ID   Y274_PYRHO              Reviewed;         317 AA.
AC   O58012;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Putative GTPase PH0274;
DE            EC=3.6.-.-;
GN   OrderedLocusNames=PH0274; ORFNames=PHBM032;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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; BA000001; BAA29346.1; -; Genomic_DNA.
DR   PIR; C71452; C71452.
DR   RefSeq; WP_010884371.1; NC_000961.1.
DR   AlphaFoldDB; O58012; -.
DR   SMR; O58012; -.
DR   STRING; 70601.3256663; -.
DR   EnsemblBacteria; BAA29346; BAA29346; BAA29346.
DR   GeneID; 1444158; -.
DR   KEGG; pho:PH0274; -.
DR   eggNOG; arCOG01226; Archaea.
DR   OMA; WMWERID; -.
DR   OrthoDB; 80898at2157; -.
DR   Proteomes; UP000000752; 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..317
FT                   /note="Putative GTPase PH0274"
FT                   /id="PRO_0000157824"
FT   BINDING         54..62
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         231..233
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   317 AA;  34606 MW;  7EECAC8F6D69B301 CRC64;
     MQPIDELIER LKKGDRRAVA KLITLVENDE SKAKVIIKKI YPLTGNAHIV GITGPPGAGK
     STLLDKLIKE ARREGLIVGV IAVDPTSPFT GGALLGDRIR MQRHSTDPGV FIRSMATRGS
     LGGLSKATND AIKILDAYGC DVIFVETVGV GQIEVDIVKT ADTVVLVTIP GLGDDVQTIK
     AGLMEIADIF VVNKADREGA DITYFELTLA LDLEKEKWEK IGWKPPIIET VGTTGKGVKE
     LWEKIKEHKK FLEESGKLAE KRRTRIEEEV KTIIAGIVAK KVEASLSEFE DIISMVLNKD
     LDPYSAADLV LEKIVGR