNGSIPQEIGNLGALNVLNLDKNQFSGSLPQAMGKLSKLYELRLSRNSLTGEIPVEIGQLQDLQSALDLSYNNFTGDIPSTIGTLSKLETLDLSHNQLTGEVPGSVGDMKSLGYLNVSFNNLGGKLKKQFSRWPADSFLGNTGLCGSPLSRCNRVRSNNKQQGLSARSVVIISAISALTAIGLMILVIALFFKQRHDFFKKVGHGSTAYTSSSSSSQATHKPLFRNGASKSDIRWEDIMEATHNLSEEFMIGSGGSGKVYKAELENGETVAVKKILWKDDLMSNKSFSREVKTLGRIRHRHLVKLMGYCSSKSEGLNLLIYEYMKNGSIWDWLHEDKPVLEKKKKLLDWEARLRIAVGLAQGVEYLHHDCVPPIVHRDIKSSNVLLDSNMEAHLGDFGLAKVLTENCDTNTDSNTWFACSYGYIAPEYAYSLKATEKSDVYSMGIVLMEIVTGKMPTDSVFGAEMDMVRWVETHLEVAGSARDKLIDPKLKPLLPFEEDAACQVLEIALQCTKTSPQERPSSRQACDSLLHVYNNRTAGYKKL
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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 germination. Receptor of the peptide hormones CIF1 and CIF2 required for contiguous Casparian strip diffusion barrier formation in roots. Required for localizing CASP proteins into the Casparian strip following an uninterrupted, ring-like domain, to trigger endodermal differentiation and thus regulate potassium ion (K) homeostasis. Involved in the maintenance of water transport and root pressure. May also be involved in the regulation of suberin accumulation in the endodermis.
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C0LGQ9
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GHR1_ARATH
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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)
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MNLSRILLLSMFFLSAMGQLPSQDIMALLEFKKGIKHDPTGFVLNSWNDESIDFNGCPSSWNGIVCNGGNVAGVVLDNLGLTADADFSLFSNLTKLVKLSMSNNSLSGVLPNDLGSFKSLQFLDLSDNLFSSSLPKEIGRSVSLRNLSLSGNNFSGEIPESMGGLISLQSLDMSSNSLSGPLPKSLTRLNDLLYLNLSSNGFTGKMPRGFELISSLEVLDLHGNSIDGNLDGEFFLLTNASYVDISGNRLVTTSGKLLPGVSESIKHLNLSHNQLEGSLTSGFQLFQNLKVLDLSYNMLSGELPGFNYVYDLEVLKLSNNRFSGSLPNNLLKGDSLLLTTLDLSGNNLSGPVSSIMSTTLHTLDLSSNSLTGELPLLTGGCVLLDLSNNQFEGNLTRWSKWENIEYLDLSQNHFTGSFPDATPQLLRANHLNLSYNKLTGSLPERIPTHYPKLRVLDISSNSLEGPIPGALLSMPTLEEIHLQNNGMTGNIGPLPSSGSRIRLLDLSHNRFDGDLPGVFGSLTNLQVLNLAANNLSGSLPSSMNDIVSLSSLDVSQNHFTGPLPSNLSSNIMAFNVSYNDLSGTVPENLKNFPPPSFYPGNSKLVLPAGSPGSSASEASKNKSTNKLVKVVIIVSCAVALIILILVAILLFCICKSRRREERSITGKETNRRAQTIPSGSGGGMVVSAEDLVASRKGSSSEILSPDEKLAVATGFSPSKTSNLSWSPGSGDSFPADQQLARLDVRSPDRLVGELHFLDDSIKLTPEELSRAPAEVLGRSSHGTSYRATLDNGVFLTVKWLREGVAKQRKEFAKEVKKFSNIRHPNVVTLRGYYWGPTQHEKLILSDYISPGSLASFLYDRPGRKGPPLAWTQRLKIAVDVARGLNYLHFDRAVPHGNLKATNILLDGAELNARVADYCLHRLMTQAGTVEQILDAGILGYRAPELAASRKPLPSFKSDVYAFGVILLEILTGRCAGDVITGEQEGVDLTDWVRLRVAEGRGAECFDSVLTQEMGSDPVTEKGMKEVLGIALRCIRSVSERPGIKTIYEDLSSI
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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 scaffolding component. Seems to act in parallel with SRK2E/OST1 in the ABA signaling pathway which regulates stomatal movement. Binds ATP. Involved in the local and/or systemic stomatal responses (e.g. stomatal closure) to light stress.
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C0LGR3
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RGI3_ARATH
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LRR receptor-like serine/threonine-protein kinase RGI3 (EC 2.7.11.1) (Protein RECEPTOR OF RGF1 1) (Protein RGF1 INSENSITIVE 3)
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MPPNIYRLSFFSSLLCFFFIPCFSLDQQGQALLSWKSQLNISGDAFSSWHVADTSPCNWVGVKCNRRGEVSEIQLKGMDLQGSLPVTSLRSLKSLTSLTLSSLNLTGVIPKEIGDFTELELLDLSDNSLSGDIPVEIFRLKKLKTLSLNTNNLEGHIPMEIGNLSGLVELMLFDNKLSGEIPRSIGELKNLQVLRAGGNKNLRGELPWEIGNCENLVMLGLAETSLSGKLPASIGNLKRVQTIAIYTSLLSGPIPDEIGYCTELQNLYLYQNSISGSIPTTIGGLKKLQSLLLWQNNLVGKIPTELGNCPELWLIDFSENLLTGTIPRSFGKLENLQELQLSVNQISGTIPEELTNCTKLTHLEIDNNLITGEIPSLMSNLRSLTMFFAWQNKLTGNIPQSLSQCRELQAIDLSYNSLSGSIPKEIFGLRNLTKLLLLSNDLSGFIPPDIGNCTNLYRLRLNGNRLAGSIPSEIGNLKNLNFVDISENRLVGSIPPAISGCESLEFLDLHTNSLSGSLLGTTLPKSLKFIDFSDNALSSTLPPGIGLLTELTKLNLAKNRLSGEIPREISTCRSLQLLNLGENDFSGEIPDELGQIPSLAISLNLSCNRFVGEIPSRFSDLKNLGVLDVSHNQLTGNLNVLTDLQNLVSLNISYNDFSGDLPNTPFFRRLPLSDLASNRGLYISNAISTRPDPTTRNSSVVRLTILILVVVTAVLVLMAVYTLVRARAAGKQLLGEEIDSWEVTLYQKLDFSIDDIVKNLTSANVIGTGSSGVVYRITIPSGESLAVKKMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHGAGKGGCVDWEARYDVVLGVAHALAYLHHDCLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTGIDLAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLPGGAHLVKWVRDHLAEKKDPSRLLDPRLDGRTDSIMHEMLQTLAVAFLCVSNKANERPLMKDVVAMLTEIRHIDVGRSETEKIKAGGCGSKEPQQFMSNEKIINSHGSSNCSFAFSDDSV
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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 PLETHORA (PLT, e.g. PLT1 and PLT2). Links RGF peptides signal with their downstream components.
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C0LGT6
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EFR_ARATH
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LRR receptor-like serine/threonine-protein kinase EFR (EC 2.7.11.1) (Elongation factor Tu receptor) (EF-Tu receptor)
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MKLSFSLVFNALTLLLQVCIFAQARFSNETDMQALLEFKSQVSENNKREVLASWNHSSPFCNWIGVTCGRRRERVISLNLGGFKLTGVISPSIGNLSFLRLLNLADNSFGSTIPQKVGRLFRLQYLNMSYNLLEGRIPSSLSNCSRLSTVDLSSNHLGHGVPSELGSLSKLAILDLSKNNLTGNFPASLGNLTSLQKLDFAYNQMRGEIPDEVARLTQMVFFQIALNSFSGGFPPALYNISSLESLSLADNSFSGNLRADFGYLLPNLRRLLLGTNQFTGAIPKTLANISSLERFDISSNYLSGSIPLSFGKLRNLWWLGIRNNSLGNNSSSGLEFIGAVANCTQLEYLDVGYNRLGGELPASIANLSTTLTSLFLGQNLISGTIPHDIGNLVSLQELSLETNMLSGELPVSFGKLLNLQVVDLYSNAISGEIPSYFGNMTRLQKLHLNSNSFHGRIPQSLGRCRYLLDLWMDTNRLNGTIPQEILQIPSLAYIDLSNNFLTGHFPEEVGKLELLVGLGASYNKLSGKMPQAIGGCLSMEFLFMQGNSFDGAIPDISRLVSLKNVDFSNNNLSGRIPRYLASLPSLRNLNLSMNKFEGRVPTTGVFRNATAVSVFGNTNICGGVREMQLKPCIVQASPRKRKPLSVRKKVVSGICIGIASLLLIIIVASLCWFMKRKKKNNASDGNPSDSTTLGMFHEKVSYEELHSATSRFSSTNLIGSGNFGNVFKGLLGPENKLVAVKVLNLLKHGATKSFMAECETFKGIRHRNLVKLITVCSSLDSEGNDFRALVYEFMPKGSLDMWLQLEDLERVNDHSRSLTPAEKLNIAIDVASALEYLHVHCHDPVAHCDIKPSNILLDDDLTAHVSDFGLAQLLYKYDRESFLNQFSSAGVRGTIGYAAPEYGMGGQPSIQGDVYSFGILLLEMFSGKKPTDESFAGDYNLHSYTKSILSGCTSSGGSNAIDEGLRLVLQVGIKCSEEYPRDRMRTDEAVRELISIRSKFFSSKTTITESPRDAPQSSPQEWMLNTDMHTM
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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.g. jasmonic acid (JA) and salicylic acid (SA)). Reduces transformation by Rhizobium radiobacter probably by inducing plant defense during the interaction. Binding to the effector AvrPto1 from P.syringae blocks the downstream plant immune response while interaction with hopD2 decreases the phosphorylation level of EFR upon elf18 treatment. Specific endoplasmic reticulum quality control components (ERD2B, CRT3, UGGT and STT3A) are required for the biogenesis of EFR.
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C0LGU0
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PRK1_ARATH
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Pollen receptor-like kinase 1 (AtPRK1) (EC 2.7.11.1) (LRR receptor-like serine/threonine-protein kinase RLK)
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MPPMQARTLSVYNVMVPLVCLLLFFSTPTHGLSDSEAILKFKESLVVGQENALASWNAKSPPCTWSGVLCNGGSVWRLQMENLELSGSIDIEALSGLTSLRTLSFMNNKFEGPFPDFKKLAALKSLYLSNNQFGGDIPGDAFEGMGWLKKVHLAQNKFTGQIPSSVAKLPKLLELRLDGNQFTGEIPEFEHQLHLLNLSNNALTGPIPESLSMTDPKVFEGNKGLYGKPLETECDSPYIEHPPQSEARPKSSSRGPLVITAIVAALTILIILGVIFLLNRSYKNKKPRLAVETGPSSLQKKTGIREADQSRRDRKKADHRKGSGTTKRMGAAAGVENTKLSFLREDREKFDLQDLLKASAEILGSGCFGASYKAVLSSGQMMVVKRFKQMNNAGRDEFQEHMKRLGRLMHHNLLSIVAYYYRKEEKLLVCDFAERGSLAINLHSNQSLGKPSLDWPTRLKIVKGVAKGLFYLHQDLPSLMAPHGHLKSSNVLLTKTFEPLLTDYGLIPLINQEKAQMHMAAYRSPEYLQHRRITKKTDVWGLGILILEILTGKFPANFSQSSEEDLASWVNSGFHGVWAPSLFDKGMGKTSHCEGQILKLLTIGLNCCEPDVEKRLDIGQAVEKIEELKEREGDDDDFYSTYVSETDGRSSKGESCESISFA
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Receptor-like kinase involved in the control of pollen germination and pollen tube polar growth.
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C0LGU7
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MDIS1_ARATH
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Protein MALE DISCOVERER 1 (AtMDIS1) (Probable LRR receptor-like serine/threonine-protein kinase At5g45840) (EC 2.7.11.1)
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MGCRWNPIGFQFSCFMFLIITLQSRSSLSLESEGFVLLKFRARVDSDPHGTLANWNVSDHDHFCSWFGVTCVDNKVQMLNLSGCSLGGTLAPELSQLSELRSLILSKNKLSGDIPNEFASFAKLEFLDLRDNNLNGVVPPELNKVLTPENLLLSGNKFAGFMTVKFLRLQSLYKVQMNKNRELSSVSADVLDCVNRKLGYCVSRRSLITRNKAKAFVLRIRATSRHYMVRRESHGKNYVVNYHPSENETSIFKRRELLEETSNLAAMPAPDTPSPSPEIITIVFPRSSGSFPALTNAKKRIPPLIPPSSPPPLPTNNTIASDPPRKFEEKSKGFKDVWLYVVIGVAAFVAMLIIVAVIFFFRKRAVKSIGPWKTGLSGQLQKAFVTGVPKLNRSELETACEDFSNIIEAFDGYTVYKGTLSSGVEIAVASTAILETREWTRAMEMTYRRRIDTMSRVNHKNFINLIGYCEEDEPFNRMMVFEYAPNGTLFEHLHDKEMEHLDWNARTRIIMGTAYCLQYMHELNPPISHTKLVSSAIYLTDDYAAKVGEVPFSGQTGSKPRKPMSGDLDQSLLPLPPEPETNVYSFGVLMLEIISGKLSDSEEEGSILKWASKYLENDNLRDMIDPTLTTYKEEELEAICDVARHCLKLDESQRPKMKYVVQQLKEVINISQEQATPRLSPLWWAELEILSSEAT
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Involved in the pollen tube perception of the female signal.
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C0LGV1
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RGI2_ARATH
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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)
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MSLQMPIPRKKALTVSHFSITLSLFLAFFISSTSASTNEVSALISWLHSSNSPPPSVFSGWNPSDSDPCQWPYITCSSSDNKLVTEINVVSVQLALPFPPNISSFTSLQKLVISNTNLTGAISSEIGDCSELIVIDLSSNSLVGEIPSSLGKLKNLQELCLNSNGLTGKIPPELGDCVSLKNLEIFDNYLSENLPLELGKISTLESIRAGGNSELSGKIPEEIGNCRNLKVLGLAATKISGSLPVSLGQLSKLQSLSVYSTMLSGEIPKELGNCSELINLFLYDNDLSGTLPKELGKLQNLEKMLLWQNNLHGPIPEEIGFMKSLNAIDLSMNYFSGTIPKSFGNLSNLQELMLSSNNITGSIPSILSNCTKLVQFQIDANQISGLIPPEIGLLKELNIFLGWQNKLEGNIPDELAGCQNLQALDLSQNYLTGSLPAGLFQLRNLTKLLLISNAISGVIPLEIGNCTSLVRLRLVNNRITGEIPKGIGFLQNLSFLDLSENNLSGPVPLEISNCRQLQMLNLSNNTLQGYLPLSLSSLTKLQVLDVSSNDLTGKIPDSLGHLISLNRLILSKNSFNGEIPSSLGHCTNLQLLDLSSNNISGTIPEELFDIQDLDIALNLSWNSLDGFIPERISALNRLSVLDISHNMLSGDLSALSGLENLVSLNISHNRFSGYLPDSKVFRQLIGAEMEGNNGLCSKGFRSCFVSNSSQLTTQRGVHSHRLRIAIGLLISVTAVLAVLGVLAVIRAKQMIRDDNDSETGENLWTWQFTPFQKLNFTVEHVLKCLVEGNVIGKGCSGIVYKAEMPNREVIAVKKLWPVTVPNLNEKTKSSGVRDSFSAEVKTLGSIRHKNIVRFLGCCWNKNTRLLMYDYMSNGSLGSLLHERSGVCSLGWEVRYKIILGAAQGLAYLHHDCVPPIVHRDIKANNILIGPDFEPYIGDFGLAKLVDDGDFARSSNTIAGSYGYIAPEYGYSMKITEKSDVYSYGVVVLEVLTGKQPIDPTIPDGLHIVDWVKKIRDIQVIDQGLQARPESEVEEMMQTLGVALLCINPIPEDRPTMKDVAAMLSEICQEREESMKVDGCSGSCNNGRERGKDDSTSSVMQQTAKYLRSSSTSFSASSLLYSSSSSATSNVRPNLK
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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 PLETHORA (PLT, e.g. PLT1 and PLT2). Links RGF peptides signal with their downstream components.
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C0LGW2
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PAM74_ARATH
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Probable LRR receptor-like serine/threonine-protein kinase PAM74 (EC 2.7.11.1) (Protein PHOTOSYNTHESIS AFFECTED MUTANT 74)
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MDSPCWLLLLLLGAFAIIGCVQAQDQQEFISLDCGLPMTEPSSYTESVTGLRFSSDAEFIQTGESGKIQASMENDYLKPYTRLRYFPEERRNCYSLSVDKNRKYLIRARFIYGNYDGRNSNPIFELHLGPNLWATIDLQKFVNGTMEEILHTPTSNSLNVCLVKTGTTTPLISALELRPLGNNSYLTDGSLNLFVRIYLNKTDGFLRYPDDIYDRRWHNYFMVDDWTQIFTTLEVTNDNNYEPPKKALAAAATPSNASAPLTISWPPDNPGDQYYLYSHFSEIQDLQTNDTREFDILWDGAVVEEGFIPPKLGVTTIHNLSPVTCKGENCIYQLIKTSRSTLPSLLNALEIYTVIQFPRSETNENDVVAVKNIEAAYKLSRIRWQGDPCVPQKYAWDGLNCSNNTDVSKPPRVLSLNLSSSGLTGIIAAAIQNLTHLEKLDLSNNTLTGVVPEFLAQMKSLVIINLSGNNLSGPLPQGLRREGLELLVQGNPRLCLSGSCTEKNSKKKFPVVIVASVASVAIIVAVLVIIFVLSKKKSSTVGALQPPLSMPMVHDNSPEPSIETKKRRFTYSEVIKMTNNFQRVVGEGGFGVVCHGTINGSEQVAVKVLSQSSSQGYKHFKAEVDLLLRVHHTNLVSLVGYCDERDHLALIYEFLPKGDLRQHLSGKSGGSFINWGNRLRIALEAALGLEYLHSGCTPPIVHRDIKTTNILLDEQLKAKLADFGLSRSFPIGGETHISTVVAGTPGYLDPEYYQTTRLGEKSDVYSFGIVLLEIITNQPVIDQSRSKSHISQWVGFELTRGDITKIMDPNLNGDYESRSVWRVLELAMSCANPSSVNRPNMSQVANELKECLVSENLRENMNMDSQNSLKVSMSFDTELFPRAR
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Required for accurate photosynthesis. {ECO:0000269|Ref.4}.
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C0LGW6
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ERL1_ARATH
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LRR receptor-like serine/threonine-protein kinase ERL1 (EC 2.7.11.1) (Protein ERECTA-like kinase 1)
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MKEKMQRMVLSLAMVGFMVFGVASAMNNEGKALMAIKGSFSNLVNMLLDWDDVHNSDLCSWRGVFCDNVSYSVVSLNLSSLNLGGEISPAIGDLRNLQSIDLQGNKLAGQIPDEIGNCASLVYLDLSENLLYGDIPFSISKLKQLETLNLKNNQLTGPVPATLTQIPNLKRLDLAGNHLTGEISRLLYWNEVLQYLGLRGNMLTGTLSSDMCQLTGLWYFDVRGNNLTGTIPESIGNCTSFQILDISYNQITGEIPYNIGFLQVATLSLQGNRLTGRIPEVIGLMQALAVLDLSDNELVGPIPPILGNLSFTGKLYLHGNMLTGPIPSELGNMSRLSYLQLNDNKLVGTIPPELGKLEQLFELNLANNRLVGPIPSNISSCAALNQFNVHGNLLSGSIPLAFRNLGSLTYLNLSSNNFKGKIPVELGHIINLDKLDLSGNNFSGSIPLTLGDLEHLLILNLSRNHLSGQLPAEFGNLRSIQMIDVSFNLLSGVIPTELGQLQNLNSLILNNNKLHGKIPDQLTNCFTLVNLNVSFNNLSGIVPPMKNFSRFAPASFVGNPYLCGNWVGSICGPLPKSRVFSRGALICIVLGVITLLCMIFLAVYKSMQQKKILQGSSKQAEGLTKLVILHMDMAIHTFDDIMRVTENLNEKFIIGYGASSTVYKCALKSSRPIAIKRLYNQYPHNLREFETELETIGSIRHRNIVSLHGYALSPTGNLLFYDYMENGSLWDLLHGSLKKVKLDWETRLKIAVGAAQGLAYLHHDCTPRIIHRDIKSSNILLDENFEAHLSDFGIAKSIPASKTHASTYVLGTIGYIDPEYARTSRINEKSDIYSFGIVLLELLTGKKAVDNEANLHQLILSKADDNTVMEAVDPEVTVTCMDLGHIRKTFQLALLCTKRNPLERPTMLEVSRVLLSLVPSLQVAKKLPSLDHSTKKLQQENEVRNPDAEASQWFVQFREVISKSSI
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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 complex with TMM involved in the recognition of the stomatal regulatory peptides EPF1, EPF2 and EPFL9/STOMAGEN.
