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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
 
 
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