ID A0A0R1WM94_9LACO Unreviewed; 1085 AA.
AC A0A0R1WM94;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=FC40_GL000715 {ECO:0000313|EMBL:KRM18926.1};
OS Ligilactobacillus hayakitensis DSM 18933 = JCM 14209.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1423755 {ECO:0000313|EMBL:KRM18926.1, ECO:0000313|Proteomes:UP000051054};
RN [1] {ECO:0000313|EMBL:KRM18926.1, ECO:0000313|Proteomes:UP000051054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18933 {ECO:0000313|EMBL:KRM18926.1,
RC ECO:0000313|Proteomes:UP000051054};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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 -!- 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
CC complex. {ECO:0000256|ARBA:ARBA00026073}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRM18926.1}.
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DR EMBL; AZGD01000090; KRM18926.1; -; Genomic_DNA.
DR RefSeq; WP_056938394.1; NZ_AZGD01000090.1.
DR AlphaFoldDB; A0A0R1WM94; -.
DR STRING; 1423755.FC40_GL000715; -.
DR PATRIC; fig|1423755.3.peg.769; -.
DR eggNOG; COG0587; Bacteria.
DR Proteomes; UP000051054; Unassembled WGS sequence.
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 CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd07431; PHP_PolIIIA; 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 NCBIfam; TIGR00594; polc; 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.
PE 4: Predicted;
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:UP000051054};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..70
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1085 AA; 123997 MW; 20D7881C33A7C4C5 CRC64;
MFAPLQVFSS YSLLKSSVRI KEYVKRGQEL GYTDLVLTDI NTMYGAIEFY QECIKRNINP
IIGLTLKYQD FEFVLLAKNY QGYKSLLRIS SNRMIEDDFT LENYHAELND LVIIIKPTIG
MLYASQQLIA TLQNNNAYLG IDPSEELNLY QGIKDKFGST FKNILLTPIN YLNPYDAFAT
KILEYIGIGT KLTSFRDYTK PGKNYLKTLE EYEIQPESEF YSAYQNACNL LNECSLILEF
PPTQLPKYQN GDNLSSEEYL KRLCFEGLNQ RISQTSAEYQ NYVDRLNAEL AVIFNMGFAD
YFLIVWDVTN YAHNHDILIG PGRGSAAGSL VSYCLYITDV DPIKYDLIFE RFLNDQRAQM
PDIDLDIPDL KRDQIIKYLH DKYGHNHVSQ IITFGTLKMK QVLRDVSRVF GLTDAELKNW
NVVLSNIKVD NLKDAFEQSL SLRNLVNDDE KNRIIFEVSS TLEGLPRHYS THAAGILLSD
DDLIDHIPVQ LGSDGILLSQ FAKNEVEQVG LLKMDFLGLK NLTILENALK IIANNYKESV
DISQIDLNDP KTLKLYQEAL TNGVFQFESG GIKNVLKNVH PTSFDDVVAV NALYRPGPQK
NIPVFITRKN NSQSIIYPAP ELEEILKSTY GVMVYQEQVM QVASKMGGFT LGEADLLRRA
MSKKNHELIT GMKLKFIQGA KKKGYSEQVA EKVYSYIAEF GDYGFNKSHA LAYSKMSFEL
AYIKVHYPAA FYISVLNSNL GNTNKIKEFI TEAKHRQISV YGPDINYGRG YFSIWKKGIM
FGLSAIKSLR RDFIKIIFEE RRKNGKFNSL NDFIVRIPQK YIKQEYLEAL IFSGAFDSIA
QDRKKAISQL PGLINNMNLI GKNQELLDIL QPKTNKSNEI IVTDEECLEK ENYYLGMYLS
KHPTEKYANL FNQLNLLNVS QVNDFTDKSK VNLMLRIKSI RIIRTKKGTQ MAFCVGDDYT
DSINLTIFPD VFKKVSSKLS EGNIIILSGQ LDFSRGKTVI VNDCKLAQEY IQKTYYIRLQ
PDVDIPEKKK ILQLLKENPG NCPVIMYDMK TGQNKKLSAK YWVNDNAVLQ ASLNKLLGSQ
NLIVK
//