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C0LGX3
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HSL2_ARATH
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LRR receptor-like serine/threonine-protein kinase HSL2 (EC 2.7.11.1) (Protein HAESA-LIKE2)
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MLTNTNLFFFLSLLLLSCFLQVSSNGDAEILSRVKKTRLFDPDGNLQDWVITGDNRSPCNWTGITCHIRKGSSLAVTTIDLSGYNISGGFPYGFCRIRTLINITLSQNNLNGTIDSAPLSLCSKLQNLILNQNNFSGKLPEFSPEFRKLRVLELESNLFTGEIPQSYGRLTALQVLNLNGNPLSGIVPAFLGYLTELTRLDLAYISFDPSPIPSTLGNLSNLTDLRLTHSNLVGEIPDSIMNLVLLENLDLAMNSLTGEIPESIGRLESVYQIELYDNRLSGKLPESIGNLTELRNFDVSQNNLTGELPEKIAALQLISFNLNDNFFTGGLPDVVALNPNLVEFKIFNNSFTGTLPRNLGKFSEISEFDVSTNRFSGELPPYLCYRRKLQKIITFSNQLSGEIPESYGDCHSLNYIRMADNKLSGEVPARFWELPLTRLELANNNQLQGSIPPSISKARHLSQLEISANNFSGVIPVKLCDLRDLRVIDLSRNSFLGSIPSCINKLKNLERVEMQENMLDGEIPSSVSSCTELTELNLSNNRLRGGIPPELGDLPVLNYLDLSNNQLTGEIPAELLRLKLNQFNVSDNKLYGKIPSGFQQDIFRPSFLGNPNLCAPNLDPIRPCRSKRETRYILPISILCIVALTGALVWLFIKTKPLFKRKPKRTNKITIFQRVGFTEEDIYPQLTEDNIIGSGGSGLVYRVKLKSGQTLAVKKLWGETGQKTESESVFRSEVETLGRVRHGNIVKLLMCCNGEEFRFLVYEFMENGSLGDVLHSEKEHRAVSPLDWTTRFSIAVGAAQGLSYLHHDSVPPIVHRDVKSNNILLDHEMKPRVADFGLAKPLKREDNDGVSDVSMSCVAGSYGYIAPEYGYTSKVNEKSDVYSFGVVLLELITGKRPNDSSFGENKDIVKFAMEAALCYPSPSAEDGAMNQDSLGNYRDLSKLVDPKMKLSTREYEEIEKVLDVALLCTSSFPINRPTMRKVVELLKEKKSLE
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Receptor-like serine/threonine-kinase acting on substrates that controls floral organ abscission. Regulated by the 'INFLORESCENCE DEFICIENT IN ABSCISSION' (IDA) family of ligands.
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C0LLJ0
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IMA8_MOUSE
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Importin subunit alpha-8 (Karyopherin subunit alpha-7)
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MATSKAPKERLKNYKYRGKEMSLPRQQRIASSLQLRKTRKDEQVLKRRNIDLFSSDMVSQALVKEVNFTLDDIIQAVNSSDPILHFRATRAAREMISQENTPPLNLIIEAGLIPKLVDFLKATPHPKLQFEAAWVLTNIASGTSEQTRAVVKEGAIQPLIELLCSPHLTVSEQAVWALGNIAGDCAEFRDCVISNNAIPHLINLISKGIPITFLRNISWTLSNLCRNKDPYPSESAVRQMLPPLCQLLLHRDNEILADTCWALSYLTKGGKEYIHHVVTTGILPRLVELMTSSELSISIPCLHTIGNIVAGTDEQTQMAIDAGMLKVLGQVLKHPKTSIQVLAAWTMSNVAAGPRHQVEQLLCNLLPILVDLLRNAELKVQKEVVCTVINIATGASQDQLTLLAHSGILEPMLSLLSAPDLEVVIIVLDIISYLLQHIDNLQEKKRLYFQIEKFGGFEKIECLQHHHNISISNSALDIIEKYFCEDGDGDSLPGPGLRV
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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)
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MNAGILGVGKYVPEKIVTNFDLEKIMDTSDEWIRTRTGIEERRIARDDEYTHDLAYEAAKVAIKNAGLTPDDIDLFIVATVTQEATFPSVANIIQDRLGAKNAAGMDVEAACAGFTFGVVTAAQFIKTGAYKNIVVVGADKLSKITNWDDRTTAVLFGDGAGAVVMGPVSDDHGLLSFDLGSDGSGGKYLNLDENKKIYMNGREVFRFAVRQMGEASLRVLERAGLEKEDLDLLIPHQANIRIMEASRERLNLPEEKLMKTVHKYGNTSSSSIALALVDAVEEGRIKDNDNVLLVGFGGGLTWGALIIRWGK
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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-ACP synthase and acetyl transacylase activities. Can use branched-chain acyl-CoAs, with a preference for 2-methylbutanoyl-CoA, the precursor of odd-numbered anteiso fatty acids, at 30 degrees Celsius, which is further increased at a low temperature. Shows weak activity with acetyl-CoA.
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C0LT23
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CERK_ORYSJ
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Ceramide kinase (OsCERK) (EC 2.7.1.138)
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MEGGGEALFLDGVGEVTVAVGDDGLSFQPLHQEVSSSCWSSIIMQPKLESKLKFSDVYAVELLEVGPVCEPWNARATVQGKINTEMNRFVIHTVTRPRKRPSPWVPCEYIFGHKDQQTCKTWVEHIKTCINKEQDRPKSLMVFVHPLCGKGRGCKNWETVAPLFERAKVKTKVIVTQRAGHAYDTLASLSDKDLKKFDGVIAVGGDGLFNEILNGLLSTRHTNSYPPTPEGFGYFRNNMKCQEHRNNDLSNSELTGDDANAISGSSNTPDDHEPLLSTTRSTGLDISSSDSSDEPCNGDQVPLVSFPNNWFRLGIIPSGSTDAIVLSTTGERDPVTSALLIILGRRISLDIAQVVRWKSSPSAEVSPTVRYAASFAGYGFYGEVIRESEKYRWMGPARYDFSGTMVFLKHRSYEAKVAFLENGNTHSLTASAENNANGVQTLQYHQNRHRKTICRTNCLICKGTSTSEQNSEDENPDSSRTACETPKWVWSKGRFLSVGAAVISCRNERAPDGLVADAHLSDGFLHLLLIRDCPLPFYLWHLTQFTKKGSDPLSFKFVEHHKTQAFTFISSHDESVWNLDGELLQACEVSVQAFRGLVNLFASGPEV
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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, ceramide phosphorylation plays a role in the modulation of PCD and CERK activity is crucial for the maintenance of cell viability.
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C0LU16
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MED21_ARATH
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Mediator of RNA polymerase II transcription subunit 21 (Mediator complex subunit 21) (RNAPII complex component SRB7)
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MDIISQLQEQVNTIAAITFNAFGTLQRDAPPVQLSPNYPEPPATTTVTDDATPFPEQPKQLSAGLVKAAKQFDALVAALPLSEGGEGAQLKRIAELQVENDLVGQELQKQLEAAEKELKQVQELFGQAADNCLNMKKPE
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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 by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Required for embryo development and defense against necrotrophic fungal pathogens.
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C0M0V4
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AAH1_SOYBN
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Allantoate deiminase 1 (EC 3.5.3.9) (Allantoate amidohydrolase 1) (GmAAH1)
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MYSATASNTFFLLSCFLLFCLLSAPSCVSMFSGIETGDLEKRDDLFPQILRDEAVARLYELGKVSDASGYLERTFLSPASMKAIDLIRKWMEDAGLRTWVDQMGNVHGRVDGANENAEALLIGSHMDTVVDAGMFDGSLGIVSAISAVKAMHVNGKLQKLKRPVEVIAFSDEEGVRFQTTFLGSGAIAGILPGTTLEISDKREVMIKDFLKENSMDITEESLLKLKYDPKSVWGYVEVHIEQGPVLEQVGFPLGVVKGIAGQTRLKVTVRGSQGHAGTVPMSMRQDPMAAAAEQIVVLESLCKHPEEYLSYDGHCSDSTVKSLSSSLVCTVGEISTWPSASNVIPGQVTYTVDIRAIDDLGREAVIYDLSKQIYQICDKRSVSCIIEHKHDAGAVICDSDLSSQLKSAAYSALKKMEGDIQDEVPTLMSGAGHDAMAISHLTKVGMLFVRCRGGISHSPQEHVLDNDVWAAGLATLSFLENLS
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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.
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C0MAL8
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THSA_STRE4
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NAD(+) hydrolase ThsA (NADase ThsA) (SeThsA) (EC 3.2.2.5)
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MFIIKGEVSRKDLIREIEKAIKSDELGAFIGAGLSIPAGFCSWKELLREPAEEIGLDVEKESDLVNLAQYYSNSKKRTSIDDLIKGQFSQLVKPTENHKLLSQLPISTFWTTNYDKLIEKALENNMKKPYVKTKDEQLRGTNHNFDAIVYKLHGDVETPEDAVITRSDYEEFGYNKRKLFREVLEGDLLTKTFLFLGFSFEDPNFNYVIGRLRVLLDEKNTRKHYCIMKRVQDADEDYEYKKARQELQIEDLNRYGIFTYLVNKYDEITEILSTLVDRFRRKTIFISGSAYSYSAYSQKTGENFIHKLSFELSKNGYHIVNGYGKGVGEFVLNGVADYCLTHKSKINDFLTLMPFPQNSSLGIDLDKLYKENREQMIESCGIAIFLFGNKEAEDIASGVMDEYELSKKHGLVCLPIEYTGGASKEIYDQTTQEISDKNTISAIEQANKQCDGDIDMSVKNIVQAVKILNKEEF
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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 inhibition of phage replication (By similarity).
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C0MHL9
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POLG_SAFV
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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 2B (P2B); Protein 2C (P2C) (EC 3.6.4.13); Protein 3A (P3A); VPg (P3B) (Protein 3B); Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C) (p22); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
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MACKHGYPLLCPLCTALDITPDGSFTLLFDNEWYPTDLLTVNLDDDVFYPLDTNMDWTDLPLIQDIVMEPQGNSNSSDKNNSQSSGNEGVIINNYYSNQYQNSIDLSANANGVGKENSKPQGQLMNILGSAADAFKNIAPLLMDQNTEEMTNLSDRVSSDTAGNTATNTQSTVGRLFGFGQRHKGKHPASCADTATDKVLAAERYYTIKLASWTKTQESFDHIRVPLPHALAGENGGVFSSTLRRHYLCKCGWRIQVQCNASQFHAGSLLVFMAPEFDTSNHSTEVEPRADTAFKVDANWQKHAQILTGHAYVNTTTKVNVPLALNHQNFWQWTTYPHQILNLRTNTTCDLEVPYVNVCPTSSWTQHANWTLVIAVLTPLQYSQGSATTIEITASIQPVKPVFNGLRHTVVNPQSPFPVTVREHAGTFFSTTPDTTVPVYGNTISTPFDYMCGEFTDLLSLCKIPTFLGNLDSNKKRIPYFSATNSTPATPLVTYQVTLSCSCMANSMLAAVARNFNQYRGSLNYLFVFTGSAMTKGKFLISYTPPGAGEPKTLDQAMQATYAIWDLGLNSSYNFTVPFISPTHYRQTSYNTPTITSVDGWLTVWQLTPLTYPLGVPNDSHILTLVSGGDDFTLRMPVTFTKYVPQGVDNAEKGKVSDDNASTDFVAEPVKLPENQTRVSFVYDRSTLSSVLQSTSDVSSKFTPSTAKNLQNSILLTPLPSDIVNNSVLPEQERWISFASPTTQKPPYKTKQDWNFIMFSPFTYYKCDLEVTLSKNDRETISSVVRYVPCGAPSDLSDQTMPQTPSLADTRDPHMWVVGQGTTNQISFVIPYTSPLSVLPSVWFNGFSNFDNSSRFGVAPNADFGRLLLQGQGTFSVHYRYKKMRVFCPRPTVFIPWPNPQDTKIKSVRPTPTLELQNPISIYRVDLFINFSDEIIQFTYKVHGRTVCQYEIPGFGLSRSGRLLVCMGEKPCQLPISTPKCFYHIVFTGSRNSFGVSIYKARYRPWKQPLHDELHDYGFSTFTDFFKAVRDYHASYYKQRLQHDIETNPGPVQSVFQLQGGVLTKSQAPMSGLQSMLLRAIGIEADCTEFTRAVNLITDLCNTWESAKTTLSSPEFWTKMVMRIVKMFAASVLYLHNPDLTTTVCLSLMAGIDILTNDSVFNWLSTKLSKFFHTPAPPIVPLLQQQSPIREANDSFNLAKNIEWAIKTIKRIVEWITSWFKQEETSPQAKLDKMLTDFPEHCNSILAMRNGRKAYTDCASAFKYFEQLYNLAVQCKRIPLATLCEKFKNKHDHAVARPEPVVVVLRGNAGQGKSVTSQIIAQAVSKLSFGRQSVYSLPPDSDYLDGYENQYSVIMDDLGQNPDGEDFKVFCQMVSSTNFLPNMAHLEKKGTPFTSNFIIATTNLPKFRPVTVAHYPAVDRRITFDLTVEAGDECVTHNGMLDVEKAFEEIPGKPQLDCFNTDCRLLHKRGVRFVCNRTKNIYNLQQVVKMVKSTIDNKVENLKKMNTLVAQSPGNDMDYVLTCLRQTNAALQDQIDELQEAFNQAQERQNFLSDWLKVSAIVFASIASLSAVCKLVSRFKNLVCPAPVQIQLSEGEQAAYSGGKKGEKQTLQVLDVQGGGKIVAQAGNPVMDYEVNIAKNMVNPITFFYADKAQVTQSCLLIKGHLFVVNRHVAETDWCAFELKGTRHERDSVQMRSVNKSGMEVDLTFVKVVKGPLFKDNSKKFCSKDDDFPARNETVTGIMNTGVPFVFTGKFLIGNQPVNTTTGACFNHCIHYRATTHRGWCGSALICHVNGKKAVYAMHSAGGGGMAAATIITQEMIEAAEKALDCLTPQGAIVEIGIDTVVHVPRKTKLRRTVAHPCFQPKFEPAVLSRYDPRTTKDVDQVAFSKHTTNLEELPSVFSMVAREYATRVFTTIGKENKILTPEQAILGLPGMDPMEKDTSPGLPYTQQGLKRAQLVNFEQGTMVQNLKEAHTKLTEGNYEDILYQSFLKDEIRPIEKIHEAKTRIVDVPPFHHCIWGRQLLGRFASRFQTNPGLDLGSAIGTDPDTDWTAFAFQLLQYKYVYDVDYSNFDASHSTAMFEVLIENFFTTENGFDERIGDYLRSLAVSRHAFEERRVLVRGGLPSGCAATSMLNTIINNIVIRAALHLTYSNFEFDDIKVLSYGDDLLIATNYQINFNLVKQRLAPFNYKITPANKTVEFPEISNLYEVTFLKRKFVRYNSCLFKPQMDTENLKAMVSYCRPGTLKEKLNSIALLAVHSGKSVYDEIFDPFRRIGIIIPEHGTMLYRWLNLFR
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[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, cellular mRNAs fail to export, and some proteins small enough for diffusion are not retained anymore (efflux) (By similarity). The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity). [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. [Capsid protein VP2]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. [Capsid protein VP3]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. [Capsid protein VP4]: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP4 is released, capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm. After genome has been released, the channel shrinks (By similarity). [Protein 2C]: Associates with and induces structural rearrangements of intracellular membranes (By similarity). It displays RNA-binding, nucleotide binding and NTPase activities (By similarity). [VPg]: Forms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains. [Protease 3C]: Cysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity). In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate cooperatively bind to the protease. Cleaves host PABP1, this cleavage is important for viral replication (By similarity).
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C0NL63
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ARO1_AJECG
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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); Shikimate dehydrogenase (EC 1.1.1.25)]
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MGVPTKISILGRESIVADFGIWRNYVAKDLLSSCSSSTYILISDTNLTPLYLEGFQRSFEDAATNVSPKPRLLTYEIPPGESSKSRETKADIEDWMLARQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSDEKFAALERDAETILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVSIGMVKEAELARHLGILNNVSVSRISKCLASYGLPTSLKDQRIKKLTAGKHCSVEQLIAYMGVDKKNDGPKKKVVLLSAIGRTHEPRASTVSNEEIQIVLAPSIEVSPGVPKGLDVTCTPPGSKSISNRALVLAALGSGTCRLKNLLHSDDTEVMLNALERLGAATFSWEDEGEVLVVSGKGGRMEASPSELYLGNAGTASRFLTTVATLARKSSVDSSVLTGNARMKQRPIGDLVDALAANGASIEYLENLGCLPLKIASSGGFAGGEINLAAKVSSQYVSSLLMCAPYAKTPVTLRLVGGKPISQPYIDMTTAMMRSFGVEVKKSETEEHTYHIPLGFYTNPVEYIVESDASSATYPLAAAAITGTSCTVPNIGSKSLQGDARFAVDVLRPMGCAVDQSDFSTRVTGPPGGILSPLPNIDMEPMTDAFLTASVLAAVARGKGSNHTTRIFGIANQRVKECNRIKAMKDELAEFGVVCREHDDGLEIDGIDRATLHHPSDGVYCYDDHRVAMSFSVLSLVTPEPTLILEKECVGKTWPGWWDSLAQTFKVKLDGKEVGKRTETNPIVHVNKSAASIFIIGMRGAGKTTSGFWVSKALQRPFIDLDDELERTEGMTIPEIIKQRGWGGFREAELSLLRRVMTEKPTGYIFACGGGVVETPEARKLLTQYHKTTGNVILVMRDIKEIMDFLKIDKTRPAYVEDMMSVWLRRKPWYEECSNVQYYSRLTGLDGMTQVSGGFNRFLKVITGEVDSLAKMRRKENTFFVSLTLPDLSLAAHILKEVTLGSDAVELRVDLLKDPQSDNEIPSVDYVAEQISVLRSRTSVPLVFTIRTKGQGGRFPDDAYDAALQLYRLAVRMGSEFVDLEISFPEQLLRTVTEMKGFSKIITSHHDPKGQLSWVNGSWIQFYNKALQYGDVIKLVGVARSIDDNISLKKFKTWAEEKHNVPIIAINMGDKGQLSRMLNGFMTPVSHPSLPFKAAPGQLSAREIRKGLSLIGEIKAKKFAVIGNPVSASRSPAMHNTLFRQMGLPHTYGTLETDNPEVAKEFIRSPGFGGASVTIPLKISIMPLLDEIAPEAMSIGAVNTIVCAPPAPDGKSQTPRLIGHNTDWQGMVRCLSDAGAYAAATPTTASAGLVIGGGGTARAAIFALQNMGYSPIYVLGRSPDKLSSMTSTFHTDHDIRILEDVKALESLPTVAIGTIPGDKPIEPHMREILCRLFDLCEKANSDTEQARGVSTKRILLEMAYKPSVTSLMQLASDSGWTVLPGLEALVAQGVYQCEYWTNITPVYEYARNAVMGVSPSEDIL
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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C0P9J6
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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)
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MASPAMVPLRQLFVDGEWRPPAQGRRLPVVNPTTEAHIGEIPAGTAEDVDAAVAAARAALKRNRGRDWARAPGAVRAKYLRAIAAKVIERKPELAKLEALDCGKPYDEAAWDMDDVAGCFEYFADQAEALDKRQNSPVSLPMETFKCHLRREPIGVVGLITPWNYPLLMATWKIAPALAAGCTAVLKPSELASVTCLELADICKEVGLPSGVLNIVTGLGPDAGAPLSAHPDVDKVAFTGSFETGKKIMASAAPMVKPVTLELGGKSPIVVFDDVDIDKAVEWTLFGCFWTNGQICSATSRLLIHTKIAKKFNERMVAWAKNIKVSDPLEEGCRLGPVVSEGQYEKIKKFISNAKSQGATILTGGVRPAHLEKGFFIEPTIITDITTSMEIWREEVFGPVLCVKEFSTEDEAIELANDTQYGLAGAVISGDRERCQRLSEEIDAGCIWVNCSQPCFCQAPWGGNKRSGFGRELGEGGIDNYLSVKQVTEYISDEPWGWYQSPSKL
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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-(trimethylamino)butanal and 4-guanidinobutanal to 4-trimethylammoniobutanoate and 4-guanidinobutanoate, respectively. Catalyzes the oxidation of betaine aldehyde to glycine betaine.
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C0QRP9
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GPMPP_PERMH
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Glucosyl-3-phosphoglycerate/mannosyl-3-phosphoglycerate phosphatase (GpgP) (MpgP) (EC 3.1.3.70) (EC 3.1.3.85)
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MVIFTDLDGTLLNHEDYSFKDAIPSLERIKKKGIPLVIVTSKTKKEVELIQKELGIEEPFIVENGAAVFFPKGYRGFNIRCDQENRYCIIKLGRDYREIRDFIEKIKDKFKIKGFGDMTVEEIVRLTDLPYDRAELAKERDFTEPFIIEDEKDIKDLEEIAEKEGFKITKGGRFYHLIGKGQDKGRAVQIVKKVFEENYGEVPLTVGLGDSRNDIPMLREVDIPILIPHINKKYESVNLPGIIKAEYPGSKGWNESIWRILNEIERGCC
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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.
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C0QRQ2
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GPGS_PERMH
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Glucosyl-3-phosphoglycerate synthase (GpgS) (EC 2.4.1.266)
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MADFFQNGVITTLQNFRNRSLEELEYELELFSKRRNMVLLLPALYSEFEGPAMPKIIQELKDIRYLYKIVLSLDRATEEEFKKVKKIMSEINTEVKVIWHDGPRMQRLYRELEEAGFNVSIPGKGRSVWMSLGYILSDADAYAIALHDCDIVNYSRELPARLLYPVVHPALDFEFSKGYYARVTHKLYGRVTRIFYTPLIRALIRILGCNRFLVYLDSFRYALSGEFAFIRTLARGIRISPTWGLEVSMLSEVYQNTSFNRICQVEVMDTYEHKHQKLVKSTSEGLVKMASDIAKTLFRVLAHDGFVFSEAFFRTLLTTYLQEARYAIEKYNALSLINGLTYDRHAEIEAIEVFVDALKKAEKEFIEDPIGVPLMSAWVRVRAALPEISDKLIRAVEEDNSDD
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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, ADP-glucose, and to a lesser extent, TDP-glucose. 3-PGA is the only acceptor for these glucosyl donors.
