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DPO3_THEMA
ID   DPO3_THEMA              Reviewed;        1367 AA.
AC   Q9ZHF6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 154.
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=TM_0576;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9826752; DOI=10.1093/nar/26.23.5300;
RA   Huang Y.P., Ito J.;
RT   "The hyperthermophilic bacterium Thermotoga maritima has two different
RT   classes of family C DNA polymerases: evolutionary implications.";
RL   Nucleic Acids Res. 26:5300-5309(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
CC   -!- FUNCTION: Required for replicative DNA synthesis. This DNA polymerase
CC       also exhibits 3' to 5' exonuclease 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; 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; AF065313; AAC80438.1; -; Genomic_DNA.
DR   EMBL; AE000512; AAD35661.1; -; Genomic_DNA.
DR   PIR; C72360; C72360.
DR   RefSeq; NP_228386.1; NC_000853.1.
DR   RefSeq; WP_004081285.1; NZ_CP011107.1.
DR   PDB; 2P1J; X-ray; 2.50 A; A/B=347-522.
DR   PDBsum; 2P1J; -.
DR   AlphaFoldDB; Q9ZHF6; -.
DR   SMR; Q9ZHF6; -.
DR   STRING; 243274.THEMA_01790; -.
DR   EnsemblBacteria; AAD35661; AAD35661; TM_0576.
DR   KEGG; tma:TM0576; -.
DR   eggNOG; COG2176; Bacteria.
DR   InParanoid; Q9ZHF6; -.
DR   OMA; YYAAYFT; -.
DR   OrthoDB; 561611at2; -.
DR   EvolutionaryTrace; Q9ZHF6; -.
DR   Proteomes; UP000008183; 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; DNA replication; DNA-directed DNA polymerase;
KW   Exonuclease; Hydrolase; Nuclease; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..1367
FT                   /note="DNA polymerase III PolC-type"
FT                   /id="PRO_0000204605"
FT   DOMAIN          358..513
FT                   /note="Exonuclease"
FT   STRAND          358..366
FT                   /evidence="ECO:0007829|PDB:2P1J"
FT   TURN            370..372
FT                   /evidence="ECO:0007829|PDB:2P1J"
FT   STRAND          375..384
FT                   /evidence="ECO:0007829|PDB:2P1J"
FT   STRAND          387..395
FT                   /evidence="ECO:0007829|PDB:2P1J"
FT   HELIX           404..410
FT                   /evidence="ECO:0007829|PDB:2P1J"
FT   HELIX           414..417
FT                   /evidence="ECO:0007829|PDB:2P1J"
FT   HELIX           423..433
FT                   /evidence="ECO:0007829|PDB:2P1J"
FT   STRAND          434..436
FT                   /evidence="ECO:0007829|PDB:2P1J"
FT   STRAND          438..441
FT                   /evidence="ECO:0007829|PDB:2P1J"
FT   HELIX           444..459
FT                   /evidence="ECO:0007829|PDB:2P1J"
FT   STRAND          467..469
FT                   /evidence="ECO:0007829|PDB:2P1J"
FT   HELIX           470..477
FT                   /evidence="ECO:0007829|PDB:2P1J"
FT   HELIX           485..491
FT                   /evidence="ECO:0007829|PDB:2P1J"
FT   HELIX           501..516
FT                   /evidence="ECO:0007829|PDB:2P1J"
SQ   SEQUENCE   1367 AA;  155363 MW;  EE5916FA70591F84 CRC64;
     MKKIENLKWK NVSFKSLEID PDAGVVLVSV EKFSEEIEDL VRLLEKKTRF RVIVNGVQKS
     NGDLRGKILS LLNGNVPYIK DVVFEGNRLI LKVLGDFARD RIASKLRSTK KQLDELLPPG
     TEIMLEVVEP PEDLLKKEVP QPEKREEPKG EELKIEDENH IFGQKPRKIV FTPSKIFEYN
     KKTSVKGKIF KIEKIEGKRT VLLIYLTDGE DSLICKVFND VEKVEGKVSV GDVIVATGDL
     LLENGEPTLY VKGITKLPEA KRMDKSPVKR VELHAHTKFS DQDAITDVNE YVKRAKEWGF
     PAIALTDHGN VQAIPYFYDA AKEAGIKPIF GIEAYLVSDV EPVIRNLSDD STFGDATFVV
     LDFETTGLDP QVDEIIEIGA VKIQGGQIVD EYHTLIKPSR EISRKSSEIT GITQEMLENK
     RSIEEVLPEF LGFLEDSIIV AHNANFDYRF LRLWIKKVMG LDWERPYIDT LALAKSLLKL
     RSYSLDSVVE KLGLGPFRHH RALDDARVTA QVFLRFVEMM KKIGITKLSE MEKLKDTIDY
     TALKPFHCTI LVQNKKGLKN LYKLVSDSYI KYFYGVPRIL KSELIENREG LLVGSACISG
     ELGRAALEGA SDSELEEIAK FYDYIEVMPL DVIAEDEEDL DRERLKEVYR KLYRIAKKLN
     KFVVMTGDVH FLDPEDARGR AALLAPQGNR NFENQPALYL RTTEEMLEKA IEIFEDEEIA
     REVVIENPNR IADMIEEVQP LEKKLHPPII ENADEIVRNL TMKRAYEIYG DPLPEIVQKR
     VEKELNAIIN HGYAVLYLIA QELVQKSMSD GYVVGSRGSV GSSLVANLLG ITEVNPLPPH
     YRCPECKYFE VVEDDRYGAG YDLPNKNCPR CGAPLRKDGH GIPFETFMGF EGDKVPDIDL
     NFSGEYQERA HRFVEELFGK DHVYRAGTIN TIAERSAVGY VRSYEEKTGK KLRKAEMERL
     VSMITGVKRT TGQHPGGLMI IPKDKEVYDF TPIQYPANDR NAGVFTTHFA YETIHDDLVK
     IDALGHDDPT FIKMLKDLTG IDPMTIPMDD PDTLAIFSSV KPLGVDPVEL ESDVGTYGIP
     EFGTEFVRGM LVETRPKSFA ELVRISGLSH GTDVWLNNAR DWINLGYAKL SEVISCRDDI
     MNFLIHKGME PSLAFKIMEN VRKGKGITEE MESEMRRLKV PEWFIESCKR IKYLFPKAHA
     VAYVSMAFRI AYFKVHYPLQ FYAAYFTIKG DQFDPVLVLR GKEAIKRRLR ELKAMPAKDA
     QKKNEVSVLE VALEMILRGF SFLPPDIFKS DAKKFLIEGN SLRIPFNKLP GLGDSVAESI
     IRAREEKPFT SVEDLMKRTK VNKNHIELMK SLGVLGDLPE TEQFTLF
 
 
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