ID C1D346_DEIDV Unreviewed; 363 AA.
AC C1D346;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Putative cobW {ECO:0000313|EMBL:ACO47835.1};
GN Name=cobW {ECO:0000313|EMBL:ACO47835.1};
GN OrderedLocusNames=Deide_2p01640 {ECO:0000313|EMBL:ACO47835.1};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OG Plasmid pDeide2 {ECO:0000313|Proteomes:UP000002208}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO47835.1, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO47835.1, ECO:0000313|Proteomes:UP000002208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC {ECO:0000313|Proteomes:UP000002208};
RC PLASMID=pDeide2 {ECO:0000313|Proteomes:UP000002208};
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
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; CP001116; ACO47835.1; -; Genomic_DNA.
DR RefSeq; WP_012695305.1; NC_012529.1.
DR AlphaFoldDB; C1D346; -.
DR KEGG; ddr:Deide_2p01640; -.
DR HOGENOM; CLU_017452_1_0_0; -.
DR OrthoDB; 9808822at2; -.
DR Proteomes; UP000002208; Plasmid pDeide2.
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; COBW-RELATED; 1.
DR PANTHER; PTHR13748:SF70; PROTEIN COBW; 1.
DR Pfam; PF02492; cobW; 1.
DR Pfam; PF07683; CobW_C; 1.
DR SMART; SM00833; 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 Plasmid {ECO:0000313|EMBL:ACO47835.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002208}.
FT DOMAIN 270..358
FT /note="CobW C-terminal"
FT /evidence="ECO:0000259|SMART:SM00833"
SQ SEQUENCE 363 AA; 39524 MW; 158B47E2D39C3378 CRC64;
MIPGHLKTPV TIVTGFLGSG KTTLLNNLLS QTHDRTLAVI VNEFGEVSID APLLDTREQG
VELHDVHGGL LAYGGEGDAF ARTLRALQSR RHTFDHVLIE TSGLAVPTAV MVTLETPEFA
GDFALDATLV VVDTPLLLEG AFQTQTDEAA ARVFDAQLEY ADVAVLNKID SLDDAQLLQA
EADVRHRAPR VRFLELAYGA RLDTQLTLGL NLHGSRRSAA HQAPVSGTPG DLSVPLHDHT
SLDGHSHGDL DAHVHSLSTH QHFHEHDPGW QSFRLTSDEV QNVPELLRTV QNVARVFPVL
RVKGFVNGTD GGRYALQAVR SRVETDPAPA RAGAPNELIF IGYHISRKKV TEALQKALPQ
RWA
//