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C0RGW8
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TCPB_BRUMB
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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)
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MSSYSSNIDRLQREIARLKADDSREMSKEKQAQSKAHKAQQAISSAKSLSTQKSKMSELERATRDGAAIGKKRADIAKKIADKAKQLSSYQAKQFKADEQAVKKVAQEQKRLSDERTKHEAFIKQSLSSMRTTASATMEAEEEYDFFISHASEDKEAFVQDLVAALRDLGAKIFYDAYTLKVGDSLRRKIDQGLANSKFGIVVLSEHFFSKQWPARELDGLTAMEIGGQTRILPIWHKVSYDEVRRFSPSLADKVALNTSLKSVEEIAKELHSLI
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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 cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide, also generates a cyclization variant of cyclic ADPR (cADPR), termed v-cADPR (probably 2'cADPR).
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C0S433
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ARO1_PARBP
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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); Shikimate dehydrogenase (EC 1.1.1.25)]
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MGVPTKISILGRESIVADFGIWRNYVAKDLLSNCASSTYILISDTNLTPLYLAGFQQSFENAAAGLSPKPRLLTYEIPPGESSKSRETKAEIEDWMLTRQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALENDADVILAAVKSKNTPDRLRFSSIQETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVSIGMVKEAELARHLGILNNVSVARIAKCLASYELPTSLKDERIKRLTAGKHCSVEQIITYMGVDKKNDGPKKKVVLLSAIGRTYEPRASTVSNEDLQVVLAPSIEVYPGFPKSLNVTCTPPGSKSISNRALVLAALGSGTCRIKNLLHSDDTEVMLTALERLGAATFSWESQGEVLVVNGNGGRMVASPKELYLGNAGTASRFLTTVATLAQKGSVASSVLTGNARMKQRPIGDLVDALKSNGADIEYLENPKSLPLKITASGGFAGGEMRLDAKVSSQYVTSLLMCAPYANEPVTLRLVGGKPVSQLYVDMTTAMMRSFGIDVKKSETEEHTYHIPRGVYKNPAEYVVESDASSATYPLAIAAMTGTSCTVPNIGSKSLQGDARFAIEVLRPMGCTVNQTDFSTSVTGTAGGKLKSLPTIDMEPMTDAFLTASVLAAVARGQGSNHTTRICGIANQRVKECNRIKAMKDELAKFGVTCREHDDGLEIDGIDRSTLRHPTEGVFCYDDHRVAMSFSVLALVAPQPTLILEKECVGKTWPGWWNTLAQTFKVKLDGKEVEVEEVEVEERAKTNGVAHLDKSAASIFIIGMRGAGKTTSGVWVSKALQRPFIDLDDELEKSEGMTIPEMIKQRGWEGFRDSELALLRRVMTEKPMGYIFACGGGVVELPEARELLTQYHKTKGNVILAMRDIKEVMDFLKIDKTRPAYVEDMMSVWLRRKPWYQECSNIQYYSRITQPDGMAQVLHGFNRFLKVITGQLDSLAQMRRKENTFFVSLTFPDLTPASNILKEVTLGSDAVELRVDLLKDPQSDSEIPSVDYVAEQISVLRSRVSVPLVFTIRTKSQGGRFPDDAYDAALQLYRLAIRMGSEFVDLELSFPKQLLRTVTEMKGFSKIIASHHDPEGLLSWANGSWIQIYNKALQYGDVIKLVGVAKTLDDNASLKKFKTWAEAKHDVPLIAINMGYKGQLSRILNGFMTPVSHPSLPFKAAPGQLSAREIRKGLSLMGEIKAKKFAVIGKPVSSSRSPAMHNALFKQMGLPHTYGRIETDNVEDVKEFILSPDFGGASVTIPLKLDIMPLLDEIAPEAEMIGAVNTIVSVPAAPGDKFQSSRLIGRNTDWQGMVRCLSDAGAYSAATPTTSSAGLIIGGGGTARAAIFALNSMSYSPIYIVGRSPEKLACMASSFPADYNIRIVDDVKALESLPMVAIGTIPGDKPIELHMREVLCEILSLCEKANVEAERKTGITPKRILLEMAYKPSVTSLMKLASDAGWTVLPGLEVLVAQGVYQSEYWTDITPVYENARKAVMGVSSSDDTIS
|
The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
|
C0SP85
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YUKE_BACSU
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Protein YukE
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MAGLIRVTPEELRAMAKQYGVESQEVLNQVDRLNRMISDLKSMWEGASSEAFADQYEQLKPSFIKMSDLLQDVNQQLDQTANTLESTDQDIANQIRG
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Required to deliver LXG toxins to target cells.
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C0SPC1
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CCRZ_BACSU
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Cell cycle regulator CcrZ (EC 2.7.1.15) (EC 2.7.1.229) (Cell cycle regulator protein interacting with FtsZ)
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MNIDMNWLGQLLGSDWEIFPAGGATGDAYYAKHNGQQLFLKRNSSPFLAVLSAEGIVPKLVWTKRMENGDVITAQHWMTGRELKPKDMSGRPVAELLRKIHTSKALLDMLKRLGKEPLNPGALLSQLKQAVFAVQQSSPLIQEGIKYLEEHLHEVHFGEKVVCHCDVNHNNWLLSEDNQLYLIDWDGAMIADPAMDLGPLLYHYVEKPAWESWLSMYGIELTESLRLRMAWYVLSETITFIAWHKAKGNDKEFHDAMEELHILMKRIVD
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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 or metabolite, and by interacting with replication initiation proteins. Has ATPase activity with D-ribose and 2-deoxy-D-ribose in vitro, but not with choline. Involved in DNA damage response.
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C0SUT9
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JMJ16_ARATH
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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)
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MGTELMRICVKEDSDDLPSVPPGFESYATFTLKRVVPATTSDKAKTPAIESVSATEQAKMEVESDEAKAARALRRRPWINHSGCDDDGDCAANNDNAASQNPDQNCDVKPALPKGVVRGCEECKDCQKVTARWHPDEARRPDLEDAPVFYPSEEEFEDTLNYIAKIRPEAEKYGICRIVPPPSWKPPCPLKEKQVWEGSKFTTRVQRVDKLQNRSSMKKISKLPNQMRKKKRKCMKMGMDSVTNGMGDPCSASTGMNELETFGFEPGPGFTLKDFQKYADEFKAQYFKKSETSTDDKCKVDNSIDCWEPALEDVEGEYWRIVDKATEEIEVLYGADLETGVFGSGFPKISSSHNASSSEDKYAKSGWNLNNFPRLPGSLLKYEGSDISGVLVPWLYIGMCFSSFCWHVEDHHLYSLNYMHWGAPKLWYGVGGKDAVKLEEAMRKHLPDLFEEQPDLLHKLVTQLSPSKLKTAGVPVHRCVQHAGEFVLTFPRAYHAGFNSGFNCAEAVNVAPVDWLPHGQIAIELYCQQGRKTSISHDKLLLGAAREVVKADWELNLLRKNTVDNLRWKAFSAKDGILAKTLKARIDMERTRREFLCNSSLALKMHSNFDATNERECCICFFDLHLSAAGCRCSPEKYSCLTHVKELCSCPWVTKYFLFRYDIDELNVLVEAVEGKLSSVYRWARQDLGLALSTDVSGSKMEIDEEGKVHKDPTPQTTALSGKDLQLKVTSKEVSKELEKTSKLSHVNLLLKEKEEQITSSHCMKPVKEETVCDSSDPNVSACQPSEGGIICMTAVKSASGKKNSQSLPNDVILLSDDEYDIPRKRGSVRRDAISSGKKLEIRERPTHVLALEASAKIAAPICQREGDSLRDTRNTISLPTNDQKTMRRDVPSSTSHAEVNAEATGLTQDICNRMATNSHGGGKPTSCKSKNSGGLAIVDVVDGTRSSSGTPSCSQNNSPDRFIRQKGPRIAKVVRRINCNVEPLSYGCVLSGKSWCSRRAIFPKGFRSRVKYINILDPTNMCFYISEILDAGRNSPLFMVYLESNPSEVFVHMSPTRCWEMVRERVNQEITKQHKAGKSDLPPLQPSGSPDGFEMFGYSSPAIVQAIEALDVNRVCTDYWDSRPYSRPQVQFPANPLLREANTSGRSNVGNLQLNPGHHISPTGINSILKVLFKKASMEELSSLQEVLSETNSDMVTELVKEEIQNRR
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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 reader. Together with MMD1, promotes gene expression in male meiocytes in an H3K9me3-dependent manner, and contributes to meiotic chromosome condensation by triggering some condensin promoters (e.g. CAP-D3 and CAP-H). Together with JMJ14 and JMJ17, required for plant growth and development. Represses leaf senescence in an age-dependent manner by demethylating H3K4me3 activating histone marks at senescence-associated genes (SAGs) loci, including WRKY53 and SAG201, thus preventing their premature expression.
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C0SV12
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JMJ29_ARATH
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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)
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MDSGVKLEHMNCFQLSYQYSWTTRKKRTLKPFMSKGSSPSSSSDSRKRKLSRAEDSDDSAVKRNAKRRRKICKVEEYYEDDDCILSDWVQRNTAKRIDKRNEEVEVMVKIESGDDCTIGKWFSDVSSKRKDKRQVEVDEDEEWEEEVTLCSKIKATSSRSRTHSLSANSPENVTDVISPCRSRSPASNVSDSIQKNDCTSSRKQSGPICHQCLKGERITLLICSECEKTMFCLQCIRKWYPNLSEDDVVEKCPLCRQNCNCSKCLHLNGLIETSKRELAKSERRHHLQYLITLMLPFLNKLSIFQKLEIEFEATVQGKLPSEVEITAAISYTDERVYCDHCATSIVDLHRSCPKCSYELCLKCCQEIREGSLSERPEMKFHYVDRGHRYMHGLDAAEPSLSSTFEDEEANPSDAKWSLGENGSITCAPEKLGGCGERMLELRRILPLTWMSDLEHKAETFLSSYNISPRMLNCRCSSLETELTRKSASRTTSSDNYLFCPESLGVLKEEELLHFQEHWAKGEPVIVRNALDNTPGLSWEPMVMWRALCENVNSTSSSEMSQVKAIDCLANCEVEINTRQFFEGYSKGRTYENFWPEMLKLKDWPPSDKFEDLLPRHCDEFISALPFQEYSDPRTGILNIATKLPEGFIKPDLGPKTYIAYGIPDELGRGDSVTKLHCDMSDAVNILTHTAEVTLSQEQISSVKALKQKHKLQNKVDKQSTEDCNEKEEEEEEELNMPEISSNENEETGSALWDIFRREDVPKLEEYLRKHCKEFRHTYCSPVTKVYHPIHDQSCYLTLEHKRKLKAEYGIEPWTFVQKLGEAVFIPAGCPHQVRNLKSCTKVAVDFVSPENIHECLRLTEEFRQLPKNHKAREDKLEASLLSL
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May function as histone H3 lysine demethylase and be involved in regulation of gene expression.
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C0VHC9
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CAP4_ACIS2
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CD-NTase-associated protein 4 (Cap4) (EC 3.1.-.-) (Endodeoxyribonuclease Cap4)
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MSASLLEKQSTGGAIARVGFGYQDAFVLRSLPLWLSQSAFSHIVSEALSDIEVCYFSSEKSLHVMYEAKNHSLTATEFWDEIRRFKSLFDTHPKNFIWFNLVCPSYNTAISPLISKIDRLRGVGSSYDDDSSVSVNGRSEYLDWCVGKKIDFSLAEFALDYVGFITFNSENSESIFLSEIQDTINIELLRSQVKQLKDQFKNLISRSSFGPIYRKDFENFICHALEEDRSQWLLDPIKINLSASSSQYQDLNLDISDFNGPDRAQKTSSDWNSLIKKAVSIGDFIHNSGDRRTLLIDGKQRMSTACMLGYVFSATRNFLLEIEHNGLIYRTDDHKQKEGQFFTKIEAVEPQGETEAIVAIGFPTAIGKDIDSTINEVKSLPRLNLESSHAIDNMETLNLAVREAKSALVSFKSENKLSKLHLFIKAPSVFAMVLGHRLNGICDIQLYDWVDGQYIPTAELNL
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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 thus abortive phage infection. A type II-C(AAAA) CBASS system. Binds cyclic nucleotide second messengers (synthesized by CdnD, the cognate CD-NTase in the CBASS operon). Ligand binding activates it to endonucleolytically degrade dsDNA to approximately 6 bp length fragments, with a preference for 5'-C or 5'-G cleavage site. The minor product of CdnD is the activating nucleotide also binds the major product (2',3',3'-cyclic AMP-AMP-AMP) but is not activated by it. Only binds DNA in the presence of ligand. Is not activated by c-di-AMP, c-di-GMP, 3'3'-cyclic GMP-AMP (3'3'-cGAMP) or 3',3',3'-cyclic AMP-AMP-GMP.
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C0Z2L5
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BZP44_ARATH
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bZIP transcription factor 44 (AtbZIP44)
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MNNKTEMGSSTSGNCSSVSTTGLANSGSESDLRQRDLIDERKRKRKQSNRESARRSRMRKQKHLDDLTAQVTHLRKENAQIVAGIAVTTQHYVTIEAENDILRAQVLELNHRLQSLNEIVDFVESSSSGFGMETGQGLFDGGLFDGVMNPMNLGFYNQPIMASASTAGDVFNC
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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.
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C1CZ84
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IRRE_DEIDV
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Radiation response metalloprotease IrrE (EC 3.4.24.-) (DNA repair regulatory protein IrrE)
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MTDPAPPPTALAAAKARMRELAASYGAGLPGRDTHSLMHGLDGITLTFMPMGQRDGAYDPEHHVILINSQVRPERQRFTLAHEISHALLLGDDDLLSDLHDEYEGDRLEQVIETLCNVGAAALLMPAELIDDLLTRFGPTGRALAELARRADVSATSALYALAERTAPPVIYAVCALSRQEDEGEGGGAKELTVRASSASAGVKYSLSAGTPVPDDHPAALALDTRLPLAQDSYVPFRSGRRMPAYVDAFPERQRVLVSFALPAGRSEPDADKPEAPGDQS
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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 radiation.
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C1FYJ9
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ARO1_PARBD
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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); Shikimate dehydrogenase (EC 1.1.1.25)]
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MGVPTKISILGRESIVADFGIWRNYVAKDLLSNCASSTYILISDTNLTPLYLAGFQQSFENAAAGLSPKPRLLTYEIPPGESSKSRETKAEIEDWMLARQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALENDADVILAAVKSKNTPDRLRFSSIQETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVSIGMVKEAELARHLGILNNVSVARIAKCLASYELPTSLKDERIKRLTAGKHCSVEQIITYMGVDKKNDGPKKKVVLLSAIGRTYEPRASTVSNEDLQVVLAPSIEVYPGFPKSLNVTCTPPGSKSISNRALVLAALGSGTCRIKNLLHSDDTEVMLTALERLGAATFSWESQGEVLVVNGNGGRMVASPKELYLGNAGTASRFLTTVATLAQKGSVASSVLTGNARMKQRPIGDLVDALKANGADIEYLENPKSLPLKITASGGFAGGEMRLDAKVSSQYVSSLLMCAPYAKEPVTLRLVGGKPVSQLYVDMTTAMMRSFGIDVKKSETEEHTYHIPRGVYKNPAEYVVESDASSATYPLAIAAMTGTSCTIPNIGSKSLQGDARFAIEVLRPMGCTVNQTDFSTSVTGTAGGKLKSLPTIDMEPMTDAFLTASVLAAVARGQGSNHTTRICGIANQRVKECNRIKAMKDELAKFGVTCREHDDGLEIDGIDRSTLRHPTEGVFCYDDHRVAMSFSVLALVAPQPTLILEKECVGKTWPGWWNTLAQTFKVKLDGKEVEVEERAETNGVAHLDKSAASIFIIGMRGAGKTTSGVWVSKALQRPFIDLDDELEKSEGMTIPEMIKQRGWEGFRDSELALLRRVMTEKPMGYIFACGGGVVELPEARELLTQYHKTKGNVILAMRDIKEVMDFLKIDKTRPAYVEDMMSVWLRRKPWYQECSNIQYYSRITQPDGMAQVLHGFNRFLKVITGQLDSLAQMRRKENTFFVSLTFPDLTPASNILKEVTLGSDAVELRVDLLKDPQSDSEIPSVDYVAEQISVLRSRVSVPLVFTIRTKSQGGRFPDDAYDAALQLYRLAIRMGSEFVDLELSFPEQLLRTVTEMKGFSKIIASHHDPEGLLSWANGSWIQIYNKALQYGDVIKLVGVAKTLDDNASLKKFKTWAEAKHDVPLIAINMGYKGQLSRILNGFMTPVSHPSLPFKAAPGQLSAREIRKGLSLMGEIKAKKFAVIGKPVSSSRSPAMHNALFKQMGLPHTYGRIETDNVEDVKEFILSPDFGGASVTIPLKLDIMPLLDEIAPEAEMIGAVNTIVSVPAAPGDKSQSSRLIGRNTDWQGMVRCLSDAGAYSAATPTTSSAGLIIGGGGTARAAIFALNSMSYSPIYIVGRSPEKLACMASSFPADYNIRIVDDVKALESLPMVAIGTIPGDKPIELHMREVLCEILSLCEKANVEAERKTGITPKRILLEMAYKPSVTSLMKLASDAGWTVLPGLEVLVAQGVYQSEYWTDITPVYENARKAVMGVSSSDDTIS
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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C1H8L1
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ARO1_PARBA
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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); Shikimate dehydrogenase (EC 1.1.1.25)]
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MGVPTKISILGRESIVADFGIWRNYVAKDLLSSCASSTYILISDTNLTPLYLAGFQQSFENAAAGLSPKPRLLTYEIPPGESSKSRETKADIEDWMLTRQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALENDADVILAAVKSKNTPERLRFSNIQETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVSIGMVKEAELARHLGILNNVSVARIVKCLASYELPTSLKDERIKRLTAGKHCSVEQIIAYMGVDKKNDGPKKKVVLLSAIGRTYEPRACTVSNEDLQVVLAPSIEVYPGFPKSLNVTCTPPGSKSISNRALVLAALGSGTCRIKNLLHSDDTEVMLTALERLGAATFSWENQGEVLVVNGNGGRMVASPKELYLGNAGTASRFLTTVATLAQNGSVASSVLTGNARMKQRPIGDLVDALKANGADIEYLENPKSLPLKITASGGFAGGEIRLSAKVSSQYVSSLLMCAPYAKEPVTLRLVGGNPVSQLYIDMTTAMMRSFGIDVKKSETEEHTYHIPRGVYKNPAEYVVESDASSATYPLAIAAMTGTSCTVPNIGSKSLQGDARFAIDVLRPMGCTVNQTDFSTSVTGPAGGKLKSIPTIDMEPMTDAFLTASVLAAVARGQGSNHTTRICGIANQRVKECNRIKAMKDELAKFGVTCREHDDGLEIDGIDRSTLCHPPEGVFCYDDHRVAMSFSILALAAEQPTLILEKECVGKTWPGWWDTLAQTFKVKLDGKEVEVEEKAETNGVAHVDKSAASIFIIGMRGAGKTTSGVWVSKALQRPFIDLDDELEKNEGMTIPEMIKQRGWEGFRDSELALLRRVMTEKPMGYIFACGGGVVELPEARELLTQYHKTKGNVILAMRDIKEVMDFLKIDKTRPAYVEDMMSVWLRRKPWYQECSNIQYYSRITQPDGMAQVLHGFNRFLKVITGKLDSLAQMRRKENTFFVSLTFPDLTPASNILKEVTLGSDAVELRVDLLKDPQSDSEIPSVDYVAEQISVLRSRVSVPLVFTIRTKSQGGRFPDDAYDAALRLYCLAIRMGSEFVDLELSFPEQLLRTVTEMKGFSKIIASHHDPEGLLSWANGSWIQIYNKALQYGDVIKLVGVAKTLDDNASLKKFKTWAEAKHDVPLIAINMGYKGQLSRILNGFMTPVSHPGLPFKAAPGQLSAREIRKGLSLMGEIKAKKFAVIGKPVSSSRSPAMHNALFKQMGLPHTYGRIETDNPEDVKEFIRSPDFGGASVTIPLKLDIMPLLDEIAPEAEMIGAVNTIVSVPAAPGDKSQSSRLIGRNTDWQGMVRCLSDAGAYSAATPTTSSAGLIIGGGGTARAAIFALNSMSYSPIYIVGRSPEKLACMASSFPADYNIRIVDDVKALESLPMVAIGTIPGDKPIELHMREVLCEILSLCEKANVEAERRTGITPKRILLEMAYKPSVTSLMKLASDAGWTVLPGLEVLVAQGVYQSEYWTDITPVYENARKAVMGVSSSDDIIS
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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C1I202
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PNPB_PSEWB
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p-benzoquinone reductase (EC 1.6.5.6) (NAD(P)H dehydrogenase (quinone))
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MPTKIQIVFYSSYGHIYKMAEAIAAGAREVGDVEVTLLQVPELMPEEVQVKSGIKGYRAAFGSIPYATPEVLAEADAIIFGTPTRFGNMCSQMRNFLDQTGGLWMSGGLIGKVGSVFTSTASQHGGQETTITSFHTTLLHHGMVIVGVPYSEPGLTNMTEISGGTPYGASTLAGADGSRQPSENELQIARFQGKHVATIAKRLANNK
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Involved in the degradation of para-nitrophenol (PNP). Catalyzes the reduction of p-benzoquinone to hydroquinone.
