ID H0GMU7_SACCK Unreviewed; 429 AA.
AC H0GMU7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=YNR029C-like protein {ECO:0000313|EMBL:EHN04943.1};
GN ORFNames=VIN7_4262 {ECO:0000313|EMBL:EHN04943.1};
OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN04943.1, ECO:0000313|Proteomes:UP000009009};
RN [1] {ECO:0000313|EMBL:EHN04943.1, ECO:0000313|Proteomes:UP000009009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VIN7 {ECO:0000313|EMBL:EHN04943.1,
RC ECO:0000313|Proteomes:UP000009009};
RX PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA Pretorius I.S., Egholm M., Chambers P.J.;
RT "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT origins.";
RL FEMS Yeast Res. 12:88-96(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ZNG1
CC subfamily. {ECO:0000256|ARBA:ARBA00034320}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHN04943.1}.
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DR EMBL; AGVY01000045; EHN04943.1; -; Genomic_DNA.
DR AlphaFoldDB; H0GMU7; -.
DR HOGENOM; CLU_017452_6_0_1; -.
DR PhylomeDB; H0GMU7; -.
DR Proteomes; UP000009009; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd03112; CobW-like; 1.
DR Gene3D; 3.30.1220.10; CobW-like, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR036627; CobW-likC_sf.
DR InterPro; IPR011629; CobW-like_C.
DR InterPro; IPR003495; CobW/HypB/UreG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13748:SF31; COBW DOMAIN-CONTAINING PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR13748; COBW-RELATED; 1.
DR Pfam; PF02492; cobW; 1.
DR Pfam; PF07683; CobW_C; 1.
DR SUPFAM; SSF90002; Hypothetical protein YjiA, C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 72..273
FT /note="CobW/HypB/UreG nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF02492"
FT DOMAIN 362..427
FT /note="CobW C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07683"
SQ SEQUENCE 429 AA; 48000 MW; EE46F152DD220AB8 CRC64;
MSALRNIKFN EEEDGELPCL VTGEENNLQE ILENVSYDGG NIVSDAKVER VNKQVGNTSA
GVTDVHEKKR IPVSIITGYL GSGKSTLLEK IALKGADKKI AVILNEFGDS SEIEKAMTIK
NGSNSYQEWL DLGNGCLCCS LKNIGVKAIE DMVERSPGKI DYILLETSGI ADPAPIAKMF
WQDEGLNSSV YIDGIITVLD CEHILKCLDD ISIDAHWHGD KVGLEGNLTI AHFQLAMADR
IIMNKYDTIE HSPEMVKQLK ERVREINSIA PMFFTKYSDT PIQNLLDIHA YDSIRISDIL
DSGSGNGTIH DDRMGTIMLN FRPLKNEEEY NNKFIKQFLQ PLLWKNFGAM SVLGGHRRDD
GRDWEVQRTK GLILIEGENP IARVIQGVRD TYDVFPGKYD GSNKECKIVL IGKYLEKESI
EELLRKTLG
//
