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DPO1_THECA
ID   DPO1_THECA              Reviewed;         834 AA.
AC   P80194;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=DNA polymerase I, thermostable;
DE            EC=2.7.7.7;
DE   AltName: Full=TAC polymerase 1;
GN   Name=polA;
OS   Thermus caldophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GK24;
RA   Kwon S.-T., Kim J.S., Park J.H., Kim H., Lee D.-S.;
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 1-21.
RC   STRAIN=GK24;
RX   PubMed=8508785; DOI=10.1111/j.1432-1033.1993.tb17905.x;
RA   Park J.H., Kim J.S., Kwon S.-T., Lee D.-S.;
RT   "Purification and characterization of Thermus caldophilus GK24 DNA
RT   polymerase.";
RL   Eur. J. Biochem. 214:135-140(1993).
CC   -!- FUNCTION: Has 5'-3' exonuclease activity and no 3'-5' exonuclease
CC       activity.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable.;
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR   EMBL; U62584; AAB81398.1; -; Genomic_DNA.
DR   PIR; S33287; S33287.
DR   AlphaFoldDB; P80194; -.
DR   SMR; P80194; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProt.
DR   GO; GO:0001882; F:nucleoside binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR   CDD; cd09898; H3TH_53EXO; 1.
DR   Gene3D; 3.30.420.10; -; 1.
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   InterPro; IPR015361; Taq_pol_thermo_exonuc.
DR   PANTHER; PTHR10133; PTHR10133; 2.
DR   Pfam; PF01367; 5_3_exonuc; 1.
DR   Pfam; PF02739; 5_3_exonuc_N; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   Pfam; PF09281; Taq-exonuc; 1.
DR   PRINTS; PR00868; DNAPOLI.
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; SSF56672; SSF56672; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
DR   TIGRFAMs; TIGR00593; pola; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA damage; DNA repair; DNA replication;
KW   DNA-binding; DNA-directed DNA polymerase; Nucleotidyltransferase;
KW   Transferase.
FT   CHAIN           1..834
FT                   /note="DNA polymerase I, thermostable"
FT                   /id="PRO_0000101257"
FT   DOMAIN          176..262
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000255"
FT   REGION          412..834
FT                   /note="Polymerase"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   834 AA;  93799 MW;  A851FF3C3076348E CRC64;
     MEAMLPLFEP KGRVLLVDGH HLAYRTFFAL KGLTTSRGEP VQAVYGFAKS LLKALKEDGY
     KAVFVVFDAK APSFRHEAYE AYKAGRAPTP EDFPRQLALI KELVDLLGFT RLEVPGYEAD
     DVLATLAKNP EKEGYEVRIL TADRDLDQLV SDRVAVLHPE GHLITPEWLW QKYGLKPEQW
     VDFRALVGDP SDNLPGVKGI GEKTALKLLK EWGSLENLLK NLDRVKPENV REKIKAHLED
     LRLSLELSRV RTDLPLEVDL AQGREPDREG LRAFLERLEF GSLLHEFGLL EAPAPLEEAP
     WPPPEGAFVG FVLSRPEPMW AELKALAACR DGRVHRAADP LAGLKDLKEV RGLLAKDLAV
     LASREGLDLV PGDDPMLLAY LLDPSNTTPE GVARRYGGEW TEDAAHRALL SERLHRNLLK
     RLQGEEKLLW LYHEVEKPLS RVLAHMEATG VRLDVAYLQA LSLELAEEIR RLEEEVFRLA
     GHPFNLNSRD QLERVLFDEL RLPALGKTQK TGKRSTSAAV LEALREAHPI VEKILQHREL
     TKLKNTYVDP LPSLVHPNTG RLHTRFNQTA TATGRLSSSD PNLQNIPVRT PLGQRIRRAF
     VAEAGWALVA LDYSQIELRV LAHLSGDENL IRVFQEGKDI HTQTASWMFG VPPEAVDPLM
     RRAAKTVNFG VLYGMSAHRL SQELAIPYEE AVAFIERYFQ SFPKVRAWIE KTLEEGRKRG
     YVETLFGRRR YVPDLNARVK SVREAAERMA FNMPVQGTAA DLMKLAMVKL FPRLREMGAR
     MLLQVHDELL LEAPQAGAEE VAALAKEAME KAYPLAVPLE VEVGMGEDWL SAKG
 
 
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