ID A0A3M9N604_9BACT Unreviewed; 955 AA.
AC A0A3M9N604;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ECO:0000313|EMBL:RNI32428.1};
GN ORFNames=EFA69_03650 {ECO:0000313|EMBL:RNI32428.1};
OS Rufibacter immobilis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=1348778 {ECO:0000313|EMBL:RNI32428.1, ECO:0000313|Proteomes:UP000271010};
RN [1] {ECO:0000313|EMBL:RNI32428.1, ECO:0000313|Proteomes:UP000271010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCC P1 {ECO:0000313|EMBL:RNI32428.1,
RC ECO:0000313|Proteomes:UP000271010};
RA Yang Y.;
RT "Rufibacter latericius sp. nov., isolated from water in Baiyang Lake.";
RL Submitted (NOV-2018) 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:RNI32428.1}.
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DR EMBL; RJJE01000002; RNI32428.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M9N604; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000271010; 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 6..267
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 361..542
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"
FT REGION 297..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 107184 MW; E52E70134323F098 CRC64;
MSTPDKRLFL LDAMALIYRA HFAFSKNPRI NSKGMNTGAA LGFTNTLVDL LNREKPTHIG
VCYDAPSKTF RHDSFVEYKA NRQAMPEDIA IAIPYVKKIV EAFGIPGMML DGYEADDIIG
TLSCKAEKAG YDVFMMTPDK DYYQLVTDHV FVYKPAFLGN AIEVIDKPKV LERWEISNVK
QVIDILGLQG DAVDNIPGIP GIGEKTAKTL IQRFGSVENL IANAHELKGK QKENVVNFAE
QGLMSKELAT IHLDVPIDFD EEGLRYDGPD TEKLAALFDE LEFRQLATRV LGTASPAVPK
PVSHKPTVGK GVKSNTPMGQ TSLFDAPAEA TAPEAGEATE TQTDEFAPRI RKTIDTTLHE
YHLLTTPEQR QQLLKYLKLQ KEVSFDTETT SIDAITARLV GISFSYLPGE AYYIPVPPHD
EEVALEIVQE FKEVLESPSI VKIGQNIKYD LVVLQRYGID VQGPLYDTML AHYLLEPDMR
HNMDLLAETY LNYTPISIET LLGKGKNQLT MDKLPALQIY EYACEDADIT LQLKNYFDPL
LEKQGLKRLF NDVENPLLAV LGHMERAGVS IDAEALAESS ISLETSIKEI EQKIFEHAGM
EFNIGSPKQL GEVLFDRMGL GGSKIKKTKT GQYATGEEIL SKLAFEHEIV QLILDHRQLT
KLKSTYVDAL PQLVCQEDNR LHTSYNQAVA ATGRLSSTNP NLQNIPIRTE KGREIRKAFV
PRDENHVLLS ADYSQIELRI MAHFSNDATM KEAFQNGLDI HASTAAKVFR VPVEEVTSDM
RRKAKTINFG IIYGISAFGL AERLAIPRRE AAEIIEAYFL EFPAVKEYMD SAINQARDQE
YVETLLGRRR YLRDINSRNQ NIRGYAERNA INAPIQGTAA DIIKIAMINI DQWLREQNLA
SRMILQVHDE LVFDVLKEEL PVVQPKIEEL MKNAFPLSVP MEVGMGTGEN WLQAH
//
