DGTL1_STRCO
ID DGTL1_STRCO Reviewed; 424 AA.
AC Q9L2E9;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN OrderedLocusNames=SCO2470; ORFNames=SC7A8.09c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR EMBL; AL939112; CAB69758.1; -; Genomic_DNA.
DR RefSeq; NP_626712.1; NC_003888.3.
DR RefSeq; WP_011028369.1; NZ_VNID01000001.1.
DR AlphaFoldDB; Q9L2E9; -.
DR SMR; Q9L2E9; -.
DR STRING; 100226.SCO2470; -.
DR GeneID; 1097904; -.
DR KEGG; sco:SCO2470; -.
DR PATRIC; fig|100226.15.peg.2511; -.
DR eggNOG; COG0232; Bacteria.
DR HOGENOM; CLU_028163_0_1_11; -.
DR InParanoid; Q9L2E9; -.
DR OMA; FGVYEDD; -.
DR PhylomeDB; Q9L2E9; -.
DR Proteomes; UP000001973; Chromosome.
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..424
FT /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT protein"
FT /id="PRO_0000205321"
FT DOMAIN 70..220
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 45895 MW; BB78D49EB9F43FD1 CRC64;
MEGTAPPTPY DPASVARYAP EPDKRPGRTA FQRDRARILH SGALRRLAGK TQVVAPGEGS
PVWDASPRTR LTHSLECAQV GRELGAALGC DPDLVEAACL AHDLGHPPFG HNGEQALNAF
AEDCGGFEGN AQSLRLLTRI EPKRFTEDGS VGLNLTRATL DAATKYPWPR GAHPAVPASP
KFGVYDDDRP VFAWLREDAP GARTCFEAQV MDWADDVAYS VHDVEDGLHA GHIDPNCLLA
DPEREAVFDA AVGRFVPAGT DHAELAAALD RLLAQDWWPH GYDGSAPAQA RLKDATSQLI
GRFCLAAEAA TRAAYGDGRL TRYAAELVVP RETRMECAVL KAVAVRYVMQ RTEQERLRAD
QRIVVAELAE ALTARAPDGL DPQFRALFDA AADDRARKRV VVDQIASLTD ASARSLHARL
TGHP