DPO3A_RICPR
ID DPO3A_RICPR Reviewed; 1182 AA.
AC O05974;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=DNA polymerase III subunit alpha;
DE EC=2.7.7.7;
GN Name=dnaE; OrderedLocusNames=RP778;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-780.
RC STRAIN=Madrid E;
RX PubMed=9274032; DOI=10.1099/00221287-143-8-2783;
RA Andersson J.O., Andersson S.G.E.;
RT "Genomic rearrangements during evolution of the obligate intracellular
RT parasite Rickettsia prowazekii as inferred from an analysis of 52015 bp
RT nucleotide sequence.";
RL Microbiology 143:2783-2795(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 822-1182.
RC STRAIN=B, and Madrid E;
RX PubMed=10486973; DOI=10.1093/oxfordjournals.molbev.a026208;
RA Andersson J.O., Andersson S.G.E.;
RT "Genome degradation is an ongoing process in Rickettsia.";
RL Mol. Biol. Evol. 16:1178-1191(1999).
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; AJ235273; CAA15204.1; -; Genomic_DNA.
DR EMBL; Y11785; CAA72479.1; -; Genomic_DNA.
DR EMBL; AJ238755; CAB56087.1; -; Genomic_DNA.
DR EMBL; AJ238756; CAB56091.1; -; Genomic_DNA.
DR PIR; D71638; D71638.
DR RefSeq; NP_221128.1; NC_000963.1.
DR RefSeq; WP_004599648.1; NC_000963.1.
DR AlphaFoldDB; O05974; -.
DR SMR; O05974; -.
DR STRING; 272947.RP778; -.
DR EnsemblBacteria; CAA15204; CAA15204; CAA15204.
DR GeneID; 57569901; -.
DR KEGG; rpr:RP778; -.
DR PATRIC; fig|272947.5.peg.814; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_5; -.
DR OMA; NECRRMG; -.
DR Proteomes; UP000002480; 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; Reference proteome; Transferase.
FT CHAIN 1..1182
FT /note="DNA polymerase III subunit alpha"
FT /id="PRO_0000103336"
FT CONFLICT 376
FT /note="I -> V (in Ref. 2; CAA72479)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1182 AA; 133463 MW; 0FE9B56969C2E52A CRC64;
MQPEFIHLRT QSSYSFLESA LTIEKVVELA LLHKMPALCL SDRGNLFGSL EFSLYAVKKK
LQPIHGVILN IQYDINAFAQ ILLIAKDETG YKNLLKLSSL TFTKNDRKIC EHIGFEDLIK
YQEGVIALCC YTDGIVGKCL LARKQEQAIL FARRLQAILG DRFYFEIMRH DLPEEQFIEN
SYIQIASELS IPIVATNKVL FSEKSMHYAH DVLLCISEGV TKEYPDRKTV SENCYFKSPA
EMRKLFSDLP NAIQNTINLR ERCYFAAHPN PPMLPNFSTQ DISETYLIRK YATEGLLARL
VTKFKAENIS LEHQEKLKTE YFTRLNYELD IICNMNFAGY FLIVSDFIKW SKKQGILVGP
GRGSGAGSVV AWSLLITDLD PIKFGLLFER FLNPERISMP DFDIDFCQER REEVINYVRS
KYGPNRVGQI ITFGKMQAKA VIKDVARVLS LPYKLADYLT ELVPFSAINP VSLEQAIREV
PELANAAKGN GLYNLEGDAE LIKLVLDTSL ILEGLHRHSS THAAGIVIAG TDLVDIVPVY
KDANADMLIV GYSMKYSEIA GLIKFDFLGL QTLTVITNCK KLLKEQGIKI DFDDMTFDDK
KTYQMLCKGK GVGVFQFESI GMKDALRRLK PDSIHDLIAL GALYRPGPME NIPTYIACKH
KLQQPDYLHK LLEPILEETY GVVIYQEQVQ RIAQVLAGYT LGAADLLRRA MGKKIKKEME
EQEEIFVKGA IANNISPSQA KSIFSTVAKF AGYGFNKAHA AAYGVISYQT AYLKANYPAE
FLVACLNLEL NNHDKINLFL QEAKDNGIKI IAPNINISEG YFSVKSSNTV ITHSTKSVIS
RLNCDIKKIA KDTAVKPLYC KDESTIIFAL GAIKGVTANF GKLVTDERKA RGAFKSITDF
IERLPPKSIN SKLLENLIKA GCFDELHDNR LQLFLSIPKL IAYSTSYHQE QESNQFSLIK
VSSLSPTILV SSDYADKNTL AFYEFEAMGL FLSNHPLTEY QGIFSRLNIL NTRDLYNKLP
NGTNRVTLAG VIQKKDSRMS ARGRFVTLVL SDPENIFELT IFSEEVLKDY VHLLDVKSLV
VVNCDVVKDE GGIKLTAKSF LSIEDVMNNR QFELQLYPQN YAELEQIITL LASRTSNGYQ
SNAKATIYLQ SKDVKHFIAK ITLSETFFLQ VQDFEVLNQY IR
