ACL_RS03520
  | Uniprot: A9NG43
Description: tRNA guanosine(34) transglycosylase Tgt EC number: 2.4.2.29 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: Guanine(34) in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine. {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087626}.; CATALYTIC ACTIVITY: Guanine(34) in tRNA + queuine = queuosine(34) in tRNA + guanine. {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087703}. Cofactor: COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777}; ; Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777} Enzyme regulation: Function [CC]: FUNCTION: Exchanges the guanine residue with 7-aminomethyl-7-deazaguanine in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). After this exchange, a cyclopentendiol moiety is attached to the 7-aminomethyl group of 7-deazaguanine, resulting in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00383991}. Pathway: PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|SAAS:SAAS00087869}. Active site: ACT_SITE 98 98 Nucleophile. {ECO:0000256|HAMAP-Rule:MF_00168}. Binding site: BINDING 99 99 Substrate. {ECO:0000256|HAMAP-Rule:MF_00168}. Calcium binding: DNA binding: Metal binding: Nucleotide binding: Site: Gene names (primary): tgt Gene names (synonym): Mass: 42,610 Subunit structure [CC]: Gene ontology (GO): metal ion binding [GO:0046872]; queuine tRNA-ribosyltransferase activity [GO:0008479]; queuosine biosynthetic process [GO:0008616]; tRNA modification [GO:0006400] Gene ontology IDs: GO:0006400; GO:0008479; GO:0008616; GO:0046872 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family. {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00571098}. Protein families: Queuine tRNA-ribosyltransferase family Coiled coil: Domain [FT]: Motif: Region: EMBL: CP000896 ProteinModelPortal: A9NG43 MEROPS: EnsemblBacteria KO: ABX81323 UniPathway: K00773 CDD: Gene3D: HAMAP: 3.20.20.105 InterPro: MF_00168 PANTHER: IPR004803;IPR002616 PIRSF: PRINTS: PROSITE: Pfam: ProDom: PF01702 SMART: SUPFAM: TIGRFAMs: SSF51713 |
739068-740202(-) >nucleotide sequence TCTGTCCTCTTTAATTGCTTGTCTAATTTCTGCCATTAAGTGCTTTAAATATGCTAAATT TTGGATAGTTACTAGTCTTTGACCTAGTTGTTCTTCTGCTTTAAATAAGTGTCTAATATA ACTCTTAGAGTACTTTGAAACACTTGATTGTAGATTTGGATCTAGACTTGACATGTCACG TTCAAATTGTTTATTTTTAATAGTCACTTTACCGGTAGTTGTAAGTGCTGTACCATGTCT AGCATTTCTAGTAGGCAGTACACAGTCAAACATATCTACACCATTAATGACGTTTTCTAG TAAGTCCTCAGGTGCACCCACACCCATTAAGTAACGCGGTTTATTAAACGGTAAAATCGG GTTTAAATGTCTTGTCATCTCATACATTTCAGCTTTTGTTTCACCAACGGATAAGCCACC AATAGAATAACCTGGAAAATCCAGTTTAATGAGTTCTTCAGCACAGTGAGTTCTTAATTC TTTATTTAAACCACCTTGTACAATTCCAAATAAAGCTTGATCAGTTTTTAATGCTTCTTT ACCTCTTTTTGCCCAACGAATCGTTCTTTCTACAGAATCCTTCATATATTCATAGGATTC ATAAGGTGGTGGACATTCATCAAAAGACATAATAATATCCGCACCTAAGTCTTCTTGAAT GCGTATCGCATCTTCTGGACCTAAGAATAATGGAGCACCAGATTTATGATGCTTGAAATG AACACCTTCTTCTTTAATATCACGTAATTTAGCAAGTGAAAATACTTGAAAACCACCGGA ATCCGTTAAAAGTGCGCCATCCCATTTCATAAATCCACGAATACCACCATGATCTTTTAC GATATCTTCACCTGGTTGTTGCCATAGGTGATAGGTGTTTGCTAAGATTAAACCTTCTGA AACTTCTTTAATTTCTTCAACTGTTAATGTTTTTACAGTAGCGAGTGTACCTACTGGCAT AAAAATAGGTGTTTCAAACACACCATGTGATGTCGTTAATTTACCAAGCCTAGCACCACT TTGCTTACAAACATGTAATACTTCATATGAAATCAAAATAAAACCACCTTCCAT >protein sequence GLILANTYHLWQQPGEDIVKDHGGIRGFMKWDGALLTDSGGFQVFSLAKLRDIKEEGVHF KHHKSGAPLFLGPEDAIRIQEDLGADIIMSFDECPPPYESYEYMKDSVERTIRWAKRGKE ALKTDQALFGIVQGGLNKELRTHCAEELIKLDFPGYSIGGLSVGETKAEMYEMTRHLNPI LPFNKPRYLMGVGAPEDLLENVINGVDMFDCVLPTRNARHGTALTTTGKVTIKNKQFERD MSSLDPNLQSSVSKYSKSYIRHLFKAEEQLGQRLVTIQNLAYLKHLMAEIRQAIKEDRLL DFKKEFYERTNYPKVSY |
© Fisunov Lab of Proteomics, 2016.