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Database: UniProt
Entry: A9V629_MONBE
LinkDB: A9V629_MONBE
Original site: A9V629_MONBE 
ID   A9V629_MONBE            Unreviewed;       394 AA.
AC   A9V629;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=Obg-like ATPase 1 {ECO:0000256|HAMAP-Rule:MF_03167};
GN   ORFNames=MONBRDRAFT_38170 {ECO:0000313|EMBL:EDQ86915.1};
OS   Monosiga brevicollis (Choanoflagellate).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX   NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ86915.1, ECO:0000313|Proteomes:UP000001357};
RN   [1] {ECO:0000313|EMBL:EDQ86915.1, ECO:0000313|Proteomes:UP000001357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX   PubMed=18273011; DOI=10.1038/nature06617;
RG   JGI Sequencing;
RA   King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA   Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA   Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA   Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA   Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA   McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT   "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT   metazoans.";
RL   Nature 451:783-788(2008).
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; CH991562; EDQ86915.1; -; Genomic_DNA.
DR   RefSeq; XP_001748154.1; XM_001748102.1.
DR   AlphaFoldDB; A9V629; -.
DR   STRING; 81824.A9V629; -.
DR   EnsemblProtists; EDQ86915; EDQ86915; MONBRDRAFT_38170.
DR   GeneID; 5893477; -.
DR   KEGG; mbr:MONBRDRAFT_38170; -.
DR   eggNOG; KOG1491; Eukaryota.
DR   InParanoid; A9V629; -.
DR   OMA; VLRCFDN; -.
DR   Proteomes; UP000001357; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis 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   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:UP000001357}.
FT   DOMAIN          24..282
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51710"
FT   DOMAIN          304..387
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   BINDING         33..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03167"
FT   BINDING         230
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03167"
SQ   SEQUENCE   394 AA;  43942 MW;  B4092AF8D1B185B7 CRC64;
     MAPKKTAAVE EDNAMLLGRL GTNLKVGIVG LPNVGKSTTF NVLTHSEAPA ENFPFCTKDP
     NEARVPVPDE RFDWLCDFHK PPSKVPAFLN VVDIAGLVKG AHEGLGLGNA FLSNIAACDA
     IFHVCRAFSD EDIVHVEGDV DPVRDLDIIS NELRLKDIAA LEKVMQPLER VALRGGDKKK
     KEEYDMLLKF KEFLAAGNDI RNGEWDRNEI DVLNEHLFLT AKPVIYLVNL SQKDFVRKKN
     KWLSKIKAWV DEHEKHPTII PYSADFELAL ALMDTDEARA KHQEEVGAAS MLSKIIKAGY
     QALNLCYFFT AGKDEVKAWT IQTGSRAPQA AGRIHTDFER GFIMAEVMNF EDFKEAGSEA
     GVKAAGKYRQ QGKTYVVQDG DIIFFKFNVT AKKK
//
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