ID A0A1M6YKZ7_9BACT Unreviewed; 970 AA.
AC A0A1M6YKZ7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=SAMN05720468_11623 {ECO:0000313|EMBL:SHL18800.1};
OS Fibrobacter sp. UWEL.
OC Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC Fibrobacter.
OX NCBI_TaxID=1896209 {ECO:0000313|EMBL:SHL18800.1, ECO:0000313|Proteomes:UP000184030};
RN [1] {ECO:0000313|EMBL:SHL18800.1, ECO:0000313|Proteomes:UP000184030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWEL {ECO:0000313|EMBL:SHL18800.1,
RC ECO:0000313|Proteomes:UP000184030};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FRBE01000016; SHL18800.1; -; Genomic_DNA.
DR RefSeq; WP_073229772.1; NZ_FRBE01000016.1.
DR AlphaFoldDB; A0A1M6YKZ7; -.
DR STRING; 1896209.SAMN05720468_11623; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000184030; 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; 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.
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:UP000184030};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 3..266
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 339..562
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 727..934
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 298..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 970 AA; 108086 MW; D5E90D69A9A3D2CD CRC64;
MAEKTLLLLD SYALAFRMFY AYSQNPLKNS AGEDVSMMHG YWGAVLRILA KHQPTHFAIA
RDVAHTKTFR HELYPDYKAN RGPMPEEMAA QMPLLGESLA ASGIPLLSEP GYEADDVMAS
TAVAAAEAGF DRILIISKDK DMSQIVNDKI HLFHLEKGAD GIDFGPDQVL EKYGLPPEKI
RDYLALMGDA SDNVPGVPKV GPKTAITLLE EYGDMDNIYA NIDNIKKKGL HDNLANNKEQ
AFLSRELVTL QTKRAFNGSL DALEYTGIHV DTLADMFKEH EINSLLRLLE KIPSKTGFVK
GSENESGTES AGESGSESVQ GAGVTRADFD MPKDVLPTYI CVDSAEVFEQ MKAEFAAAPL
IGVDTETDGL DPMQCGLVGL CIAAVDASES VVDAESKRTD YTVSKGYYIP LNHRDEIGFP
QPVAKGGNFD INLVKEWFVD FFSKVPEPAE GPTRAFVFHN AKFDLHVLAR AFGLTQQQID
NANIIDTLIA AWMLSPGENG LGLDNQVMQK LQHEMIPIEN LIGRGKSQIT FDRTPIAAAT
EYGAEDAVYT LRLWAPLQKQ LQKYDYEKYF YQQEMPLLKV LYQMESVGIA VNVPSLKTLE
FELQRRIENL EKDICDMAGT EFNIGSPKQL AEVMFDTLGL REVKKRSTDA TVLEELFYET
ASPFVASVIE YRELKKMQST YVSVLPTLVN PETKRIHTSF IQWGTATGRL SSRDPNLQNI
PVRSDLGKKI RAAFVPQNPD NVILAVDYSQ IELRMLAHLS GDEALIDSYR NNIDIHARTA
AAIYGVPLEN VTSDMRRDAK VVNFGVLYGM TAFRLSRDLK IPMGQAKDFI TGYFDMFQGV
QMFIESTKAN AHRDGYVETL SGRRRYIAGI DSSDRMESQM AERMAVNTPV QGSAADLIKI
AMIRIQKRIN DEALPLKMML QVHDELVFEC PRDRVEELSA MVKSEMENAM KLQVPLVASV
GFGENWLIAH
//
