ID Q6BG38_PARTE Unreviewed; 409 AA. AC Q6BG38; DT 16-AUG-2004, integrated into UniProtKB/TrEMBL. DT 16-AUG-2004, sequence version 1. DT 16-OCT-2019, entry version 115. DE RecName: Full=Adenylyltransferase and sulfurtransferase MOCS3 homolog {ECO:0000256|HAMAP-Rule:MF_03049}; DE AltName: Full=UBA4 homolog {ECO:0000256|HAMAP-Rule:MF_03049}; DE AltName: Full=Ubiquitin-like protein activator 4 homolog {ECO:0000256|HAMAP-Rule:MF_03049}; DE Includes: DE RecName: Full=Adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_03049}; DE EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_03049}; DE Includes: DE RecName: Full=Sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_03049}; DE EC=2.8.1.- {ECO:0000256|HAMAP-Rule:MF_03049}; GN ORFNames=GSPATT00000337001 {ECO:0000313|EMBL:CAK55902.1}, PTMB.185 GN {ECO:0000313|EMBL:CAH03382.1}; OS Paramecium tetraurelia. OC Eukaryota; Alveolata; Ciliophora; Intramacronucleata; OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium. OX NCBI_TaxID=5888 {ECO:0000313|Proteomes:UP000000600}; RN [1] {ECO:0000313|EMBL:CAH03382.1, ECO:0000313|Proteomes:UP000000600} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAH03382.1, RC ECO:0000313|Proteomes:UP000000600}; RX PubMed=15296759; DOI=10.1016/j.cub.2004.07.029; RA Zagulski M., Nowak J.K., Le Mouel A., Nowacki M., Migdalski A., RA Gromadka R., Noel B., Blanc I., Dessen P., Wincker P., Keller A.-M., RA Cohen J., Meyer E., Sperling L.; RT "High coding density on the largest Paramecium tetraurelia somatic RT chromosome."; RL Curr. Biol. 14:1397-1404(2004). RN [2] {ECO:0000313|EMBL:CAH03382.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAH03382.1}; RA Nowak J.K., Migdalski A., Gromadka R., Zagulski M.; RT "Paramecium megabase sequencing project."; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:CAK55902.1, ECO:0000313|Proteomes:UP000000600} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK55902.1, RC ECO:0000313|Proteomes:UP000000600}; RX PubMed=17086204; DOI=10.1038/nature05230; RG Genoscope; RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M., RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A., RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., RA Guigo R., Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., RA Klotz C., Koll F., Le Mouel A., Lepere G., Malinsky S., Nowacki M., RA Nowak J.K., Plattner H., Poulain J., Ruiz F., Serrano V., Zagulski M., RA Dessen P., Betermier M., Weissenbach J., Scarpelli C., Schaechter V., RA Sperling L., Meyer E., Cohen J., Wincker P.; RT "Global trends of whole-genome duplications revealed by the ciliate RT Paramecium tetraurelia."; RL Nature 444:171-178(2006). RN [4] {ECO:0000313|EMBL:CAK55902.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK55902.1}; RG Genoscope; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at CC tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and CC tRNA(Gln). Acts by mediating the C-terminal thiocarboxylation of CC the sulfur carrier URM1. Its N-terminus first activates URM1 as CC acyl-adenylate (-COAMP), then the persulfide sulfur on the CC catalytic cysteine is transferred to URM1 to form CC thiocarboxylation (-COSH) of its C-terminus. The reaction probably CC involves hydrogen sulfide that is generated from the persulfide CC intermediate and that acts as nucleophile towards URM1. CC Subsequently, a transient disulfide bond is formed. Does not use CC thiosulfate as sulfur donor; NFS1 probably acting as a sulfur CC donor for thiocarboxylation reactions. {ECO:0000256|HAMAP- CC Rule:MF_03049}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03049}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_03049}; CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine- CC tRNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03049, CC ECO:0000256|SAAS:SAAS00001783}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03049, CC ECO:0000256|SAAS:SAAS00337557}. