ID A0A261EYI3_9BIFI Unreviewed; 1014 AA.
AC A0A261EYI3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=PSSU_0680 {ECO:0000313|EMBL:OZG51897.1};
OS Pseudoscardovia suis.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Pseudoscardovia.
OX NCBI_TaxID=987063 {ECO:0000313|EMBL:OZG51897.1, ECO:0000313|Proteomes:UP000216454};
RN [1] {ECO:0000313|EMBL:OZG51897.1, ECO:0000313|Proteomes:UP000216454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24744 {ECO:0000313|EMBL:OZG51897.1,
RC ECO:0000313|Proteomes:UP000216454};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
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:OZG51897.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MWWQ01000006; OZG51897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261EYI3; -.
DR Proteomes; UP000216454; Unassembled WGS sequence.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000216454};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 52..312
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 770..977
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1014 AA; 109792 MW; 70D0FB778904431E CRC64;
MAQQIEDGES MNKESINEEP LNTEATEGSA SDGAHGDAAT GASADTLVAS NGRLLVVDGH
SLAFRAFFAL PVDNFSTSWG QPTNAVWGFA KMLSNVIATE KPTHIGVAFD MAGGTFRQKM
LPQYKGTRDA APEELLSQLP IIQQMLKAMG VTYIEKQGYE GDDIIGTLAT MGENAGFDTL
VLSGDRDAFQ LVDSRITVLY PGHHFKDLKH MTPQAIEEKY KVTPQQYPDL AAMRGEQADN
IPGVPGVGDG FAAKWINQYG GLEQIIEHAD EITGKKGEAL RDSIDQVRLN RRVNALVRDL
DLGVSVEDLR MKAPDRAAVD ELFAHLEFSK RTEGTILKPF PKGEASERVK LDLSGLQAAP
SDAAKDDTPV RTPIIDDVAA ADVPQWLREH CLAALAPETG KASAADTEAN GADAVSEDAS
DASDAPQHAG VPADAIWSLD AQPRQTGKES NVMPRLARLT ILAPDSHVAS LSASNITPQI
AKELSQEFAN RAGSLAVHGY KEAIHLFDSA GLTMPEPWID TKLAAYLDSA GSKQDLEDVI
TRVLPTGALE SAAPDTATEE LSLFDDPLDS TAEVQQAARR TVAVAALAHV LAGRIEERHE
TRLLHDIEYP VSRILARMES TGAAVDGQRL RDLFDTFAAG AHQAEDAAWD AAGRQLNLQS
PKQVQGVLFD DFKLAPVGRT KSGGYKTDSD SLMELAIRNA GDERASGFIT ALLRYREIVK
LKQCVETLQK SVDPDDGLIH TTFEQAVTAT GRLSSANPNL QNVPNRNAQG REIRSAFVPG
DGFVSLLSSD YSQVELRIMA HLSGDQALIE AFRSGKDFHR YVASLVYQVP VDQITPDQRS
HVKAMSYGLA YGLSTYGLAQ QLRISPAAAD VLKSKYFSTF GKVHDYLESL VADARRKGYT
ETMFGRRRYI PDLTAKSWQR RDAAERAALN APIQGTAADI MKIAMIRVDQ ALSAAHARSR
VVLQIHDELV LELAPGEQDE VTNLVKDAME HAVELSVPLD VSTGVGSDWQ LAAH
//
