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Database: UniProt
Entry: A0A267DKM4_9PLAT
LinkDB: A0A267DKM4_9PLAT
Original site: A0A267DKM4_9PLAT 
ID   A0A267DKM4_9PLAT        Unreviewed;       398 AA.
AC   A0A267DKM4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-SEP-2023, entry version 22.
DE   RecName: Full=Obg-like ATPase 1 {ECO:0000256|HAMAP-Rule:MF_03167};
GN   ORFNames=BOX15_Mlig025502g3 {ECO:0000313|EMBL:PAA49706.1};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA49706.1, ECO:0000313|Proteomes:UP000215902};
RN   [1] {ECO:0000313|EMBL:PAA49706.1, ECO:0000313|Proteomes:UP000215902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DV1 {ECO:0000313|EMBL:PAA49706.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:PAA49706.1};
RA   Berezikov E.;
RT   "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT   model organism for stem cell research.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:PAA49706.1}.
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DR   EMBL; NIVC01003808; PAA49706.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A267DKM4; -.
DR   STRING; 282301.A0A267DKM4; -.
DR   Proteomes; UP000215902; 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:UP000215902}.
FT   DOMAIN          24..283
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         231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03167"
SQ   SEQUENCE   398 AA;  44949 MW;  7B2EB68CE4D46C87 CRC64;
     MPPKKKGADE PKNPPIIGRM GSNLKIGIVG LPNVGKSTFF NVLTKSSAPA ENFPFCTIDP
     HESRVAVPDD RWEWLCEHWK PASRVPAYLN VWDIAGLVKG ASEGQGLGNA FLSNIRGVDA
     LFHMVRAFDC QEVTHIEGEV DPIRDLEIIS EELRLKDEAY IVKEFEKLEK VVTRGGDKSK
     TALFEAFQKV HRIVVEEKRS LRFEQWNDKE IDLLNEHLFI TAKPIVYLVN LSEKDFIRKK
     NKWLPKIKEW IDQHDPGAAV IPLSAELEFK WADMTDEQRA EFSKEHGVSS ALGKIISTGY
     KALQLQYFFT AGKDEVKAWT IPLNTKAPQA AGKIHSDMEN GFIMAEVMSF EDYKECGSES
     EVKAKGKYKQ KGRDYVVQDG DIIFFKFNAG AGLTAKKK
//
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