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DPO3_ALKHC
ID   DPO3_ALKHC              Reviewed;        1433 AA.
AC   Q9KA72;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=DNA polymerase III PolC-type {ECO:0000255|HAMAP-Rule:MF_00356};
DE            Short=PolIII {ECO:0000255|HAMAP-Rule:MF_00356};
DE            EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_00356};
GN   Name=polC {ECO:0000255|HAMAP-Rule:MF_00356}; OrderedLocusNames=BH2418;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
CC   -!- FUNCTION: Required for replicative DNA synthesis. This DNA polymerase
CC       also exhibits 3' to 5' exonuclease activity. {ECO:0000255|HAMAP-
CC       Rule:MF_00356}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00356};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00356}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-C family. PolC
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00356}.
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DR   EMBL; BA000004; BAB06137.1; -; Genomic_DNA.
DR   PIR; B83952; B83952.
DR   RefSeq; WP_010898571.1; NC_002570.2.
DR   AlphaFoldDB; Q9KA72; -.
DR   SMR; Q9KA72; -.
DR   STRING; 272558.10175038; -.
DR   EnsemblBacteria; BAB06137; BAB06137; BAB06137.
DR   KEGG; bha:BH2418; -.
DR   eggNOG; COG2176; Bacteria.
DR   HOGENOM; CLU_003297_2_0_9; -.
DR   OMA; YYAAYFT; -.
DR   OrthoDB; 561611at2; -.
DR   Proteomes; UP000001258; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
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:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.150.700; -; 2.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_00356; DNApol_PolC; 1.
DR   InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR   InterPro; IPR040982; DNA_pol3_finger.
DR   InterPro; IPR024754; DNA_PolC-like_N_II.
DR   InterPro; IPR028112; DNA_PolC-type_N_I.
DR   InterPro; IPR029460; DNAPol_HHH.
DR   InterPro; IPR006054; DnaQ.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR006308; PolC_gram_pos.
DR   InterPro; IPR044923; PolC_middle_finger_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF14480; DNA_pol3_a_NI; 1.
DR   Pfam; PF11490; DNA_pol3_a_NII; 1.
DR   Pfam; PF07733; DNA_pol3_alpha; 2.
DR   Pfam; PF17657; DNA_pol3_finger; 1.
DR   Pfam; PF14579; HHH_6; 1.
DR   Pfam; PF02811; PHP; 1.
DR   Pfam; PF00929; RNase_T; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   TIGRFAMs; TIGR00573; dnaq; 1.
DR   TIGRFAMs; TIGR01405; polC_Gram_pos; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA replication; DNA-directed DNA polymerase; Exonuclease;
KW   Hydrolase; Nuclease; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..1433
FT                   /note="DNA polymerase III PolC-type"
FT                   /id="PRO_0000204574"
FT   DOMAIN          419..575
FT                   /note="Exonuclease"
SQ   SEQUENCE   1433 AA;  162126 MW;  B1DEF38B3612D59F CRC64;
     MNEEQRVRQE RFKLLMEQLL IPEDVTANHL KDGKIEKLTI KKDERRWHFQ LSIPTVLPAS
     IYELLADRLV QTFSHIAKVS FQIQYGQPDL SEQVWQSYWP LIVAKLTNIS QPLKEMLEKQ
     TPRFDGKRLV IQVGNETEAI ALKRKLTEPL QQAVQSFGFP AVQLDAEVKE SKQAFEKFVE
     QRKQEDHSKV VEAILEKKKL EQQVEKKMKE EKLTIGYPIK DEPVPLETIV EEERRITVQG
     YIFAAETKEL RSGRTLLTFK ITDYTDSILV KMFSRDKEDI PLLQAVKKGM WVKVRGGVQN
     DTFVRDLVMI ANDVNEVSGK ETKDEAPDDE KRVELHLHTA MSQMDGISSA GAYVTQASKW
     GHKAIAITDH GVVQAFPEAY GASQKHGIKV IYGVEANLVD DGVPIAYNEA HIPLLDSEFV
     VFDVETTGLS AVYNKIIELA AVKVKNGEII DRFERFADPH EPLTNTIIEL TGITDDMLKG
     QPEVEQVLNE FHAFIGDAVL VAHNASFDMG FLNTGFQKMG LGEAKNPVID TLELGRFLYP
     TLKNHRLNTL CKKFDIELVS HHRAIYDAEA TGHLLWRMVK DATERDILYH DQLNDNMGEG
     NFHRQRPSHC ILLAQTQEGL KNLYKLVSMA HVEYFYRTPR IPRSQLQKHR EGILVGSGCD
     KGEVFEGMMQ KTPQEVEEIA KFYDYIEVQP LANYEHLIEK ELVKSREALQ EIVANIVKLG
     EQLGKPVVAT GNAHYLKEED YIYRKILIAS QGGANPLNKQ TLPQVHFRTT SEMLEAFAFL
     GEEKAKEIVV TNTNHIADQI EEIHPIPDKL YTPKIEGADE EIRQMSYNRA RKIYGDPLPE
     IVEARLEKEL KSIIGHGFAV IYLISHKLVK KSLDDGYLVG SRGSVGSSFV ATMTEITEVN
     PLPPHYVCPN CHHSHFFNDG SVGSGYDLPD ENCPKCGTPY VKDGQDIPFE TFLGFKGDKV
     PDIDLNFSGE YQPRAHNYTK ELFGESYVYR AGTIGTVAEK TAYGYVKGYQ SDHDLHFRGA
     EIDRLVTGCT GVKRTTGQHP GGIIVVPDYM DIHDFCPIQF PADDRGAEWK TTHFDFHSIH
     DNLLKLDILG HDDPTVIRML QDLSGIDPKT IPTDDPEVMK IFSGPDVLGV TEEQILCKTG
     TLGIPEFGTR FVRQMLEETK PSTFSELVQI SGLSHGTDVW LNNANELIYN GTCELKDVIG
     CRDDIMVYLI YKGLEPSLAF KIMEFVRKGK GLQPEWIEEM KKHDVPDWYI GSCLKIKYMF
     PKAHAAAYVL MAVRIAYFKV HYPILYYASY FTVRADDFDL DTMVKGSAAI RAKIEEINGK
     GLDASPKEKS LLTVLELALE MVERGFSFQK VDLYRSEATE FLVEGNTLIP PFNALTGVGT
     NAAINIVKAR DEREFLSKED LQQRSKITKT VLENLDAHGC LEGLPESNQL SLF
 
 
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