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C1ITJ8
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HMR1_BOVIN
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Major histocompatibility complex class I-related gene protein (MHC class I-related gene protein) (Class I histocompatibility antigen-like protein)
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MMLLLPLIIVLMMKLSDARTHSLRYFRLGISEPGYGIPEFISAGYVDSHPITMYNSVSQLKEPRALWMEENLAPDHWERYTQLLRGWQQAFKVELKQLQHHYNHSGFHTYQRMIGCELLEDGSITGFLQYAYDGQDFLIFNKDTLSWMAMDNVADIIRRVWEANRHELQYQKNWLEEECIAWLKRFLEYGKDALQRTEPPKVRVNHKETFPGITTLYCRAYGFYPPEISINWMKNGEEIFQDTDYGGILPSGDGTYQTWVSVELDPQNGDIYSCHVEHGGVHMVLQGFQESETILLVVKAVGFIVLAIALAGVGILAWRKRPRGKNKVICLSTPEH
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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 surveillance of the microbial metabolome at mucosal epithelial barriers (By similarity). Signature pyrimidine-based microbial antigens are generated via non-enzymatic condensation of metabolite intermediates of the riboflavin pathway with by-products arising from other metabolic pathways such as glycolysis. Typical potent antigenic metabolites are 5-(2-oxoethylideneamino)-6-D-ribitylaminouracil (5-OE-RU) and 5-(2-oxopropylideneamino)-6-D-ribitylaminouracil (5-OP-RU), products of condensation of 5-amino-6-D-ribityaminouracil (5-A-RU) with glyoxal or methylglyoxal by-products, respectively (By similarity). May present microbial antigens to various MAIT cell subsets, providing for unique recognition of diverse microbes, including pathogens that do not synthesize riboflavin. Upon antigen recognition, elicits rapid innate-type MAIT cell activation to eliminate pathogenic microbes by directly killing infected cells (By similarity). During T cell development, drives thymic selection and post-thymic terminal differentiation of MAIT cells in a process dependent on commensal microflora (By similarity). Acts as an immune sensor of cancer cell metabolome. May present a tumor-specific or -associated metabolite essential for cancer cell survival to a pan-cancer TCR on a non-MAIT CD8-positive T cell clone, triggering T cell-mediated killing of a wide range of cancer cell types (By similarity).
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C1JCT1
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POL_SINV3
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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]
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MSEKTQTFVQNETHVLDMTSDFKSDLSLEKVTSSVEQTDDLVSKIINNNDLDIKDLSFLRNLLLSTLQYLGIAKFVAINITLSILSILMLLINSCAKFTRIVNLSSHILNIITTLGLYFQVSSMEIEEITQTFENEFGTYDDDKILSHYIKICNLPNRKDVYEYISLNDLKYKIKLPDISFYELKNDILSKNKNLHLWIFQKFTDEFLAMWFGVQPYRISNLREMLVISRQGFIPKDLFNEIRKLCNMGVSVIISFIQSKLFDEPFKKRDCTQALKDASVISSPFDTLWNLISKQVCDNSAEERFTQTILDFTSEFDNFLGIPNYKFAKNQKLVNTISKSLDACAKFIRDCPKDKQTEIFPLQGLHTATVKRRNEILTNVMPKFARQEPFVVLFQGPGGIGKTHLVQQLATKCVNSFYQDHEDDYIEISPDDKYWPPLSGQRVAFFDEAGNLNDLTEDLLFRNIKSICSPAYFNCAAADIEHKISPCPFELVFATVNTDLDTLQSKISSTFGQASVFPIWRRCIVVECSWNEKELGPFNYKNPSGHRSDYSHITMNYMSYDDKTQKLALEKEINFDTLFDMIRLRFRKKQQEHDTKISILNNEIQRQSNSKQHFSVCLYGEPGQGKTYNLNKLITTFANATNLKIGSEEKPSIHIFDDYIKDENDENCSKFMDIYNNKLPNNSVIFSATNVYPKTHFFPTFFLTNLIYAFIQPFKQVGLYRRLGFDGYTDIPNSSVNAPIFVQNFKFYERKQHICYFLSLEFLKNIICYIFFFLYFPLKFIKKIDLIEIKDVNKYVYDRYINFLSLSKQIEIVEYPPNLENVEFDFRFNMNKFHRVSFNNPFELDKYIHFNKNSYENLLHFDWKMYLSPRVKHRLALSYEKFFITISEVNKEIIIEELKRYVLLFKQFNIDPNMEINLGEYGSFYYINGKIHLMTINIESNVSEIPVFTDGDYVYISEHKIPVIDLFDNININSKYNLSFDQSIALNSFKTGDSFYSNAKVRKSLSKFVLLNYQTKFKLYLKEAKDKVKNFIETPIGHLLSILLTIFVICYASFKIYSKFSNFFSKDQAIEDQRKGEKKIKKITNYDSDGVQPQRKGEKKIKKVTNYDSDGVQPQSNVKVEEEIKLVFDPTGQKLLFGNDFTSELETLVELEKDDEEFTKSKIDNKSMAGLRREVRRRRYARSKKAQIEKQEVLTLPDVNGFEGGKPYFQIAEEKARKNLCQIYMIANNENCIASKFSDHIVCYGLFVFKKRLASVGHIVEALKCAPGYNLYAGCDQFNGKLYKMNLVRNYRKRELSVWDVDCPNDFVDLTSFFIPKEELYDAENCNTVLGRFGMNKREVYLYGNCEFIQEFFKVDNKGAQEFGYIDWATVDITLTTGGDCGLPYYICERKKFHNKIMGLHFAGNNVNHKTIGMSALIYKEDLVVWKGAERQSKCKFCDVKDIIIAQPDIPKEKYKGYNHEIVWNSLHESSPTTLNEELEHYLNIFPKFTGTIIKHSGDKFYGSVKHSHTQFISKFKTELTVTNGWKLSTAGDCQFESNHISPNTEVMYRVVDVQFNSIFKAFKSQPYIKNFRLIANVYEKDGKQRVTILTIIPVSDFNVKQQTVRQALVPLHLNEDEEVYVTEDVSDIFKTAIKRKQRGILPDVPYETVENETVEILGITHRNMTPEPAQMYKPTPFYKLALKFNLDHKLPVNFNMKDCPQEQKDMMVLDRLGQPNPRITQSLKWAHKDYSPDYELRKYVKEQYMCNIMEYYAGCNLLTEEQILKGYGPNHRLYGALGGMEIDSSIGWTMKELYRVTKKSDVINLDSNGNYSFLNNEAAQYTQELLKISMEQAHNGQRYYTAFNELMKMEKLKPSKNFIPRTFTAQDLNGVLMERWILGEFTARALAWDENCAVGCNPYATFHKFATKFFKFKNFFSCDYKNFDRTIPKCVFEDFRDMLIQANPHMKNEIYACFQTIIDRIQVSGNSILLVHGGMPSGCVPTAPLNSKVNDIMIYTAYVNILRRADRGDITSYRYYRDLVCRLFYGDDVIIAVDDSIADIFNCQTLSEEMKILFGMNMTDGSKSDIIPKFETIETLSFISRFFRPLKHQENFIVGALKKISIQTHFYYATDDTPEHFGQVFKTIQEEAALWEEEYFNKIQSYIQEIIRKFPEISKFFNFESYKSIQKRYIMNGWNEFVKLEKLDLNLNKKKSSKVTGIHSKQYSKFLKFLSRIENEKAALEGNFNKESVNTWYFKMSKAMHLNEIFQKGLISKPLAEFYFNEGQKMWDCNITFRRSKDDLPFTFSGSGTTKACAREQAAEEALVLFSQEDEIVRQINDIQSDCKFCKKMIRYKKLLSGVSIQRQMNVSKITENHVPSAGMMATDPSVAPDSGIATNTQTPSISRVLNPIARALDNPAGTGAPFDKHTYVYNVFTRWPEMSTVVNKSLAAGAEVFKISLDPNKLPKRILQYIQFHKTIIPQIEVQILIGGAAGTVGWLKVGWVPDASTAKKYSLDDLQLVASETINLNSTITMSMIINDSRRNGMFRLTKSDPEPWPGIVCLVEHPITNVQRNDDVNYPVIVSVRLGPDCQLMQPYNDLN
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[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.
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C1JCT2
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POLFS_SINV3
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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]
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MSEKTQTFVQNETHVLDMTSDFKSDLSLEKVTSSVEQTDDLVSKIINNNDLDIKDLSFLRNLLLSTLQYLGIAKFVAINITLSILSILMLLINSCAKFTRIVNLSSHILNIITTLGLYFQVSSMEIEEITQTFENEFGTYDDDKILSHYIKICNLPNRKDVYEYISLNDLKYKIKLPDISFYELKNDILSKNKNLHLWIFQKFTDEFLAMWFGVQPYRISNLREMLVISRQGFIPKDLFNEIRKLCNMGVSVIISFIQSKLFDEPFKKRDCTQALKDASVISSPFDTLWNLISKQVCDNSAEERFTQTILDFTSEFDNFLGIPNYKFAKNQKLVNTISKSLDACAKFIRDCPKDKQTEIFPLQGLHTATVKRRNEILTNVMPKFARQEPFVVLFQGPGGIGKTHLVQQLATKCVNSFYQDHEDDYIEISPDDKYWPPLSGQRVAFFDEAGNLNDLTEDLLFRNIKSICSPAYFNCAAADIEHKISPCPFELVFATVNTDLDTLQSKISSTFGQASVFPIWRRCIVVECSWNEKELGPFNYKNPSGHRSDYSHITMNYMSYDDKTQKLALEKEINFDTLFDMIRLRFRKKQQEHDTKISILNNEIQRQSNSKQHFSVCLYGEPGQGKTYNLNKLITTFANATNLKIGSEEKPSIHIFDDYIKDENDENCSKFMDIYNNKLPNNSVIFSATNVYPKTHFFPTFFLTNLIYAFIQPFKQVGLYRRLGFDGYTDIPNSSVNAPIFVQNFKFYERKQHICYFLSLEFLKNIICYIFFFLYFPLKFIKKIDLIEIKDVNKYVYDRYINFLSLSKQIEIVEYPPNLENVEFDFRFNMNKFHRVSFNNPFELDKYIHFNKNSYENLLHFDWKMYLSPRVKHRLALSYEKFFITISEVNKEIIIEELKRYVLLFKQFNIDPNMEINLGEYGSFYYINGKIHLMTINIESNVSEIPVFTDGDYVYISEHKIPVIDLFDNININSKYNLSFDQSIALNSFKTGDSFYSNAKVRKSLSKFVLLNYQTKFKLYLKEAKDKVKNFIETPIGHLLSILLTIFVICYASFKIYSKFSNFFSKDQAIEDQRKGEKKIKKITNYDSDGVQPQRKGEKKIKKVTNYDSDGVQPQSNVKVEEEIKLVFDPTGQKLLFGNDFTSELETLVELEKDDEEFTKSKIDNKSMAGLRREVRRRRYARSKKAQIEKQEVLTLPDVNGFEGGKPYFQIAEEKARKNLCQIYMIANNENCIASKFSDHIVCYGLFVFKKRLASVGHIVEALKCAPGYNLYAGCDQFNGKLYKMNLVRNYRKRELSVWDVDCPNDFVDLTSFFIPKEELYDAENCNTVLGRFGMNKREVYLYGNCEFIQEFFKVDNKGAQEFGYIDWATVDITLTTGGDCGLPYYICERKKFHNKIMGLHFAGNNVNHKTIGMSALIYKEDLVVWKGAERQSKCKFCDVKDIIIAQPDIPKEKYKGYNHEIVWNSLHESSPTTLNEELEHYLNIFPKFTGTIIKHSGDKFYGSVKHSHTQFISKFKTELTVTNGWKLSTAGDCQFESNHISPNTEVMYRVVDVQFNSIFKAFKSQPYIKNFRLIANVYEKDGKQRVTILTIIPVSDFNVKQQTVRQALVPLHLNEDEEVYVTEDVSDIFKTAIKRKQRGILPDVPYETVENETVEILGITHRNMTPEPAQMYKPTPFYKLALKFNLDHKLPVNFNMKDCPQEQKDMMVLDRLGQPNPRITQSLKWAHKDYSPDYELRKYVKEQYMCNIMEYYAGCNLLTEEQILKGYGPNHRLYGALGGMEIDSSIGWTMKELYRVTKKSDVINLDSNGNYSFLNNEAAQYTQELLKISMEQAHNGQRYYTAFNELMKMEKLKPSKNFIPRTFTAQDLNGVLMERWILGEFTARALAWDENCAVGCNPYATFHKFATKFFKFKNFFSCDYKNFDRTIPKCVFEDFRDMLIQANPHMKNEIYACFQTIIDRIQVSGNSILLVHGGMPSGCVPTAPLNSKVNDIMIYTAYVNILRRADRGDITSYRYYRDLVCRLFYGDDVIIAVDDSIADIFNCQTLSEEMKILFGMNMTDGSKSDIIPKFETIETLSFISRFFRPLKHQENFIVGALKKISIQTHFYYATDDTPEHFGQVFKTIQEEAALWEEEYFNKIQSYIQEIIRKFPEISKFFNFESYKSIQKRYIMNGWNEFVKLEKLDLNLNKKKSSKVTGIHSKQYSKFLKFLSRIENEKAALEGNFNKESVNTWYFKMSKAMHLNEIFQKGLISKPLAEFYFNEGQKMWDCNITFRRSKDDLPFTFSGSGTTKACAREQAAEEALVLFSQEDEIVRQINDIQSDCKFCKKMIRYKKLLSGVSIQRQMNVSKITENHVPSAGMMATDPSVAPDSGIATNTQTPSISRVLNPIARALDNPAGTGAPFDKHTYVYNVFTRWPEMSTVVNKSLAAGAEVFKISLDPNKLPKRILQYIQFHKTIIPQIEVQILIGGAAGTVGWLKVGWVPDASTAKKYSLDDLQLVASETINLNSTITMSMIINDSRRNGMFRLTKSDPEPWPGIVCLVEHPITNVQRNDDVNYPVIVSVRLGPDCQLMQPYNDLNLSGGTDPDPDPEPDPDPEPGPDPEPGVDELDLSKYIPNQLIDLLICNSYVPNNVSVDFLSTYPNLNFSIHNITDVVVSSKPYTLALFETESQINSASVWRGDLTQLSVFIQYKFYTRVEAYNKVTTVHTDKWTPNFDGTVYKPVDVKIEHAYGTYELTTMWLTSYGLVMEWSLDESRVFYGTYKTDSNGRRWLIDGNTPIARSDHCFIVSSPDLLSDDKAYYNNPIGAKQGGKLVDGAQIYRIFKTESGGYRSDPFVPETYWPSETPYNADWSGVKMPYQIRKVIQTGNNLAGKHLDGDLKMCAMIRQGSSSTQSTDNYFYPIYVHNFSALLKQMNLILKERKTKYIKFDLQVGGKPFAQMGFGDGAFIGRTTMFRQIRAAITNVILLKNIVGVDDLSGLQALPTSGFADWVVKAQSTNSKFLNDFYNDKISIERQASLGIAAAIGAGQGLFGGLSAQWQWQQQADWSRQMQRERLDMMEKLANINNQARLNQLTQSGAQQRITQQAAYQQQMNALGAGSVSAQNGMYTPSNYTPLPSYKSNTTNYYNNSVYHTDNNITNNPSNTSLTNNINNFNPELFQQQRERMPTPSEAYDNSKGFVPQPGTSKSIATENINPNYKDEEHIYEPIEQQNHEYADIDYNAMNISRENKNSSNFGNVGILDHQYADIDYDAMKIARDQQNSSKFGNVGVLNHQYAELDFSKNNTRKNSQILDNSLYSKTQPSSKMIDNSLYGINPNKMVENQNYEPASMERKNSIYSSNLNSSNNLKFNNIPNFKGPTNLNISGAKPAGFGSGIIQPAINKYTDFSKPN
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[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.
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C1K5M2
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CPT1_SOLLC
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Dimethylallylcistransferase CPT1, chloroplastic (EC 2.5.1.28) (Cis-prenyltransferase 1) (SlCPT1) (Neryl-diphosphate synthase 1)
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MSSLVLQCWKLSSPSLILQQNTSISMGAFKGIHKLQIPNSPLTVSARGLNKISCSLNLQTEKLCYEDNDNDLDEELMPKHIALIMDGNRRWAKDKGLEVYEGHKHIIPKLKEICDISSKLGIQIITAFAFSTENWKRSKEEVDFLLQMFEEIYDEFSRSGVRVSIIGCKSDLPMTLQKCIALTEETTKGNKGLHLVIALNYGGYYDILQATKSIVNKAMNGLLDVEDINKNLFDQELESKCPNPDLLIRTGGEQRVSNFLLWQLAYTEFYFTNTLFPDFGEEDLKEAIMNFQQRHRRFGGHTY
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Uses dimethylallyl diphosphate and isopentenyl diphosphate to catalyze the cis-prenyl chain elongation and produce the 10 carbon product neryl diphosphate.
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C1PGW1
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TED7_ZINVI
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Protein TRACHEARY ELEMENT DIFFERENTIATION-RELATED 7A (TED7-1)
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MASPLSQSVFPHFPPPSPAATPPPAPTTPSTPPPHFISPPPHSVPPPSPPHSVPPPLHPVPPPSPPHPVSPPPHTVPPPSPPHPVSPPPHTVPPPSPPHPVFPPPHTVPPPSPHFVPPPPNMVPPPSPPHANPPPPPPPHSVPPPPHTVPPPPPPPHIIPPPAHALSPPPPHIIPPPPPSPSNHSTTIVVIFVSCGGVFFLAFAMAALWCFLKKKKKKMVQKAENIHFDEHRKVTERIEQGPHGTETAILSVEDDIHIEEDIKKSELENFRKGLHLNYGNTYNIDTGKPSSSFGHHYLHG
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Involved in the secondary cell wall (SCW) formation of vessel elements (e.g. protoxylem and metaxylem), thus promoting tracheary element (TE) differentiation.
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C3K613
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FADB_PSEFS
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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)]
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MIYEGKAITVKALESGIVELKFDLKGESVNKFNRLTLNELRQAVDTIKADASIKGVIVSSGKDVFIVGADITEFVDNFKLPDAELVAGNLEANKIFSDFEDLNVPTVAAINGIALGGGLEMCLAADFRVMSATAKIGLPEVKLGIYPGFGGTVRLPRLIGADNAIEWIAAGKENRAEDALKVGAVDAVVAPDKLAEAALNLIKGAISGEFDYKAKRQPKLEKLKLNAIEQMMSFETAKGFVAGQAGPNYPAPVEAIKTIQKAANFGRDKALEVEAAGFVKLAKTSAAQSLIGLFLNDQELKKKAKAYDEIARDVKQAAVLGAGIMGGGIAYQSASKGTPILMKDINEHGIEQGLAEAAKLLVGRVDKGRMTAAKMAEVLNGIRPTLSYGDFGHVDLVVEAVVENPKVKQAVLAEVEAQVKDDTILASNTSTISISLLAKALKRPENFVGMHFFNPVHMMPLVEVIRGEKSSELAVATTVAYAKKMGKNPIVVNDCPGFLVNRVLFPYFGGFAKLVSAGVDFVRIDKVMEKFGWPMGPAYLMDVVGIDTGHHGRDVMAEGFPDRMKDDRRSAIDALYEAKRLGQKNGKGFYAYEADKKGKQKKVADPSVHEVLAPVIYEQREVSDEDIINWMMIALCLETVRCLEDGIVETAAEADMGLVYGIGFPPFRGGALRYIDSIGVAEFVALADKYADLGPLYHPTAKLREMAKNGQSFFG
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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}.
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C3SBW0
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PNMT_THLFG
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Pavine N-methyltransferase (TfPavNMT) (EC 2.1.1.300)
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METKQTKKEAVANLIKRIEHGEVSDEEIRGMMKIQVQKRLKWGYKPTHEQQLAQLVTFAQSLKGMEMAEEVDTLDAELYEIPLPFLHIMCGKTLKFSPGYFKDESTTLDESEVYMMDLYCERAQIKDGQSILDLGCGHGSLTLHVAQKYRGCKVTGITNSVSQKEFIMDQCKKLDLSNVEIILEDVTKFETEITYDRIFAVALIEHMKNYELFLKKVSTWIAQYGLLFVEHHCHKVFAYQYEPLDEDDWYTEYIFPSGTLVMSSSSILLYFQEDVSVVNHWTLSGKHPSLGFKQWLKRLDDNIDEVKEIFESFYGSKEKAMKFITYWRVFCIAHSQMYSTNNGEEWMLSQVLFKKK
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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 berbamine.
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C3UVB0
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ACD_DESML
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Glutaryl-CoA dehydrogenase (GDH(Des)) (EC 1.3.99.32)
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MDFNLSKELQMLQKEVRNFVNKKIVPFADQWDNENHFPYEEAVRPMGELGFFGTVIPEEYGGEGMDQGWLAAMIVTEEIARGSSALRVQLNMEVLGCAYTILTYGSEALKKKYVPKLSSAEFLGGFGITEPDAGSDVMAMSSTAEDKGDHWLLNGSKTWISNAAQADVLIYYAYTDKAAGSRGLSAFVIEPRNFPGIKTSNLEKLGSHASPTGELFLDNVKVPKENILGKPGDGARIVFGSLNHTRLSAAAGGVGLAQACLDAAIKYCNERRQFGKPIGDFQMNQDMIAQMAVEVEAARLLAYKAAAAKDEGRLNNGLDVAMAKYAAGEAVSKCANYAMRILGAYGYSTEYPVARFYRDAPTYYMVEGSANICKMIIALDQLGVRKANR
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Catalyzes the dehydrogenation of Glutaryl-CoA to glutaconyl-CoA.
