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Database: UniProt
Entry: S7Q3J7_GLOTA
LinkDB: S7Q3J7_GLOTA
Original site: S7Q3J7_GLOTA 
ID   S7Q3J7_GLOTA            Unreviewed;       402 AA.
AC   S7Q3J7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Rhodanese domain-containing protein {ECO:0000259|PROSITE:PS50206};
GN   Name=UBA4 {ECO:0000256|HAMAP-Rule:MF_03049};
GN   ORFNames=GLOTRDRAFT_116767 {ECO:0000313|EMBL:EPQ54132.1};
OS   Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS   rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX   NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ54132.1, ECO:0000313|Proteomes:UP000030669};
RN   [1] {ECO:0000313|EMBL:EPQ54132.1, ECO:0000313|Proteomes:UP000030669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ54132.1,
RC   ECO:0000313|Proteomes:UP000030669};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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}.
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DR   EMBL; KB469304; EPQ54132.1; -; Genomic_DNA.
DR   RefSeq; XP_007867463.1; XM_007869272.1.
DR   AlphaFoldDB; S7Q3J7; -.
DR   STRING; 670483.S7Q3J7; -.
DR   GeneID; 19300230; -.
DR   KEGG; gtr:GLOTRDRAFT_116767; -.
DR   eggNOG; KOG2017; Eukaryota.
DR   HOGENOM; CLU_013325_1_2_1; -.
DR   OMA; MIYDALE; -.
DR   OrthoDB; 53913at2759; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000030669; 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:UP000030669};
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          306..400
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   ACT_SITE        192
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         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT   BINDING         65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT   BINDING         72..76
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT   BINDING         89
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT   BINDING         133..134
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT   BINDING         178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT   BINDING         250
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"
SQ   SEQUENCE   402 AA;  43099 MW;  032B66A040E0FFAA CRC64;
     MSAAGLNHLD DYQRYGRQMI LDGFGLPGQV ALQNASVVVV GAGGLGCPAL QYLAASGIGR
     IGIVDHDVVE LSNLHRQILH TEQRVGMPKA ESAAEAIRTL NSKIKINIYT EALSALNALD
     ILSSYDVILD CTDNAPTRYL LSDTAVALGK PLVSGAAQKF DGQLCVYNLN NEGPCYRCIF
     PKPPAPEHAG TCEETGILGT VTGVIGTLQA LEAIKLLAGM HEGKASLLIY SALGVPPFRS
     IKLRSRRPTC PACGQEGLKE GQIRDTDYVA FCGGGPPDWE KKGMMQGDPG LRITPTKLND
     ILASEAASHT KILDVRPRTE FGICHLWESI NIPLKELSAN PTTTASVLED GVKEVYVVCR
     LGNDSQIAAD ALRALRRDVV VKDVIGGLKA WSRDVDPDFP VY
//
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