DGTL2_LISIN
ID DGTL2_LISIN Reviewed; 465 AA.
AC Q927I2;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01213};
GN OrderedLocusNames=lin2806;
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
CC -!- SIMILARITY: Belongs to the dGTPase family. Type 3 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01213}.
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DR EMBL; AL596173; CAC98032.1; -; Genomic_DNA.
DR PIR; AH1782; AH1782.
DR RefSeq; WP_003772902.1; NC_003212.1.
DR AlphaFoldDB; Q927I2; -.
DR SMR; Q927I2; -.
DR STRING; 272626.lin2806; -.
DR PRIDE; Q927I2; -.
DR EnsemblBacteria; CAC98032; CAC98032; CAC98032.
DR GeneID; 61171151; -.
DR KEGG; lin:lin2806; -.
DR eggNOG; COG0232; Bacteria.
DR HOGENOM; CLU_028163_2_0_9; -.
DR OMA; ICYTIID; -.
DR OrthoDB; 370035at2; -.
DR Proteomes; UP000002513; 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 Gene3D; 1.10.3410.10; -; 1.
DR Gene3D; 1.10.3550.10; -; 1.
DR HAMAP; MF_01213; dGTPase_type3; 1.
DR InterPro; IPR023293; dGTP_triP_hydro_central_sf.
DR InterPro; IPR027432; dGTP_triphosphohydrolase_C.
DR InterPro; IPR006261; dNTPase.
DR InterPro; IPR020779; dNTPase_1.
DR InterPro; IPR023024; dNTPase_3.
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.
FT CHAIN 1..465
FT /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT protein"
FT /id="PRO_0000205330"
FT DOMAIN 63..252
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 465 AA; 53485 MW; 149494D38D41C9B8 CRC64;
MKWDKLLNDK RRRESGVTRS KNTDVRSAFE NDFQRIVMSA SFRRLQDKTQ VFPLEKSDFV
RTRLTHSMEV STIAKSMGNM VTHTIQEEKL DQDFTKDHAD KIPEILACAG LLHDMGNPPF
GHFGEESIRE WFRDNLATIT YKNKSLAEIL TPQMKEDFYY FEGNAQVLRV VSKLHYLFDQ
YGLNLTFATL NAVIKYPVSS LKVNKKQIKS KKLGYFYADE SLFNEITTAT EALDNRHPLT
YLLEVADDIA YLNADLEDGV KKGIVNITQI LKGFEEVEEH NKVTAACYNE LKKKSERYEG
QEESFIVQQW LASNVRGQLI NRSLEVFYEN YDAIMAGTFN DSLIDASSAE QLVQILQSLS
FTYIYQDKGI VESEIAGNEI ISKLLETFIP AVIYYDSETP ERQTAKDKRL LTLISDNYLG
CYRKNAEGES ETMKLYLRLL LVTDFICGMT DSYAKDLYQR LNGLS