ID M4RCF9_9BIFI Unreviewed; 1024 AA.
AC M4RCF9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=DNA polymerase I {ECO:0000256|RuleBase:RU004460};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU004460};
GN Name=polA {ECO:0000256|RuleBase:RU004460};
GN ORFNames=D805_0888 {ECO:0000313|EMBL:AGH41155.1};
OS Bifidobacterium thermophilum RBL67.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1254439 {ECO:0000313|EMBL:AGH41155.1, ECO:0000313|Proteomes:UP000011835};
RN [1] {ECO:0000313|EMBL:AGH41155.1, ECO:0000313|Proteomes:UP000011835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RBL67 {ECO:0000313|EMBL:AGH41155.1,
RC ECO:0000313|Proteomes:UP000011835};
RX PubMed=23640377;
RA Jans C., Lacroix C., Follador R., Stevens M.J.;
RT "Complete Genome Sequence of the Probiotic Bifidobacterium thermophilum
RT Strain RBL67.";
RL Genome Announc. 1:E00191-13(2013).
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; CP004346; AGH41155.1; -; Genomic_DNA.
DR AlphaFoldDB; M4RCF9; -.
DR KEGG; btp:D805_0888; -.
DR PATRIC; fig|1254439.12.peg.882; -.
DR HOGENOM; CLU_004675_0_0_11; -.
DR Proteomes; UP000011835; Chromosome.
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:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
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; cd06140; DNA_polA_I_Bacillus_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; 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 PRINTS; PR00868; DNAPOLI.
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};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 22..284
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 780..987
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 318..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1024 AA; 110686 MW; 653C1B6904BBE389 CRC64;
MPTMSDNSQA QNAQQGAADK DFRGTLLVVD GHSLAFRAYF ALPVENFSTA SGQATNAVWG
FAKMLAQVIE TEHPDKLAVA FDVKGGTFRN DLLPQYKGTR EAAPEDLLSQ LPLIQEMLAA
LGVTYIEKPG FEGDDIIGTL ATMGERERYR TLVLSGDRDA FQLVDDVITV LYPGHHFKDL
KHMTPQAVEE KYHVTPQQYP DLAALRGETA DNIPGVPGVG DGYAAKWIGQ YGSLQGIIEH
ADEIGGKKGQ ALRDNLDQVK LNRKVNALVR DLDLGVGMND FDFGPMNREQ LSALFSKLEF
GVRTRNLVVK AFSGGNSASA ALPDTTQTAS ADADERPGES VSLVRDCPAS LIRDWAQRYQ
AQHAANTDAT TLAESEQSKT VAVAPAQSAA KPVPATAGTP ASPEASSSSD TPDSDTYEST
ERRSEPEKTA TSSIVIDHHA VSAPKVAQGW VLYADGDSKP GAPHCTGVAL LAGDEALAFT
PPLEPDVAAA IQTFIDANHD TMIVHGYKEH LHLLESIGIH LRRPAFDTKL ACYLVLPDYH
PDSLEQAAVR FADIHLDQPE RPAQGQLDLD GLDDSGAAQS QDDATITAKL ATIKELAVRL
SATLDEREQY GLLRSLELPV SEVLHRMEDA GACVDQTRLV AMRDQFAADA AQAQEIAWRA
AGSEVNLQSP KQLSSVLFDK LGLRPLRKTK SGQYKTDAAT LTALYAQSAN GNEQANDFLG
ALLRHRETNK LKQIVQTLID ATNPHDSRIH TTFEQTVAAT GRLSSVDPNL QNIPNRNAMG
REIRSAFVPG PGFSSLLSCD YSQVELRIMA DLSGDEALIE AFRSGADFHK YVASLVYQVP
VDDITPDQRS HVKAMSYGLA YGLSTYGLAQ QLHISPAEAD VLKEKYFATF GKVHDYLESL
VSNARKVGYT ETLFGRRRYF PGLSSSNARA RNAAERAALN APIQGSAADI MKIAMIRADQ
ALRDAGVASR IILQIHDELV VEIAPGEEEQ VSALVSDAME HAVSLAVPLD VSVGIGADWQ
LAAH
//
