ID Q6BG38_PARTE Unreviewed; 409 AA. AC Q6BG38; DT 16-AUG-2004, integrated into UniProtKB/TrEMBL. DT 16-AUG-2004, sequence version 1. DT 07-APR-2021, entry version 123. 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; Sar; 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., Guigo R., RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F., RA Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H., RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M., RA Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E., RA 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 tRNA CC wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts CC by mediating the C-terminal thiocarboxylation of the sulfur carrier CC URM1. Its N-terminus first activates URM1 as acyl-adenylate (-COAMP), CC then the persulfide sulfur on the catalytic cysteine is transferred to CC URM1 to form thiocarboxylation (-COSH) of its C-terminus. The reaction CC probably involves hydrogen sulfide that is generated from the CC persulfide 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 donor for CC thiocarboxylation reactions. {ECO:0000256|HAMAP-Rule:MF_03049}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03049}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03049}; CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03049}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03049}. CC -!- SIMILARITY: In the N-terminal section; belongs to the HesA/MoeB/ThiF CC family. UBA4 subfamily. {ECO:0000256|HAMAP-Rule:MF_03049}. 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 HOGENOM; CLU_013325_1_2_1; -. 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: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|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_03049}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03049}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03049}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP- KW Rule:MF_03049}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_03049}; Reference proteome {ECO:0000313|Proteomes:UP000000600}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03049}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_03049}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03049}. FT DOMAIN 320..407 FT /note="Rhodanese" FT /evidence="ECO:0000259|PROSITE:PS50206" FT NP_BIND 102..106 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT NP_BIND 163..164 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT ACT_SITE 218 FT /note="Glycyl thioester intermediate; for FT adenylyltransferase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT ACT_SITE 368 FT /note="Cysteine persulfide intermediate; for FT sulfurtransferase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT METAL 203 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT METAL 206 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT METAL 275 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT METAL 278 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT BINDING 74 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT BINDING 95 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT BINDING 119 FT /note="ATP" FT /evidence="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 //