ID A0A0K1JJ11_9MICO Unreviewed; 413 AA.
AC A0A0K1JJ11;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000256|HAMAP-Rule:MF_01212};
GN ORFNames=VV02_13135 {ECO:0000313|EMBL:AKU16583.1};
OS Luteipulveratus mongoliensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Luteipulveratus.
OX NCBI_TaxID=571913 {ECO:0000313|EMBL:AKU16583.1, ECO:0000313|Proteomes:UP000066480};
RN [1] {ECO:0000313|EMBL:AKU16583.1, ECO:0000313|Proteomes:UP000066480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MN07-A0370 {ECO:0000313|EMBL:AKU16583.1,
RC ECO:0000313|Proteomes:UP000066480};
RA Juboi H., Basik A., Shamsul S.S., Arnold P., Schmitt E.K., Sanglier J.-J.,
RA Yeo T.;
RT "Luteipulveratus halotolerans sp. nov., a novel actinobacterium
RT (Dermacoccaceae) from Sarawak, Malaysia.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01212}.
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DR EMBL; CP011112; AKU16583.1; -; Genomic_DNA.
DR RefSeq; WP_052592047.1; NZ_CP011112.1.
DR AlphaFoldDB; A0A0K1JJ11; -.
DR STRING; 571913.VV02_13135; -.
DR KEGG; lmoi:VV02_13135; -.
DR PATRIC; fig|571913.6.peg.2673; -.
DR OrthoDB; 9803619at2; -.
DR Proteomes; UP000066480; Chromosome.
DR GO; GO:0016793; F:triphosphoric monoester hydrolase activity; IEA:InterPro.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR HAMAP; MF_01212; dGTPase_type2; 1.
DR InterPro; IPR006261; dNTPase.
DR InterPro; IPR023023; dNTPase_2.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR026875; PHydrolase_assoc_dom.
DR NCBIfam; TIGR01353; dGTP_triPase; 1.
DR PANTHER; PTHR11373:SF32; DEOXYGUANOSINETRIPHOSPHATE TRIPHOSPHOHYDROLASE; 1.
DR PANTHER; PTHR11373; DEOXYNUCLEOSIDE TRIPHOSPHATE TRIPHOSPHOHYDROLASE; 1.
DR Pfam; PF01966; HD; 1.
DR Pfam; PF13286; HD_assoc; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS51831; HD; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01212, ECO:0000313|EMBL:AKU16583.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000066480}.
FT DOMAIN 62..214
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 45215 MW; 173425F3088589D4 CRC64;
MSGPYDARSR ERWVQEDPEL KRADRDDFAR DRARLVHSAA LRRLSQKTQM HQPTVDDFVR
NRLTHSLEVA QIGREFGAAL GCNADVVDTA CLAHDLGHPP FGHNGETALD ALAADFGGFE
GNAQTLRLLT RLEAKRAHAD GRSAGLNLTR ASLDASIKYP WARGESPTPT RKFGVYADDV
DVFSWVRADV PADAPTRRCL EAQVMDWSDD VAYSVHDVED AIASGLVDLR ALRSGAVVEE
IAGIAQRLHA PEIETEALTA ALGRALEAGA MPNVHDGTRG SLAALKDTTS RLIGHFVQTV
EEATRERFGG GSLTRYDADV VIPDDVWAEC VMLKAVAAHF VLLTDTRQRL HADQRDVVIA
LFGAYRDRPE RLDPIYAMDF ADGADDAARL RVVVDQVASM TDGRAIELAQ AWT
//
