ID A0A0K8JHB0_9FIRM Unreviewed; 1129 AA.
AC A0A0K8JHB0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
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:CUH96895.1};
GN ORFNames=P22_3007 {ECO:0000313|EMBL:CUH96895.1};
OS Propionispora sp. 2/2-37.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Propionispora.
OX NCBI_TaxID=1677858 {ECO:0000313|EMBL:CUH96895.1, ECO:0000313|Proteomes:UP000041641};
RN [1] {ECO:0000313|EMBL:CUH96895.1, ECO:0000313|Proteomes:UP000041641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2/2 {ECO:0000313|EMBL:CUH96895.1};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-2015) 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}.
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DR EMBL; CYSP01000014; CUH96895.1; -; Genomic_DNA.
DR RefSeq; WP_054261030.1; NZ_CYSP01000014.1.
DR AlphaFoldDB; A0A0K8JHB0; -.
DR STRING; 1677858.P22_3007; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000041641; 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 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; 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:CUH96895.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000041641};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CUH96895.1}.
FT DOMAIN 4..71
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1129 AA; 127041 MW; 4A76C7636747F214 CRC64;
MDFVHLHTHT EYSLLDGASR ISDLMKRTRE LGMQSIAITD HGSMYGVIDF YKQAGKHGIK
PIIGCEVYTA PRSRWEKTAV EGESYYHLIL LAENNEGYRN LLELVSRAYT EGFYYKPRID
KELLIQYNRG LICLSACIAG EIPSLILRGE LSKATELAQE YRDIFGRDNF FLELQDHGLP
EQKQVNKHLL EMSKQLDIGI VATNDLHYVN KEDAECHDVL LCIQMGKTVD DVGRMRFPNQ
EFYLKSPEEM NGLFADWPEA LLNTCKIAER CQVDFDFNTF HLPEFPVPDQ LSADEYLHSL
CKQELPKRYT TISQEITKRL AYELDVIKRM GYSSYFLIVW DFINYARQNH IPVGPGRGSA
AGSIVAYLLR ITNIDPLQYD LLFERFLNPE RVTMPDIDID FCYVQRSKII DYVSSRYGAD
RVAQIITFGT MAAKAAIRDV GRALNMSYGE VDRIAKLVPN ELGVTLKKAL TMSMELRDAY
QSEPSVRKLV DLAMAVEGLP RHASTHAAGL VIAKEPLTHY VPLQNSAEGF LTTQYDKDCV
EEIGLLKMDL LGLRTLTVIG DCLQLLRDNR KIDIDIDNIP LADKVTCEML ANGDTVGVFQ
MESGGMTNLV KDLKPESFDD LIPLVALYRP GPLGSGMVAD FIDGRHEKKK VTYLHPLLKP
ILQDTFGVIL YQEQVMRIAS ELAGFTLGQA DLLRRAMGKK KHEVLAAQRD NFLRGAERRG
IEQKLAMEIF DLMAHFADYG FNKSHSAAYA LVAYQTAYLK AHYPCEFMAA LLSSVMGTNE
KVGFYIEECR RRGIKICPPD INASQASFNV EGDSIRFGLA GVKNVGENAI NNILTARQQG
GHFTSIVDFC TRVDMRVVNK RVIESLVKCG AFDSIKAKRA QLLEVLDRAV EVAAGRQRDL
ASGQMGLFGE ETLQDVDDLI LPDIAELPID RLLAYEKEMT GFYVTGHPLD KYRDKMKTLV
PIGKISDYPE GKKIKIAGLI TTAKRINTKS GEMMCFFTLE DFTEQIEVVV FPRLFQKSGA
MLAVDMPVAV TGKINRNEDS NKIIADDLMV LDQFGPEVRI TIRKDQENAH IFSQLKAVFN
EFHGSAVVFL HLVDSARVIK TEQQYWITPS TAAIQAIESI LGDNGVSIT
//
