GenomeNet

Database: UniProt
Entry: Q7NZZ0_CHRVO
LinkDB: Q7NZZ0_CHRVO
Original site: Q7NZZ0_CHRVO 
ID   Q7NZZ0_CHRVO            Unreviewed;       928 AA.
AC   Q7NZZ0;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 150.
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   ECO:0000313|EMBL:AAQ58455.1};
GN   OrderedLocusNames=CV_0779 {ECO:0000313|EMBL:AAQ58455.1};
OS   Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS   12614 / NCIMB 9131 / NCTC 9757).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Chromobacterium.
OX   NCBI_TaxID=243365 {ECO:0000313|EMBL:AAQ58455.1, ECO:0000313|Proteomes:UP000001424};
RN   [1] {ECO:0000313|EMBL:AAQ58455.1, ECO:0000313|Proteomes:UP000001424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 /
RC   NCTC 9757 {ECO:0000313|Proteomes:UP000001424};
RX   PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA   Vasconcelos A.T.R., de Almeida D.F., Almeida F.C., de Almeida L.G.P.,
RA   de Almeida R., Goncalves J.A.A., Andrade E.M., Antonio R.V., Araripe J.,
RA   de Araujo M.F.F., Filho S.A., Azevedo V., Batista A.J., Bataus L.A.M.,
RA   Batista J.S., Belo A., vander Berg C., Blamey J., Bogo M., Bonato S.,
RA   Bordignon J., Brito C.A., Brocchi M., Burity H.A., Camargo A.A.,
RA   Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B.,
RA   Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Pasa T.B.C., Duran N.,
RA   Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S.,
RA   Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A.,
RA   Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA   Grattapaglia D., Grisard E.C., Guimaraes C.T., Hanna E.S., Hungria M.,
RA   Jardim S.N., Laurino J., Leoi L.C.T., Fassarella L., Lima A.,
RA   Loureiro M.F., Lyra M.C.P., Macedo M., Madeira H.M.F., Manfio G.P.,
RA   Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B.,
RA   Meissner R.D.V., Menck C.F.M., Moreira M.A.M., Nascimento F.F.,
RA   Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA   Pedrosa F.O., Pena S.J.D., Perreira J.O., Perreira M., Pinto L.S.R.C.,
RA   Pinto L.S., Porto J.I.R., Potrich D.P., Neto C.E.R., Reis A.M.M.,
RA   Rigo L.U., Rondinelli E., dos Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA   Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA   Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA   Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA   Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT   "The complete genome sequence of Chromobacterium violaceum reveals
RT   remarkable and exploitable bacterial adaptability.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
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; AE016825; AAQ58455.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7NZZ0; -.
DR   STRING; 243365.CV_0779; -.
DR   KEGG; cvi:CV_0779; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_004675_0_0_4; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000001424; 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:UP000001424};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          1..256
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          331..517
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          686..892
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   REGION          289..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   928 AA;  101555 MW;  2E53950409D8D468 CRC64;
     MKTLLLIDGS SYLYRAFHAM PDLRSPDGRP VGAVYGMVNM LRRLEKEVEF DYSACVFDAK
     GKTFRDDLYP EYKANRPSMP EELASQITAV HDVVQASGWP MLVVPGVEAD DVIGTLARLG
     AAAGMKVIVS TGDKDMAQLV TPDVTLVNTM TNELLDEAGV KEKFGVPPSL IIDYLTLIGD
     KVDNVPGVDK CGPKTAVKWL EEYGSLDAII AQAGSVGGKV GENLRAALDW LPMGRRLITI
     DCDVDLEADL PHGLPGLQHG QKDKPRLAEL FQDLGFRTFY REVTEGAEMP AVAQRGEDAP
     RGGEAQGDMF AEPAAPAAPP ALSAGALERH YETILTEAQL DAWLARLMAA KVVSFDTETT
     SLDPMQARIV GVSFSVEAGH AAYLPLEHHY AGAPQQLPLE AALAKLKPWL EDASKKKCGQ
     NLKYDCHVLA NHGIALAGIA DDSMLASYVL ESHQRHNMDD LARRHLGENT VSYEEICGKG
     AKQIGFSEVD VDIAANYAAE DADITLRLNQ FFAGQLFGDL EKVYRDIELP VAEVLFKMER
     HGVLIDRDKL AAQSHQLGSQ MLELEQRAYE LAGQPFNLNS PKQLQEILFG KLAIPTKGVK
     KTPSGGYSTD ESVLEQLALD HPLPKCILEY RGLAKLKSTY TDKLPTLIYP QTGRVHTTYA
     QAVAITGRLA SNDPNLQNIP VRTAEGRRVR EAFIAPAGWQ IVSADYSQIE LRIMAHLSDD
     EGMLKAFASG EDIHRATAAE VFGVELAAVT SDQRRAAKAI NFGLIYGMSA FGLAAQLDIE
     RSAAQQYIDR YFMRYPGVAE YMQATREKAR EQGYVETVFG RRLYLPDIKL SNPGRRAGAE
     RAAINAPMQG TAADLIKLAM IAVQDWLERD GLQSKLIMQV HDELVLEVPQ AELEQVKRRL
     PEIMAGAAEL KVPLLAEVGA GDSWEAAH
//
DBGET integrated database retrieval system