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C3VD30
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ZAR1L_MOUSE
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Protein ZAR1-like (Zygote arrest protein 1-like) (Zygote arrest protein 2)
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MERLFCVPCGYGTTDPLTYPGPWRHCQQQNWPQNMGAPIFLARLRVPANVSQSCMNPYNRAQLQAVSTQMDPNLSLWLRSVHTTEVGVQVSLRVDKSVQCSQGSQTLHSSSLSDRTSSRKPTEAWEVGRRALIRRPQDGEDEESQEELTGPTEASQLLLPTWSRDREEQFPRLKELGEEYAHSPQDRKGKQFLELKYGYFHCKDCKRRWESAYVWCISGTNKVYFKQLCNKCQKSFNPYRVEEIQCQTCLRVCCSCSPKKRHIDVRRPHRQELCGHCKDKKFSCSVFFSLK
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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 similarity). Binds to the 3'-UTR of maternal mRNAs, inhibiting their translation.
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C3VPR6
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NLRC5_MOUSE
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Protein NLRC5
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MDAESIRLNNENLWAWLVRLLSKNPEWLSAKLRSFLPTMDLDCSYEPSNPEVIHRQLNRLFAQGMATWKSFINDLCFELDVPLDMEIPLVSIWGPRDEFSKQLGAGEESCPGPQLYHGAKRPFQSYGSSPRRKNSKKQQLELAKKYLKLLKTSAQQWHGGVCPGAWLTPHSPQTYIPPVLQWSRATAPLDAQEGATLGDPEAADNIDVSIQDLFSFKAHKGPRVTVLLGKAGMGKTTLAYRLRWRWAQGQLDRFQALFLFEFRQLNMITQLPTLPQLLFDLYLMPESEPDAVFQYLKENAQEVLLIFDGLDEALHADSVGTDNAGSALTLFSELCHGNLLPGCWVMTTSRPGKLPSCVPTEAATVHMWGFDGLRVEKYVTCFFSDLLSQELALKEMRTNARLRGMCAIPALCTVTCFCLRRLLPGSSPGQSAALLPTITQLYLQMVETFSPSETLLDTSILGFGKVALRGLDTGKVVFSVEDISPQLMSFGAVHSLLTSFCIHTRPGHEEIGYAFVHLSLQEFFAALYLMASHTVDKDTLVEYVTLNSHWVLRTKGRLGLSDHLPAFLAGLASHTCHMFLCQLAQQDRAWVGSRQAAVIQVLRKLASRKLTGPKMIELYHCVAETQDLELARFTAQSLPSRLSFHNFPLTHADLAALANILEHRDDPIHLDFDGCPLEPHCPEALVGCGQVENLSFKSRKCGDAFAEALCRSLPTMGSLKTLGLTGSRITAQGISHLIQTLPLCSQLEEVSLHDNQLKDPEVLSLVELLPSLPKLQKLDLSRNSFSRSILLSLVKVAITCPTVRKLQVRELDLIFYLSPVTETATQQSGASDVQGKDSLKEGQSRSLQLRLQKCQLRIRDAEALVELFQKSPQLEEVNLSGNHLEDDGCRLVAEAASQLHIAQKLDLSDNGLSQTGVTYVLKAMSTCGTLEDLHISLLNNTVVLTFAQEPREQEGSCKGRAPLISFVSPVTSELSQRSRRIRLTHCGFLAKHTETLCEALRASCQTHNLDHLDLSDNSLGGKGVILLTELLPGLGPLKSLNLSRNGLSMDAVFSLVQCLSSLQWVFHLDVSLESDCIFLRGAGTSRDALEPKFQTGVQVLELSQRYTSRSFCLQECQLEPTSLTFLCATLEKSPGPLEVQLSCKSLSDDSLKILLQCLPQLPQLSLLQLRHTVLSSRSPFLLADIFNLCPRVRKVTLRSLCHAVLHFDSNEEQEGVCCGFPGCSLSQEHMETLCCALSKCNALSQLDLTDNLLGDIGLRCLLECLPQLPISGWLDLSHNNISQEGILYLLETLPSYPNIQEVSVSLSSEQIFRMCFSKKEGAGTSLRLCECSFSPEQVSKLASSLSQAQQLTELWLTKCHLDLPQLTMLLNLVNRPTGLLGLRLEEPWVDSVSLPALMEVCAQASGCLTELSISEIQRKLWLQLEFPHQEGNSDSMALRLAHCDLETEHSHLMIQLVETYARLQQLSLSQVSFNDNDGTSSKLLQNILLSSCELKSFRLTFSQVSTKSLTHLAFGLGHCHHLEELDFSNNSLREEDTELLMGALQGTCRLKKLHLSFLPLGASSLALLIQGLSRMTLLQDLCLSHNQIGDVGTQCLAAILPKLPELRKFDLSHNQIGDVGTQCLAAILPKLPELRKFNLSHNQIGHVGTQCLAAILPKLPELRKFDLSRNQIGDVGTQCLAAILPKLPELRKFDLSGNRIGPAGGVQLVKSLTHFEHLEEIKLGNNALGEPTALELAQRLPPQLRVLCLPSSHLGPEGALGLAQALEQCPHIEEVSLAENNLAGGVPRFSKRLPLLRQIDLEFCKIEDQAARHLAANLTLFPALEKLLLSGNLLGDEVAAELAQVLPQMGQLKKVNLEWNRITARGAQLLAQGLVQGSCVPVIRLWNNPILNDVAQSLQSQEPRLDFSITDQQTL
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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.
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C3W4R6
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PA2A1_MACLB
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Acidic phospholipase A2 1 (Vl-PLA2-1) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
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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 in 3-sn-phosphoglycerides.
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C3W947
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CTSR_GEOSE
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Transcriptional regulator CtsR (Class three stress gene repressor)
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MPNISDIIEQYLKQVLNMSDQDIVEIKRSEIANKFRCVPSQINYVINTRFTLERGYIVESKRGGGGYIRIMKVKTKSEAQLIDQLLELIDHRISQSSAEDVIKRLMEEKVISEREAKMMLSVMDRSVLYIDLPERDELRARMLKAMLTSLKYK
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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 negatively autoregulates its own synthesis (By similarity).
|
C4AMC7
|
WASH3_HUMAN
|
Putative WAS protein family homolog 3 (Protein FAM39DP)
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MTPVRMQHSLAGQTYAVPLIQPDLRREEAVQQMADALQYLQKVSGDIFSRISQQVEQSRSQVQAIGEKVSLAQAKIEKIKGSKKAIKVFSSAKYPAPERLQEYGSIFTGAQDPGLQRRPRHRIQSKHRPLDERALQEKDFPVCVSTKPEPEDDAEEGLGGLPSNISSVSSLLLFNTTENLGKKYVFLDPLAGAVTKTHVMLGAETEEKLFDAPLSISKREQLEQQVPENYFYVPDLGQVPEIDVPSYLPDLPGITNDLMYIADLGPGIAPSAPGTIPELPTFHTEVAEPLKVDLQDGVLTPPPPPPPPPPAPEVLASAPPLPPSTAAPVGQGARQDDSSSSASPSVQGAPREVVDPSGGRATLLESIRQAGGIGKAKLRSMKERKLEKKQQKEQEQVRATSQGGHLMSDLFNKLVMRRKGISGKGPGAGEGPGGAFARVSDSIPPLPPPQQPQAEEDEDDWES
|
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 transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration (By similarity). In T-cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL proposed to be implicated in T cell proliferation and effector function. In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T-cell activation. Involved in Arp2/3 complex-dependent actin assembly driving Salmonella typhimurium invasion independent of ruffling (By similarity). Involved in the exocytosis of MMP14 leading to matrix remodeling during invasive migration and implicating late endosome-to-plasma membrane tubular connections and cooperation with the exocyst complex (By similarity). Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By similarity).
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C4B644
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CPVDH_PSEAH
|
Vitamin D(3) 25-hydroxylase (EC 1.14.15.15) (Cytochrome P450)
|
MALTTTGTEQHDLFSGTFWQNPHPAYAALRAEDPVRKLALPDGPVWLLTRYADVREAFVDPRLSKDWRHTLPEDQRADMPATPTPMMILMDPPDHTRLRKLVGRSFTVRRMNELEPRITEIADGLLAGLPTDGPVDLMREYAFQIPVQVICELLGVPAEDRDDFSAWSSVLVDDSPADDKNAAMGKLHGYLSDLLERKRTEPDDALLSSLLAVSDEDGDRLSQEELVAMAMLLLIAGHETTVNLIGNGVLALLTHPDQRKLLAEDPSLISSAVEEFLRFDSPVSQAPIRFTAEDVTYSGVTIPAGEMVMLGLAAANRDADWMPEPDRLDITRDASGGVFFGHGIHFCLGAQLARLEGRVAIGRLFADRPELALAVGLDELVYRESTLVRGLSRMPVTMGPRSA
|
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 displays 25-hydroxylase activity on vitamin D(2) and 7-dehydrocholesterol. May play a role in the biosynthesis of steroid metabolic intermediates.
|
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); Shikimate dehydrogenase (EC 1.1.1.25)]
|
MATPTVIKILGRDSIVADPGIWKRHVAQDLLTNCPSSTYILISDTTLTPLYVPSFQQAFEAAASSVTPKPRLLTYAIPPGEVSKSRQTKAEIEDWMLSRQPPCGRDTVIIALGGGVIGDLIGYVSATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTTHGKNLIGAIWQPEKIYLDMEFLNTLPEREFINGMAETAAISSEEDFAALERNADAILAAVKSENTTERPRFSGIQEILKLTILASARFKADVVSKDEREGGLRNLLNFGHSIGHAIEGILAPQILHGECVAIGMVKEAELARHLGILKSVAVSRLVKCLASYGLPTSLKDSRVRRLSAGKHCSVEQLLAFMAVDKKNAGPMKKVVLLSSIGSTHEQKASVVSNKDIKIVLAPSIEVSPGVPHALEITCVPPGSKSISNRALVLAALGSGTCRIKNLLHSDDTEVMLSALERLGAATFSWEEEGEVLVVHGKGGRLQASPDALYLGNAGTASRFLTTVATLANKSTVDSTILTGNARMKQRPIGALVDSLRTNGAGIKYMETTGCLPLKIDASGGFAGGHISLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGKPISQPYIDMTTAMMRSFGIDVKKSTSEEHTYHIPQGRYMNPTEYIIESDASSATYPLAVAAITGTTCTIPNIGSKSLQGDARFAVDVLRPMGCEVNQSSFSTTVTGPRNGALNALPNVDMEPMTDAFLTASVLAAVATAGSTSTTRIFGIANQRVKECNRIKAMKDELAKFGVTCREHEDGLEIDGIDRSALLRLPHGVYCYDDHRVAMSFSVLSLAASHPTLILEKECVGKTWPAWWDTLAQLFKANLEGVELKSEKKKAEKPAASLFIIGMRGAGKTTSGLWASKVLKRPFIDLDVELESKLGKSIPEIIKEQGWEGFRANELALLRQVLSEKPTGYVFACGGGIVETEEARDLLTQYQKAHGNVLLVMRDINAVMDFLKIDKTRPAYVEDMMGVWLRRKPWFQQCSNIQYYSQQSDPSKMGSALESFSRFLRVVTGEVDHLALMKKKPQSFFVSLTLPDLRPSVDILNDITLGSDAVELRVDLLVDPSSSSEMPSVDYVAEQISILRSRVSVPLVFTIRTKSQGGRFPDDAHNAALDLYRLAIRMGSEFVDLEVTFPEYVLRAVTEMKGVSKIIASHHDVANRLSWRNGSWTQFYNKALQYGDIIKLVGIASQLDDNIALREFKIWAKKAHDIPVIAINMGERGRLSRILNGFMTPVSHPKLPFKAAPGQLSAKEIREGLSLMGEIESKKFAIVGKPISASRSPALHNALFADVGLPHVYGRLETDDVQNVKDLIHAPDFGGASITIPLKLDIMPLLDEIAPEAKVIGAVNTIVPAPREPGDVKKGPRLIGYNTDWQGMVQCLRHGGAVSPSTSNDPAPGLVIGGGGTARAAIHALHSMGYSPIYLVGRSESKLNDMALSFPATYNLQILKDAESLEILPSVAIGTIPGDQPIDPSMREVLCRLFEMAARIDAELKELAPKRVLLEMAYKPTVTPLSQLASDCGWATIPGLEALVGQGVYQFQLWTGITPVFRDARAAVMNADADI
|
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 response.
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C4LVG4
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ACTP_ENTH1
|
Actophorin (EhActo)
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MAGIQLADEVTSVYNDFKLSHKYRYIVFKMNDGMTEVVVEKTAEKNATYDDFLKDLPEKSARYAVYDLEYDTPEGLRQKIIFYLWTPEGCKIREKMLYSATKATIKQALVGLSAEIQATDAGELNLDEVIAKVKTISK
|
Actin-binding protein that severs actin filaments.
|
C4LZC2
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PFP_ENTH1
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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)
|
MSLSALHKYRLQYKPVLPKHIADIDNITIEEGAKTQSAVNQKELSELFKHTYGLPICNIVAGKNADIHRVIRCGFILSGGPAAGGHNVVAGLFDGLMKGNKENKLYGFRCGAGGILSNDYIEITAELVDKHRNTGGFDLVGSGRTKIETEEQFATAFKHITALKLNAMVVVGGDDSNTNAALLAEYFAAHGSDCVFVGVPKTIDGDLKNQYIETSFGFDTACKTYSELIGNIQRDAISSRKYWHFIKVMGRSASHIALEAALETQPTYCIISEEVEDKKMTVSQIASEIADIVIERHKKGLNFGVVLIPEGLVEFIPEVKALIKELNNLLAHKKEEYSKITEFSAQKAFVCENISESCAATFKNLPDNIAKQLLLDRDPHGNVNVSAIETESFVSGIVKAEIVKRGIKVPFTPVHHFFGYEGRCAFPSNFDSTYCYALGYTAFILLALKKTGQICCISGLQKPAEEWICGGVPLTIMMNMEQRNGEMKPVIKKALVEIEGKPFKFYQSKRAQWASAEDFVFPGAIQYFGPSEVCDQPTKTLLLEQN
|
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 gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. {ECO:0000255|HAMAP-Rule:MF_03185, ECO:0000269|PubMed:11262402, ECO:0000269|PubMed:178659, ECO:0000269|PubMed:4372217, ECO:0000269|PubMed:9445396}.
|
C4M1P9
|
DBR1_ENTH1
|
Lariat debranching enzyme (EC 3.1.4.-) (Intron debranching enzyme) (RNA lariat debranching enzyme)
|
MATEQIQHIAIVGCVHGKYREMYRQLSEYEKSTGKEISFVICTGDMQTLRYEADLVYLKVPPKYKQMGDFHLYYEGKEKAPYLTLFIGGNHESSNVLLHLYNGGFVCFNMYYLGVCSCININGLRIVGVSGIYKSFDEKKPYTYPPSPNDVVSLFHTRNYVIQMLSNLSQSSQIDISLSHDWPQGIVMKGNYKQLYRFQPGFKKDGASLGSPINKVILNTLKPKYWISGHMHCEYHAEEGPTHFIALGKIGYKNAISYLDLPLKQKTDLEYDKDWVCNLIMTWPAFSNKAQFPDLSYSISELLSKRTKELDKKIIELWEKYIGLKIIYDSDTFDIQFTSRRFYIEKIYNELNIN
|
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.
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C4M4P4
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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, stimulates the activity of optic nerve Na(+)/Ca(2+) exchanger.
|
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]
|
MPNRSFGVFPSVIYETRLGLSHQMRRPIGQPLSKLSQVSQPNQILQRNYQYKFPRIPRPKRNVLYYTFKRPQLSSATILRTVPSKIRNFSSRAKSKVKSSGRRRKFMSRWLALSSISVVLYGVVNKIKHKGIQRNSSLEPDENHSVKPNSWTLYAYSTLPLKAISRVWGQFNSFELPIWLRSPSYKFYAYVFGVNLDEVAEPDLSKFRNLGEFFYRTIKPETRPIDIDAEMVSPCDGKVLKFGIIENGEIEQVKGMTYSINALLGQQKLAAPVHRINYQLDDDDVVRRHEEFARLNGISYTIDDIIGGRGENIHHSYMNQGDQSLRKSSASQVYEVSNDIAKKSSFDKQLYFAVIYLAPGDYHRFHSPSNWVTTLRRHFVGELFSVAPFFQKTLQNLFILNERVALLGYWKHGFFSMIPVGATNVGSIKINFDKDLVTNSIYESDSYAQTSFPSSDTSSCREEDESTPLIKRSSSRTKKVIKNSCYEATYANASKILRGQPLSKGQEIGGFKLGSTVVLVFEAPKTFHFTLAENMKLKMGQRIGELR
|
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); Shikimate dehydrogenase (EC 1.1.1.25)]
|
MSGLIEKVSILRNDSIHVGYNMSSHIVDEILTKKASSTYVLITDSNIVKMGHLQTFVDEFNRLIPSKRPGSRILTYVVPPGEANKNRATKAAIEDYLLEKGCTRDTFILAIGGGVIGDMIGYVAATFMRGVRFVQIPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPDYVFVDVAFLETLPEREFINGMAEVVKTAAIWNEQEFSRLETYSKRFLKVIRDRRVDDSVDLTSLKEHIIKLVLESIKVKAEVVTLDEREGGLRNLLNFGHSIGHAIEAILTPQALHGECVSIGAVLEAELSRYLGILSPVAVSRLYKCFAAYGLPVSIADKLVQKRTNGKKCPVDVLLQKMAIDKKNDGSKKKVVLLSKIGKCYEPKASYVNDEDLRFVLTDEVLVKDFNSAPSTAVVVPPGSKSISNRALILAALGKGECKIKNLLHSDDTEHMLNAVAALKGADISFDDNGETVVVTGNGGNFTATDAEIYLGNAGTASRFLTSVASIVKPDSNTTHVILTGNARMQERPIGPLVDALRTNGSDIEYLNREGSLPLKIKSGNGLKGGRIELAATISSQYVSSVLMCAPYASEPVTLSLVGGKPISLLYVDMTIAMMKSFGIEVTKSTTEPYTYHVPQGHYVNPAEYVIESDASSATYPLAFAAMNGTQVTIPNIGSSSLQGDARFAVDVLKPMGCKVEQTATSTTVQGPTKGTLKPLPLVDMEPMTDAFLTASVVAAIANDTNQSTSIVGISNQRVKECNRIEAMITQLAKFGVRAKELEDGIEVFGIDYHHLKTPSDGVYTYDDHRVAMSLSLLAGLAESPVLIQERHCTGKTWPGWWDILHTTFNVELDGHEAVVETTTAKANEDKSIIVIGMRAAGKSTLSHVIAQTLKGFKVVDLDDVFVEKYGDIREFIKENSWELFREKEAMIAKEAFKNYSKNTVISTGGGIVETEASRKLLKQQMKDGHIVLHLHRDIEETVVFLSQDKTRPAYVDEINQVWERRKNLYKECSNYFFFSPHCQTEREFFTLKKTFSKFINRITGGAVPSIPNGRSAFVCLTYEDLAPVSSKLTRVTNGCDAVELRVDLLKQHDSHFISNQIGILRNQTSVPILFTIRTKSQGGRFPDDSYEDIERLLNLAIKLGVEYVDLELSLPESLLDSVASKRQFTKIIGSHHDFSGTVKWNNVEWENKYLLALKLNVDIIKFVGTATSLNDNWELEHFRSLHTDKPFIGINMGPLGKVSRVFNTILTPVTHKDLPSSAAPGQLTLKEINEYFGQFGGSSRKKFYIVGKPISHSKSPELHKTFYDEFGLSHTFDKFETDDAAKVFNDLVKGNDELGGCAVTIPLKIDMLKYVNELTDSAKSIGALNTIIPIGDGRFIGDNTDWIGIRDSLHQAGCEIAPESSVGLVVGGGGTSRAAVYALHQMGCSKIYMLNRTPSKLSEIKNHFPSNYNIHIVDSLDAIDEDDKLDAAVSTVPGDKPLDDQLISLLKKLLEKKRGHAVLLEAAYKPRETPIMALAFSRGWKVVPGSKMLVNQGIEQFYKWTGYQFSSHIDL
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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); Shikimate dehydrogenase (EC 1.1.1.25)]
|
MSQVEKVSILGSDSIHVGYGIQDHIVEETLTNLKSSTYVIITDSNMEATAPYQTLSSKFEAGLKEFRPESRLFYYAVSPGENNKSRETKAQVEDFLLQKGCTRDTVIIAVGGGVVGDMIGFVAATFMRGVRVVQVPTTLLAMVDSSIGGKTAVDTPLGKNFVGAFHQPKYVFVDVSFLTTLPTRQFINGMAEVVKTAAIWNEEEFTRLENFAKTFIAVVTSDNIDLATIKDDLVKTVLESIRVKADVVSADEKESSLRNLLNFGHTIGHAIEAIVTPQALHGECVAVGMVKEAELARYWGVLSPVAVARLVNCIAAYNLPTSVGDKIFVQRIGHKRHFIQINTLLEKMAIDKKNDGSKIRTVILEAIGKCYQLKAHEVSKQDLSFVLTDETLVHPFQEETTPKENVVIPPGSKSISNRALILAALGKGTVRIKNLLHSDDTKHMLAAVAALKGAEISTEDNGDTIVVKGNGGNFITCDEQLYLGNAGTASRFLTTVASLVNVNEQSNDYTVLTGNARMQERPVGPLVNALRANGSEIEYLNNEGSLPLKIKAGKGLKGGRVELAATISSQYVSSILMCAPYAEKEVTLALVGGKPISQLYIDMTIAMMKDFGISVTRDPHEEHTYHIPKGVYSNPGVYEVESDASSATYPLAFAAMTGTSCTVPNIGSSSLQGDARFAVDVLKPMGCTVEQTSTSTTVRGPSKGSLKPLTHVDMEPMTDAFLTASVVAAIANSSVPTQITGIANQRVKECNRILAMVDELAKFGVRAEELPDGIEIYGIDYKNLKVPSLENRGVCTYDDHRVAMSFSLLAGMCPEPVLITERSCTGKTWPGWWDVLHTKFGVELEGYEEPKDLNDPALLVNKEVNGDKSIVVIGMRAAGKSTLSRWIADFMGFELIDLDTVFEQTHGDIREYIKANGWGRFRELEAGIMKEYLTKCSSRHVISTGGGIVESEESRDILKSYTKTGGIVLHLHRDLDETIVFLSSDTTRPAYVSEIKDVWARREKWYHECSNYHFYSSHCGTEEEFKKLRHSFVSYLKTITGAGLSPVPKGRSFVLSLACSDLNDIAENLEDIVAGCEAIELRVDLLKDYSPSFVADQTAVLRKFVNLPIIYTIRTKGQGGNFPDEDVQALEQLSYLGIKLGVDYLDVQLSNSEKFVKSIIEKKAFTKIIATHIDLAGLPWTRAEWDNKYNQGISLNADVIQLVGFAHAFQDNIDLEQFRANHTITPLIAFNAGEHGKLSRVLNRTLTPVTSELLSNVSGNGQLTVGEINRCFSEIGGLSRRNFYIVGNPISHSRSPQLHTAGYEKLNLPHRFSKFETDYAQKVYEEVMTKPGFGGLAVTIPLKLDIMKYVSELSESAKIIGAVNTVTPLDGQPGKFYGDNTDWYGITQSFVRHGVPSFGNSSVNGMVVGGGGTSRAAAFALHQMGCKKIYMVNRTTSKLHEIKSSLPSDFNIEVLETVDQVEAADPVSLVVSCVPADKPLDSELLNKVERILYHGKNQEKRSFVPTLLDAAYKPRVTPIMKIAEEKFGWAVVPGVEMLVNQGVLQFKVHTVFTPPYKNVYEAVVDDNV
|
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)
|
MSTNKITFLLNWEAAPYHIPVYLANIKGYFKDENLDIAILEPSNPSDVTELVGSGKVDMGLKAMVHTLAAKARGFPVTSIGSLLDEPFTGICYLEGSGITSDFQSLKGKRIGYVGEFGKIQVDELTKHYGMTPDDYVAVRCGMNVAKYILEGTIDCGIGIECIQQVELEEALKEQGKDSNDAKMLRIDKLAELGCCCFCTILYIANDKFIAENPQAVKKFLKAIKRATDYMLAHPREAWAEYGNFKPTMQTDLNTKKFQRCYAYFSESLYNVHRDWRKVNNYGKRLDILPENYVPNYTNEYLSWPEPKEVDDPEKAQDLMLKHQEECKTCGGYKRLVLA
|
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 can only undergo a single turnover, which suggests it is a suicide enzyme.
