ID V6Q5L7_9ENTE Unreviewed; 1108 AA.
AC V6Q5L7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=T233_00411 {ECO:0000313|EMBL:EST90429.1};
OS Vagococcus lutrae LBD1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=1408226 {ECO:0000313|EMBL:EST90429.1, ECO:0000313|Proteomes:UP000018126};
RN [1] {ECO:0000313|EMBL:EST90429.1, ECO:0000313|Proteomes:UP000018126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LBD1 {ECO:0000313|EMBL:EST90429.1,
RC ECO:0000313|Proteomes:UP000018126};
RX PubMed=24371201;
RA Lebreton F., Valentino M.D., Duncan L.B., Zeng Q., Manson McGuire A.,
RA Earl A.M., Gilmore M.S.;
RT "High-Quality Draft Genome Sequence of Vagococcus lutrae Strain LBD1,
RT Isolated from the Largemouth Bass Micropterus salmoides.";
RL Genome Announc. 1:e01087-13(2013).
CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC responsible for most of the replicative synthesis in bacteria. This DNA
CC polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain
CC is the DNA polymerase. {ECO:0000256|ARBA:ARBA00025611}.
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 -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC subfamily. {ECO:0000256|ARBA:ARBA00009496}.
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:EST90429.1}.
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DR EMBL; AYSH01000006; EST90429.1; -; Genomic_DNA.
DR RefSeq; WP_023605756.1; NZ_AYSH01000006.1.
DR AlphaFoldDB; V6Q5L7; -.
DR STRING; 1408226.T233_00411; -.
DR PATRIC; fig|1408226.3.peg.400; -.
DR eggNOG; COG0587; Bacteria.
DR Proteomes; UP000018126; 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 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 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: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; SSF50249; Nucleic acid-binding proteins; 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 Reference proteome {ECO:0000313|Proteomes:UP000018126};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..71
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1108 AA; 126612 MW; C1764E4A3DEE331D CRC64;
MVLASLQTFS AYSLLQSTIE IERYVAQASE KGYQAVALTD INVMHGMLDL KKACEKYEIK
PLYGMTLRYP SGESSSETFD IVLLAKNQHG YQNLMRLSSN IQLSESVSTV YEYMDYFEEM
IVLLPPEGSE ISFLVEKGDT KQAQTWLSQL KKKVPSKDIY GGLALYQSRE SSEALLSFYH
NERLNTVPLP LHRYLLPEHH MAVEVMDSIQ NGNTLQWDEL EKNGPYYLTE GTIFAQTYEQ
LFGKHVLDCL KTIVDECNVT LELHQSLLPH FDVPTTDNAA SYLRKLCYQF LPERVSGDLD
VYEERLEKEL TIIHQMGFDD YFLIVWDVMA FTRREKIVTG AGRGSAAGSL VSYVLGITDV
DPIQYGLLFE RFLNPERHTM PDIDLDIPDN RRDEVLAYVY QRYGANHVAQ IATFGTMAAK
MVLRDVARVF GLSQNEANQW ANAVPNTLKI TLDEAYTQSK ELRDLVTTSG RNQQLYEIAR
VLEGLPRHVS THAAGVVISD KPLTKFVPLM AGSQEIPLTQ FTMHDVEAVG LLKMDFLGLR
NLSILDETMQ HIRYHYRQEI NHHEIPMNDP KTLALFQKGE TVGVFQFESN GIRHVLRQVQ
PTSIEDIAAV NALYRPGPME NIDLFVKRKH GLLPIEYPDD SLKDILDVTY GVMIYQEQVM
QVASKMAGFS LGQADILQRA ISKKIKHTML EQRQAFITGA TRQGYSSKTA ETVYQYIEKF
ANYGFNRSHA MAYSFVGYQM AYFKVHYPAC FYVSLLSSVR NNNQKVILYI QDARKAGVIV
VGPDINESFA RFTLKKNTIR FGFGSLKGIR RDFIQNIVEE RRAHGPFTSL DNFLLRIDNK
WLKEDYILPL IQVGAFDKLH QNRRQLVVDL ESHLKNILIS GGSLDLLEMM TLKKERVADY
DLSEKLAQEE ALVGVYLSGH PVKEYRVLKM MQQCVSISDV EIGKPVRLLG YIKQVRQIKT
KKGEFMAFVT VSDETGEISL TVFPQLYRKE RKLLEENRVI LVQGKVEESR YNQEKQVLAS
EIQAATAFDE KIGKQICYLK IEKDHNEKED LAAIKAITKK HSGITPIIIY VEQSDQKFVL
SDEFWVSDTQ VTKKELSYIL GETNVVFR
//
