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DPO3_THEP1
ID   DPO3_THEP1              Reviewed;        1367 AA.
AC   A5IJJ8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=Tpet_0342;
OS   Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS   RKU-1).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=390874;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermotoga petrophila RKU-1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000702; ABQ46371.1; -; Genomic_DNA.
DR   RefSeq; WP_011943006.1; NC_009486.1.
DR   AlphaFoldDB; A5IJJ8; -.
DR   SMR; A5IJJ8; -.
DR   STRING; 390874.Tpet_0342; -.
DR   PRIDE; A5IJJ8; -.
DR   EnsemblBacteria; ABQ46371; ABQ46371; Tpet_0342.
DR   KEGG; tpt:Tpet_0342; -.
DR   eggNOG; COG2176; Bacteria.
DR   HOGENOM; CLU_003297_2_0_0; -.
DR   OMA; YYAAYFT; -.
DR   Proteomes; UP000006558; 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; 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; PF07733; DNA_pol3_alpha; 1.
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; 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; Transferase.
FT   CHAIN           1..1367
FT                   /note="DNA polymerase III PolC-type"
FT                   /id="PRO_1000048496"
FT   DOMAIN          358..513
FT                   /note="Exonuclease"
SQ   SEQUENCE   1367 AA;  155335 MW;  7D45C70EF71E04B0 CRC64;
     MEKIENLKWK DVTFESIEID PDAGVVLVSV EKFSSEVENL VSLLEKETRF RVIVNGAQKS
     NGDLKGKILS LLNGNVPYIK DVVFEGNRLI LKVLGDFARD RIASKLRSTK KQLDELLPPG
     TEIMFEVVEP PEDLLKKEVP QPEKREEPKG EELKIEDENH IFGQKPRKIV FTPSKIFEYN
     KKTSVKGKVF KIEKIEGKKT VLLIYLTDGE DSLICKVFND VEKVEGKISL GDVIVATGDL
     LLENGEPTLY VKGITKLPEA KRMDNSPVKR VELHAHTKFS DQDAITDVNE YVKRAKEWGF
     PAVALTDHGN VQAIPYFYDA AKEAGIKPIF GIEAYLVSDV EPVIRNLSYD SSFENATFVV
     LDFETTGLDP QVDEIIEIGA VKIQDGQIVD EYHTLIKPSR EISRRSSEIT GITQEMLENK
     RSIEEVLPEF LGFLENSIIV AHNANFDYRF LRLWIKKVMG LDWERPYIDT LALAKSLLKM
     RSYSLDSVVE KLGLGPFRHH RALDDARVTA QVFLRFVEMM KKIGITKLSE IENLKDTIDY
     TALKPFHCTI LVQNKKGLKN LYKLVSDSYI KYFYGVPRIL KSALIENREG LLVGSACISG
     ELGRAALEGA SDSELEEIAK FYDYIEVMPL DVIAEDEEDL DRERLKEVYR RLYRIAKKLN
     KFVVMTGDVH FLDPEDARGR AALLAPQGNR NFENQPALYL RTTEEMLEKA MEIFEDEEIA
     REVVIENPNR IADMIEEVQP LEKKLHPPII ENADEIVRSL TMKRAYEIYG DPLPEIVQKR
     VERELNAIIN HGYAVLYLIA QELVQKSMSD GYVVGSRGSV GSSLVANLLG ITEVNPLPPH
     YRCPECKYFK VVEDDRYGAG YDLPDKKCPV CGAPLRKDGH DIPFETFMGF EGDKVPDIDL
     NFSGEYQERA HRFVEELFGK DHVYRAGTIN TIAEKSAVGY VRSYEEKTGK KLRKAEMERL
     VSMITGVKRT TGQHPGGLMI IPKDKEVYDF TPIQYPANDR NAGVFTTHFA YETIHDDLVK
     IDALGHDDPT FIKMLKDLTG IDPMTIPMDD PDTLAIFSSV KPLGVDPVEL ESDVGTYGIP
     EFGTEFVRGM LVETRPKSFA ELVRISGLSH GTDVWLNNAR DWINLGYAKL SDVISCRDDI
     MNFLIHKGME PSLAFKIMEN VRKGKGITEE MESEMRKLKV PEWFIESCKR IKYLFPKAHA
     VAYVSMAFRI AYFKVHYPLQ FYAAYFTIKG DQFDPVLVLK GKEAIKRRLR ELKAMTGKDV
     QKKNEESVLE VVLEMILRGF SFLPPDIFKS DAKKFLIEGN SLRIPFNKLP GLGDSVAESI
     VRAREEKPFT SVEDLMKRTK VNKNHIELMR SLGVLGSLPE TEQFTLF
 
 
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