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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 lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}.
|
C5C7X8
|
GYRB_MICLC
|
DNA gyrase subunit B (EC 5.6.2.2)
|
MVDAMPENPAEEPTAASAAPNPEAVPDAVGQPEAPVKDRKVPGEYGASAITVLEGLEAVRKRPGMYIGSTGPRGLHHLVYEVVDNSVDEALAGYATGIDVTLQADGGVRVADDGRGIPVDLHPTEGRPTVEVVMTILHAGGKFGGGGYAVSGGLHGVGISVVNALSRRVDTEVRRQGHVWRMSFADGGVPQGELVKGEATDATGTVQTFYPDAEIFDSIEFDYETLRARFQQMAFLNKGLRITLTDERVQESNEVVDDEIAGEGAAGEDVAENGLAEDAEQEPQRRSVTYLYENGLLDYVQHLNSAKKVEYVHDDVIAFEAEDFSDGRSMAVEVAMQWTSAYSESVHTYANTINTHEGGTHEEGFRAALTSLVNRYAREKEILKPKEDNLSGEDIREGLTAVISVKLSEPQFEGQTKTKLGNSEARGFVSKAVTDHLGDWFERNPGPAKEIIRKAIMASHARLAARKARDNARRKSPLESFGMPGKLADCSSKDPERCEVYIVEGDSAGGSAKQGRNPETQAILPLRGKILNVERARLDKALGNAEIQSMITAFGTNIGEEFDISKLRYHKIVLMADADVDGQHITTLLLTVLFRYMRPLIEAGHVFLAQPPLYRIKWSNAPHDYVFSDEERDAAVEAGLAKGWRYPKDNGVQRYKGLGEMNYQELWDTTMDPEHRTLLQVTMEDAAAADAVFSMLMGEDVESRRTFIQQNAKDIRFLDV
|
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 manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. {ECO:0000255|HAMAP-Rule:MF_01898}.
|
C5C7X9
|
GYRA_MICLC
|
DNA gyrase subunit A (EC 5.6.2.2)
|
MSDETTPQTPDEPVEGAPIPGTPQTGLDIEVEHYVLPEGAADKVEPVDLESEMKRSYLDYAMAVIVGRALPDVRDGLKPVHRRVLYAMYDGGYRPDRAFNKSARVVGDVMGNYHPHGDTAIYDALVRLIQDWVQRYPLALGQGNFGSPGNDGAAAQRYTETKMAPLAMEMVRDIDEDTVDMQDNYDGKQQEPVVLPARYPNLLVNGSSGIAVGMATNIPPHNMREVAAGVQWYLEHPEATREELLEALLARVHGPDFPTGAQILGRKGIEEVYRTGRGPITMRAVVNVEEIQGRTCLVVTELPYMTNPDNLAAKIAEMVRDGKISGIADMRDETSGRTGQRLVIVLKRDAVAKVVLNNLYKHTELQSNFSANMLALVDGVPRTLSLDGFVHHWVKHQIDVIVRRTAFRKRKAEERAHILRGLLKALDMLDEVIATIRRSASADVAREALKELLDIDDVQAQAILQMQLRQLAALESQKIQDEYDDLMAKIAEYNRILESPQRQREVISEELAEIVAKHGDDRRTEIMAGFDGDMSIEDLIPEEEMVVSITRGGYVKRTRIDQYRSQARGGKGVRGATLRGDDVVEHFLTVSTHHWLLFFTNFGRVYRIKTYELLEAGRDAKGQHVANLLAFQPDERIAQIQPLVDYGRAPYLVLATRGGLVKKTPLLDYDTNRTAGLIAIKLREGDELVSARVVSPDDDLILISHKGQSLRFTATDEALRPMGRATSGVTGMKFRDDDSLLTMDVVEEDGYVFTVTDGGFAKRTHVDEYRLQNRGGLGIKVAKLVDDRGELAGGLVVREDQEVLVVMASGKVVRSAVAGVPAKGRDTMGVIFAKPDKRDRIVAVTLNNEQEMEAKADAEAEAGPDVPLDADIDPTDPVAAPEDALTQDAGEGADGGEQ
|
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 manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. {ECO:0000255|HAMAP-Rule:MF_01897}.
|
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); Shikimate dehydrogenase (EC 1.1.1.25)]
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MKVELSKVPILGKDVVHVGFDIADHIVDTIFQSCPSSTYVVINDTNVEKIPHYVDLCGELQAKLKSGSRILQYSVKPGEAHKTREQKAAIEDYLLSEGCTRDTVIIAVGGGVIGDMIGYVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAVDTPLGKNFIGAFWQPQFVFVDIKWLETLPKREFINGIAEVIKTACIWNAEEFARLEENADLFLQVVNGSKTTQVSVQGQVHELSLTNIDAMLEHVYRLVLESIKVKTHVVSSDEREAGLRNLLNFGHTIGHAYEAILTPQALHGECVSIGMIKEAELSRYLNILSPTQVARLTKILAAYGLPISPDQKWFKDLTLNKKTPLDVLLKKMSIDKKNDGSKKKAVLLETIGKCYGTSAHVVSDEDIRFVLTDETLVYPFKTLENGQEKTIVPPGSKSISNRALILAALGEGTCKIKNLLHSDDTKHMLHAVQQLKGATITWEDNGETVVLKGHGGSTLQATAEPLYLGNAGTASRFLTSVAALVNSTSSQKSVVLTGNARMQERPIGPLVDSLRENGISIDYLNKEKSLPLKINTDSNFKGGRIELAATVSSQYVSSILMCAPYAEEPVTLALVGGKPISKLYIDMTIKMMEKFGIYVKASTEEPNTYHIPKGHYVNPPEYVIESDASSATYPLAYAAMTGTTVTVPNIGFESLQGDARFARDVLKPMGCSVTQTETSTTVTGPPVGGLKPLKHVDMEPMTDAFLTACVVAAVAHDGKEGSRNTTTIEGIANQRVKECNRILAMVDELAKFGVEANELPDGIQVHGLSSIDKLKVPEAIHSYDDHRVAMSFSLLAGMVGATKDALSEPVRILERSCTGKTWPGWWDVLHTQLGAKLDGSEPLQSAVKKNSNSSIVIIGMRAAGKTTVSSWCANALGFKFLDLDTVFEEQYKKGSVKEFVAEHGWDAFRATETKIFEESVKKYGEGYVLSTGGGIVEGAASRKSLKQFASQGGIVLHLHRDIDETIKFLNSDPTRPAYNEDIRNVWERREEWYKECANFTFYAPHCTSSTQFNQLRKTFETFIRTISGKREVKIPTNRSSFVCLTFDDLAAHKEKIPDITAGCSAVELRVDQLKSYDLDFVAKQLSILRLASSSLPIIFTIRTKSQGGQFPDDDKSTLGSLLSLALEVGVEFVDMELTLSSELQYSLVNNKRNTKIIGSHHDFDAKFDWNDSEWENRYNQALSLDVDVVKFVGTAKDFEDNLKLEQFRLQHTAKPLIAINMTDVGKMSRVLNTVLTPVTSSLLPSASAPGQLTLSQINEIYTLLGGFSAKNFYVVGSPISHSRSPVLHNTGYKILGLPHKFEKFETSSASEVKDKLLSKCKLGGLAVTIPLKLDIMEFMDELSESAKLIGAVNTVIPLGDGKFKGDNTDWLGIYNSFLANGVPENVRGNSGFVIGAGGTSRAAVYALHQLGCSDIHLVNRTVEKPHDLKKSFPSEYNLHVLEDSQQAEGISGSVALAVSCVPADKPLDDNLLARVRAVLAKAQGTSFKPTLLEAAYKPAVTPMMKTASDEFSWHIIPGSQMLVHQGVAQFQLWTGFRAPFNAIYSAVTEEQA
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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C5DRQ1
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MMM1_ZYGRC
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Maintenance of mitochondrial morphology protein 1
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MESNYTGMDGNWALNGTVSVGNGTLISVDEFLHNALPMHLQALFQDGNSQGPLLTMEDLEKAIEFKRASQELVNDNVLAPDGLFVELLRQQEKTLPRLISATSNTQGSFSSWSFAQGLIVGQVSVVLVLIFFIKFFIFSDSSTKTNPNPAKNSSSTNSLSGLSSESRSFISPHFFTSIMNRKGNEQAESNDDENERSRQIDDILEKTYYNVDTHPAESLDWFNVLIGQTIQQLREEAWKKDNIVYSLNAFIERKAQELPSYLDSIKITELDIGHDFPIFSNCRIQYSPNSNGRKLEAKIDIDLNDRLAVGIETRLLLNYPKPLTASLPINVTVSIIRFQACLTVSLTKAEEFVPTSPESVDEDDNDGYFLMFSFAPEYRMEFETQSLIGARSKLENIPKIGSLVEYQIKKWFVERCVEPRFQFIKLPSVWPRSKNTREGKADVDESEPGRETHY
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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 similarity). Preferentially binds to glycerophospholipids such as phosphatidylcholoine (PC), phosphatidic acid (PA), phosphatidylglycerol (PG), and phosphatidylserine (PS), but not to phosphatidylethanolamine (PE). The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids (By similarity). {ECO:0000255|HAMAP-Rule:MF_03103, ECO:0000269|PubMed:29078410}.
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C5DVG6
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ARO1_ZYGRC
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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); Shikimate dehydrogenase (EC 1.1.1.25)]
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MVKFEKVPILGKESIHVGYDIHTDMVQTIINDCRSSTYVVVNDTNLSKVPYCQDFVQELRSSLPEGSRLLQYAVKPGEANKTRSTKADIEDYLLSKGCTRDTVIIAIGGGIIGDMVGFVAATFMRGVRVVQVPTSLLAMVDSSIGGKTAVDTPLGKNFIGAFWQPQFVLVDVKWLETLPRREFINGMAEVIKTACIWNGLEFERLESNAELFLRVVNGSKVIKVNGLSTGEVNDIHYTNIEAMLEHTFKLVLESIKVKAEVVSSDERESSLRNLLNFGHSVGHAYEAILTPQALHGECVSIGMIKEAELSRYLGILSPTQVSRLTKILAAYGLPISPEEKWFKDLTLQKKTPLDVLLQKMSIDKKNDGSKKKVVILESIGKCYGKSAHYVNDEDLKFVLTDETLVYPFSNIPQEQAKTIVPPGSKSISNRALILAALGKGTCKIKNLLHSDDTKHMLTAVQELKGASITWEDNGETVVLEGHGGETLTASADPLYLGNAGTASRFLTTLAALVNSSSKQDYVVLTGNARMQQRPIGPLVDSLRTNGTKIDYLKSEGSLPLKIYTSTPFKGGRIELAATVSSQYVSSVLMCAPYAENPVTLALVGGKPISQLYVDMTIKMMEKFGIKVEVSTTEPYTYHIPKGQYTNPPEYIIESDASSATYPLAFAAMTGTTVTVPNIGYESLQGDARFAIEVLRPMGCKVEQTANSTTVTGPPTGSLRPLKHVDMEPMTDAFLTASVVAAVAHDNDTDSANVTTIEGIANQRVKECNRIEAMSTELAKFGVATKELPDGIQIHGINSLDLLQLPSNSTGPIGIESYDDHRVAMSLSLLAGMVNYSKSHPAADIKPVRILERRCTGKTWPGWWDVLHTELGAHLDGAEPLGYLSGKKTKRSVVLIGMRAAGKSTLGRWCSQILGYELCDLDVLFEKQYAKGTVKDFVAEHGWDKFREAEANLFKETVEQYGDGGYVFSAGGGLVENEVSREHLKKYASDGGVVLHLHRDIEETIVFLQSDPTRPAYMEEIRDVWERREKWYNECSNFAFLAPHCSNEKEFQHLRKSFANYITAITGNREVQVPNKRSAFVCLTFGDLTEKASVLPSIVRGCDAVELRVDHLAKYDSQFVSKQLSTLRTATNDLPIVFTLRTKKQGGKFPDEDYTGMARLFDVALKACVEYIDLELTLPIDVQYKVSNTKGYTKIIGSHHDFGAKYPWKDPEWENRYNQALSLDVDVIKFVGTATKFEDNLALERFREEHKSKPLIAINMGEIGKISRVLNPILTPITSEHLPNSSAPGQLTLAQINKIFASMGGITSKKFFVVGNPVSHSRSPVLHNTGYKLNGLPHHFDRFETDSAQVVKETLLDGEPSLGGLAVTIPLKLDIMKYMNQLTDAARVIGAMNTVIPLGNHHFKGDNTDWIGIKHSLTSNGVPEKVSNVAGLVIGAGGTSRAAIYSLHNLGCHRIFVINRTVSKSIELRDSFPQEYNVVAAETTQQIDHLNEHIGIAVSCVPADKDLDTELLAKLERFLHKGKHNSFVPTLLEAAYKPDVTPVMKLAHDKYQWQVVPGRELLVHQGVAQFEIWTGAKAPFQEIFNAVTRD
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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C5FQ73
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ARO1_ARTOC
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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); Shikimate dehydrogenase (EC 1.1.1.25)]
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MEQPTTIQILGRDSIVADFGIWRRHVARDLLETLSSSTYILISDTNIAPLYVPEFERAFEEAAAEKSPKPRLLTYKIAPGESSKGRETKAEIEDWMLSCQPPCGRDTVLIALGGGVIGDLAGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPEKIYLDMEFLNTLPQREFTNGMAEVIKTAAISSETTFAELEQNADAIAAALKTENTPERSRFSGIQEILKRTILASARFKADVVSKDEREGGLRNLLNFGHSIGHAIEAILAPQILHGECVAIGMIKEVELARYLGILKGAAVARLAKCLTRYGLPTSLKDARIRRLSAGKKCPVDKLIAFMAVDKKNDGPMKKVVLLSAIGRTHEQKASVVSNEELKVVLAPSIEVLPGIPKPLNVTCTPPGSKSISNRALVLAALGSGVCRIRNLLHSDDTEVMLNALEALGAATFSWEEEGEVLVVNGKGGKLEASAHELYLGNAGTASRFLTTVATLSNEKDDVSHNILTGNARMKQRPIGDLVDALKSNGVSVDYLEQQGSLPLKVPACGGFKGGAIELAAKVSSQYVSSLLMCAPYAKEKVTLKLVGGKPISETYIAMTAAMMKSFGIDVEKSTTEEYTYHIQQGQYKNPPEYIIESDASSATYPLAIAAMSGTTCTIPNIGSKSLQGDARFAVDVLRPMGCDVKQTNSSTTVTGPTNGALKPIANVDMEPMTDAFLTASVLAAVANDKSGNTTRIYGIANQRVKECNRIKAMKDELAKFGVTCREHDDGIEIDGIDSSELKVPVNGVHCYDDHRVAMSFSVLAAAAASQPTLILEKECVGKTWPAWWDALAQTFKVKLDGKELVNDNVVDIQKSTKSIASIFIIGMRGAGKTTSGYSISKALNRPFIDLDTELENVEGMPIPEIIKQKGWEGFRDAELALLKRMMAEKPTGYIFACGGGIVETKEARDLLINYHKNKGNVFLIMRNIKKVIEFLEIDKTRPAYIEDMMGVWLRREPWYQECSNLQYYSHHSERSELDAALQGFTRFLNVVMGNTDHLALLKKKDHSFFVSLTLPDLQLSADILRAATFGSDAIELRVDLLKDPSSTSGVPSVGYVAEQMSFLRSHASQPLIFTIRTKAQGGQFPDDAVDKALELYKLAIRMGSEFVDLELSFPNDLLHAVTEMKGFSKIIASHHDVNSQLSWSNGSWIQYYNKALQHGDIIKLIGVAKTFEDNMALQQFKSWAEKSYPVPIIAINMGNKGRLSRILNRFMTPVSHPALPFKAAPGQVSAKDIRQALTLMGELDAKKFALFGKPISASRSPALHNALFTQAGFPHDYGLLETDKAENVEKFIRSDDFGGASVTIPLKEQIMGLLDEISPEAKIIGAVNTIVPITVSGRPPRLIGYNTDWQGMARCLKDAGAICSNNGESALTIGSGGTARAAIYSLHSMGYSPIYLVGRTPSNLSKLASSFPAEYNIQVVQDIKSVQAAPKVAISTIPGDQELENPLPELITQIMEKGQDSSRECILLDMAYKPDVTTMARLASPAGWKIIKGLEVLVAQGIYQFEHWTGLMPIYEDARAAVMNI
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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C5G6D7
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CABC2_BACT4
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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)
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MLILSFLCPAFLNAQIVTDERMFSFEEPQLPACITGVQSQLGISGAHYKDGKHSLEWTFEPNGRLELRKDLKFEKKDPTGKDLYLSAFIVWIYNEQPQDAAIEFEFLKDGRKCASFPFGINFKGWRAAWVCYERDMQGTPEEGMNELRIVAPDAKGRLFIDHLITATKVDARQQTADLQVPFVNAGTTNHWLVLYKHSLLKPDIELTPVSDKQRQEMKLLEKRFRDMIYTKGKVTEKEAETIRKKYDLYQITYKDGQVSGVPVFMVRASEAYERMIPDWDKDMLTKMGIEMRAYFDLMKRIAVAYNNSEAGSPIRKEMRRKFLAMYDHITDQGVAYGSCWGNIHHYGYSVRGLYPAYFLMKDVLREEGKLLEAERTLRWYAITNEVYPKPEGNGIDMDSFNTQTTGRIASILMMEDTPEKLQYLKSFSRWIDYGCRPAPGLAGSFKVDGGAFHHRNNYPAYAVGGLDGATNMIYLFSRTSLAVSELAHRTVKDVLLAMRFYCNKLNFPLSMSGRHPDGKGKLVPMHYAIMAIAGTPDGKGDFDKEMASAYLRLVSSDSSSAEQAPEYMPKVSNAQERKIAKRLVENGFRAEPDPQGNLSLGYGCVSVQRRENWSAVARGHSRYLWAAEHYLGHNLYGRYLAHGSLQILTAPPGQTVTPTTSGWQQEGFDWNRIPGVTSIHLPLDLLKANVLNVDTFSGMEEMLYSDEAFAGGLSQGKMNGNFGMKLHEHDKYNGTHRARKSFHFIDGMIVCLGSDIENTNMDYPTETTIFQLAVTDKAAHDYWKNNAGEGKVWMDHLGTGYYVPVAARFEKNFPQYSRMQDTGKETKGDWVSLIIDHGKAPKAGSYEYAILPGTDRKTMTAFAKKPAYSVLQQDRNAHILESPSDRITSYVLFETPQSLLPGGLLQRTDTSCLVMVRKESADKVLLTVAQPDLALYRGPSDEAFDKDGKRMERSIYSRPWIDNESGEIPVTVTLKGRWKVVETPYCKVVSEDKKQTVLRFLCKDGASYEVELEK
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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 sulfate, heparin or heparan sulfate.
