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DPO3A_RICFE
ID   DPO3A_RICFE             Reviewed;        1207 AA.
AC   Q4UK40;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=RF_1244;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
CC   -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC       responsible for most of the replicative synthesis in bacteria. This DNA
CC       polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain
CC       is the DNA polymerase (By similarity). {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   -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, epsilon
CC       and theta chains) that associates with a tau subunit. This core
CC       dimerizes to form the PolIII' complex. PolIII' associates with the
CC       gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC       and with the beta chain to form the complete DNA polymerase III complex
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CP000053; AAY62095.1; -; Genomic_DNA.
DR   RefSeq; WP_011271544.1; NC_007109.1.
DR   AlphaFoldDB; Q4UK40; -.
DR   SMR; Q4UK40; -.
DR   STRING; 315456.RF_1244; -.
DR   EnsemblBacteria; AAY62095; AAY62095; RF_1244.
DR   KEGG; rfe:RF_1244; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_5; -.
DR   OMA; NECRRMG; -.
DR   OrthoDB; 561611at2; -.
DR   Proteomes; UP000008548; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.1600; -; 1.
DR   InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR   InterPro; IPR041931; DNA_pol3_alpha_thumb_dom.
DR   InterPro; IPR040982; DNA_pol3_finger.
DR   InterPro; IPR029460; DNAPol_HHH.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   InterPro; IPR004805; PolC_alpha.
DR   PANTHER; PTHR32294; PTHR32294; 1.
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   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF89550; SSF89550; 1.
DR   TIGRFAMs; TIGR00594; polc; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA replication; DNA-directed DNA polymerase;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..1207
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000280957"
SQ   SEQUENCE   1207 AA;  135675 MW;  061B7DD575BBDD96 CRC64;
     MRPEFIHLRT QSSYSFLESA LTIEKVVELA SSNKMPAICL ADKGNLFGSL EFALYAVKKG
     LQPIHGVILN IKYDIDIFAQ ILLIAKDETG YKNLLKLSSL TFTKNDRKLC DHIDFEDLIE
     YQEGLIALCC YTDGIVGKCL LARSEEQAML FARKLQDILG DRFYFEIMRH DLPEEQFIED
     SYIRIAAELA IPLVATNKVL FSEKTMHDAH DVLLCISAGV TKEYPDRKTV SENCYFRSPH
     EMIELFSDLP SAIQNTVNLR ERCYFAAHAN PPMLPNFATK DISETDLIRK DAKEGLLARL
     ATKFKSENIP LQNQEELKTE YFARLNYELD IICNMNFAGY FLIVSDFIKW SKKEGILVGP
     GRGSGAGSVV AWSLLITDLD PIKFGLLFER FLNPERISMP DFDIDFCQER REEVINYVRS
     KYGNNRVGQI ITFGKMQAKA VIKDVARVLS LPYKFADYLT ELVPFSAVNP VSLEQAMREV
     PELANAAKGN GLYNLEGEAE LIKLVLDTSL ILEGLHRHSS THAAGIVIAG TDLVDIVPVY
     KDANSDMLVV GYSMKYSEIA GLIKFDFLGL QTLTVITDCK KLLKEQGIEV DFNNMTFDDN
     KTYQMLCKGK GVGVFQFESI GMKDALRRLK PDSIHDLIAL GALYRPGPME NIPTYIACKH
     KLQQPDYLHE LLKPILEETY GVVIYQEQVQ RIAQILAGYT LGAADLLRRA MGKKIKKEME
     EQEEIFVKGA IANNISESQA KSIFATVAKF AGYGFNKAHA AAYGVISYQT AYLKANYPAE
     FLVACLNLEL NNHDKINLFL QEAKDSGIKI IAPNINISEG YFSVKSVIPQ AATCHPQGPL
     CHPRVGGYPE KVKTVLNHES MKMDSRFCGN DIKGSRNDIE DTGYDKEKST IIFALGAIKG
     VTPNFGKLVT DERKARGAFK SITDFIERLP LKSINSKLLE NLIKSGCFDE LHDNRLQLFS
     SISKLLAYSA SYHAEQESNQ FSLIKVSSLS PNILIASDYA DNNTLAFYEF ESMGLFISNH
     PLTQYQEIFS RLNILNTADL HNNLPDGTNR VNLAGVIQKK DSRMSARGRF VTLVLSDPEN
     IFELSIFSEE VLKDYVHLLD VKSLVVVNCD IVKDEGGIKL TAKSFSSIED AINNKQFELQ
     LYPQNHEELR QIVTLLAART NNRDQSNAKA TIYLQSEGVK NFVAKITLPE KFFLQGQDFE
     ILKGYSK
 
 
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