ID A0A256CSK9_9GAMM Unreviewed; 918 AA.
AC A0A256CSK9;
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|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=B9T19_00080 {ECO:0000313|EMBL:OYQ81116.1};
OS Ignatzschineria sp. F8392.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Ignatzschineriaceae; Ignatzschineria.
OX NCBI_TaxID=1980117 {ECO:0000313|EMBL:OYQ81116.1, ECO:0000313|Proteomes:UP000215803};
RN [1] {ECO:0000313|EMBL:OYQ81116.1, ECO:0000313|Proteomes:UP000215803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F8392 {ECO:0000313|EMBL:OYQ81116.1,
RC ECO:0000313|Proteomes:UP000215803};
RA Gulvik C.A.;
RT "Wohlfahrtiimonas and Ignatzschineria genomes.";
RL Submitted (APR-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}.
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:OYQ81116.1}.
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DR EMBL; NEFF01000001; OYQ81116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A256CSK9; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000215803; 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 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 2..258
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 320..505
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 674..881
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 918 AA; 101969 MW; 3C8CAA2AC3629173 CRC64;
MSKTFLVVDG SNFLFRAFHA LPPLKSPDGR PTGAIRGVIS MFEKLVREFK PDYLGVIFDA
SGKSFRNDLF EDYKAHRPPM PDDLRAQIEP LYEIIDLMGF PRISIPGIEA DDVIATLAVE
AKAKGLRTII ASSDKDLAQL VEDDVITMYD GMKNEMLGRS EIFEKYGVYP EQVRDYLALM
GDSADNIPGI QGVGPKTAAK WIHEWGDLDA IVENAEKIKG KVGERLRDSL EILALSKELT
TLLLNAPLPV KVEDLTPNPP FIERLREVYQ DFGFRQLLLE LDQAGGGESF VPPVAQSVAS
DQLELAAHWI NPTLPAKKSY RTILDLAELE QYLSLIPETA LLALDTETDG LEFMRSHLVG
LSLSVAPGDA IYIPFKQAGL ENPLAIDAVM ARLKPILEDE KTPKVGQNIK FDWHILKRHG
VELRGIVDDT MLASYIYDPT GNRHNMDALA ELYLGFKTTP FEEIAGKGRS QKRFDEIDIE
IASFYACEDA DITLQLQRSI LPRLRSEVTQ YKVYQEIEVP LISVLAKMEH EGILVDAQHL
ESLSAEFGEN LAELEAKAYE LAGEEFNMSS SKQVGEILFE KLGLPVIKKT PKGAPSTAED
VLQKLAEDYP LPKIIIEYRE FSKLRSTYTD SLVAEINPDT GRVHTSFNQA QTSTGRLSSS
NPNLQNIPIR TKEGRRIREA FIAKEGSTLL AADYSQIELR LMAHFSQDEM MLKAFNEGKD
IHAATAAEVF GIPLEKVTGA ERRAAKAINF GLIYGMGAFG LAKQLGISRT QAQEYISLYF
SRYTGVLNYM EEAKEKAKEK GYVETALGRR LYLPGIHSSN AIARSGAERV AINAPLQGTA
ADIIKLAMLK VDRSLAENPH LSAKMLLQVH DELILETPIE QMEEVRALLV DAMTDVLKLD
VPLIVEVGSG KNWDETAG
//
