DPO3A_DEIRA
ID DPO3A_DEIRA Reviewed; 1335 AA.
AC Q9RX08;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=DNA polymerase III subunit alpha;
DE Short=Pol III catalytic subunit;
DE EC=2.7.7.7;
GN Name=dnaE; OrderedLocusNames=DR_0507;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-1035.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=19303848; DOI=10.1016/j.cell.2009.01.018;
RA Slade D., Lindner A.B., Paul G., Radman M.;
RT "Recombination and replication in DNA repair of heavily irradiated
RT Deinococcus radiodurans.";
RL Cell 136:1044-1055(2009).
CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC responsible for most of the replicative DNA synthesis in bacteria as
CC well as the bulk of DNA synthesis/repair after ionizing radiation (IR)
CC (PubMed:19303848). The alpha chain is the catalytic subunit
CC (PubMed:19303848). Following severe irradiation (7 kGy of gamma
CC irradiation) genomic DNA is fragmented. DNA is progressively degraded
CC for the first 1.5 hours after IR, in a step promoted by RecA and
CC counterbalanced by DNA Pol I and Pol III, followed by massive DNA
CC synthesis and genome reassembly in the next hour. Optimal priming of
CC DNA synthesis requires both RecA and RadA, Pol III initiates DNA
CC synthesis while both Pol I and Pol III are required for its contination
CC (PubMed:19303848). This DNA polymerase also exhibits 3' to 5'
CC exonuclease activity (By similarity). {ECO:0000250|UniProtKB:P10443,
CC ECO:0000269|PubMed:19303848}.
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 -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
CC {ECO:0000305|PubMed:19303848}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC subfamily. {ECO:0000305}.
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DR EMBL; AE000513; AAF10085.1; -; Genomic_DNA.
DR PIR; H75511; H75511.
DR RefSeq; NP_294230.1; NC_001263.1.
DR RefSeq; WP_010887152.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RX08; -.
DR SMR; Q9RX08; -.
DR STRING; 243230.DR_0507; -.
DR EnsemblBacteria; AAF10085; AAF10085; DR_0507.
DR KEGG; dra:DR_0507; -.
DR PATRIC; fig|243230.17.peg.684; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_0; -.
DR InParanoid; Q9RX08; -.
DR OMA; NECRRMG; -.
DR OrthoDB; 561611at2; -.
DR Proteomes; UP000002524; Chromosome I.
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:0006281; P:DNA repair; 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 1: Evidence at protein level;
KW Cytoplasm; DNA damage; DNA repair; DNA replication;
KW DNA-directed DNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..1335
FT /note="DNA polymerase III subunit alpha"
FT /id="PRO_0000103320"
FT REGION 442..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1035
FT /note="S->P: Temperature sensitive, viability decreases
FT 10(5)-fold at 37 degrees Celsius; cells recover at 30
FT degrees more slowly than wild-type from heat shock; at 37
FT degrees cells swell and accumulate aberrant nucleoids. DNA
FT synthesis stops immediately on temperature upshift; if
FT combined with a polA deletion viability at 37 degrees
FT decreases further. Greater than wild-type levels of DNA
FT degradation post-IR."
FT /evidence="ECO:0000269|PubMed:19303848"
SQ SEQUENCE 1335 AA; 149277 MW; 79885052416D3458 CRC64;
MTVSDAPTPH IHLPDGSCCQ PKKFAHLHQH TQYSLLDGAA KLKDLLKWAK EVTPEGQTPA
LAMTDHGNMH GAVHFYNYAM GMEVKPIIGY EAYVVPGFGT RRDRSRAQDG EKGIFHLTLL
ARDFEGYQNL CRLSSRGYTE GYYYKPRIDH ELLQEHHKGI IAFSGCLGSE VQQLLMQGRE
DDARARLLWY RELFGDNYFI EIQDHGLPEQ KKNNPILKAW AQELGIGMVA TNDGHYVKKS
DATAHETLLA IQTKATLADE NRFKFPCDEF YVKNLEEMQR ALPVSEWGEE PFDNTAHIAE
LCNVELPVGK KRQYQMPQLP IPEGRSMAEE LRVQTYAGAV KRYPAHLTEG LLRDYAARSL
AELGEADAAR VLKRTGGCDS ASCDLDTLYT LLAFLGSEWE ARGKEAGEKY TPYPALEKME
QDGESGTLPA YAHADCRAAR RQDSDTSIEL DPDTDDEETT RSHHRYALKL LRRAEYELSV
INNMGFPDYF LIVADYINWA KDHDISVGPG RGSGAGSLVA YAIRITNLDP LEFELLFERF
LNPDRISMPD FDIDFNDARR TEVIGYVQEK YGTDKVAQIA TFGTMASKAC LKDVARVMGL
EYAKVDKVSK LIPIKFGKSY SLEQAREAVP DIQQMLAEDA QLLEAYEFAQ KLEGLTRHAS
VHAAGVVIGR EELTNLVPVM RDTSGEGQVC QYDMKSVEDI GLIKMDFLGL RTLSFLDEAK
RILRESGTDF EEKYGDFDHI PFDDEKTYEL MSRGDTKGVF QLEGAGIADA SRRLKPRRLA
DIIALSALYR PGPMENIPTY VRRHHGIEEV DYDKDGFPNS KQWLEKILQE TYGIPVYQEQ
IMQIASEVAG YSLGGADLLR RAMGKKDAEE MKRQRQLFVV GAKEKGVPED EGNKLFDMLD
AFANYGFNKS HSAAYGVITY QTAWLKANYP VQFMAALLTV ERRDSDKVAE YVSDARKMDL
HVLPPDINRS SSDFAVAGEE ILFGLYAIKG LGESAVLRIL EEREKAGAFK SLADFCSRLG
NKVCNRKALE SLIKSGAFDA FGERHQLIES LEDALEDAAG TAEINARAQS GMSMMFGMEE
VKKERPLRSS IAPYSDLERL AIEKEALGLY ISGHPLEQHE GLREAASCRV SDLDAWFALQ
NVAPGKRQKA VLAGMIEGVV KKPTKSGGMM ARFILADESG QMELVAFSRA YDRIEPKLVN
DTPALVIVEL EAEDGGLRAI AEEIVSIEQL SEVPKVMYVT IDLETASPDA LGDFQSVLDE
YAGSMPTYLR LETPEQFVVY QLDHGMGSPE AIRALNQTFA WADAHLAYDQ QTILGRFAPK
PPAWMNRQQG GGMRA