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C5G8R4
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ARO1_AJEDR
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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); Shikimate dehydrogenase (EC 1.1.1.25)]
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MGVPTKISILGRESIVADFGIWRNYVAKDLLNSCSSSTYILISDTNITPLYLDGFQKSFDDAAANLSPKPRLLTYEIPPGESSKSRETKAGIEDWMLTRQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALEDDAEIILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVAIGMVKEAELARHLGILNNVSVSRISKCLASYGLPTSLKDERIRKLTADKHCSVEQLITYMGVDKKNDGPKKKVVLLSAIGRTHEPRASTVSNEEIQIVLAPSIEVSPGVPKNLNVTCTPPGSKSISNRALVLAALGSGTCRLKNLLHSDDTEVMLNALERLGAATFSWENEGEVLVVNGKGGKMKASPDELYLGNAGTASRFLTTVATLAQKSSVDSSVLTGNARMKQRPIGDLVDALAANGAGVEYLENSGSLPLKIAASGGFAGGEINLAAKVSSQYVSSLLMCAPYAKKPVTLRLVGGKPISQTYIDMTTTMMRSFGIDVKKSETEEHTYHIPLGFYISPAEYIVESDASSSTYPLAVAAITGTSCTVPNIGSKSLQGDARFAVEVLRPMGCTVDQKDFSTTVTGPANGILRPLPNVDMEPMTDAFLTASVLAAVARGGGSNHTTRIFGIANQRVKECNRIKAMKDELAKFGVTCREHDDGLEIDGIDRSTLRHPSDGVYCYDDHRVAMSFSVLSLVAPQPTLILEKECVGKTWPGWWDSLAQTFKVKLDGKEVEKKTGRGGIVHLDKPAASIFIIGMRGAGKTTSGVWVSKALQRPFIDLDDELERTEGMTIPEIIKQRGWEGFREAELSLLRRVMTEKPTRYIFACGGGIVETPEARKLLIQYHKTKGNVILVMRDIKEIMDFLKIDKTRPAYVEDMMSVWLRRKPWYQECSNVQYFSRLTGLDGMAQVLGGFNRFLKVITGQVDSLAQMRSKENTFFVSLTLPDLAPAAPILKEVTLGSDAVELRVDLLKDPQSDSEIPSVDYVAEQISVLRSRTSVPLVFTIRTKAQGGRFPDDAYDAALQLYRLAIRMGSEFVDLEISFPEQLLRTVTEMKGFSKIIASHHDPKGELSWANGSWIQFYNKALQYGDVIKLVGVARSLDDNASLKKFKTWAEEKHDVPIIAINMGDKGQLSRMLNGFMTPVSHPSLPFKAAPGQLSAREIRKGLSLIGEIKSKKFAVIGNPVSASRSPAMHNALFRQMGLPHIYGTLETEDPEIVKKFIRSPDFGGASITIPLKLDIMPLLDEIAPEAVSIGAVNTIVCAPPAPDDQSQAPRLIGRNTDWQGMVRCLSDAGAYPAATPTTTSAGLVIGGGGTARAAIFALQSMGYSPIYVVGRSPDKLSSMTSTFAPDHDIRILEDVKALESLPTVAIGTIPGDKPIEPHMREILCELFDLCEKANSDAEQARGISTKRILLEMAYKPSVTSLMQLASDSGWTVLPGLEALVAQGVYQCEYWTDITPVYEDARNAVMGVQPKDDDIST
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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C5H429
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DBR2_ARTAN
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Artemisinic aldehyde Delta(11(13)) reductase (EC 1.3.1.92)
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MSENPPTLFSAYKMGNFNLSHRVVLAPMTRCRAINAIPNEALVEYYRQRSTAGGFLITEGTMISPSSAGFPHVPGIFTKEQVEGWKKVVDAAHKEGAVIFCQLWHVGRASHQVYQPGGAAPISSTSKPISKKWEILLPDATYGTYPEPRPLAANEILEVVEDYRVAAINAIEAGFDGIEIHGAHGYLLDQFMKDGINDRTDEYGGSLENRCKFILQVVQAVSAAIATDRVLIRISPAIDHTDAMDSDPRSLGLAVIERLNKLQFKLGSRLAYLHVTQPRYTADGHGQTEAGANGSEEEVAQLMKTWRGAYVGTFICCGGYTRELGLQAVAQGDADLVAFGRYFVSNPDLVLRLKLNAPLNRYDRATFYTHDPVVGYTDYPSLDKGSLL
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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.
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C5H431
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POLG_WSLV
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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 NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
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MATKGMNKSRARSRGVNMVAARVKNLAVKVKNKTKQSARGLRGFLLFLVAQIFWARKLTPQVKRLWRMVDKVQGLRILKNIRNIVTNLMKGLAGRKKKRSLTVPLVLLLIPLIAYSATVTRQRGLGLLLNVTFADVGKTYEVEGGNCSVNTLDAGKWCEDYVEYECVTLSEGEEPDDLDCWCYGVDNVRVTYGRCKSGGSRRSRRSAVITPHVDKGLTTRQEKWLPTKIGEQQLQKVEKWIMRNPLYALGAVALAYFVGTSNVQRVVIAILLLGIGPAYSTHCLGIPKRDFIRGLDGNTWVSVVLEQGSCVTLIADNKPSVDIWLSSIVVDTPTLVRKVCYASSVTGSKATGACPTMGDAHMSEEGNEEWECKRSYSDRGWGNGCGLFGKGSIVACAKFSCTHEMEVYQIDATKIEYTISAQVHSGAKKDDWENHTKLVTFVPTTGTSTVAFTGYGNFGLECHVQMMVDLSNSYLVKVGTDAWLVNKQWVHDITLPWQSGTGGHWRDKHFMVDFEEPHAVTMKALVLGSQEGALRTALSGAMVVELNSNRYSLKGGHVTCKAYMNNLILKGSTYSMCKRGMSFAKQPVETDHGTAVMQIKVTTGAPCRIPVIAADSMAGTENRGSVITTNPIAASNNDEVLVEISPPFGESYIIVGNGDDKLTYHWQRSGSTIGNLFTETMKGAQRMIITGEHSWDFGSTGGFFSSIAKAVHTVFGAAFHAIFGGLSWITKILIGGLLIWLGLNSRSSSMSMGFICIGALLLVLATGVGAEVGCSLSWKQREMKCGDGVFVFKDSDDWFSKYQYIPEDPKTMATLIHQAHQDGLCGLSSVSDLEHRMWYSRVDEINAILDENEVDLTVVVQESDAVYLRGSHAFPRPKSELKYGWKTWGKNIIFNPSRKNGTFIIDGKSKAECPFNKRVWNSIRVEEFGTGVYQTRVFMRPEFDYTKLCDTGTLGAAVKGSVSAHGDPMFWMESEEINGTWMITTLEALNYRECEWPSSHTLDGAKVVESDMFMPRSLAGPISKHNHIPGYKVQTSGPWHNVPLEIKREECPGTTVVVDEKCDDRAKSVRSTTDSGKIIPEWCCRSCTMPPVSFWGPDGCWYSMEVRPKHTNEAHLVKSWVVASKGDVDPFSLGLLMLFLCSDMFLMKRFSMRAILVGSLVMLGAMTLGSLSYLDLLRYAITVGMYMAEINSGGDVTHLALLAVFRVRAGFVSMLALKRLWSPREGFVATCGIVMVQLALGDILSTDIMEWLNAAGMAVLIIKSIVEPKRCNAVLPLLCLLTPLTVAEIQRAVMFVCSIVIFVTVWQTDSVSTRKTIPLVALTVCSFFKWTSPFLGIVCYLAFTRLPQRSWPLGETMAAVGLVGVLAGMGLKDMNGMLGPVAVGGVLLIVMSLSGKVDGLVIKKVADVTWDEDAEISGASHRYDVEQTDTGEFKLRNEEPAPWIQVAVLTIAILSAATHPACLAVVTIGWFAWQKTTTRSGVLWDIPTVVPPEEVSYLEDGVYTINQNSFLGLAQKGVGVVKDGVFHTMWHVTRGAFLLHAGKRMTPSWANVKEDLISYGGGWKLDAKWDGSEEVQLIAVSPGKVPVNVQTTPSVFQLKNGKEIGAVNLDYPSGTSGSPILNKNGDVIGLYGNGILIGNNTYVSAIAQSDSVEEGGTEQLQDIPTMLKKGMLTVLDFHPGAGKTRIYLPQILKECEKLKLKTLVLAPTRVVLSEMREAMPKMSIKYHTQAFSNTSTGKEIIDAMCHATLTHRMLEPTRVTNWEVVIMDEAHFMDPASIAARGWAAHRSRARECATIFMSATPPGTSNEFPESNGMIEDVKKDVPSEPWTKGHEWILEDRRPTAWFLPSIRIANSIANCLRKADRTVVVLNRKTFEKEYPTIKSKKPDFILATDIAEMGANLKVERVIDCRTAYKPILVDDATKVMVKGPLRISASSAAQRRGRIGRDPNRDTDTYIYGDSTTEDNGHYVCWTEGSMLLDNMEIRNGMIAPLYGVEGTKTTTSPGETRLREDQRKVFRELVKRLDMPVWFSWQVAKAGLKVQDRSWCFDGEDDNTLLNDNGEPILARSPGGAKKPLKPRWVDTRVCSDNASLIDFIKFAEGRRSASGILLGLQGFPEFLSGKMREAIDTVTVLYTSDTGSRAYKHALAMMPEATTIFLLVMLAIICTSGVIMFFLAPKGLSRMSMAMMTMLVSAYLMSLGGMNPVQISCVMLVFFIFMVVLIPEPGTQRSTYDNQIIYLLVGVLSLILLVAANEMELLEKTKRDIFGAVVVEEAKRWTFPEFDLRPGAAWTVYVGLVTPGNPMLHHWIKIDYGNISLSGITQNAQVLGLMDRGIPFIKMNMSVVILLLSAWNGITLLPLFAGMGAAALHWGFILPGLRAQAAKAAQKRVYHGVAKNPVVDGNPTVDIDDAPGMPAMYEKKLALVILLALSILNLVLTRTPFATAEMVVLGSAAVGPLIEGDTNAYWNGPIAVAFSGLMRGNYYATIGLAYNGWLAKQTRRGKAAGVTLGEVWKRQLNMLGKQEFERYKVPDITEVDRTAARRYLKEGRTDVGISVSRGAAKIRWLHERGYLRITGRVLDLGCGRGGWSYYAAAQKEVMSVKGYTLGIEGHEKPIHMQTLGWNIVKFKDKSNVFTMPTEPSDTLLCDIGESSSNPLVERDRTMKVLENFERWKHVNTENFCVKVLAPYHPDVIEKLERLQLRFGGGIVRVPFSRNSTHEMYYISGARNNITHMVNTTSRSLLRRMTRPSGKAIIEGDVFLPTGTRSVASEAGTIDHEALKLRVDQIKAEYSKTWTHDSNHPYRTWHYLGSYLCKATGSSSSMINGIVKMLSMPWDKFESVTLLAMTDTTPFGQQRVFKEKVDTKAPPPPPGTRAIMRVVNAWLFQHLARKKKPRICTREEFVAKVRSHAALGAYLEEQDKWKSASEAVQDPQFWKLVDDERKLHLQGQCRTCVYNMMGKREKKPSEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWVSRENSGGGVEGTGLQYLGYILKELGGKTGGNMYADDTAGWDTRITEEDLEDEQEILKYMDEKHKKLAWAVTELAYKNKVVKVMRPGPGGLTFMDIISRRDQRGSGQVVTYALNTVTNLKVQLIRMAEAEHVITNFDVDTVSQKTLQDLRCWLDRFGADRLSRMAVSGDDCVVKPIDDQFADALTHLNSMSKIRKDIDDWKPSQGWASWEDVPFCSHHFHELILKDGRSIIAPCRDQDELIGRARVSPGNGWMIRETACLSKAYAQMWLLMYFHRRDLRVMANAINSTVPVDWVPTGRTTWSIHGKGEWMTTEDMLQVWNRVWIEDNPHQTDKTPITEWRDIPYLPKSIDKTCNSLVGTTQRASWARDIKHTVHRIRGLVGNEKYTDYLATMDRFRELDESGPGEVLW
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[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 cell nucleus where it modulates host functions. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity). [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition.
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C5H8J1
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EME1B_ARATH
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Crossover junction endonuclease EME1B (EC 3.1.22.-) (Essential meiotic endonuclease 1B) (AtEME1B)
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MNDHILISDGEDQTTPLPSLSKRARKYPISAILISDSDPTPQKQPPESSFTPIFVPETPLSDDFSVVKCSFGSRALASNREDKFSGKRIISLDSEFEDSPRPETSKKNESVLAGLREPRFGLEAETSEAYYKNTRIPETNLDDDTSWMHEVSFRSSPTNDTIEVVSDQEKEDISVEKIGRKKKIRTTTLPVPGEALPKKRQSKEDKTSAMEEKKLRKEQERLEKAASKAEEAERKRLEKEKKKWEKGKLALKSIVAEIDTKVLEGSIGGLLLSRFSEKGITIHVGPNPIERSIVWTMTIPEDIAPLFPQGPKIPYLLLVYDAEEFCNLVANGKFLEIISRVQDRYPSYTVCCLTNKLMSYVKKREKEEYKNPGNWRRPPIDEVLAKLTTHYVKVHSRHCVDEAEVAEHIVGLTSSLASCQFRKKLTMLSVSANGALVSKDSVDKHLIKKSPWLKALVAIPKVQPRYALAVWKKYPSMKSLLKVYMDRNKSVHEKEFLLKDLKVEGLVGGDIRLGEICSKRIYRVLMSHDGAIKTDDVENGAAFFTDSPGVN
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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. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. Plays a role in DNA repair and in genotoxic stress-induced homologous recombination (HR) in somatic cells. Mediates a subset of meiotic recombination events that are insensitive to crossover interference.
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C5I9X1
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ALDH1_ARTAN
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Aldehyde dehydrogenase 1 (EC 1.2.1.-) (Artemisinic aldehyde oxidase) (Artemisinate synthase) (Dihydroartemisinic aldehyde oxidase)
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MSSGANGSSKSASHKIKFTKLFINGEFVDSISGNTFDTINPATEEVLATVAEGRKEDIDLAVKAAREAFDNGPWPRMSGEARRKIMLKFADLIDENADELTTLEVIDGGKLFGPVRHFEVPVSSDTFRYFAGAADKIRGATLKMSSNIQAYTLREPIGVVGHIIPWNGPAFMFATKVAPALAAGCTMVIKPAEHTPLTVLFLAHLSKLAGVPDGVINVVNGFGKTAGAAVSSHMDIDMVTFTGSTEVGRTVMQAAALSNLKPVSLELGGKSPLIVFDDADVDKAAEFAILGNFTNKGEMCVAGSRVFVQEGIHDVFVKKLEGAVKAWATRDPFDLATRHGPQNNKQQYDKVLSCINHGKKEGATLVTGGKPFGKKGYYIEPTLFTNVTDDMTIAKEEIFGPVISVLKFKTVEEVIKRANATKYGLASGVFTKNIDVVNTVSRSIRAGAVWVNCYLALDRDAPHGGYKMSGFGREQGLEALEHYLQIKTVATPIYDSPWL
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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 as proton donors (Ref.1). {ECO:0000269|Ref.1, ECO:0000303|PubMed:27488942}.
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C5JKE6
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ARO1_BLAGS
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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); Shikimate dehydrogenase (EC 1.1.1.25)]
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MGVPTKISILGRESIVADFGIWRNYVAKDLLNSCSSSTYILISDTNITPLYLDGFQKSFDDAAANLSPKPRLLTYEIPPGESSKSRETKAGIEDWMLTRQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALEDDAEIILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVAIGMVKEAELARHLGILNNVSVSRISKCLASYGLPTSLKDERIRKLTADKHCSVEQLITYMGVDKKNDGPKKKVVLLSAIGRTHEPRASTVSNEEIQIVLAPSIEVSPGVPKNLNVTCTPPGSKSISNRALVLAALGSGTCRLKNLLHSDDTEVMLNALERLGAATFSWENEGEVLVVNGKGGKMKASPDELYLGNAGTASRFLTTVATLAQKSSVDSSVLTGNARMKQRPIGDLVDALAANGAGVEYLENSGSLPLKIAASGGFAGGEINLAAKVSSQYVSSLLMCAPYAKKPVTLRLVGGKPISQTYIDMTTTMMRSFGIDVKKSETEEHTYHIPLGFYISPAEYIVESDASSSTYPLAVAAITGTSCTVPNIGSKSLQGDARFAVEVLRPMGCTVDQKDFSTTVTGPANGILRPLPNVDMEPMTDAFLTASVLAAVARGGGSNHTTRIFGIANQRVKECNRIKAMKDELAKFGVTCREHDDGLEIDGIDRSTLRHPSDGVYCYDDHRVAMSFSVLSLVAPQPTLILEKECVGKTWPGWWDSLAQTFKVKLDGKEVEKKTGTGGIVHLDKPAASIFIIGMRGAGKTTSGVWVSKALQRPFIDLDDELERTEGMTIPEIIKQRGWEGFREAELSLLRRVMTEKPTGYIFACGGGIVETPEARKLLIQYHKTKGNVILVMRDIKEIMDFLKIDKTRPAYVEDMMSVWLRRKPWYQECSNVQYFSRLTGLDGMAQVLGGFNRFLKVITGQVDSLAQMRSKENTFFVSLTLPDLAPAAPILKEVTLGSDAVELRVDLLKDPQSDSEIPSVDYVAEQISVLRSRTSVPLVFTIRTKAQGGRFPDDAYDAALQLYRLAIRMGSEFVDLEISFPEQLLRTVTEMKGFSKIIASHHDPKGELSWANGSWIQFYNKALQYGDVIKLVGVARSLDDNASLKKFKTWAEEKHDVPIIAINMGDKGQLSRMLNGFMTPVSHPSLPFKAAPGQLSAREIRKGLSLIGEIKSKKFAVIGNPVSASRSPAMHNALFRQMGLPHTYGTLETEDPEIVKKFIRSPDFGGASITIPLKLDIMPLLDEIAPEAVSIGAVNTIVCAPPAPDDQSQAPRLIGRNTDWQGMVRCLSDAGAYPAATPTTTSAGLVIGGGGTARAAIFALQSMGYSPIYVVGRSPDKLSSMTSTFAPDHDIRILEDVKALESLPTVAIGTIPGDKPIEPHMREVLCELFDLCEKANSDAEQARGISTKRILLEMAYKPSVTSLMQLASDSGWTVLPGLEALVAQGVYQCEYWTDITPVYEDARNAVMGVQPKDDDIST
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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C5M1X2
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ARO1_CANTT
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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); Shikimate dehydrogenase (EC 1.1.1.25)]
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MSIEKVPILGKETIHVGYGIQDHIVTEVVDNLASSTYVIVTDTNVEKTPQFSKLTNDFTKVLNEKRPDSRVLTYSVPPGENNKNRATKAAVEDFLLQQGCTRDTVIIAVGGGVIGDMIGFVAATFMRGVRVVQVPTTLLAMVDSSVGGKTAIDTPLGKNFIGAFHQPQYVFIDVSYLESLPTRQFINGMAEVVKTAAIWNEEEFTRLENFSKQFLSVVTAKNPDLLSIKEELVKTVLESVRVKAEVVSSDEKESSLRNLLNFGHTIGHAIEAIVTPEALHGECVSIGMIKEAELARYLGILPPVAVARLSKCLVAYGLPVTIDDKLFLQRVGPKRHNIEIDLLLKKMSIDKKNDGSKIRSVILESIGKCYQLKAHEVSKQDLTFVLTDEVLVHPFKQPPQENVITPPGSKSISNRALILAALGTGTVRIKNLLHSDDTKHMLAAVAALKGAEITTEDNGETIVLKGNGGDLVTCDEELYLGNAGTASRFLTTVASLVGKSESNDHVVLTGNARMQERPIGPLVDALRSNGSEVQYLNKEGSLPLKITAGNGLKGGRIELAATISSQYVSSILMCAPYAKEPVTLALVGGKPISQLYIDMTCAMMKSFGIEVTKSTTEDYTYHIPKGTYKNPAEYVIESDASSATYPLAFAAMTGTSCTVPNIGSSSLQGDARFAVDVLKPMGCKVEQTATSTTVTGPPRGQLKPLPHVDMEPMTDAFLTASVVAAVAQGDSSTTITGIANQRVKECNRIEAMITELAKFGVKADELPDGIEIHGIDIADLKTPSIEKRGVCSYDDHRVAMSFSLLSGLCKEPVLILERSTTGKTWPGWWDILHSKFNIELDGYEPPFGTDKEGTKASDKSIIIIGMRGTGKSTLSEWLASFMGFKSLDMDVYLEEKLGNDIKSLIKEKGWEYFREQEAAIAKECFSKFSKGYVLSTGGGIVEGAENRQRLKDYITAGGIVLHLHRDLEETVSFLSVDTTRPAYTSEVKEVWLRREQWYDDCSNYHFYSSHCNTEEEFDHLRKSFVNFIKIITGTEKASIPSGRSAALSLTVPDLNAISSQLGDIAVGAEAVELRVDLLKETSSSFIADQIAVIRKHIDLPIIYTVRTESQGGKFPDNKVEELRNLLLLGVKLGVAFIDVELTAPVEVIEEIIIKKGYTRVIASYNDIAGKLGWSNVEWTNKYNQGVSINADIVKLIGRASSLQDNLELEVFRKQNTLKPLLAVNLGSQGKLSQVLNTIFTPITQESLPNEDGLLTIKEINQIYFDIGGLTAKKFWVIGSPIQHSRSPNLHNAAYKALNLPFTFDRFESTDADQVYKELINKPDFGGLAITMPLKLDIMKYATELSDAAQKIGAVNTLVPLEGGYLGDNTDWVGITSSFTRAGVPPNPRVNGLVIGAGGTSRAAIYALHQIGCEKIYLANRTTSKLNEIKDSFPKEYNLEVLETEDQAEKAQNVGLAVSCVPADKPLDESLLQKVEKILANGEKSSNGFKSTLLEASYKPRVTPMMKIADEKFKWRAIPGVEMLVNQGDRQFQIHTGFTAPYDVIHRAVVEE
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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C5MSH2
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POLG_SALVA
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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 3.4.22.28) (Picornain 3C) (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
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MEGSNGFSSSLAGLSSSRSSLRLLTHFLSLPTLPVNIYLNARRHSGWYRSPPTLPVNIYLNEQFDNLCLAALRYPGHKLYPSVHTLFPDVSPLKIPHSVPAFAHLVQRQGLRRQGNSITNIYGNGNDVTTDVGANGMSLPIAVGDMPTASTSEAPLGSNKGGSSTSPKSTSNGNVVRGSRYSKWWEPAAARALDRALDHAVDATDAVAGAASKGIKAGAAKLSNKLSGSQTTALLALPGNIAGGAPSATVNANNTSISSQALLPSVNPYPSTPAVSLPNPDAPTQVGPAADRQWLVDTLSWSETIAPLTVFSGPKALTPGVYPPTIEPNTGVYPLPAALCVSHPESVFSTAYNAHAYFNCGFDVTVVVNASQFHGGSLIVLAMAEGLGDITPADSSTWFNFPHTIINLANSNAATLKLPYIGVTPNTSTEGLHNYWTILFAPLTPLAVPTGSPTTVKVSLFVSPIDSAFYGLRFPVPFPAPQHWKTRAVPGAGTYGSVVAGQEIPLVGYAPAAPPRDYLPGRVHNWLEYAARHSWERNLTWTSADEVGDQLVSYPIQPEALANTQTNTAFVLSLFSQWRGSLQISLIFTGPAQCYGRLLLAYTPPSANPPTTIDEANNGTYDVWDVNGDSTYTFTIPFCSQAYWKTVDIGTSSGLVSNNGYFTVFVMNPLVTPGPSPPSATVAAFLHVADDFDVRLPQCPALGFQSGADGAEVQPAPTSDLSDGNPTTDPAPRDNFDYPHHPVDPSTDLAFYFSQYRWFGLNESLTPLDATGGLFYHISLNPINFQQSSLLSVLGAFTYVYANLSLNINVSAPSQPCTFYVFYAPPGASVPSVQTLAELSFFTHTATPLNLAAPTNITVSIPYSSPQSVLCTSFGGFGLQNGGDAGNLHSNTWGTLILYVDLPQSDSVSVSAYISFRDFEAYVPRQTPGVGPVPTSTSIVRVARPTPKPRTARRQGGTLADLILSPESRCFIVAHTTAPFYSILLVNPDEEYAISMFSHGDESILQYSSRSGTRLTPTAPAFFLCAAASVDTVLPYSISQSHLWLTDLTGIPLRAVPPLTLFLSAGAALCAGAQTLIAVAQGGSTPETPPTPNRALLRRQGLGDLPDAAKGLSAALESVARVAGDANIATSSQAIATSINSLSNSIDGATSFMQNFFSGLAPRNPTSPLQHLFAKLIKWVTKIIGSLIIICNNPTPSALIGVSLMLCGDLAEDITEFFSNLGNPLAAVFYRCARALGLSPTPQSAAQAAGGRQGVRDYNDIMSALRNTDWFFEKIMTHIKNLLEWLGVLVKDDPRTKLNGQHEKILELYTDSVTASSTPPSELSADAIRSNLDLAKQLLTLSHAANSVTHIQLCTRAITNYSTALSAISLVGTPGTRPEPLVVYLYGPPGTGKSLLASLLASTLAQALSGDPNNYYSPSSPDCKFYDGYSGQPVHYIDDIGQDPDGADWADFVNIVSSAPFIVPMADVNDKGRFYTSRVVIVTSNFPGPNPRSARCVAALERRLHIRLNVTARDGVAFSAAAALQPSNPPSATRYCKFANPLTQFSMFNLAVDYKSVVLPNTPLTCFDELVDFVLSSLRDRASVNSLLSGMVRTDVTRQGGNADAPAPSAAPLPSVIPSVPSQDPFTRAVNENRPVSFLSKIWSWRAPIFAASSFLSLIAATLTIVRCLRDLRSTQGAYSGTPVPKPRKKDLPKQPVYSGPVRRQGFDPAVMKIMGNVDSFVTLSGTKPIWTMSCLWIGGRNLIAPSHAFVSDEYEITHIRVGSRTLDVSRVTRVDDGELSLLSVPDGPEHKSLIRYIRSASPKSGILASKFSDTPVFVSFWNGKSHSTPLPGVVDEKDSFTYRCSSFQGLCGSPMIATDPGGLGILGIHVAGVAGYNGFSARLTPERVQAFLSHLATPQSVLYFHPPMGPPAHVSRRSRLHPIPPAFGAFPITKEPAALSRKDPRLPEGTDLDAITLAKHDKGDIATPWPCMEEAADWYFSQLPDNLPVLSQEDAIRGLDHMDAIDLSQSPGYPWTTQGRSRRSLFDEDGNPLPELQEAIDSVWDGGSYIYQSFLKDELRPTAKARAGKTRIVEAAPIQAIVVGRRLLGSLINHLQGNPLQHGSAVGCNPDIHWTQIFHSLTSFSNVWSIDYSCFDATIPSVLLSAIASRIAARSDQPGRVLDYLSYTTTSYHVYDSLWYTMIGGNPSGCVGTSILNTIANNIAVISAMMYCNKFDPRDPPVLYCYGDDLIWGSNQDFHPRELQAFYQKFTNFVVTPADKASDFPDSSSIFDITFLKRYFVPDDIHPHLIHPVMDEQTLTNSIMWLRGGEFEEVLRSLETLAFHSGPKNYSAWCEKIKAKIRENGCDATFTPYSVLQRGWVSTCMTGPYPLTG
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[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 composed of 60 copies of each VP0, VP1, and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity). [Capsid protein VP0]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP1 and VP3 (By similarity). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity). [Capsid protein VP3]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP1 (By similarity). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity). [Protein 2C]: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3. [Protein 3A]: Serves as membrane anchor via its hydrophobic domain. Plays an essential role in viral RNA replication by recruiting PI4KB at the viral replication sites, thereby allowing the formation of rearranged membranous structures where viral replication takes place (By similarity). [VPg]: Forms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains. [Protease 3C]: Cysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity). In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate cooperatively bind to the protease (By similarity).
