GenomeNet

Database: UniProt
Entry: A0A077ZZ82_STYLE
LinkDB: A0A077ZZ82_STYLE
Original site: A0A077ZZ82_STYLE 
ID   A0A077ZZ82_STYLE        Unreviewed;       402 AA.
AC   A0A077ZZ82;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
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   Name=Contig6672.g7140 {ECO:0000313|EMBL:CDW73808.1};
GN   ORFNames=STYLEM_2796 {ECO:0000313|EMBL:CDW73808.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW73808.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW73808.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW73808.1};
RA   Swart Estienne;
RL   Submitted (JUN-2014) 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; CCKQ01002703; CDW73808.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A077ZZ82; -.
DR   EnsemblProtists; CDW73808; CDW73808; STYLEM_2796.
DR   InParanoid; A0A077ZZ82; -.
DR   OMA; MIYDALE; -.
DR   OrthoDB; 53913at2759; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000039865; Unassembled 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-UniRule.
DR   GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:InterPro.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:InterPro.
DR   CDD; cd00757; ThiF_MoeB_HesA_family; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 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; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR10953:SF102; ADENYLYLTRANSFERASE AND SULFURTRANSFERASE MOCS3; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03049};
KW   Cytoplasm {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}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03049};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039865};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03049};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_03049};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03049}.
FT   DOMAIN          307..400
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   ACT_SITE        193
FT                   /note="Glycyl thioester intermediate; for
FT                   adenylyltransferase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT   ACT_SITE        359
FT                   /note="Cysteine persulfide intermediate; for
FT                   sulfurtransferase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT   BINDING         67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT   BINDING         74..78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT   BINDING         91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT   BINDING         135..136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT   BINDING         176
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT   BINDING         253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT   BINDING         256
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
SQ   SEQUENCE   402 AA;  45036 MW;  9AE4A98279F26C86 CRC64;
     MEQREVKELS NEEYMRYSRQ LIMGSIGIEG QKKLKNAKVL IIGAGGLGSP ASFYLSGAGV
     GTIGLVDGDI VDESNLHRQI IHTEDRVGIN KTLSAKQQIA MFNRHIDVVT YQTHLTPENA
     REIVQDWDIV MDGSDNAKAR YLINDICMIL KKPLVSGSAL QMEGQITVYG YNGGPCYRCM
     FPVPPPAHTV TNCADGGVLG VVPGIIGNLE ALEIIKIILG FKDEQILTKR MIFFDAASMR
     FRNVKLRDRN PRCQVCGDEP SITDPSLIDY DDFCQTKCNK YALIQIPSEN NITVEEFQKE
     YERLKEQADD IALVDVRGKI QYDIVSLPGS LNLPLKKMME DPESIKKLTQ EKKTVFIMCR
     RGNASKEATE FILKNLDIHN VKNVQGGIQE YITKIDPSLP IY
//
DBGET integrated database retrieval system