ID B1Y301_LEPCP Unreviewed; 381 AA.
AC B1Y301;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000256|HAMAP-Rule:MF_01212};
GN OrderedLocusNames=Lcho_3399 {ECO:0000313|EMBL:ACB35657.1};
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB35657.1, ECO:0000313|Proteomes:UP000001693};
RN [1] {ECO:0000313|EMBL:ACB35657.1, ECO:0000313|Proteomes:UP000001693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC {ECO:0000313|Proteomes:UP000001693};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) 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; CP001013; ACB35657.1; -; Genomic_DNA.
DR RefSeq; WP_012348404.1; NC_010524.1.
DR AlphaFoldDB; B1Y301; -.
DR STRING; 395495.Lcho_3399; -.
DR KEGG; lch:Lcho_3399; -.
DR eggNOG; COG0232; Bacteria.
DR HOGENOM; CLU_028163_1_0_4; -.
DR OrthoDB; 9803619at2; -.
DR Proteomes; UP000001693; 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:SF43; DEOXYGUANOSINETRIPHOSPHATE TRIPHOSPHOHYDROLASE-LIKE PROTEIN; 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:ACB35657.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001693}.
FT DOMAIN 61..197
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 381 AA; 43067 MW; DA4A5AD74EE1113D CRC64;
MAVYASDPAI SRGRRHAEEP APTRNPFQRD RDRIVHSTAF RRLVYKTQVF LNHEGDLFRT
RLTHTLEVAQ LGRSIGRALG LHEDLIEAIA LAHDLGHTPF GHAGQDALHE RMRGHGGFEH
NLQSLRVVDV LEERYPAFDG LNLSFETREG ILKHCPLRVA RWIDQHEPGG IGRRFIERSQ
PSLEAQLANL ADEIAYNAHD VDDGVRSGLI TLDQACSLPL LARHRDAALR EHPSLAQGKQ
RRLLFETLRR MLSAQVYDVI DATAAALRRH APRSADEVRQ LPPLVQFSPA MRAASTDLKR
WLYRSLYRHP QVMASTEPAK RIVAELFDAY VARPSEMPAD YAGAPLLHRS VSDYIAGMTD
RFAIREHERL TGARLFERVP G
//
