DPO3A_SACEN
ID DPO3A_SACEN Reviewed; 1194 AA.
AC P34699; A4FLS4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 2.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=DNA polymerase III subunit alpha;
DE EC=2.7.7.7;
GN Name=dnaE; Synonyms=polC; OrderedLocusNames=SACE_5815;
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Saccharopolyspora.
OX NCBI_TaxID=405948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 931-1194.
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=1732208; DOI=10.1128/jb.174.3.725-735.1992;
RA Andersen J.F., Hutchinson C.R.;
RT "Characterization of Saccharopolyspora erythraea cytochrome P-450 genes and
RT enzymes, including 6-deoxyerythronolide B hydroxylase.";
RL J. Bacteriol. 174:725-735(1992).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM420293; CAM04999.1; -; Genomic_DNA.
DR EMBL; M83110; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A42606; A42606.
DR AlphaFoldDB; P34699; -.
DR SMR; P34699; -.
DR STRING; 405948.SACE_5815; -.
DR EnsemblBacteria; CAM04999; CAM04999; SACE_5815.
DR KEGG; sen:SACE_5815; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_11; -.
DR OMA; KQRFHLC; -.
DR Proteomes; UP000006728; 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 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; 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; 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..1194
FT /note="DNA polymerase III subunit alpha"
FT /id="PRO_0000103337"
FT DNA_BIND 1028..1102
FT /note="OB"
FT CONFLICT 931
FT /note="A -> R (in Ref. 2; M83110)"
FT /evidence="ECO:0000305"
FT CONFLICT 1077
FT /note="V -> L (in Ref. 2; M83110)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1194 AA; 131197 MW; 77A8755083D640B3 CRC64;
MPVDPFVHLH VHTEYSMLDG AAKVGALFAE AQRLEMPAVG MTDHGNMFGA DEFYQQAKKT
GIKPIIGIEA YLAPGSRFHK KPVFWGEAKQ RGTDEYGEGG DVSGAGAYTH MTMLARNATG
LRNLFTLSSR ASMEGQYRKP RMDRELVAEY AEGIIATTGC PSGEVQTRLR LRQFDEAMQA
ASDYKDIFGA ENFFLELMDH GLPIERSVRE GLLKIAKELG LKPVATNDSH YVTADQAESH
GALLCVQSGK TLNDESRFKF DGDGYYLKSA AEMREYWDKE VPGAADNTLL IAERVESYED
VWSFQDRMPR VTDGSGKTER QLLEAEVEQY LPTRYPEGAT QECLDRIKVE LDVLDTKGYC
AYFLVVGDLT RWAKSQGIHV GPGRGSAAGS LLAYILHITN LDPLEHGLIF ERFLNPERDS
PPDIDLDFDD RRRDEVLQYA IDKYGRDKVA QVITFGKIKT KAAIKDSARV HHGQPGFAIA
DKISKALPPP IAAKDIPLSG IVDPQHERYA EAAEVRNLIE TDPSVSQIFD TARGLEGLIR
NAGVHACAVI LSSQPLMGTV PLWARDDGSI ITGWDYPSCE AIGLLKMDFL GLSNLTILGD
ALKMVKANHD REIDLSNLGL DDAKTYELLA RGESLGVFQL EGGGMRELLK RMQPTEFADI
VACNALYRPG PMEVNAHNDY ADRKNGKKPV EPIHPDLDEP LKDILSETYG LIVYQEQIMA
IAQKVAGYSL GRADILRRAM GKKKKEVLDQ EFEGFQAGMR EQGFRDEAID KLWATVLPFA
GYAFNKSHAA GYALVAYWTA YLKANYPAEY MAALLTSNGD NKDKMAVYLA ECRRMGVKVL
SPDVNDSLND FTAVGSDIRF GLSAVRNVGS NVVASIAKVR EDKGRYSSFT DFLDKSETVA
CNKRVIESLI KAGAFDSLGH TRMSLAQHHE AAVDAVIGLK RQQALGQFDL FGGGDDAGGE
ESSSPLAHLQ FTPDEWPRKQ MLSYEREMLG LYVSAHPLDG AERLLAPYQD TGIAELVGGE
REAGKDQVKI AGMISGIQRR INKNGHPWAI VTLEDLDASV EVLFFPKSYE MFADCLVEDT
AIAVKGRINE REGTISIFAS DAVPVDISAA ETDPGTSPAF VIKVPASRVD RSLVAELKRT
LQAHSGTVPV HVKLQGPRGV TRLALSSDYF VSTENGLQGE LKGLLGAGCF ETVL
