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DPO3_STAS1
ID   DPO3_STAS1              Reviewed;        1438 AA.
AC   Q49X49;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 122.
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=SSP1504;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE18649.1; -; Genomic_DNA.
DR   RefSeq; WP_011303258.1; NZ_MTGA01000034.1.
DR   AlphaFoldDB; Q49X49; -.
DR   SMR; Q49X49; -.
DR   STRING; 342451.SSP1504; -.
DR   EnsemblBacteria; BAE18649; BAE18649; SSP1504.
DR   KEGG; ssp:SSP1504; -.
DR   PATRIC; fig|342451.11.peg.1506; -.
DR   eggNOG; COG2176; Bacteria.
DR   HOGENOM; CLU_003297_2_0_9; -.
DR   OMA; YYAAYFT; -.
DR   OrthoDB; 561611at2; -.
DR   Proteomes; UP000006371; 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; -; 1.
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; 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..1438
FT                   /note="DNA polymerase III PolC-type"
FT                   /id="PRO_1000048482"
FT   DOMAIN          422..578
FT                   /note="Exonuclease"
SQ   SEQUENCE   1438 AA;  162441 MW;  7CD4F6D814A2510C CRC64;
     MAMTNEEKFK ILADQIKITE HLDSEILENS ELTRVDVKTS DRTWVFQITF PHFLTIENYL
     LFTGAIIEEF KTIADVKCNF TVKDKTNQDE FAIKYFSHCI DQTKLSPKVK GQLKQKRLIM
     SGDVLKVMCQ NDVERDHFDK ACNGSLIAAY QQCGFNISKV VFETDSAVND GDLASLEAHI
     QEEDEKSARE ATEKLEKMKA EKAKQQDNNE SDVSKCQIGK PIQVENVRQI DSIIEEEFKA
     AVEGVIFDIN LKELKSGRHI VELKVTDYTD SLVLKMFTRK NKDDLAHFKA LSVGKWVRAQ
     GRIEEDTFVR DLVMMMSDIE EIKKATKQDK AEDKRVEFHL HTSMSQMDGI PNISDYVDQA
     AKWGHKAIAV TDHNVVQAFP DAHSAAEKNG IKMIYGMEGM LVDDGVPIAY KPKDCDLKTA
     TYVVFDVETT GLSNQYDKII ELAAVKVKDG EIIDKFERFS NPHERLSETI KNLTHISDDM
     LVDAPEIEEV LTEFKSWVGD AIFVAHNASF DMGFIDTGYE HVGIGASTNG VIDTLELSRT
     INTEYGKHGL NFLAKKYGVE LTQHHRAIYD TEATAYMFIK MLKQLEALGV HNHQDINTSL
     SNEDAYKRAR PNHVTLIVQN QDGLKNLFKI VSASLVQYYY RTPRIPRSLL DEYREGILVG
     SACDEGEVFT AVMQKDQSQV ERIAKYYDFI EVQPPALYQD LIDRELVRDN ETLHEIYNRL
     IRAGDVNNIP VIATGNAHYL NEHDAIARKI LIAAQPGNPL NRSTLPKAHF RTTDEMLDEL
     HFLGEEKAYE LVVQNTNDLA DKIERVVPIK DELFTPRMEG ANEEIREMSY DNAKALYGDD
     LPQIVIDRLE KELESIIGNG FSVIYLISQR LVKKSLNDGY LVGSRGSVGS SFVATMTEIT
     EVNPLPPHYI CPECKQSEFF DDGSVGSGFD LPDKKCESCG CDLIKEGQDI PFETFLGFKG
     DKVPDIDLNF SGEYQPEAHN YTKELFGEDK VFRAGTIGTV AEKTAFGFVK GYLNDQGIHK
     RGAEIDRLVK GCTGVKRTTG QHPGGIIVVP DYMDIYDFTP VQFPADDQGS SWMTTHFDFH
     SIHDNVLKLD ILGHDDPTMI RMLQDLSGID PKTIPVDDKE TMGIFSSPEP LGVTSDEILC
     KTGTFGVPEF GTGFVRQMLE DTKPTTFSEL VRISGLSHGT DVWLGNAQDL IRSGKCDLAS
     VICCRDDIMV YLMYNGLEPS LAFKTMEFVR KGKGLTDDMV EAMVDNEVPD WYLDSCRKIK
     YMFPKAHAAA YVLMAVRIAY FKVHYPLYYY ASYFTVRASD FDLISMIKDK ESIRNTVNDM
     YSRYMDLAKK EKDTLTVLEI MNEMAQRGYR MQPISLEKSK AFEFIIEGDT LIPPFIAVPG
     LGENVAQRIV EARDEGPFLS KEDLNKKAGL SQKVIEYLDE LGSLPNLPDK AQLSIFDM
 
 
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