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Database: UniProt
Entry: A0A0Q6W167_9BURK
LinkDB: A0A0Q6W167_9BURK
Original site: A0A0Q6W167_9BURK 
ID   A0A0Q6W167_9BURK        Unreviewed;       403 AA.
AC   A0A0Q6W167;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000256|HAMAP-Rule:MF_01212};
GN   ORFNames=ASD15_17000 {ECO:0000313|EMBL:KQV79734.1};
OS   Massilia sp. Root351.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV79734.1, ECO:0000313|Proteomes:UP000051876};
RN   [1] {ECO:0000313|EMBL:KQV79734.1, ECO:0000313|Proteomes:UP000051876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root351 {ECO:0000313|EMBL:KQV79734.1,
RC   ECO:0000313|Proteomes:UP000051876};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV79734.1, ECO:0000313|Proteomes:UP000051876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root351 {ECO:0000313|EMBL:KQV79734.1,
RC   ECO:0000313|Proteomes:UP000051876};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01212}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQV79734.1}.
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DR   EMBL; LMDJ01000033; KQV79734.1; -; Genomic_DNA.
DR   RefSeq; WP_057157852.1; NZ_LMDJ01000033.1.
DR   AlphaFoldDB; A0A0Q6W167; -.
DR   OrthoDB; 9803619at2; -.
DR   Proteomes; UP000051876; Unassembled WGS sequence.
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:KQV79734.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051876}.
FT   DOMAIN          72..215
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
SQ   SEQUENCE   403 AA;  45702 MW;  0ED35AB56E5526AC CRC64;
     MYSAETIAYA REQEALVRPL EYRVHQQHDS RSDGREDAMR DYARVLYAAS FRRLQGKMQL
     LGVDANQSNR NRLTHSLEVA QIARSIAADM GLERCVVSET CALAHDIGNP PFGHYGEKIL
     NSLCTEHGGF EGNAQAFRIL RTLEKRHYGY AGLNLTVRTL FGITKYFHTR TENARKFLYD
     EDHAFLSGEL ARHGITARKS IDAQIMDLSD EIAYAAHDVE DALSFGIITV GEIAHEFKIS
     ADYAAAYPQF SAIADRAHNE ALKCEQQASS EEYSIVLRKE LTSEIVHTLC RDLAVVDGQL
     GYRSAELLAK GLKSLLWKAI LRKKDVQLYE KRGEKIIRGL FEVLTDKQYN KDNILLPPEL
     RCLKDSRERL VIDYIAGMMD SYAAQEYERY FGPGSLDAIY RRG
//
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