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-OCT-2020, entry version 121.
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   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:0032446; P:protein modification by small protein conjugation; 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
//