ID A0A061D7C3_BABBI Unreviewed; 430 AA.
AC A0A061D7C3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=CobW/P47K domain containing protein, putative {ECO:0000313|EMBL:CDR96443.1};
GN ORFNames=BBBOND_0303470 {ECO:0000313|EMBL:CDR96443.1};
OS Babesia bigemina.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5866 {ECO:0000313|EMBL:CDR96443.1, ECO:0000313|Proteomes:UP000033188};
RN [1] {ECO:0000313|Proteomes:UP000033188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bond {ECO:0000313|Proteomes:UP000033188};
RX PubMed=24799432; DOI=10.1093/nar/gku322;
RA Jackson A.P., Otto T.D., Darby A., Ramaprasad A., Xia D., Echaide I.E.,
RA Farber M., Gahlot S., Gamble J., Gupta D., Gupta Y., Jackson L.,
RA Malandrin L., Malas T.B., Moussa E., Nair M., Reid AJ., Sanders M.,
RA Sharma J., Tracey A., Quail M.A., Weir W., Wastling J.M., Hall N.,
RA Willadsen P., Lingelbach K., Shiels B., Tait A., Berriman M., Allred D.R.,
RA Pain A.;
RT "The evolutionary dynamics of variant antigen genes in Babesia reveal a
RT history of genomic innovation underlying host-parasite interaction.";
RL Nucleic Acids Res. 42:7113-7131(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ZNG1
CC subfamily. {ECO:0000256|ARBA:ARBA00034320}.
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DR EMBL; LK391709; CDR96443.1; -; Genomic_DNA.
DR RefSeq; XP_012768629.1; XM_012913175.1.
DR AlphaFoldDB; A0A061D7C3; -.
DR STRING; 5866.A0A061D7C3; -.
DR EnsemblProtists; CDR96443; CDR96443; BBBOND_0303470.
DR GeneID; 24564984; -.
DR KEGG; bbig:BBBOND_0303470; -.
DR VEuPathDB; PiroplasmaDB:BBBOND_0303470; -.
DR OMA; HNEFTEN; -.
DR OrthoDB; 276495at2759; -.
DR Proteomes; UP000033188; Chromosome 3.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd03112; CobW-like; 1.
DR Gene3D; 3.30.1220.10; CobW-like, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR036627; CobW-likC_sf.
DR InterPro; IPR011629; CobW-like_C.
DR InterPro; IPR003495; CobW/HypB/UreG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13748:SF31; COBW DOMAIN-CONTAINING PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR13748; COBW-RELATED; 1.
DR Pfam; PF02492; cobW; 1.
DR Pfam; PF07683; CobW_C; 1.
DR SUPFAM; SSF90002; Hypothetical protein YjiA, C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000033188}.
FT DOMAIN 13..232
FT /note="CobW/HypB/UreG nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF02492"
FT DOMAIN 326..420
FT /note="CobW C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07683"
SQ SEQUENCE 430 AA; 46662 MW; A037DC4A4D9068CD CRC64;
MEATEVQGDR KIPVTLVTGF LGSGKTTFIQ RLLKERHGMR IAVLQNEFSP EMGIEKPVLS
AGGASVFELP NGCLCCSMKD GIVEAVESIL QFRCDFDWLV VEAAGNVDPL ELASNFWLDP
ESPLLLDGVL SVTCPAVIQA VLSGANNNAA PSPNNRKIKD GDIEAPKLLE ECTAAPIRGT
DDAGAPTRPS GDRRFKLLGN ETLDDKNMLN LMRKQLSVAD VIIINKIDEL DCHFGDGHQS
GAEASAAQMQ NGGSGSISSV FADFTSMLKD MNPTAKVLKT SFCNVDFESV MNLQMFAASR
IMTFLSEGHH DHHHPRNGDH SSSNVFIKSQ GVYSLDYVNT FVSHLLWESG ATVYRCKGIF
KARKDCPMVT DADGATSVFQ LQGVGMLFEI SETEVADLDD NRFLFIGPGI DADKIRNALQ
LPPDTASENL
//
