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-SEP-2015, entry version 85.
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};
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, ECO:0000256|SAAS:SAAS00165445};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_03049, ECO:0000256|SAAS:SAAS00165445};
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:SAAS00001788}.
CC   -!- SIMILARITY: Contains 1 rhodanese domain. {ECO:0000256|HAMAP-
CC       Rule:MF_03049}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       HesA/MoeB/ThiF family. UBA4 subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_03049}.
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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   ProteinModelPortal; Q6BG38; -.
DR   STRING; 412030.XP_001423300.1; -.
DR   EnsemblProtists; CAK55902; CAK55902; GSPATT00000337001.
DR   GeneID; 2898600; -.
DR   GeneID; 5009084; -.
DR   KEGG; ptm:GSPATT00000337001; -.
DR   KEGG; ptm:PTMB.185; -.
DR   HOGENOM; HOG000281219; -.
DR   InParanoid; Q6BG38; -.
DR   KO; K11996; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000000600; Chromosome.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
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; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008641; F:small protein activating enzyme activity; IEA:InterPro.
DR   GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:InterPro.
DR   GO; GO:0018192; P:enzyme active site formation via L-cysteine persulfide; IEA:UniProtKB-HAMAP.
DR   GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:InterPro.
DR   Gene3D; 3.40.250.10; -; 1.
DR   Gene3D; 3.40.50.720; -; 1.
DR   HAMAP; MF_03049; MOCS3_Uba4; 1.
DR   InterPro; IPR028885; MOCS3/Uba4.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
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:SAAS00307343};
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:SAAS00001785};
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:SAAS00135679};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03049,
KW   ECO:0000256|SAAS:SAAS00307325};
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:SAAS00001782}.
FT   DOMAIN      320    407       Rhodanese. {ECO:0000256|HAMAP-Rule:
FT                                MF_03049}.
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
//