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DPO3A_RICCN
ID   DPO3A_RICCN             Reviewed;        1181 AA.
AC   Q92GB2;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=RC1211;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL03749.1; -; Genomic_DNA.
DR   PIR; C97851; C97851.
DR   RefSeq; WP_010977776.1; NC_003103.1.
DR   AlphaFoldDB; Q92GB2; -.
DR   SMR; Q92GB2; -.
DR   EnsemblBacteria; AAL03749; AAL03749; RC1211.
DR   KEGG; rco:RC1211; -.
DR   PATRIC; fig|272944.4.peg.1388; -.
DR   HOGENOM; CLU_001600_0_0_5; -.
DR   OMA; NECRRMG; -.
DR   Proteomes; UP000000816; 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..1181
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000280956"
SQ   SEQUENCE   1181 AA;  132594 MW;  6368457F2ED3A1DC CRC64;
     MRPEFIHLRT QSSYSFLESA LTIEKVVELA SSNKMPAICL ADKGNLFGSL EFALCAVKKG
     LQPIHGVILN IKYDIDIFAQ ILLIAKDETG YKNLLKLSSL TFTKNDRKIC DHIDFEDLIE
     YQEGLIGLCC YTDGIVGKCL LARNEEQAML FARKLQEILG DRFYFEIMRH ELPEEQFIED
     SYIRIAAELA IPLVATNKVL FSEKSMHDAH DVLLCISAGV TKEYLDRKTV SENCYFKSPH
     EMIELFSDLP SAIQNTVNLR ERCYFAAHAN PPMLPNFATE NISETDLIKK DAKEGLLARL
     ATKFKSENIA LENQEALKTE YFARLNYELD IICNMNFAGY FLIVSDFIKW SKKEGILVGP
     GRGSGAGSVV AWSLLITDLD PIKFGLLFER FLNPERISMP DFDIDFCQER REEVINYVRS
     KYGNNRVGQI ITFGKMQAKA VIKDVARVLS LPYKFADYLT ELVPFSAVNP VSLEQAMREV
     PELANAAKGN GLYNLDGEAE LIKLVIDTSL ILEGLHRHSS THAAGIVIAG TDLVDIVPVY
     KDANSDMLIV GYSMKYSEIA GLIKFDFLGL QTLTVITDCK KLLKEQGIEV DFNNMTFDDN
     KTYQMLCKGK GVGVFQFESI GMKDALRRLK PDSIHDLIAL GALYRPGPME NIPTYIACKH
     KLQQPDYLHE LLQPILEETY GVVIYQEQVQ RIAQVLAGYT LGAADLLRRA MGKKIKKEME
     EQEEIFVKGA IANNISESQA KSIFATVAKF AGYGFNKAHA ASYGVISYQT AYLKANYPAA
     FLVACLNLEL NNHDKINLFL QEAKDNGIKI IAPNINISEG YFSVKFSDTV IPHSVKPVIP
     RLDRGIQKIS KDTVVKPRCD IAGAIIFALG AIKGVTPNFG KLVTDERKAR GAFKSITDFI
     ERLPPKSINS KLLENLIKSG CFDELHDNRL QLLSSIPKLL SYSTAYHEEQ ESNQFSLIKV
     SSLSPTILVS SDYADKNTLA FYEFEAMGLF ISNHPLTEYQ EIFSRLNILN TADLHNNLPD
     GTNRVNLAGV IQKKDSRMSA RGRFVTLVLS DPENIFELSI FSEEVLKDYV HLLDVKSLVV
     VNCDIVKDEG GIKLTAKSFS SIEDAINNKQ FELQFYPQNH EELRQIVTLL AARINNEDQS
     NAKATIYLQS ADVKNFVAKI TLPEKFLLQG QDFEILKGYS K
 
 
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