ID Q9KVN3_VIBCH Unreviewed; 934 AA.
AC Q9KVN3;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 149.
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 OrderedLocusNames=VC_0108 {ECO:0000313|EMBL:AAF93286.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277 {ECO:0000313|EMBL:AAF93286.1, ECO:0000313|Proteomes:UP000000584};
RN [1] {ECO:0000313|EMBL:AAF93286.1, ECO:0000313|Proteomes:UP000000584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961
RC {ECO:0000313|Proteomes:UP000000584};
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D., Ermolaeva M.D.,
RA Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.,
RA Utterback T., Fleishmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003852; AAF93286.1; -; Genomic_DNA.
DR PIR; B82364; B82364.
DR RefSeq; NP_229767.1; NC_002505.1.
DR RefSeq; WP_000940283.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KVN3; -.
DR SMR; Q9KVN3; -.
DR STRING; 243277.VC_0108; -.
DR DNASU; 2614459; -.
DR EnsemblBacteria; AAF93286; AAF93286; VC_0108.
DR KEGG; vch:VC_0108; -.
DR PATRIC; fig|243277.26.peg.101; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR HOGENOM; CLU_004675_0_1_6; -.
DR Proteomes; UP000000584; Chromosome 1.
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; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
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:UP000000584};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 7..267
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 335..522
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 691..898
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 934 AA; 103875 MW; B23F2AF96769F1F7 CRC64;
MAHIPDNPLI LIDGSSYLYR AFHAYPGTMS NGEIPTNAIY GVVNMIRSMM RQFASDRMAV
IFDAKGKTFR DEMYDQYKAH RPPMPDELRC QVEPLHQVIR AMGLPLLAIE GVEADDVIGT
LARQASQAGM PVLISTGDKD MAQLVDDNIT LINTMTNVVL DREGVIEKFG IPPELIIDYL
ALMGDKVDNI PGVPGVGEKT ATALLQGIGG LEALYANLDK IAALGFRGSK TMAQKLEENR
GNAKLSYQLA TIKCDVELEE SPQTLLKQTP DRDALMSLYG KLAFKSWLTE LLDGGTGIVT
ADEQTKTSSV TVSTAATHAA AIPESPAAHI DRSQYQTILN EQDFQLWLEK LKQAELFAFD
TETDNLDYMV ANLVGMSFAV AEGEAAYLPV AHDYLDAPQQ LERDWVIAQL KPLLEDESKA
KVGQNLKYDA SVMARYGVEL RGIRHDTMLQ SYVYNSVGGK HDMDSLALRF LQHSCISFEQ
VAGKGKNQLT FNQIALEEAA QYAAEDADVT LRLHQRIHPL IEQDAKLEQV YREIEMPLVP
VLSRIERTGV MIDDMLLSAQ SQEIALRLDQ LEQNAYELAG QPFNLSSPKQ LQTILFEQMK
LPVLQKTPSG TPSTNEEVLQ ELALDYPLPK VLIEYRGLAK LKSTYTDKLP KMINPSTGRV
HTSYHQAVTA TGRLSSTDPN LQNIPVRNEE GRRIRQAFVA PHGWKIMAVD YSQIELRIMA
HLSGDQALLD AFRDGKDIHA ATAAEIIGVP IDQVSSEQRR RAKAVNFGLI YGMSAFGLAK
QLGIPRGEAQ EYMDKYFERY PGVMQYMEDT RSRAAQLGYV ETIFGRRLHL PEITSRNAMR
RKAAERAAIN APMQGTAADI IKKAMLLVDE WIEREGDGRV KLLMQVHDEL VFEVKESSLS
EIESKVQQLM ESAAELAVPL VAEAGHGDNW EQAH
//
