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Database: UniProt
Entry: A0A0G0MUL5_9BACT
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Original site: A0A0G0MUL5_9BACT 
ID   A0A0G0MUL5_9BACT        Unreviewed;       577 AA.
AC   A0A0G0MUL5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=UT30_C0012G0017 {ECO:0000313|EMBL:KKR04106.1};
OS   Candidatus Uhrbacteria bacterium GW2011_GWF2_39_13.
OC   Bacteria; Candidatus Uhrbacteria.
OX   NCBI_TaxID=1618995 {ECO:0000313|EMBL:KKR04106.1, ECO:0000313|Proteomes:UP000033935};
RN   [1] {ECO:0000313|EMBL:KKR04106.1, ECO:0000313|Proteomes:UP000033935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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}.
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:KKR04106.1}.
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DR   EMBL; LBWG01000012; KKR04106.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0MUL5; -.
DR   Proteomes; UP000033935; Unassembled WGS sequence.
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: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   InterPro; IPR010994; RuvA_2-like.
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; SSF47781; RuvA domain 2-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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Sodium {ECO:0000256|ARBA:ARBA00023053};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          6..320
FT                   /note="DNA-directed DNA polymerase X"
FT                   /evidence="ECO:0000259|SMART:SM00483"
FT   DOMAIN          58..77
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          98..117
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          133..152
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          344..423
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   577 AA;  65138 MW;  44FBF99EAEB02644 CRC64;
     MSPKKITNKE IIEIFREIAL YLRAEDVAFK PQAYEVAAES LSSLQQELSD LYQTCGATYL
     DQIPGVGKSM IEKIEEIIVT GKLSFYVELK KKYPFDMMAL SRIQNIGPKT AMKLYRELGV
     KTLRDLERAA KANKIADLPG MGKKTQDIIV RGIQYLKQDT GRRLIHDVLP FAEELIGKLK
     TVKGTTHVNI AGSLRRRKET IGDIDLLATS SKPEVLIKAF KNLPQVYEVL EEGSNKLMVR
     YINGLQGDLL ILPPEEYGAA LVHFTGSREH NIFLRERAIN KKMKLSKHGL WKGSVRITSR
     TEKQVYKHLG LEWIAPELRV GSDEIEKAAK KQLPDLIEYG SLKGDLQIQT TWSDGIGSIE
     EMANAAKAYG LSYMAVTDHT HSLHIAQGLD EKRLKQQAEE IDVLNKKIKG FTILKSTECE
     ILKDGKLDLS DTRLKTLDIV SVSVHGHIQM TKKDMTQRII RALKHPLVNI LFHPTGRVVT
     KREGYELDMD QIIKAAREYH VALEINGSAR LDLHEHYIRQ AIGEGVKLVI SSDAHDSTHL
     EYLDYGIAQA RKGWCTKADI LNTKPLKKFL AALKKEK
//
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