ID V9VWS8_9RHOB Unreviewed; 934 AA.
AC V9VWS8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=METH_18835 {ECO:0000313|EMBL:AHD02398.1};
OS Leisingera methylohalidivorans DSM 14336.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=999552 {ECO:0000313|EMBL:AHD02398.1, ECO:0000313|Proteomes:UP000018780};
RN [1] {ECO:0000313|EMBL:AHD02398.1, ECO:0000313|Proteomes:UP000018780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14336 {ECO:0000313|EMBL:AHD02398.1,
RC ECO:0000313|Proteomes:UP000018780};
RG DOE Joint Genome Institute;
RA Klenk H.-P., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (SEP-2013) 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 ---------------------------------------------------------------------------
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; CP006773; AHD02398.1; -; Genomic_DNA.
DR RefSeq; WP_024091898.1; NC_023135.1.
DR AlphaFoldDB; V9VWS8; -.
DR STRING; 999552.METH_18835; -.
DR KEGG; lmd:METH_18835; -.
DR PATRIC; fig|999552.6.peg.3733; -.
DR HOGENOM; CLU_004675_0_0_5; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000018780; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 7..270
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 328..523
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 691..894
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 934 AA; 102535 MW; 7830B4EA7FD0529E CRC64;
MSGTQFGKGC HLHLIDGSAF IFRAYHALPP LTRKSDGLPI GAVAGFCNML FKQVEDNKGP
DAPTHVAVIF DYSGKSFRNE MYDQYKANRP PAPEDLVPQF PLTREATRAF NIACKEVEGF
EADDIIATLA HQARDAGGRV TIISSDKDLM QLVGGGVEML DAMKNKRIDS DGVVEKFGVG
PDRVVDVQAL AGDSVDNVPG APGIGIKTAA LLINEFGDLE TLLDRAEEIK QPKRRQTLID
KREQIELSKK LVQLDCSMEL DFTLDDLEVM EPDAETLLTF LSEMEFRTLT KRLADQLGMD
APAIPEAPAA AAAAAAAPDS VPFDKEKYEC VRDAAGLQAW VDRIRQRGWV AVDTETTGLD
EMVVDLVGIS LCVEPGEACY IPLAHKAGGD DLFGGEGLSE GQMPLEEAVA ILKGVLEDPA
VLKIGQNMKY DAKILHRYGV DVAPIDDTML MSYALHAGMH GHGMDTLSER YLDHTPIPIK
PLLGSGKSAI TFDRVPIEDA VPYAAEDADI TLRLWQTFKP QLHQERVTTV YETLERPLVP
VLADMERNGI KVDRDTLSRM SNAFAQKMAA LEAEIHELAG QTFNVGSPKQ LGEILFDKMG
IEGGKKGKTG AYATGADILE DLATEHDLPA RVLDWRQLSK LKSTYTDALQ DHINPDTGRV
HTSYAQTGAS TGRMASTDPN LQNIPVRTEE GRRIREAFVA EEGNVLLSLD YSQIELRILA
HMAGIDALKQ AFAEGQDIHA MTASEMFEVP LDEMTPEIRR QAKAINFGVI YGISGFGLAR
NLRIPRKDAQ GFIDRYFERF PGIRRYMDQT VEFAKEHGFV QTLFGRKIHT AEINAKGPKA
GFAKRAAINA PIQGTAADVI RRAMVRMPEA IAHLPARMLL QVHDELLFEV PESAVEETIE
TARRVMETAA DPAVHLDVKL VVDAGRGQNW AEAH
//
