ID   DGT1B_DEIRA             Reviewed;         433 AA.
AC   Q9RTF6;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein 2 {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=DR_1808;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR   EMBL; AE000513; AAF11362.1; -; Genomic_DNA.
DR   PIR; D75352; D75352.
DR   RefSeq; NP_295531.1; NC_001263.1.
DR   RefSeq; WP_010888443.1; NZ_CP015081.1.
DR   AlphaFoldDB; Q9RTF6; -.
DR   SMR; Q9RTF6; -.
DR   STRING; 243230.DR_1808; -.
DR   EnsemblBacteria; AAF11362; AAF11362; DR_1808.
DR   KEGG; dra:DR_1808; -.
DR   eggNOG; COG0232; Bacteria.
DR   HOGENOM; CLU_028163_0_0_0; -.
DR   InParanoid; Q9RTF6; -.
DR   OMA; SIECQIM; -.
DR   OrthoDB; 370035at2; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0008832; F:dGTPase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006203; P:dGTP catabolic process; IBA:GO_Central.
DR   CDD; cd00077; HDc; 1.
DR   HAMAP; MF_01212; dGTPase_type2; 1.
DR   InterPro; IPR006261; dNTPase.
DR   InterPro; IPR020779; dNTPase_1.
DR   InterPro; IPR023023; dNTPase_2.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR026875; PHydrolase_assoc_dom.
DR   PANTHER; PTHR11373:SF32; PTHR11373:SF32; 1.
DR   Pfam; PF01966; HD; 1.
DR   Pfam; PF13286; HD_assoc; 1.
DR   SMART; SM00471; HDc; 1.
DR   TIGRFAMs; TIGR01353; dGTP_triPase; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..433
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein 2"
FT                   /id="PRO_0000205304"
FT   DOMAIN          61..248
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   433 AA;  50255 MW;  419B95C1B5348DC3 CRC64;
     MTAIVEPTWE ERRTPEAAHE DDARSQYRKD YSRIIHSAAL RRLQTKTQVL GLGDSDFYRT
     RLTHSLEVAQ IGVGILLEIQ RRFAGSNIEK YLPDERLLEA ICLSHDYGHP PFGHGGERAL
     NFAMREYGGF EGNAQTFRIL SKLEKYSQNS GLNPTRRTLL GVLKYPTTYS NSMTNDFRRG
     TDIDKYPDAE LKPPKCIYDC DLDVLDWVLK IFCSEDVTEF KKLDYKCKPL HKSLDCSLME
     TADDIAYTVH DLEDCIKLKL INREMWDAYI KSADYSEATR LEIEKWNQRI FSKEGNLVKQ
     GISNMVYFFI HSVIQYEHEE LSHPILKYGF KLGEEAARLR SAIQKIITNE VIKTHRVRVL
     ESKGQRMIFS IFGELVRDPE SFLPRETLDK YNKATGNLRM RVICDYVSGM TDEYATKTYQ
     RFFTPKFGSV FDV