ID A0A0B5F7S3_STRA4 Unreviewed; 1271 AA.
AC A0A0B5F7S3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
DE AltName: Full=Error-prone DNA polymerase {ECO:0000256|ARBA:ARBA00017273};
GN ORFNames=SLNWT_6146 {ECO:0000313|EMBL:AJE86522.1};
OS Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 /
OS NBRC 107858).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1081613 {ECO:0000313|EMBL:AJE86522.1, ECO:0000313|Proteomes:UP000031523};
RN [1] {ECO:0000313|EMBL:AJE86522.1, ECO:0000313|Proteomes:UP000031523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858
RC {ECO:0000313|Proteomes:UP000031523};
RA Lu C.;
RT "Enhanced salinomycin production by adjusting the supply of polyketide
RT extender units in Streptomyce albus DSM 41398.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00024632};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC subfamily. {ECO:0000256|ARBA:ARBA00007391}.
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DR EMBL; CP010519; AJE86522.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B5F7S3; -.
DR KEGG; sals:SLNWT_6146; -.
DR Proteomes; UP000031523; 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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd07431; PHP_PolIIIA; 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 PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR PANTHER; PTHR32294:SF4; ERROR-PRONE DNA POLYMERASE; 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 damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000031523};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..72
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 1105..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1271 AA; 135579 MW; 6B9C29CA1316D527 CRC64;
MPGFTHLHAA SGYSLRYGAS HPERLAARAA ERGMDALALT DRNTLAGAVR FAKACAREGI
RPLFGVELAV AETQRPGRDA SGVRRAPVRG GAFVDESSPR VTFLAREGAL GWASLCRLVS
AAHTAEGEPL LSRAALPAEG LTVLLGPASD VGRALAAGRP DRAARLLAPW RELFGEDLRL
EAVWHGREGT GPGSLRLAAR TVGFAAEQRV RPVLSNDVRY ADPGAGPVAD VLDAARRLVP
VDARGELDSG ERWLKDAGAM RQAAERVVEA AGYRRDTAHR LLEQTRDTAA ACRVDPEDDL
GMGSVRFPEP HLVGAAGRTA QRALASRAAA GMLLRGYDRG PGARGYWERM HHELDIIAHH
GFASYFLTVA QVVDDIRGLG IRVAARGSGA GSLINHLLGI AHADPLAHDL LMERFLSTRR
FVLPDIDIDV ESARRLEAYR AILARFGAER VATVAMPETY RVRHAIRDVG AALSLDPADI
DRIAKAFPHI RARDARSAMR ELPELRPLAE EMRQQGGRRR LWELVEALDA LPRGVAMHPC
GVLLSDASLH ARTPVVPTSG EQLPMSQFDK EDVEDLGLLK LDVLGVRMQS AMAHAVAEVE
RASGERVDLD AVPEGDPLTY RLIRSTETLG CFQIESPGQR DLVGRLQPAD FQDLVVDISL
FRPGPVAADM VRPFIEARHG RAPVRYPHPD LEEPLRETYG VVVFHEQIIR IVDIMTGCGR
GEADRVRRGL SDPESQGRIR VWFAQHATGR GYDAATVART WEIIEAFGSY GFCKAHAVAF
AVPTYQSAWL KAHHPAAFYA GLLTHDPGMY PKRLLLADAR RRGVPVLPLD VNRSAVAHRI
ELVSEEGRFE ERAAGRRAAP RWGIRLALGD VHGIGEAEAA RIERAQPYSS LLDFWERGRP
GKPVAQRLAQ VGALDAFGAN RRDLQLHLSE LHRGARGSYG EQLPLAGGRG TAPAGLPDLG
DAERLSAELG VLGMDASRHL MGDHTEFLTE LGVRSARRLR AARHGETVLV AGAKAATQTP
PIRSGKRVIF TTLDDGTGLV DLAFFDDAHA ACAHTVFHSW LLLVRGVVQR RGPRSLSVVG
EAAWNLADLS ELRATGGLDA VARRLAAEPP GPGPAGSRPA GPGADRARPG AAGPGADRTA
MERAATDRAA TGAGAATAGS GDSDAGDSDA GDGGAGDGRA GDGATGDGEA RGSKTGGSET
GGSETGGIEV GDGEVGNGEV EDGQVGADGT GGRRIRMSTG YEMHPWADLR PAGEGNGPPR
KLWHQSPGSA G
//
