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Database: UniProt
Entry: W0RH33_9BACT
LinkDB: W0RH33_9BACT
Original site: W0RH33_9BACT 
ID   W0RH33_9BACT            Unreviewed;      1002 AA.
AC   W0RH33;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=DNA polymerase I {ECO:0000256|ARBA:ARBA00020311, ECO:0000256|RuleBase:RU004460};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|RuleBase:RU004460};
GN   Name=polA {ECO:0000256|RuleBase:RU004460};
GN   ORFNames=J421_1151 {ECO:0000313|EMBL:AHG88688.1};
OS   Gemmatirosa kalamazoonensis.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatirosa.
OX   NCBI_TaxID=861299 {ECO:0000313|EMBL:AHG88688.1, ECO:0000313|Proteomes:UP000019151};
RN   [1] {ECO:0000313|EMBL:AHG88688.1, ECO:0000313|Proteomes:UP000019151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBS708 {ECO:0000313|EMBL:AHG88688.1,
RC   ECO:0000313|Proteomes:UP000019151};
RX   PubMed=24699952;
RA   Debruyn J.M., Radosevich M., Wommack K.E., Polson S.W., Hauser L.J.,
RA   Fawaz M.N., Korlach J., Tsai Y.C.;
RT   "Genome Sequence and Methylome of Soil Bacterium Gemmatirosa
RT   kalamazoonensis KBS708T, a Member of the Rarely Cultivated Gemmatimonadetes
RT   Phylum.";
RL   Genome Announc. 2:e00226-14(2014).
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 5'-3' exonuclease activity. {ECO:0000256|RuleBase:RU004460}.
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         ECO:0000256|RuleBase:RU004460};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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DR   EMBL; CP007128; AHG88688.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0RH33; -.
DR   STRING; 861299.J421_1151; -.
DR   KEGG; gba:J421_1151; -.
DR   PATRIC; fig|861299.3.peg.1167; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_004675_0_0_0; -.
DR   InParanoid; W0RH33; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000019151; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd08637; DNA_pol_A_pol_I_C; 1.
DR   CDD; cd06139; DNA_polA_I_Ecoli_like_exo; 1.
DR   CDD; cd09898; H3TH_53EXO; 1.
DR   CDD; cd09859; PIN_53EXO; 1.
DR   Gene3D; 3.30.70.370; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR   InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR   InterPro; IPR002421; 5-3_exonuclease.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR020045; DNA_polI_H3TH.
DR   InterPro; IPR018320; DNA_polymerase_1.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   NCBIfam; TIGR00593; pola; 1.
DR   PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR   PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR   Pfam; PF01367; 5_3_exonuc; 1.
DR   Pfam; PF02739; 5_3_exonuc_N; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   Pfam; PF01612; DNA_pol_A_exo1; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00474; 35EXOc; 1.
DR   SMART; SM00475; 53EXOc; 1.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU004460};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU004460};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU004460};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004460};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU004460}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019151};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          13..283
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          322..592
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          760..966
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   REGION          398..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1002 AA;  110683 MW;  44485D4CFBFD42C0 CRC64;
     MPDATPAATP PVAPPPRLFL VDGYALIYRA FFALISRPLR TSRGENTSAA WGIVNFLNRL
     ITTHKPEYLG WVHDSGLSFR HEQYPAYKAT REKLTEELQD DFDRGMERIC QLLEAYRIPI
     ISMAGYEADD VIGSLAKKGT NAGLQVVVVS GDKDFHQLVR PGVWLLNPGR GGPAAVDEQW
     VSVENGSERL GVPPERTTDY LALVGDSSDN VPGVKGIGDK GAQELIAEFG DLETILANVD
     KITKKRPREA LQAGADSARL SKELVTILCD LDVPFDLEKF RIEEPDREAL KPLYAELEFT
     ALLKDVVASA APAEKAKEAV TYETVDTVQA MKRLVARARK ARTIAVDTET VVDPSSPTKI
     DPLRSTLVSL SIALAPGEAY YLPLAHRMWE PPQAELALGI PDAPGDRSPT DAPEDRGLFS
     GGDEPGGEPI VAAPKKKKAA AKKAASAPEP AGIGGRMIAE RGAQPPKNLP PLLSDEMRPL
     VELLEDESVS KTLQNAKYDV LALRRAGVTL RGVDFDTMLA SYVLDPGRRS HGMDVLAAEF
     LDYTMIAYED LTGKGKGQLA FDVVPVEAAR DYSCEDADIT LRLREIFEPQ LESQGLTTLF
     REVEMPLVCV LAEMEWTGIA IDVEHFKSLK ERFQAERERV EKEIYVEAGE EFNINSNPQL
     RVLLFEKLGL PVKKRTPTGP STDASVLTEL ADEGHVIPQL LMEYREIFKL EGTYIDTLPA
     LVHPETGRIH TTYSQAVAAT GRLSSNDPNL QNIPIRKELG RDIRRGFVPR KGWKLMAADY
     SQIELRLLAH FSGDPAFVQA FNSGGDIHRQ TAAIIFGVPL DDVTKEMRGR AKTINFATIY
     GQGAHALSRQ LKIANAEARE FIATYFERFR GVREYLEGQV EFAREHGYVE TLFKRRRYIP
     ELKEKNFNIR AFGERVAQNA PIQGSAADLI KVAMIRIDRA LRERGLSTKM LLQVHDELVF
     EVPVPELADV TALVRAEMEG AASLSVPLLV EVGVGDNWLE AK
//
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