DGTL1_CORGL
ID DGTL1_CORGL Reviewed; 424 AA.
AC Q8NND1;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN Name=dgt; OrderedLocusNames=Cgl2273, cg2494;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
CC -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR EMBL; BA000036; BAB99666.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20615.1; -; Genomic_DNA.
DR RefSeq; NP_601473.1; NC_003450.3.
DR RefSeq; WP_011015002.1; NC_006958.1.
DR AlphaFoldDB; Q8NND1; -.
DR SMR; Q8NND1; -.
DR STRING; 196627.cg2494; -.
DR KEGG; cgb:cg2494; -.
DR KEGG; cgl:Cgl2273; -.
DR PATRIC; fig|196627.13.peg.2206; -.
DR eggNOG; COG0232; Bacteria.
DR HOGENOM; CLU_028163_0_1_11; -.
DR OMA; FGVYEDD; -.
DR Proteomes; UP000000582; 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..424
FT /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT protein"
FT /id="PRO_0000205302"
FT DOMAIN 67..217
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 46151 MW; C977B573CE648654 CRC64;
MYPYSDADAF RRQPERAKSS QLRTSAVDTR SAFARDRARV LHSAALRRLA DKTQVVGPND
GDTPRTRLTH SLEVAQIARG IGAGLDLDPD LCDLAGLCHD IGHPPYGHNG ENALNEVAAA
CGGFEGNAQT LRILTRLEPK IVSDEGESFG LNLSRAALDA ACKYPWAKTN ADGSVNKKYS
AYDEDAEILA WIRQGHEDLR PPIEAQVMDF SDDIAYSVHD VEDGIVSGRI DLKVLWDLVE
LAALADKGAA AFGGSPAELI EGAASLRELP VVAAAADFDF SLRSYAALKA MTSELVGRYV
GSTIESTKKT HAGIDVGRMH GDLIIPETAA SEVKLLKTLA VLYVMDDPGH LARQNRQRDR
IFRVFDYLVL GAPGSLDPMY RQWFIEADSE SEQIRVIVDQ IASMTESRLE RLARNAADIS
GFLG