ID   DGTL1_COREF             Reviewed;         426 AA.
AC   Q8FNH1;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=CE2173;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000035; BAC18983.1; -; Genomic_DNA.
DR   RefSeq; WP_006768176.1; NZ_GG700683.1.
DR   AlphaFoldDB; Q8FNH1; -.
DR   SMR; Q8FNH1; -.
DR   STRING; 196164.23494015; -.
DR   PRIDE; Q8FNH1; -.
DR   EnsemblBacteria; BAC18983; BAC18983; BAC18983.
DR   KEGG; cef:CE2173; -.
DR   eggNOG; COG0232; Bacteria.
DR   HOGENOM; CLU_028163_0_1_11; -.
DR   OMA; AYDEDAH; -.
DR   OrthoDB; 370035at2; -.
DR   Proteomes; UP000001409; Chromosome.
DR   GO; GO:0008832; F:dGTPase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006203; P:dGTP catabolic process; IEA:InterPro.
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..426
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein"
FT                   /id="PRO_0000205301"
FT   DOMAIN          67..217
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   426 AA;  46554 MW;  3D1833A471C4B5AF CRC64;
     MYPYSESDAQ RLHQEAPKAS QLAHSEVDLR SDFSRDRARV LHSAALRRLA DKTQVVGPRD
     GDTPRTRLTH SLEVAQIARG MGSGLGLDPE LSELAGLCHD IGHPPYGHNG EKALNEVAAA
     CGGFEGNAQT LRILTRLEPK VVSADGTSFG LNLTRAALDA ACKYPWTKTS PDGTINRKYG
     AYDEDAHILE WVRRGHTDLR PSLEAQTMDF SDDIAYSVHD VEDGIVAGRI DLKVLWDLVE
     LAALAQKGAR AFGGDPEELI EGAATLRELP VVAAAADFDA SLSSYAALKA MTSELVGRYV
     GSTIAATRAA ARLGEYEFGR MHGELVIRPE ADREVRLLKT LAVLYVMDDP GHLARQDRQR
     DRIFRVFDYL TLGAPGSLDP MYRQWFLEAD DDAGRARVVV DQIASMTESR LERLARNASG
     ISGFLG