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Database: UniProt
Entry: A0A1Q1FGE0_9EURY
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ID   A0A1Q1FGE0_9EURY        Unreviewed;       580 AA.
AC   A0A1Q1FGE0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=DNA polymerase beta {ECO:0000256|ARBA:ARBA00020020};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
DE            EC=4.2.99.18 {ECO:0000256|ARBA:ARBA00012720};
DE   AltName: Full=5'-deoxyribose-phosphate lyase {ECO:0000256|ARBA:ARBA00035717};
DE   AltName: Full=AP lyase {ECO:0000256|ARBA:ARBA00035726};
GN   ORFNames=BV210_03755 {ECO:0000313|EMBL:AQL41883.1};
OS   Halorientalis sp. IM1011.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halorientalis.
OX   NCBI_TaxID=1932360 {ECO:0000313|EMBL:AQL41883.1, ECO:0000313|Proteomes:UP000187924};
RN   [1] {ECO:0000313|EMBL:AQL41883.1, ECO:0000313|Proteomes:UP000187924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IM1011 {ECO:0000313|EMBL:AQL41883.1,
RC   ECO:0000313|Proteomes:UP000187924};
RA   Zhao D., Kumar S., Zhou J., Wang R., Xiang H.;
RT   "Isolation and genome sequence of Halorientalis hydrocarbonoclasticus sp.
RT   nov., a hydrocarbon-degrading haloarchaeon.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC         deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC         dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC         2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC         COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC         ChEBI:CHEBI:167181; EC=4.2.99.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00024490};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00024632};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end 2'-deoxyribose-2'-deoxyribonucleotide-DNA = (2E,4S)-
CC         4-hydroxypenten-2-al-5-phosphate + a 5'-end 5'-monophospho-2'-
CC         deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:76255, Rhea:RHEA-
CC         COMP:13180, Rhea:RHEA-COMP:18657, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:136412, ChEBI:CHEBI:195194, ChEBI:CHEBI:195195;
CC         Evidence={ECO:0000256|ARBA:ARBA00035582};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CP019067; AQL41883.1; -; Genomic_DNA.
DR   RefSeq; WP_077205348.1; NZ_CP019067.1.
DR   AlphaFoldDB; A0A1Q1FGE0; -.
DR   STRING; 1932360.BV210_03755; -.
DR   GeneID; 30958780; -.
DR   KEGG; hali:BV210_03755; -.
DR   OrthoDB; 8999at2157; -.
DR   Proteomes; UP000187924; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd00141; NT_POLXc; 1.
DR   CDD; cd07436; PHP_PolX; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.150.110; DNA polymerase beta, N-terminal domain-like; 1.
DR   Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR   InterPro; IPR010996; DNA_pol_b-like_N.
DR   InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR   InterPro; IPR037160; DNA_Pol_thumb_sf.
DR   InterPro; IPR002008; DNA_pol_X_beta-like.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   InterPro; IPR029398; PolB_thumb.
DR   InterPro; IPR022311; PolX-like.
DR   InterPro; IPR047967; PolX_PHP.
DR   PANTHER; PTHR36928; PHOSPHATASE YCDX-RELATED; 1.
DR   PANTHER; PTHR36928:SF1; PHOSPHATASE YCDX-RELATED; 1.
DR   Pfam; PF14791; DNA_pol_B_thumb; 1.
DR   Pfam; PF14520; HHH_5; 1.
DR   Pfam; PF14716; HHH_8; 1.
DR   Pfam; PF02811; PHP; 1.
DR   PIRSF; PIRSF005047; UCP005047_YshC; 1.
DR   PRINTS; PR00870; DNAPOLXBETA.
DR   SMART; SM00278; HhH1; 3.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SMART; SM00483; POLXc; 1.
DR   SUPFAM; SSF47802; DNA polymerase beta, N-terminal domain-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF89550; PHP domain-like; 1.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
PE   4: Predicted;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA synthesis {ECO:0000256|ARBA:ARBA00022634};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Exonuclease {ECO:0000313|EMBL:AQL41883.1};
KW   Hydrolase {ECO:0000313|EMBL:AQL41883.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Nuclease {ECO:0000313|EMBL:AQL41883.1};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187924};
KW   Sodium {ECO:0000256|ARBA:ARBA00023053};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          1..326
FT                   /note="DNA-directed DNA polymerase X"
FT                   /evidence="ECO:0000259|SMART:SM00483"
FT   DOMAIN          53..72
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          93..112
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          128..147
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          350..430
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   580 AA;  62152 MW;  42CFEFEA34B0CE8B CRC64;
     MSRNAEVASL LEEFADLLEA KDVEYKPRAY RRAAENIRGH PAAIEHLAAD GEDGVKEIEG
     VGDAIASKVV EYVETGGIEE LDELRNDLPV DMAALTSVEG VGPKTVGTLY DALGITTLDE
     LEDAAENGEI QEISGFGEKT ELNILDGVAF AREAHERELL GEARPYGDRV RDFLSGVDAV
     ESVELAGSIR RWRPTIGDVD VLVGSDDADA VISAFTDWDA AETVIEAGES KASLRIDDFR
     VDLRVVDAGE FGSALQYFTG SKDHNVRLRN RAIDRDLKMN EYGIFDVSEV DDPDADQRAG
     DRVGGETEEE MYDALDLPWI PPELREDRGE IAAAADGELP DLLSEDDVRG DLHIHTAWSD
     GGNTIREMAE AAAAFGHDYL AITDHATGPG MVGGVGLEDD ELREQIDEIR AVDDEVEVDL
     FAGVEANIGA DGSISVADDV LEALDLVVAS PHAGLDGDGT DRLVSAVEHP EVNVLGHPTG
     RMLNQRGGLD VDIERLAEAA ADAGVALEIN SDPRRLDIDG SLVKPAIESG ATVAIDTDAH
     QPGTLSYVRY GVHTARRGWA EADDVLNTRG ADGLGEFLGL
//
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