ACL_RS05930
  | Uniprot: A9NHG7
Description: tRNA sulfurtransferase ThiI EC number: 2.8.1.4 Annotation score: 4 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: L-cysteine + 'activated' tRNA = L-serine + tRNA containing a thionucleotide. {ECO:0000255|HAMAP-Rule:MF_00021}.; CATALYTIC ACTIVITY: [IscS]-SSH + [ThiS]-COAMP = [IscS]-SH + [ThiS]-COSH + AMP. {ECO:0000255|HAMAP-Rule:MF_00021}. Cofactor: Enzyme regulation: Function [CC]: FUNCTION: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. {ECO:0000255|HAMAP-Rule:MF_00021}. Pathway: PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00021}. Active site: Binding site: BINDING 265 265 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}.; BINDING 287 287 ATP; via amide nitrogen. {ECO:0000255|HAMAP-Rule:MF_00021}.; BINDING 296 296 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}. Calcium binding: DNA binding: Metal binding: Nucleotide binding: NP_BIND 181 182 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}.; NP_BIND 206 207 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}. Site: Gene names (primary): thiI Gene names (synonym): Mass: 46,583 Subunit structure [CC]: Gene ontology (GO): cytoplasm [GO:0005737]; ATP binding [GO:0005524]; sulfurtransferase activity [GO:0016783]; tRNA adenylyltransferase activity [GO:0004810]; tRNA binding [GO:0000049]; thiamine biosynthetic process [GO:0009228]; thiamine diphosphate biosynthetic process [GO:0009229]; tRNA thio-modification [GO:0034227] Gene ontology IDs: GO:0000049; GO:0004810; GO:0005524; GO:0005737; GO:0009228; GO:0009229; GO:0016783; GO:0034227 Chain: CHAIN 1 412 Probable tRNA sulfurtransferase. /FTId=PRO_1000074196. Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the ThiI family. {ECO:0000255|HAMAP-Rule:MF_00021}.; SIMILARITY: Contains 1 THUMP domain. {ECO:0000255|HAMAP-Rule:MF_00021}. Protein families: ThiI family Coiled coil: Domain [FT]: DOMAIN 58 163 THUMP. {ECO:0000255|HAMAP-Rule:MF_00021}. Motif: Region: EMBL: CP000896 ProteinModelPortal: A9NHG7 MEROPS: EnsemblBacteria KO: ABX81797 UniPathway: K03151 CDD: Gene3D: HAMAP: 3.40.50.620 InterPro: MF_00021 PANTHER: IPR014729;IPR020536;IPR004114;IPR003720 PIRSF: PRINTS: PROSITE: Pfam: PS51165 ProDom: PF02568;PF02926 SMART: SUPFAM: SM00981 TIGRFAMs: |
1249243-1250482(-) >nucleotide sequence AAAATCAGTGGTAGGGGTAATAATCATTGTTTGAACATTCTTAAGTGCATCTTCTAAGAG TTCTTTAAACTCAAATCTAGATTCTTCTTTCAATGCTTGGTCAATGGTTGGTTTAGTAAC TGGGTTTCTTGGTACATAAATTGAGCAGCAATCATTAAACGGTAAAATAGATATATCATA TGTATCTATTTTCTTAGATATATTAATAATATCATTTTTGTCATAAGTAATAACCGGTCT TAAAATAGGTATAGAGGTTACATTTTCAATAACTTTAATACTACTTAAGGTTTGACTTGC TACCTGGCCAACGGATTCACCATTAATTAAGGTATCTAAACCATGTTGATTTGCATAGAT TTCACCTAATCTGTAGAACATACGACGCATGATCGTAATAATGTACGGATCTGCTACATA ACTTAGTATCGCTTCATGTATTTTAGTAAACGGTACAAGATGTAGTTTAATCTTATTATA TGGTGTATAGTATGCTAATTTTTTTGCAATTTCTATAACCTTTTGAACAGATTCTAATGG TGTAAGTGGTGTGGATTCAAAGTGGAATAATTCCACATCAATGCCTTGCTTCATCATAAG ATGTGCCGCCACTGGGGAATCAATACCACCAGATAACATCACTAAGCCTTTACCACCTAA ACCTATTGGAAAACCACCTAGTGCAGGTATTTTACCAACATAGATATAAGTGCCTTCGCT TCTTAGTTCAATATCTAAAACTGTTTCAGGATTTCTCACTTCTACTTTTAACCCGTCAAA TGATGGAAGTACGAGTGATGCCACTTTTTGTGAGATTTCTAAAGATTTTAGTGGATAGTT TTTATCCGTTCTCTTCGTCTCTATTTTAAATGTTGTAGGAAGTTTAACTTCCTTTTGAAT CACTTCTTTTGCAAGCTGTGCAATAGATTCAATATCTTTTGTTGTTTTGTAGATGTAACT AAATGAGTGTATACCGGATACATATCCTAGTTGTTTAATCACTTCATCACTATCTACTTC ATTAAAATGAACATATATACGATCATGTTGGAAAGTATACTCTACATTTACGTTTTTTAA CTTACTTCTTATATTTTTTTTAATCTGGCCGATGAATTTAGGTTTGTTCTTACCTTTTAG TACTAAATCACCAAAGCGAATTAAAATTGCCTTTTCCAT >protein sequence IKQLGYVSGIHSFSYIYKTTKDIESIAQLAKEVIQKEVKLPTTFKIETKRTDKNYPLKSL EISQKVASLVLPSFDGLKVEVRNPETVLDIELRSEGTYIYVGKIPALGGFPIGLGGKGLV MLSGGIDSPVAAHLMMKQGIDVELFHFESTPLTPLESVQKVIEIAKKLAYYTPYNKIKLH LVPFTKIHEAILSYVADPYIITIMRRMFYRLGEIYANQHGLDTLINGESVGQVASQTLSS IKVIENVTSIPILRPVITYDKNDIINISKKIDTYDISILPFNDCCSIYVPRNPVTKPTID QALKEESRFEFKELLEDALKNVQTMIITPTTDFEIALHGFDVKDALSSYTQE |
© Fisunov Lab of Proteomics, 2016.