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Database: UniProt
Entry: A0A1V4J293_9CLOT
LinkDB: A0A1V4J293_9CLOT
Original site: A0A1V4J293_9CLOT 
ID   A0A1V4J293_9CLOT        Unreviewed;      1192 AA.
AC   A0A1V4J293;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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:OPJ65817.1};
GN   ORFNames=CLCHR_03900 {ECO:0000313|EMBL:OPJ65817.1}, D2A34_04925
GN   {ECO:0000313|EMBL:RII36729.1};
OS   Clostridium chromiireducens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=225345 {ECO:0000313|EMBL:OPJ65817.1, ECO:0000313|Proteomes:UP000191056};
RN   [1] {ECO:0000313|EMBL:OPJ65817.1, ECO:0000313|Proteomes:UP000191056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23318 {ECO:0000313|EMBL:OPJ65817.1,
RC   ECO:0000313|Proteomes:UP000191056};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium chromiireducens DSM 23318.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RII36729.1, ECO:0000313|Proteomes:UP000265930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C1 {ECO:0000313|EMBL:RII36729.1,
RC   ECO:0000313|Proteomes:UP000265930};
RA   Xing M., Wei Y., Ang E.L., Zhao H., Zhang Y.;
RT   "Genome of Clostridium chromiireducens C1, DSM12136.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:OPJ65817.1}.
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DR   EMBL; MZGT01000004; OPJ65817.1; -; Genomic_DNA.
DR   EMBL; QXDJ01000001; RII36729.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4J293; -.
DR   STRING; 225345.CLCHR_03900; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000191056; Unassembled WGS sequence.
DR   Proteomes; UP000265930; 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; 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   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:OPJ65817.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191056};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OPJ65817.1}.
FT   DOMAIN          8..75
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1192 AA;  135775 MW;  685543BE9B6161DF CRC64;
     MMEEKQFCHL HLHTEYSLLD GSGKVGKLMK RAKELGMKSI AITDHGVLYG LVDFFKAAKD
     NDIKPILGCE VYVVPKSRHI KQPDKENSTY HLVLLVKDKV GYENLMKIVS VASIEGFYYK
     PRVDYDYLRK HSEGLIALSA CLGGEVQSCH LKGNYEKAKE TALIYKEIFN GDFYLEIQNH
     GMEEQKKVNE ENIKLSKETG IPLVATNDVH YISKEDSKSH DILMCIQTAK TIDDPHRRRY
     PSDQFYLKSA EEMWDMFSYV PEAIENTIKI TEQCNYEYKF HESKLPKFPL EEGQDPFEYL
     RDTCYKGLIE RYDVFEQLRD SDLDYNKINE IILKREEAKE YIDRLEYELE VIGQMGYVDY
     FLIVWDFIRF SYESGIPTGP GRGSAAGSIV AYTLGITKID PIKYSLIFER FLNPERVSMP
     DIDSDFCYER RQEVIDYVVD KYGADNVSQI ITFGTMAARL CIRDVGRAMN YSYAEVDRIA
     KMIPTMLGIT IEKALDLNPE LKLAYDSDER VKALIDVSKD LEGLPRHSST HAAGVVIASR
     PLVEYVPLQK NDEMIVTQFG MNTLEELGLL KMDFLGLRTL TVMNDAVKMI KENRGIDVDL
     DKIDFEDEEV YKMIGDGNTA GVFQLESPGM TSFMKELKPD SFEDIIAGIS LYRPGPMAEI
     PRYIEGKRNP EKATYLTKEL EPILKVTYGC LVYQEQVMQA VRDLAGYSMG RSDMVRRAMS
     KKKHKVMEEE RKNFIHGIVE NGEVVVPGCV RNGISEEVAN KIFDSMMDFA SYAFNKSHAA
     AYAVVGYQTA YLMKYYPVEM IAAMLNSIMG ISEKVAYYIG IAEDLGIQVL PPNINESFSR
     FTVKGNKIRF GLAAIKNVGA NVVDSIAKAR EEKGKFESLV DFINKMDPSS INKRAVECLI
     KAGALDDFKV FRSKMLAVHE KLIDNISSDK KRNIDGQISL FASEELKNPE VNYPNIKEFN
     KRNLLAMEKE MTGLYITGHP LDDYAQSLKM QTTNEISKIF LVQETLDDAL ESDIGEVNIF
     NRQDTLQDND RVILGGILAS VNQKVTRNNS IMAFLKLEDL TGTIEVIVFP KTLDKVKELC
     VTDSLVIVKG RLSLKEDEPP KLICESIEPL EKINSSKVYL RVEDTIAAKE LNKKLKELLV
     KEYIGDTPIY IFANKEKQKF RVPRDRWISL ESDAISLLKD NLGEENIKIQ DA
//
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