ID A0A1T5DTZ2_9BACI Unreviewed; 1027 AA.
AC A0A1T5DTZ2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=SAMN06295926_10742 {ECO:0000313|EMBL:SKB74853.1};
OS Lysinibacillus sp. AC-3.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1680467 {ECO:0000313|EMBL:SKB74853.1, ECO:0000313|Proteomes:UP000190941};
RN [1] {ECO:0000313|EMBL:SKB74853.1, ECO:0000313|Proteomes:UP000190941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC-3 {ECO:0000313|EMBL:SKB74853.1,
RC ECO:0000313|Proteomes:UP000190941};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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 -!- 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}.
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DR EMBL; FUYW01000007; SKB74853.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5DTZ2; -.
DR STRING; 1680467.SAMN06295926_10742; -.
DR Proteomes; UP000190941; 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 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 Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR004013; PHP_dom.
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.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..121
FT /note="PHP"
FT /evidence="ECO:0000259|Pfam:PF02811"
FT DOMAIN 272..529
FT /note="Bacterial DNA polymerase III alpha subunit NTPase"
FT /evidence="ECO:0000259|Pfam:PF07733"
FT DOMAIN 532..695
FT /note="DNA polymerase III alpha subunit finger"
FT /evidence="ECO:0000259|Pfam:PF17657"
FT DOMAIN 768..856
FT /note="DNA polymerase helix-hairpin-helix motif"
FT /evidence="ECO:0000259|Pfam:PF14579"
FT DOMAIN 952..1020
FT /note="OB"
FT /evidence="ECO:0000259|Pfam:PF01336"
SQ SEQUENCE 1027 AA; 115774 MW; D903E2FBE7B47B5A CRC64;
MTHVYTKMHT SADLLQSTIR LEQLIPFLQE QNTQACAIVN SKLYGLLPFC KALQQANIHA
VLGLSINVQW QDRKVPIVLY AQTQEGYQHL LKISSAVSIR EDNTLPWKWL EGYAAGCVAL
LSSDDLVETE DWTEVASALN KVFGKHLFMG IARPAGMKAE KEETFVTWCE TMNITLVASQ
SCYFLRPEDH FAFEVARAID SGEKLTDTMQ SAHLQGYFAP TEEEWRSWFA DHPEWLASSA
TMLASCTAEI PEMHVQMPKF PVPTGETAES LLVKETFAGL AERLKQAEIP KVYQERLQYE
LEIICSMGFA DYFLIVADFM HFAKENRILT GPGRGSSASS LVAYSLSITQ VDPLVYGLLF
ERFLNPERVT LPDIDIDFVD SKRQKVIHYV AQKYGKANVA QIITFGTLSA KAVARDVARV
FGFDAETLEK ISKMIPNKPG ITLQKAVAES QGLQGWLAED EKHRRWLEVA LKLEGVPRNS
STHAAGIVLS PSPLVNTIPI EEGHDGIYCT QWPMGDVEAC GLVKMDFLGL RNLTILEQVR
WSIYKSGGPW IEFELIPMQD EKTFQLLQMG DTLGIFQLES EGMKQALSDI QPTHFLDIVA
VNALYRPGPM DFIPMYARRK AGRESVTMPH PALEPILRET FGVIVYQEQI MQIASVMAGF
TMGQADLLRR AVSKKNRQVL EEQRTAFVDG AMKQGFDVHV AEEVYALIVR FADYGFPKSH
AVAYSVISYQ MAYLKAHFPQ SFYSALLSNA TGNVEKILQL ENEAKEKGIS FYPPSLKQST
KFFTVEKDGI RYSLSGIKGV PYTFIEKVYA LRQAKPEALD NIFDMAVALS AQHFKPKVME
SLIFAGALDY LDKDRAVLIA TLEAALKHAE LLRPTEDIDI ESTTTFSFGK PKYMEAEAMP
QKEKLLREKE SLGFYISAHP VTEERAFWNE VNSTCRELKQ ARDGTYVKML GMIEEVKKIR
TKKGEQMAFV QLQDEFGAIS VTLFPQVFHL VQELLLEDEL LYIEGTLERR FGKPQVKVKH
AQATKRI
//
