ID A0A1Q3PZG8_9BACT Unreviewed; 955 AA.
AC A0A1Q3PZG8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=BGO32_06700 {ECO:0000313|EMBL:OJV26109.1};
OS Bacteroidetes bacterium 37-13.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1895921 {ECO:0000313|EMBL:OJV26109.1, ECO:0000313|Proteomes:UP000185627};
RN [1] {ECO:0000313|EMBL:OJV26109.1, ECO:0000313|Proteomes:UP000185627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=37-13 {ECO:0000313|EMBL:OJV26109.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OJV26109.1}.
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DR EMBL; MKTC01000028; OJV26109.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3PZG8; -.
DR STRING; 1895921.BGO32_06700; -.
DR Proteomes; UP000185627; Unassembled WGS sequence.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 11..273
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 362..543
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 712..919
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 955 AA; 107599 MW; 102B1F754542E93A CRC64;
MAATNTDWKD NKLFLLDAFA LIYRAYFAFI KSPLRNSKGM NVSAISGFTQ TLIELIQKEK
PTHIAVVFDS NEEETTRAVG YEFYKANRQA MPEDIALSIP WIKQIIAAMK IPILEVPGYE
ADDIIGTLAK QKAREGHLVY MVTPDKDYAQ LVEENIKIYK PGRQGNDIEI LGVNEILAKW
EIDNPEQVID ILGLWGDSVD NIPGIPGVGE KTAKKLIKEY GSMENIIANA ANIKGKLGEN
IKEYAEQGKI SKHLATIILD VPLNVTDEDL HLDEPDTEAI STLFTELEFR TLGRKLLGEK
FSVNNNTAGK TEIPTQRSNT GTQVDLFSAF ETQTQAQPEV KGKNIKNTEH NYIVATDNLE
LKQEGTTFIS IEELLQKLSQ ADEFCFDTET SSLDYFTLQI VGLSFSIRAG EAFYVPCPKN
FEEAKQLVHR FKTVLESATK IKIGQNVKFD LHVLRKYDVQ VAEPIYDTML AHYLVEPDMK
HGMDYLSETY LGYTPVHIEE LIGKRGKRQG SMQDVALHEI AEYAAEDADI TLQLKQVLAP
MVKQVEVEKV LQEIEHPLVP VLADMEHEGV KIDSDFLNDY SKELNADLVQ LQSKIYEYAG
LQFNIDSPKQ LGDILYKEMK LPFEGKKTST GQLSTNEEAL QALTKHHPIA EVLLNYREIG
KLKSTYVDAL PQLVHPKTGR VHTTFNQTIA ATGRLSSVSP NLQNIPIRSE RGQQVRKAFI
ARDEEHIFVS ADYSQIELRL VAEISGDEAM LSAFDHGMDI HAATAAKVYG VDVKDVTKAQ
RSNAKMVNFG IIYAISAFGL SQRLGIARKE AAELIENYFK QFPGIKNYMD STLNFAREHG
YVQTIMGRKR FLKDINSRNF TVRGFAEREA INAPVQGSAA DLIKIAMINI HREFQKQNLR
TKMTLQVHDE LVFDTHRDEL EIVKPIIEDK MVNAIKTRVP IIVEIGTGKN WLEAH
//