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC HesA/MoeB/ThiF family. UBA4 subfamily. {ECO:0000256|HAMAP- CC Rule:MF_03049, ECO:0000256|SAAS:SAAS00535337}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR548612; CAH03382.1; -; Genomic_DNA. DR EMBL; CT867985; CAK55902.1; -; Genomic_DNA. DR RefSeq; XP_001347009.1; XM_001346973.1. DR RefSeq; XP_001423300.1; XM_001423263.1. DR STRING; 5888.CAK55902; -. DR EnsemblProtists; CAK55902; CAK55902; GSPATT00000337001. DR GeneID; 2898600; -. DR GeneID; 5009084; -. DR KEGG; ptm:GSPATT00000337001; -. DR KEGG; ptm:PTMB.185; -. DR eggNOG; KOG2017; Eukaryota. DR eggNOG; COG0476; LUCA. DR HOGENOM; HOG000281219; -. DR KO; K11996; -. DR OMA; GTIGAMQ; -. DR UniPathway; UPA00988; -. DR Proteomes; UP000000600; Chromosome. DR Proteomes; UP000000600; Partially assembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central. DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IBA:GO_Central. DR GO; GO:0042292; F:URM1 activating enzyme activity; IBA:GO_Central. DR GO; GO:0018192; P:enzyme active site formation via cysteine modification to L-cysteine persulfide; IEA:UniProtKB-UniRule. DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:InterPro. DR Gene3D; 3.40.250.10; -; 1. DR HAMAP; MF_03049; MOCS3_Uba4; 1. DR InterPro; IPR028885; MOCS3/Uba4. DR InterPro; IPR001763; Rhodanese-like_dom. DR InterPro; IPR036873; Rhodanese-like_dom_sf. DR InterPro; IPR000594; ThiF_NAD_FAD-bd. DR InterPro; IPR035985; Ubiquitin-activating_enz. DR Pfam; PF00581; Rhodanese; 1. DR Pfam; PF00899; ThiF; 1. DR SMART; SM00450; RHOD; 1. DR SUPFAM; SSF69572; SSF69572; 1. DR PROSITE; PS50206; RHODANESE_3; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03049, KW ECO:0000256|SAAS:SAAS00885939}; KW Complete proteome {ECO:0000313|Proteomes:UP000000600}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03049, KW ECO:0000256|SAAS:SAAS00001796}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03049, KW ECO:0000256|SAAS:SAAS00135730}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03049, KW ECO:0000256|SAAS:SAAS00001794}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03049, KW ECO:0000256|SAAS:SAAS00885830}; KW Reference proteome {ECO:0000313|Proteomes:UP000000600}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03049, KW ECO:0000256|SAAS:SAAS00885834}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_03049, KW ECO:0000256|SAAS:SAAS00001792}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_03049, ECO:0000256|SAAS:SAAS00416189}. FT DOMAIN 320 407 Rhodanese. {ECO:0000259|PROSITE:PS50206}. FT NP_BIND 102 106 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}. FT NP_BIND 163 164 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}. FT ACT_SITE 218 218 Glycyl thioester intermediate; for FT adenylyltransferase activity. FT {ECO:0000256|HAMAP-Rule:MF_03049}. FT ACT_SITE 368 368 Cysteine persulfide intermediate; for FT sulfurtransferase activity. FT {ECO:0000256|HAMAP-Rule:MF_03049}. FT METAL 203 203 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}. FT METAL 206 206 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}. FT METAL 275 275 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}. FT METAL 278 278 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}. FT BINDING 74 74 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_03049}. FT BINDING 95 95 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}. FT BINDING 119 119 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}. SQ SEQUENCE 409 AA; 46394 MW; FD4B69B2FBFCFEA9 CRC64; MKEYIEYLQN LLKQNKIEFE QEEDFIQHKV SQINNEFGYE HINRYKRQMI LSEIGLTGQK QIHLAKVLIV GAGGIGAPAI YYLAGAGVGT IGLVDGDSVD VSNLHRQIIH NNYRQGMNKC ESAKLQINEF NPLVNVITYK HHLSSANAIE IFQNYDVILD ATDNPATRYL INDTAIYLNK PLVSGSSVGW EGQITVYGMQ GPCYRCLFPQ CPKTVQNCNE AGVFGVMPGL IGLIEALQAI KIIIGQQTLS QKMILIDGLR DVYKVVKLRG QQKDCIACQK QIKINDYDYA SFAQTICSSS IPYRGGYKEI EWKDFLQIQR SEKVALLDVR PSSQYNIIKL DGFTNLPYSQ IDQLQVEEYK DKEIYIMCRR GNNSRLACEY LKDKTPNIYN IIGGIDLYAK LYDPKMPLL //