DPO3A_XYLFT
ID DPO3A_XYLFT Reviewed; 1193 AA.
AC Q87EY0;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=DNA polymerase III subunit alpha;
DE EC=2.7.7.7;
GN Name=dnaE; OrderedLocusNames=PD_0165;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
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; AE009442; AAO28059.1; -; Genomic_DNA.
DR RefSeq; WP_004572983.1; NC_004556.1.
DR AlphaFoldDB; Q87EY0; -.
DR SMR; Q87EY0; -.
DR PRIDE; Q87EY0; -.
DR EnsemblBacteria; AAO28059; AAO28059; PD_0165.
DR GeneID; 58015722; -.
DR KEGG; xft:PD_0165; -.
DR HOGENOM; CLU_001600_0_0_6; -.
DR OMA; NECRRMG; -.
DR Proteomes; UP000002516; 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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.1600; -; 1.
DR Gene3D; 2.40.50.140; -; 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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
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 Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF50249; SSF50249; 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..1193
FT /note="DNA polymerase III subunit alpha"
FT /id="PRO_0000103360"
SQ SEQUENCE 1193 AA; 133311 MW; AE3B76C6C861C978 CRC64;
MSTSSFVHLH IHTEFSLADS TIRVPEKPEQ AHPKKAKQAN LLSRAVELGL PALAVTDLNN
LFALIKFYKA AETVGIKPIS GADLLIAEPE HPPWGMTLLC RDHAGYLNLS QLISRGWLEG
HRPEGGVAVH PDWVRDHHKN LFALIGRHSL AGQLLAKGRA DLAEQQLADW QHVFGDGLHL
ELTRTGRDGE EPFNQFALQV AGIRGIPVIA SNDVRFLVQS DFLAHEARVC IASGRMLDDP
KRPRTYSEQQ YLRSSEEMAA LFADIPDALD NTRTLAQRCN IEMRLGTYFL PNYPVPNDET
LDSWIRKQSH EGLEARLLKH PLAPGQTRED YVTRLEFELD TIIKMGFSGY FLIVADFIQW
GKQQGIPIGP GRGSGAGSLV AWALLITDLD PLPYNLLFER FLNPERVSMP DFDIDFCMER
RDEVISYVAR KYGRERVSQI ITYGTMAAKA VVRDVGRVLG FPYGLVDSVA KLIPSTLGIT
LKDAMGEGET NDNASAELIQ RYQAEEDVQE LLNLARQLED LTRNAGKHAG GVVIAPNPLT
EFCPLFAEHD ENGRGKNPVT QFDKNDVEEV GLVKFDFLGL RTLTIIDWAV KAINKRHARA
CIDPVDITAL PLDDIPTYKD VFASGNTSAV FQFESSGMRR LLKDARPDRF EDLIALVSLY
RPGPMDLIPE FTARKHGVQE TIYPDPRTKN ILKDTYGIMV YQEQVMQMAQ IVGGYSLGSA
DLLRRAMGKK VPAEMAKHRE IFREGAAKGG MDAVKADEIF DLMEKFAGYG FNKSHAAAYA
LVSYQTAWLK RHYPAEFMAA TLSSDMDNTD KVVGFLDEAR NLNLKVLRPN INHSAYMFEA
THADTIQYGL GAIKGVGQSV CEAIVKERLH YGPYTSLLDF CTRVTSAKLN RRALEAMIHA
GALDELGKNR ASVMLQLPEV IKATEQMSRE RESGQNSLFG NADPGTPVIQ LDLPECEEWP
LTRMLNGERE TLGLYFSGHP FDPYRKQVKE LVGCDLNTSA LERILGSQQR GNGEKRTWQP
EVNTILAGLV VSVRRKGDSQ VFVQLEDGRG RIECSAFSDA LAEFGHLLTR DRILIVKGGL
REDEFNGGYS LRIRQCWDYA QLCTDYAQRL LLRVDLRTSH AWERIDAILA RYRPGNTPLR
LDLLLNSTHG PVAGTLDLSG GQSVRIEQSL LDKLQKDPAV SKLKVKYTPP WVQ