ID A0A1Y0EN47_9BURK Unreviewed; 946 AA.
AC A0A1Y0EN47;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=CCO03_10255 {ECO:0000313|EMBL:ARU05016.1};
OS Comamonas serinivorans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=1082851 {ECO:0000313|EMBL:ARU05016.1, ECO:0000313|Proteomes:UP000196138};
RN [1] {ECO:0000313|EMBL:ARU05016.1, ECO:0000313|Proteomes:UP000196138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26136 {ECO:0000313|EMBL:ARU05016.1,
RC ECO:0000313|Proteomes:UP000196138};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) 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 -!- SUBUNIT: Single-chain monomer with multiple functions.
CC {ECO:0000256|ARBA:ARBA00011541}.
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; CP021455; ARU05016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0EN47; -.
DR KEGG; cser:CCO03_10255; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000196138; Chromosome.
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};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022839};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Reference proteome {ECO:0000313|Proteomes:UP000196138};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 15..275
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 350..536
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 704..910
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 321..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 946 AA; 103188 MW; 0E8220C2F27CB6B8 CRC64;
MTQTQEPAGG HALSGQTLLL VDGSSYLYRA YHAMPDLRAD PLDPTSPPTG AIRGMINMLG
SLRQDFPEAQ YVACVFDASG KTFRDDLYAA YKANRSPMPD DLRAQIEPIN TVVQLLGWTV
LTIPGIEADD VIGTLARAGE ARGMQVVISS GDKDLAQLVT EHVTIIDTMS GKKRDLAGVQ
AEFGVPANRM IDYQTLVGDS VDNVPGVSKV GPKTAAKWLN EYGSLDALIA QADAVKGAAG
ENLRKALDWL PTGRQLVTIR TDCDLSPALN AQATGTATVD DPIHALPVRP ADAAALAQFY
EQYGFRSLAK SIAAGHTTLG GAGKGGRAKA GPAPETDLPA GKSEVGELRY TTILTWAQFD
EWLARIDAAE LTALDTEATS LDEMQATLVG ISLSVQPGEA AYIPLMHTQP GTPEQLPLDE
VLARLKPWLE DASKPKLGQN FKYDRHVFAN HGMTVRGYVH DTMLASYVLE VHRAHSLESL
ADRHLGRTGL SYEDVCGKGV NQIPFAEVDL DTATRYACED ADQTLDVHRA LWPRLAADER
LRGIYALEIE TSERLFRVER NGVQIDAGTL ARQSNDLGRR ILEAEEKAYE LAGQPFKLGS
PKQIGEILFG KLGIPPLKKT PSGVPSTDED VLEQLAEDYP LPATILEHRS LSKLKSTYTD
KLPQMASPLD GRVHTHYAQA VAVTGRLSSV DPNLQNIPVR TADGRRIREA FVAPPGRLIA
SADYSQIELR IMAHLSGDAA LLKAFREGLD VHRATASEVF GVAPDQVSSE QRRYAKVINF
GLIYGMSAFG LAKNLNIERS AAKSWIERYF ERYPGVRRYM DDTVDFARSH GYVETVFGRR
LYLPEINGGN GPRKRAAERQ AINAPMQGTA ADLIKKAMCA VQDKLDAQGR QTLIIMQVHD
ELVFEVPEAE VDWVREEVPQ LMASVAELQV PLLAEVGVGL NWEEAH
//
