ID K0KQ92_WICCF Unreviewed; 394 AA.
AC K0KQ92;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 13-SEP-2023, entry version 49.
DE RecName: Full=Obg-like ATPase 1 {ECO:0000256|HAMAP-Rule:MF_03167};
GN Name=OLA1 {ECO:0000256|HAMAP-Rule:MF_03167,
GN ECO:0000313|EMBL:CCH43584.1};
GN ORFNames=BN7_3137 {ECO:0000313|EMBL:CCH43584.1};
OS Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS 3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH43584.1, ECO:0000313|Proteomes:UP000009328};
RN [1] {ECO:0000313|EMBL:CCH43584.1, ECO:0000313|Proteomes:UP000009328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX PubMed=23193139; DOI=10.1128/EC.00258-12;
RA Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA Tauch A., Kohler T., Brinkrolf K.;
RT "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL Eukaryot. Cell 11:1582-1583(2012).
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}.
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:CCH43584.1}.
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DR EMBL; CAIF01000084; CCH43584.1; -; Genomic_DNA.
DR AlphaFoldDB; K0KQ92; -.
DR STRING; 1206466.K0KQ92; -.
DR eggNOG; KOG1491; Eukaryota.
DR HOGENOM; CLU_018395_1_2_1; -.
DR InParanoid; K0KQ92; -.
DR Proteomes; UP000009328; Unassembled WGS sequence.
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; IPR004095; TGS.
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.
DR PROSITE; PS51880; TGS; 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:UP000009328}.
FT DOMAIN 21..284
FT /note="OBG-type G"
FT /evidence="ECO:0000259|PROSITE:PS51710"
FT DOMAIN 306..389
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT BINDING 30..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03167"
FT BINDING 232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03167"
SQ SEQUENCE 394 AA; 44426 MW; AD9EE81258F9A12A CRC64;
MPPKKQVEEK KVLLGRPGNN LKSGIVGLAN VGKSTFFQAI TRCPLGNPAN YPYATIDPEE
ARVIVPSPRL DKLNEIYKPK SLVPAHITVY DIAGLTRGSS TGEGLGNSFL SHIRAVDAIY
QVVRCFDDAE IIHIEGDVNP YRDLEIISNE LRLKDIEFCE KHLEGVHKIT KRGGQSLEVK
QKKEEGELVL RIIELLKNGQ RVANQNWTPK EVEVINTMFL LTAKPSIYLI NLSERDYIRK
KNKHLLMIKE WVDKYSPGDV IIPFSVSLEE RLSQMETDEE RAEEEKKIGA TSMLPKIITT
MRQKLDLISF FTAGADECRE WTIRKGTKAP QAAGVIHNDL MNTFILAQVN KYEDIIEYKD
EVALKAAGKM LQKGKDYVVE DGDVIYFRAG AGKN
//
