(data stored in ACNUC7421 zone)

SWISSPROT: C1AT34_RHOOB

ID   C1AT34_RHOOB            Unreviewed;       914 AA.
AC   C1AT34;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   30-AUG-2017, entry version 65.
DE   RecName: Full=DNA polymerase I {ECO:0000256|RuleBase:RU004460};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU004460};
GN   Name=polA {ECO:0000256|RuleBase:RU004460,
GN   ECO:0000313|EMBL:BAH48966.1};
GN   OrderedLocusNames=ROP_07190 {ECO:0000313|EMBL:BAH48966.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48966.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48966.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48966.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 5'-3' exonuclease activity.
CC       {ECO:0000256|RuleBase:RU004460}.
CC   -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
CC       diphosphate + DNA(n+1). {ECO:0000256|RuleBase:RU004460}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000256|RuleBase:RU004460}.
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DR   EMBL; AP011115; BAH48966.1; -; Genomic_DNA.
DR   RefSeq; WP_012687965.1; NC_012522.1.
DR   ProteinModelPortal; C1AT34; -.
DR   STRING; 632772.ROP_07190; -.
DR   EnsemblBacteria; BAH48966; BAH48966; ROP_07190.
DR   KEGG; rop:ROP_07190; -.
DR   PATRIC; fig|632772.20.peg.782; -.
DR   eggNOG; ENOG4105C2M; Bacteria.
DR   eggNOG; COG0258; LUCA.
DR   eggNOG; COG0749; LUCA.
DR   HOGENOM; HOG000020997; -.
DR   KO; K02335; -.
DR   OMA; ETGRVHT; -.
DR   OrthoDB; POG091H00PR; -.
DR   Proteomes; UP000002212; 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-dependent DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.40.50.1010; -; 1.
DR   InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR   InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR   InterPro; IPR020045; 5-3_exonuclease_C.
DR   InterPro; IPR002421; 5-3_exonuclease_N.
DR   InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR018320; DNA_polymerase_1.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN_domain-like.
DR   InterPro; IPR012337; RNaseH-like_dom.
DR   Pfam; PF01367; 5_3_exonuc; 1.
DR   Pfam; PF02739; 5_3_exonuc_N; 1.
DR   Pfam; PF00476; DNA_pol_A; 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; SSF47807; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
DR   TIGRFAMs; TIGR00593; pola; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1AT34.
DR   SWISS-2DPAGE; C1AT34.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   DNA damage {ECO:0000256|RuleBase:RU004460};
KW   DNA repair {ECO:0000256|RuleBase:RU004460};
KW   DNA replication {ECO:0000256|RuleBase:RU004460};
KW   DNA-binding {ECO:0000256|RuleBase:RU004460};
KW   DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU004460};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00636373};
KW   Nuclease {ECO:0000256|SAAS:SAAS00636380};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU004460,
KW   ECO:0000313|EMBL:BAH48966.1};
KW   Transferase {ECO:0000256|RuleBase:RU004460,
KW   ECO:0000313|EMBL:BAH48966.1}.
FT   DOMAIN       23    285       53EXOc. {ECO:0000259|SMART:SM00475}.
FT   DOMAIN      326    503       3'-5' exonuclease. {ECO:0000259|SMART:
FT                                SM00474}.
FT   DOMAIN      670    877       POLAc. {ECO:0000259|SMART:SM00482}.
SQ   SEQUENCE   914 AA;  99559 MW;  3184F3A031F13266 CRC64;
     MSPATTPRST TSPASGAAAP SDDRPTLMLL DGHSLAFRAF YALPAENFKT HSGQVTNAVY
     GFTSMLINLL RDEQPTHVAA AFDVSRQTFR AEKFPEYKAN RSKAPDEFKG QVEITKDVLG
     ALGIPVMAEE GFEADDIIAT LTTQAEALGY RVLVVTGDRD SLQLVTDGVT VLYPKKGVSD
     LTRFTPAAVE EKYGLTPAQY PDFAALRGDP SDNLPGIPGV GEKTATKWIK EYGDLVGLVD
     NVDKVRGKVG DALRENLPNV LLNRELTEMV RDVPLPYTPD QLMLAQWDRE KIHALFDDLE
     FKVLRDRLFA TLAPVEAEAE EGFEVRGSAL EPGAVADWLS LHASTGERSG VSVVGTRTPY
     GGDVTAIAVA AADGEGAYIA TASATPEDEK ALGDWLADAE QPKALHEAKW AMHALRGRGW
     VLGGLTSDTA LAAYLVRPGQ RTFNLDDLSL RYLRRELRVE ETGQEQLSLL DDADQVDAEA
     AETEILSARA VLDLAAALDT ELDNIESTAL LSEMELPLLE VLAVIEASGI AVDGTHLHDL
     QSRFAAEVSE AAEAAYGVIG KQINLGSPKQ LQVVLFDELE MPKTKKTKTG YTTDAEALQN
     LFEKTSHPFL EHLLAHRDAT RLKVTVDGLL KTVAEDGRIH TTFNQTVAAT GRLSSTEPNL
     QNIPVRTDAG RQIRDGFVVG EGYDSLLTAD YSQIEMRIMA HVSGDAGLIE AFNTGEDLHS
     FVGARAFGVP IEEVTPELRR RVKAMSYGLA YGLSAFGLAA QLKISTEEAK SQMEAYFARF
     GGVRDYLHEV VEQARKDGYT STLYGRRRYL PDLTSDNRQR REVAERAALN APIQGTAADI
     IKVAMINVQR SLREAGLKSR MLLQVHDELV LEVVDSEREQ VEQLVRDKMS SAIELSVPLD
     VSVGTGRSWD AAAH
//

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