Y249_PYRAB
ID Y249_PYRAB Reviewed; 324 AA.
AC Q9V225; G8ZG85;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Putative GTPase PYRAB02490;
DE EC=3.6.-.-;
GN OrderedLocusNames=PYRAB02490; ORFNames=PAB2398;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
CC -!- FUNCTION: May have GTPase activity. May also bind and hydrolyze ATP.
CC May function as chaperone (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ArgK/MeaB
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ248283; CAB49173.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69626.1; -; Genomic_DNA.
DR PIR; F75215; F75215.
DR RefSeq; WP_010867373.1; NC_000868.1.
DR AlphaFoldDB; Q9V225; -.
DR SMR; Q9V225; -.
DR STRING; 272844.PAB2398; -.
DR PRIDE; Q9V225; -.
DR EnsemblBacteria; CAB49173; CAB49173; PAB2398.
DR GeneID; 1495139; -.
DR KEGG; pab:PAB2398; -.
DR PATRIC; fig|272844.11.peg.267; -.
DR eggNOG; arCOG01226; Archaea.
DR HOGENOM; CLU_043725_1_0_2; -.
DR OMA; WMWERID; -.
DR OrthoDB; 80898at2157; -.
DR PhylomeDB; Q9V225; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005129; GTPase_ArgK.
DR InterPro; IPR027417; P-loop_NTPase.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00750; lao; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; GTP-binding; Hydrolase; Nucleotide-binding.
FT CHAIN 1..324
FT /note="Putative GTPase PYRAB02490"
FT /id="PRO_0000157823"
FT BINDING 52..60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 229..231
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 324 AA; 35694 MW; 0DDF2A86F1DC55A4 CRC64;
MIDELIERMK KGDRRATARL ITLVENDEEK AREIIRKIYP LTGNAYIVGI TGPPGAGKST
LLDKLIKEAR KEGLIVGVIA IDPTSPFTGG ALLGDRIRMQ RHSTDPGVFI RSMATRGSLG
GLAKATNDAI KVLDAYGCDV IFVETVGVGQ VEVDIVKTAD TVVLVTVPGL GDDVQTIKAG
LMEIADIFVI NKADKEGADA TYFELNLALD LESDKWRELG WRPPVVETVA TMNKGIKELW
DKIKEHREFL ERSGRLKEKR RKRIEEEIKT IVSGIIAGKV EASIKRGEFE EIIRRVSQKD
IDPYSAADMI LKEIIGGGLS VQEN