(data stored in ACNUC7421 zone)

SWISSPROT: Q758F4_ASHGO

ID   Q758F4_ASHGO            Unreviewed;       393 AA.
AC   Q758F4;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 109.
DE   RecName: Full=Obg-like ATPase 1 {ECO:0000256|HAMAP-Rule:MF_03167};
GN   Name=OLA1 {ECO:0000256|HAMAP-Rule:MF_03167};
GN   ORFNames=AGOS_AEL192W {ECO:0000313|EMBL:AAS52493.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52493.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52493.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Hydrolyzes ATP, and can also hydrolyze GTP with lower
CC       efficiency. Has lower affinity for GTP. {ECO:0000256|HAMAP-
CC       Rule:MF_03167}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03167}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. OBG GTPase family. YchF/OLA1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03167}.
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DR   EMBL; AE016818; AAS52493.1; -; Genomic_DNA.
DR   RefSeq; NP_984669.1; NM_210022.1.
DR   STRING; 33169.AAS52493; -.
DR   EnsemblFungi; AAS52493; AAS52493; AGOS_AEL192W.
DR   GeneID; 4620853; -.
DR   KEGG; ago:AGOS_AEL192W; -.
DR   HOGENOM; HOG000087628; -.
DR   InParanoid; Q758F4; -.
DR   KO; K19788; -.
DR   OMA; VLRCFDN; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATPase activity; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR   CDD; cd04867; TGS_YchF_OLA1; 1.
DR   CDD; cd01900; YchF; 1.
DR   Gene3D; 1.10.150.300; -; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   HAMAP; MF_00944; YchF_OLA1_ATPase; 1.
DR   InterPro; IPR004396; ATPase_YchF/OLA1.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR031167; G_OBG.
DR   InterPro; IPR006073; GTP_binding_domain.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR012676; TGS-like.
DR   InterPro; IPR023192; TGS-like_dom_sf.
DR   InterPro; IPR013029; YchF_C.
DR   InterPro; IPR041706; YchF_N.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   Pfam; PF06071; YchF-GTPase_C; 1.
DR   PIRSF; PIRSF006641; CHP00092; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF81271; SSF81271; 1.
DR   TIGRFAMs; TIGR00092; TIGR00092; 1.
DR   PROSITE; PS51710; G_OBG; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q758F4.
DR   SWISS-2DPAGE; Q758F4.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03167};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03167};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03167};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03167};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          21..284
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51710"
FT   NP_BIND         30..35
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03167"
FT   BINDING         232
FT                   /note="ATP; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03167"
SQ   SEQUENCE   393 AA;  44049 MW;  C47853011209ADBF CRC64;
     MPPKKQVEEK KVLLGRPGNN LKAGIVGLAN VGKSTFFQAI TRCPLGNPAN YPFATIDPEE
     ARVIVPSPRF DSLCDVYKPA SKVPAHLTVY DIAGLTKGAS KGEGLGNAFL SHIRSVDSIY
     QVVRCFDDAE IIHIEGDVDP VRDLDIINTE LRLKDIEFAE KHLEAVEKIT KRGGQSLEVK
     QKKEEAELVK RIIELLKSGQ RVANQSWSTK EVEVINSMFL LTAKPSIYLI NLSERDYIRK
     KNKHLLKIKE WIDKYSPGDL IIPFSVCLEE RLSHMSAEEA VEECEKIGVQ SAFPKIITTM
     RQKLDLISFF TCGPDEVREW TIRNGTKAPQ AAGVIHNDLM NTFILAQIMK YEDVMEYKDD
     NAIKAAGKLL QKGKDYVVED GDIIYFRAGA GKN
//

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