ID A0A1M5AXM1_9GAMM Unreviewed; 912 AA.
AC A0A1M5AXM1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=SAMN04487965_2003 {ECO:0000313|EMBL:SHF35031.1};
OS Microbulbifer donghaiensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=494016 {ECO:0000313|EMBL:SHF35031.1, ECO:0000313|Proteomes:UP000184170};
RN [1] {ECO:0000313|EMBL:SHF35031.1, ECO:0000313|Proteomes:UP000184170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7063 {ECO:0000313|EMBL:SHF35031.1,
RC ECO:0000313|Proteomes:UP000184170};
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 -!- 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; FQVA01000001; SHF35031.1; -; Genomic_DNA.
DR RefSeq; WP_073274176.1; NZ_FQVA01000001.1.
DR AlphaFoldDB; A0A1M5AXM1; -.
DR STRING; 494016.SAMN04487965_2003; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000184170; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 9..270
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 310..497
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 666..876
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT COILED 529..556
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 912 AA; 100582 MW; 30F9E40F11CFFFA7 CRC64;
MTDKNSNAAP LILVDGSSYL YRAFHALPPL TTSKGKPTGA VRGVIAMLRR HLKEHPHSTV
AVVFDAKGKT FRDELFADYK SHRPPMPDDL REQIQPIHDV IDAMGLPRLV VDGVEADDVI
GTLALEAQKQ GREVIISTGD KDMAQLVRPG ITLVNTMSNT EMDSDGVREK FGIGPELIID
FLALMGDKAD NIPGVPGVGE KTALALLQNL GGLEAIYADL DAIAPLGFRG AKTLGKKMAE
HRDAADMSYK LATIKTDVEM PYHPQELHNA EPHTDKLIEL FGELEFRGWL EELSAEPAEE
AMADAVERDY IIITEMADFD AWLQQLQEAD IFAFDTETTS LNYMQAKLVG VSFAVEPYRA
AYVPLAHDYM GAPAQLPFDE VLQKLKPLLE DDKQKKVGQN LKYDSHILAN YGIELRGIER
DTMLESYVLD STASRHDMDS LALKYLGEKT VHFEDIAGKG AKQLTFNQIE LDKAGPYAAE
DADITLRLHR ELSGRLAKEP SLEMVLDEIE MPLLPVLARI ERNGAYIDAK MLAAQSSELE
QKMRELEQQA FAVAGEEFNL GSTKQLGAIL FDKLQIPVIK KTPKGAPSTA EPVLQELALS
HELPALIMQY RGLAKLKNTY TDKLPLMIDP ATGRVHTSYH QAVAATGRLS SSDPNLQNIP
IRSEEGRRIR QAFTADPRVD GGSVIIAADY SQIELRIMAH LSGDKGLVDA FAQGADIHRA
TAAEVFEVAA DDVSDEQRRR AKAINFGLIY GMSAFGLAKQ LGIPRADAQT YIDRYFERYP
GVLQYMENTR KQASEKGYVE TLFGRRLYLP EINSRNGMQR QAAERTAINA PMQGTAADII
KRAMIAVDAW LAEQGLASKL IMQVHDELVL EVPASEVKQV TAGIVELMQG AAELHVPLIV
DLGQGTSWDE AH
//