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C5PA86
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ARO1_COCP7
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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); Shikimate dehydrogenase (EC 1.1.1.25)]
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MAAPTTIKILGRDSIVADFGIWKRHVADDLLTNCSSSTYILISDTTLTPLYVPSFQAAFENAASGLTPKPRLLTYAIPPGELSKSRQTKADIEDWMLSRQPPCGRDTVIIALGGGVIGDLIGYVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPHGKNLIGAIWQPQKIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEDFAALEKNADAILSAVKSENTPERPRFGGIQEILKLTILASARFKADVVSKDEREGGLRNLLNFGHSIGHAIEGILAPQILHGECVAIGMVKEAELARHLGLLKNVAVPRLVKCLASYGLPTSLKDSRIRRLSAGKHCSVDQLLAFMAVDKKNAGPKKKVVLLSAIGRTHEQQASVVSNEDIKIVLAPSIEVSPGVPKSLQVTCTPPGSKSISNRALVLAALGSGTCRIKNLLHSDDTEVMLNALERLGAATFSWEEEGEVLVVHGNGGTLKASPEELYLGNAGTASRFLTTVATLANNGTVSSTVLTGNARMKQRPIGALVDSLRANGAGVEYLETNGCLPLKIDASGGFAGGEISLAAKISSQYVSSLLMCAPYAKEPVTLKLVGGKPISQQYIDMTTAMMRSFGIDVKRSTTEEHTYHIPQGKYVNPAEYIIESDASSATYPLAVAAITGTTCTIPNIGSKSLQGDARFAVDVLRPMGCEVSQSEYSTTVTAPKDGVLKPLPNVDMEPMTDAFLTASVLAAVATGSPNRTTRIFGIANQRVKECNRIRAMKDELAKFGVICREHDDGLEIDGIDRSTLLQPPHGVHCYDDHRVAMSFSVLSLTAPKPTLILEKECVGKTWPGWWDTLAQLFKAKLEGVELKSSTKQKAEKPAASIFIIGMRGAGKTTSGLWAAKALKRPFIDLDVELESTIGKTIPEIIKERGWEGFREAELALLQKVIREKPTGYVFACGGGIVETQEGRDLLVQYHKANGNVLLLMRDIKEVMDFLKIDKTRPAYVEDMMGVWLRRKPWYQQCSNFQFYSQQSTQDEMGRALESFSRFLRVITGEVDHLSLLKKKPQSFFVSLTLPDLRPSAEILGDVTLGSDAVELRVDLLVDPSSANDIPSVDYVAEQISMLRSRVSLPLVFTIRTKSQGGRFPDDAHDAALDLYRLAVRMGSEFVDLEVTFPEHILRAVTEMKGFSKIIASHHDVSGSLSWANGSWGQFYNKALQYGDIIKLVGVAKCLDDNIALRKFKTWAQDAHEIPVIAINMGEKGRLSRILNGFMTPVSHPKLPFKAAPGQLSAQDIRKGLSLMGEIEPRKFAIFGKPVSASRSPAMHNALFAQVGLPHAYSRLETDNVEDVREFIHAPDFGGASVTIPLKLDIMPLLDEISPEAQVIGAVNTIVPIPRGPGDMTGYPRLIGYNTDWQGMVRCLRHGKAISPSFADTAVPGLVIGGGGTARAAIHALYSMSYSPIYLIGRSEAKVAEMASTFPEKYSVQVLKDATSLENLPMVAIGTIPGDRPIDPSMREVLCRLFENAARVDSELSAKGEVPAKRVLLEMAYKPDITPLSQLASDSGWSTIPGLEALVGQGVHQFELWTGITPVYQDARAAVMNPGTDNRG
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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C6HCG7
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ARO1_AJECH
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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); Shikimate dehydrogenase (EC 1.1.1.25)]
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MGVPTKISILGRESIVADFGIWRNYVAKDLLSSCSSSTYILISDTNLTPLYLEGFQRSFEDAATNVSPKPRLLTYEIPPGESSKSRETKADIEDWMLARQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALERDAETILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVTADEREGGLRNLLNFGHSIGHSIEAILAPQVLHGECVSIGMVKEAELARHLGILNNVSVSRISKCLASYGLPTSLKDQRIKKLTAGKHCSVEQLIAYMGVDKKNDGPKKKVVLLSAIGRTHEPRASTVSNEEIQIVLAPSIEVSPGVPKGLDVTCTPPGSKSISNRALVLAALGSGTCRLKNLLHSDDTEVMLNALERLGAATFSWEDEGEVLVVSGKGGRMEASPSELYLGNAGTASRFLTTVATLARKSSVDSSVLTGNARMKQRPIGDLVDALAANGASIEYLENLGCLPLKIAASGGFAGGEINLAAKVSSQYVSSLLMCAPYAKTPVTLRLMGGKPISQSYIDMTTAMMRSFGVEVKKSETEEHTYHIPLGFYTNPVEYIVESDASSATYPLAAAAITGTSCTVPNIGSKSLQGDARFAVDVLRPMGCAVDQSDFSTRVTGPPGGILSPLPNIDMEPMTDAFLTASVLASVARGKGSNHTTRIFGIANQRVKECNRIKAMKDELAQFGVVCREHDDGLEIDGIDRATLHHPSDGVYCYDDHRVAMSFSVLSLVTPEPTLILEKECVGKTWPGWWDSLAQTFKVKLDGKEVGKRIETNPIVHVNKSAASIFIIGMRGAGKTTSGFWVSKALQRPFIDLDDELERTEGMTIPEIIKQRGWGGFREAELSLLRRVMTEKPTGYIFACGGGVVETPEARKLLTQYHKTTGNVILVMRDIKEIMDFLKIDKTRPAYVEDMMSVWLRRKPWYEECSNVQYYSRLTGLDGMTQVSGGFNRFLKVITGEVDSLAKMRRKENTFFVSLTLPDLGLAAHILKEVTLGSDAVELRVDLLKDPQSDNEIPSVDYVAEQISVLRSRASVPLVFTIRTKGQGGRFPDDAYDAALQLYRLAVRMGSEFVDLEISFPEQLLRTVTEMKGFSKIIASHHDPKGQLSWVNGSWIQFYNKALQYGDVIKLVGVARSIDDNISLKKFKTWAEEKHNVPIIAINMGDKGQLSRMLNGFMTPVSHPSLPFKAAPGQLSAREIRKGLSLIGEIKAKKFAVIGNPVSASRSPAMHNTLFRQMGLPHTYGTLETDNPEVAKEFIRSPDFGGASVTIPLKLSIMPLLDEIAPEAMSIGAVNTIVCAPPAPDGKSQTPRLIGHNTDWQGMVRCLSDAGAYAAATPTTASAGLVIGGGGTARAAIFALQNMGYSPIYVLGRSPDKLSSMTSTFHTDHDIRILEDLKALESLPTVAIGTIPGDKPIEPHMREILCRLFDLCEKANSDTEQARGVSTKRILLEMAYKPSVTSLMQLASDSGWTVLPGLEALVAQGVYQCEYWTNITPVYEYARNAVMGVLPSEDIS
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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C6K2K4
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NETO2_RAT
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Neuropilin and tolloid-like protein 2 (Brain-specific transmembrane protein containing 2 CUB and 1 LDL-receptor class A domains protein 2)
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MALEQLCAVLKVLLITVLVVEGIAVAQKTQDGQNIGIKHVPATQCGIWVRTSNGGHFASPNYPDSYPPNKECIYILEAAPRQRIELTFDERYYIEPSFECRFDHLEVRDGPFGFSPLIDRYCGMKSPALIRSTGRFMWIKFSSDEELEGLGFRAKYSFIPDPDFTYLGGILNPIPDCQFELSGADGIVRSSQVEQEEKTKPGQAVDCIWTIKATPKAKIYLRFLDYQMEHSNECKRNFVAVYDGSSAIENLKAKFCSTVANDVMLKTGVGVIRMWADEGSRLSRFRMLFTSFVEPPCTSSTFFCHSNMCINNSLVCNGVQNCAYPWDENHCKEKKKAGLFEQITKTHGTIIGVTSGIVLVLLIISILVQVKQPRKKVMACKTAFNKTGFQEVFDPPHYELFSLREKEISADLADLSEELDNYQKLRRSSTASRCIHDHHCGSQASSVKQSRTNLSSMELPFRNDFAQPQPMKTFNSTFKKSSYTFKQTHDCPEQALEDRVMEEIPCEIYVRGRDDSAQASISIDF
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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 sensitivity of kainate receptors. Slows the decay of kainate receptor-mediated excitatory postsynaptic currents (EPSCs), thus directly influencing synaptic transmission.
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C6KEF6
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POLG_HKV1
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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 3.4.22.28) (Picornain 3C) (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
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MMEGSNGFSSSLAGLSSSRSSLRLLTHLLSLPPPNRDARRHSGWYRSPPTLPVNVYLNEQFDNLCLAALRYPGCKLYPSVYTLFPDVSPFKIPQSIPAFAHLVQRQGLRRQGNPTTNIYGNGNEVTTDVGANGMSLPIAVGDMPTASSSEAPLGSNKGGSSTSPKSTSNGNVVRGSRYSKWWEPAAARALDRALDHAVDATDAVAGAASKGIKAGATKLSNKLAGSQTTALLALPGNIAGGAPSATVNANNTSISSQALLPSVNPYPSTPAVSLPNPDAPTQVGPAADRQWLVDTIPWSETTPPLTVFSGPKALTPGTYPPTIEPNTGVYPLPAALCVSHPESVFTTAYNAHAYFNCGFDVTVVVNASQFHGGSLIVLAMAEGLGDITPADSSTWFNFPHAIINLANSNSATLKLPYIGVTPNTSTEGLHNYWTILFAPLTPLAVPTGSPTSVKVSLFVSPIDSAFYGLRFPIPFPTPQHWKTRAVPGAGSYGSVVAGQEIPLVGYAPAAPPRDYLPGRVRNWLEYAARHSWERNLPWTAADEVGDQLVSYPIQPETLANTQTNTAFVLSLFSQWRGSLQISLIFTGPAQCYGRLLLAYTPPSANPPTTIEEANNGTYDVWDVNGDSTYTFTIPFCSQAYWKTVDIGTSSGLVSNNGYFTIFVMNPLVTPGPSPPSATVAAFLHVADDFDVRLPQCPALGFQSGADGAEVQPAPTSDLSDGNPTTDPAPRDNFDYPHHPVDPSTDLAFYFSQYRWFGLNEDLTPLNVTGGLFYHVSLNPVNFQQNSLLSVLGAFTYVYANLSLNINVSAPLQACTFYIFYAPPGASVPSTQTLAELSFFTHTATPLNLAAPTNITVSIPYASPQSVLCTSFGGFGLQNGGDPGNLHSNTWGTLILYVDLPQSDSVSVSAYISFRDFEAYVPRQTPGVGPIPTSTSIVRVARPTPKPRTVRRQGGTLADLILTPESRCFIVAHTTAPYYSILLVNPDEEYAISMFTHGDESILRYSSRGGTRLAPTAPAFFLCAAASVDTILPYPISQSHLWLSDLTGIPLRAVPPLTLFLSAGAALCAGAQTLIAVAQGGSAPDTPPTPNRALFRRQGLGDLPDAAKGLSAALENVAKVAGDADIATSSQAIASSINSLSNSIDGATTFMQNFFSGLAPKNPTSPLQHLFAKLIKWVTKIIGSLIIICNNPTPSALIGVSLMLCGDLAEDITEFFSNLGNPLAAVFYRCARALGLSPTPQSAAQAAGGRQGVRDYNDIMSALRNTDWFFEKIMSHIKNLLEWLGVLVKDDPRTKLNSQHEKILELYTDSVTASSTPPSELSADAIRSNLDLAKQLLTLSHAANSVTHIQLCTRAITNYSTALSAISLVGTPGTRPEPLVVYLYGPPGTGKSLLASLLASTLAQALSGDPNNYYSPSSPDCKFYDGYSGQPVHYIDDIGQDPDGADWADFVNIVSSAPFIVPMADVNDKGRFYTSRVVIVTSNFPGPNPRSARCVAALERRLHIRLNVTARDGAAFSAAAALKPSEPLAATRYCKFSNPLTQFSMFNLAVDYKSIVLPNTPLSCFDELIDFILGSLRDRASVNSLLSGMVRTDVARQGGNADAPAPSAAPLPSVLPSVPSQDPFVRAVNENRPVSFLSKIWSWRAPIFAASSFLSLIAATLTIVRCLRDLRSTQGAYSGTPVPKPRKKDLPKQPVYSGPVRRQGFDPAVMKIMGNVDSFVTLSGSKPIWTMSCLWIGGRNLIAPSHAFVSDDYEITHIRVGSRTLDVSRVTRVDDGELSLISVPDGPEHKSLIRYIRSASPKSGILASKFSDTPVFVSFWNGKPHSTPLPGVVDEKDSFTYRCSSFQGLCGSPMIATDPGGLGILGIHVAGVAGYNGFSARLTPERVQAFLSNLATPQSVLHFHPPMGPPAHVSRRSRLHPSPAFGAFPITKEPAALSRKDPRLPEGTDLDAITLAKHDKGDIATPWPCMEEAADWYFSQLPDSLPVLSQEDAIRGLDHMDAIDLSQSPGYPWTTQGRSRRSLFDEDGNPVPELQKAIDSVWDGGSYIYQSFLKDELRPTAKARAGKTRIVEAAPIQAIVVGRRLLGSLINHLQGNPLQYGSAVGCNPDIHWTQIFHSLTPFSNVWSIDYSCFDATIPSVLLSAIASRIASRSDQPGRVLDYLSYTTTSYHVYDSLWYTMVGGNPSGCVGTSILNTIANNIAIISAMMYCNKFDPRDPPVLYCYGDDLIWGSNQDFHPRELQAFYQKFTNFVVTPADKASDFPDSSSIYDITFLKRYFVPDDIHPHLIHPVMDEATLTNSIMWLRGGEFEEVLRSLETLAFHSGPNNYSTWCEKIKAKIRENGCDATFTPYSVLQRGWVSTCMTGPYPLTG
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[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 composed of 60 copies of each VP0, VP1, and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity). [Capsid protein VP0]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP1 and VP3 (By similarity). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity). [Capsid protein VP3]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP1 (By similarity). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity). [Protein 2C]: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3. [Protein 3A]: Serves as membrane anchor via its hydrophobic domain. Plays an essential role in viral RNA replication by recruiting PI4KB at the viral replication sites, thereby allowing the formation of rearranged membranous structures where viral replication takes place (By similarity). [VPg]: Forms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains. [Protease 3C]: Cysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity). In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate cooperatively bind to the protease (By similarity).
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C6KEM4
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AADH2_MAIZE
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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)
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MAPPQTIPRRGLFIGGAWREPCLGRRLPVVNPATEATIGDIPAGTAEDVEIAVAAARDAFSRDGGRHWSRAPGAVRANFLRAIAAKIKDRKSELALLETLDSGKPLDEASGDMDDVAACFEYYADLAEALDGKQQSPISLPMENFKSYVLKEPIGVVGLITPWNYPLLMATWKVAPALAAGCTTILKPSELASVSCLELGAICMEIGLPPGVLNIITGLGPEAGAPLSSHSHVDKVAFTGSTETGKRIMISAAQMVKPVSLELGGKSPLIVFDDIGDIDKAVEWTMFGIFANAGQVCSATSRLLLHEKIAKKFLDRLVAWAKNIKVSDPLEEGCRLGSVISEGQYEKIKKFISTARSEGATILYGGGRPQHLRRGFFLEPTIITDVSTSMQIWQEEVFGPVICVKEFRTESEAVELANDTHYGLAGAVISNDQERCERISKALHSGIIWINCSQPCFVQAPWGGNKRSGFGRELGEWGLDNYLTVKQVTKYCSDEPWGWYQPPSKL
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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-(trimethylamino)butanal and 4-guanidinobutanal to 4-trimethylammoniobutanoate and 4-guanidinobutanoate, respectively.
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