ID   B0RIK2_CLASE            Unreviewed;      1170 AA.
AC   B0RIK2;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   02-SEP-2026, entry version 111.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   Name=dnaE {ECO:0000313|EMBL:CAQ01493.1};
GN   OrderedLocusNames=CMS1382 {ECO:0000313|EMBL:CAQ01493.1};
OS   Clavibacter sepedonicus (Clavibacter michiganensis subsp. sepedonicus).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=31964 {ECO:0000313|EMBL:CAQ01493.1, ECO:0000313|Proteomes:UP000001318};
RN   [1] {ECO:0000313|EMBL:CAQ01493.1, ECO:0000313|Proteomes:UP000001318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / ICMP 2535 / C-1
RC   {ECO:0000313|Proteomes:UP000001318};
RX   PubMed=18192393; DOI=10.1128/JB.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT   sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC         diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC         COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC         EC=2.7.7.7; Evidence={ECO:0000256|ARBA:ARBA00049244};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC       subfamily. {ECO:0000256|ARBA:ARBA00009496}.
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; AM849034; CAQ01493.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RIK2; -.
DR   STRING; 31964.CMS1382; -.
DR   KEGG; cms:CMS1382; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_11; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000001318; 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-EC.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   CDD; cd04485; DnaE_OBF; 1.
DR   CDD; cd12113; PHP_PolIIIA_DnaE3; 1.
DR   Gene3D; 1.10.150.870; -; 1.
DR   Gene3D; 1.10.10.1600; Bacterial DNA polymerase III alpha subunit, thumb domain; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 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; IPR004805; DnaE2/DnaE/PolC.
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   NCBIfam; TIGR00594; polc; 1.
DR   NCBIfam; NF004226; PRK05673.1; 1.
DR   PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR32294:SF0; DNA POLYMERASE III SUBUNIT ALPHA; 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; PHP domain-like; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:CAQ01493.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001318};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAQ01493.1}.
SQ   SEQUENCE   1170 AA;  129372 MW;  2546FB44036D2001 CRC64;
     MPRNDSFVHL HVHSEYSMLD GAARVGPLVQ AAAEQGMPAV AITDHGNVFG AFDFWKQAKA
     AGVKPIIGTE AYITPGTHRG DRTRIRWGNG GQDDVSGSGA YTHLTMLAET TEGMHNLFRL
     SSRASLEGYY FKPRMDRELL STYAKGLIAT TGCPSGEVQT RLRLGQYDEA VKAAADFRDI
     FGAENYFCEV MDHGLGIERR IMTDLHRLAK DLGLPLVATN DLHYTHEHDA TSHAALLCVQ
     SGTTLDDPNR FKFDADEFYL KTAQQMRHLF RDHEEACDNT LLIAERCDVQ FNESANYMPR
     YPVPEGESEQ TWFVKEVERG LVRRYPRGFS DDVRKRADYE VGVIAQMGFP GYFLVVADFI
     NWSKENGIRV GPGRGSGAGS MVAYAMGITD LDPLEHGLLF ERFLNPDRVS MPDFDVDFDD
     RRRGEVIRYV TDKYGDERVA QIVTYGTIKA KQALKDSSRV LGYPFSMGDK LTKAMPPAIM
     GKDIPLSGIL DTEHPRYREA GDFREVLAMD PEAQKVFETA QGIENLKRQW GVHAAGVIMS
     SEPLIDIIPI MKREQDGQIV TQFDYPACES LGLIKMDFLG LRNLTIIDDA LNNIESNRGE
     KLVLEDLGLD DQGAYDLLAR GDTLGVFQLD GGPMRSLLRM MKPDNFEDIS AVIALYRPGP
     MGANSHTNYA LRKNGLQEIT PIHPELEEPL REVLGTTHGL IVYQEQVMSV AQKLAGFTLA
     QADLLRRAMG KKKKSELDKQ FEGFSQGMKD NGYSMAAVKA LWDILLPFSD YAFNKAHSAA
     YGVVSYWTAY LKAHYPAEYM AALLTSVGDS KDKMALYLNE CRRMGIKVLP PDVNESIGFF
     AAAGADIRFG LGAVRNVGAN VVEALRGART EQGAFESFDD FLKKVPLPVA NKRTVESLIK
     AGAFDSLGDT RRALLEVHEG MIDASVSDKR AAMNGQVGFD FDSLWDEPQH ARKVPERPEW
     AKRDKLAFER EMLGLYVSDH PLAGLEIPLA KLASTGIAEL LATDASMDGE TVTLAGLLTS
     VQHRTARNSG NQYGMVQLED FGGEITCMFM GKAYQEFAPA LQSDTVVVIR GRVSTRDDGM
     NIHAFSMFQP DLGQSLGSGP LLISLAENRA TTETVMGLND VLIRHSGDTE VRLQLVKGDS
     GRVFEIPYPV TVSADLYGEL KSLLGPNCLG
//