ID G8B7U5_CANPC Unreviewed; 396 AA.
AC G8B7U5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 13-SEP-2023, entry version 46.
DE RecName: Full=Obg-like ATPase 1 {ECO:0000256|HAMAP-Rule:MF_03167};
GN Name=OLA1 {ECO:0000256|HAMAP-Rule:MF_03167};
GN OrderedLocusNames=CPAR2_105660 {ECO:0000313|CGD:CAL0000150161,
GN ECO:0000313|EMBL:CCE40530.1};
OS Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS parapsilosis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE40530.1, ECO:0000313|Proteomes:UP000005221};
RN [1] {ECO:0000313|Proteomes:UP000005221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2] {ECO:0000313|Proteomes:UP000005221}
RP GENOME REANNOTATION.
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA Berriman M., Butler G.;
RT "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT response of the pathogenic yeast Candida parapsilosis.";
RL BMC Genomics 12:628-628(2011).
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; HE605203; CCE40530.1; -; Genomic_DNA.
DR AlphaFoldDB; G8B7U5; -.
DR STRING; 578454.G8B7U5; -.
DR EnsemblFungi; CPAR2_105660-T; CPAR2_105660-T-p1; CPAR2_105660.
DR CGD; CAL0000150161; CPAR2_105660.
DR VEuPathDB; FungiDB:CPAR2_105660; -.
DR eggNOG; KOG1491; Eukaryota.
DR Proteomes; UP000005221; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR CDD; cd04867; TGS_YchF_OLA1; 1.
DR CDD; cd01900; YchF; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.150.300; TGS-like domain; 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-bd.
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 NCBIfam; TIGR00092; redox-regulated ATPase YchF; 1.
DR PANTHER; PTHR23305; OBG GTPASE FAMILY; 1.
DR PANTHER; PTHR23305:SF11; OBG-LIKE ATPASE 1; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51710; G_OBG; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03167}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03167};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03167};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03167}; Reference proteome {ECO:0000313|Proteomes:UP000005221}.
FT DOMAIN 22..285
FT /note="OBG-type G"
FT /evidence="ECO:0000259|PROSITE:PS51710"
FT BINDING 31..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03167"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03167"
SQ SEQUENCE 396 AA; 44234 MW; 31FD478F895F4733 CRC64;
MPPKKKGVQE KPILLGRPGN NLKCGIVGLA NVGKSTFFQA ITKSPLGNPA NYPFATIEPE
EARVVVPSER FDKLCEMYKP KSEVPAFLTV YDIAGLTKGA ASGEGLGNNF LSNIRAVDAI
FQMTRAFDDA DIIHINDEVN PVADLDIVKD ELRLKDIEFA TKYLEGIEKI TKRGGQSLEV
KQKKEEAELV KRIIKLLEDG QRVYNQTWTA KEVDSINQML LLTAKPVIYL INLSEKDYIR
KKNKHLLKIK EWVDKNSPGD LIVPVSVSLE EKLAGMGSDE EREAYCKEIG AQSALPKIIV
AMRQKLDLIS FFTGGPDEVR EWTIRKWYTA PQAAGTIHTD LERTFILAQV IKYNDLIEYG
DEASVKAAGK LLQKGKDYFV EDGDIIYVKA AEGKAR
//
