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DPO1_CALBD
ID   DPO1_CALBD              Reviewed;         850 AA.
AC   Q59156; B9MS85;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=DNA polymerase I;
DE            Short=Pol I;
DE            EC=2.7.7.7;
GN   Name=polA; OrderedLocusNames=Athe_1441;
OS   Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320)
OS   (Anaerocellum thermophilum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX   NCBI_TaxID=521460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Bolchakova E.V., Novikov A.A., Zverlov V.V., Galina V.,
RA   Velikodvorskaya G.V.;
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1888 / DSM 6725 / Z-1320;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Kataeva I., Adams M.W.W.;
RT   "Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 3'-5' and 5'-3' exonuclease activity. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR   EMBL; X98575; CAA67184.1; -; Genomic_DNA.
DR   EMBL; CP001393; ACM60539.1; -; Genomic_DNA.
DR   RefSeq; WP_015907902.1; NC_012034.1.
DR   AlphaFoldDB; Q59156; -.
DR   SMR; Q59156; -.
DR   STRING; 521460.Athe_1441; -.
DR   PRIDE; Q59156; -.
DR   EnsemblBacteria; ACM60539; ACM60539; Athe_1441.
DR   GeneID; 31772786; -.
DR   KEGG; ate:Athe_1441; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_004675_0_0_9; -.
DR   OMA; NRPPMPD; -.
DR   OrthoDB; 1220182at2; -.
DR   Proteomes; UP000007723; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
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: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; 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   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   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; SSF56672; SSF56672; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
DR   TIGRFAMs; TIGR00593; pola; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Exonuclease; Hydrolase; Nuclease;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..850
FT                   /note="DNA polymerase I"
FT                   /id="PRO_0000101231"
FT   DOMAIN          1..288
FT                   /note="5'-3' exonuclease"
FT   REGION          470..850
FT                   /note="Polymerase"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        451
FT                   /note="N -> S (in Ref. 1; CAA67184)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        774
FT                   /note="A -> P (in Ref. 1; CAA67184)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        831
FT                   /note="A -> R (in Ref. 1; CAA67184)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   850 AA;  98130 MW;  AAEAC6DB4525A7FD CRC64;
     MKLVIFDGNS ILYRAFFALP ELTTSNNIPT NAIYGFVNVI LKYLEQEKPD YVAVAFDKRG
     REARKSEYEE YKANRKPMPD NLQVQIPYVR EILYAFNIPI IEFEGYEADD VIGSLVNQFK
     NTGLDIVIIT GDRDTLQLLD KNVVVKIVST KFDKTVEDLY TVENVKEKYG VWANQVPDYK
     ALVGDQSDNI PGVKGIGEKS AQKLLEEYSS LEEIYQNLDK IKSSIREKLE AGKDMAFLSK
     RLATIVCDLP LNVKLEDLRT KEWNKERLYE ILVQLEFKSI IKRLGLSEVV QFEFVQQRTD
     IPDVEQKELE SISQIRSKEI PLMFVQGEKC FYLYDQESNT VFITSNKLLI EEILKSDTVK
     IMYDLKNIFH QLNLEDTNNI KNCEDVMIAS YVLDSTRSSY ELETLFVSYL NTDIEAVKKD
     KKIVSVVLLK RLWDELLRLI DLNSCQFLYE NIERPLIPVL YEMEKTGFKV DRDALIQYTK
     EIENKILKLE TQIYQIAGEW FNINSPKQLS YILFEKLKLP VIKKTKTGYS TDAEVLEELF
     DKHEIVPLIL DYRMYTKILT TYCQGLLQAI NPSSGRVHTT FIQTGTATGR LASSDPNLQN
     IPVKYDEGKL IRKVFVPEGG HVLIDADYSQ IELRILAHIS EDERLISAFK NNVDIHSQTA
     AEVFGVDIAD VTPEMRSQAK AVNFGIVYGI SDYGLARDIK ISRKEAAEFI NKYFERYPKV
     KEYLDNTVKF ARDNGFVLTL FNRKRYIKDI KSTNRNLRGY AERIAMNSPI QGSAADIMKL
     AMIKVYQKLK ENNLKSKIIL QVHDELLIEA PYEEKDIVKE IVKREMENAV ALKVPLVVEV
     KEGLNWYETK
 
 
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