ID A0A1M6BAL7_9FIRM Unreviewed; 1179 AA.
AC A0A1M6BAL7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=SAMN02746098_04129 {ECO:0000313|EMBL:SHI45791.1};
OS Desulfosporosinus lacus DSM 15449.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1121420 {ECO:0000313|EMBL:SHI45791.1, ECO:0000313|Proteomes:UP000183954};
RN [1] {ECO:0000313|EMBL:SHI45791.1, ECO:0000313|Proteomes:UP000183954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15449 {ECO:0000313|EMBL:SHI45791.1,
RC ECO:0000313|Proteomes:UP000183954};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQXJ01000018; SHI45791.1; -; Genomic_DNA.
DR RefSeq; WP_073031768.1; NZ_FQXJ01000018.1.
DR AlphaFoldDB; A0A1M6BAL7; -.
DR STRING; 1121420.SAMN02746098_04129; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000183954; 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; SSF160975; AF1531-like; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..79
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1179 AA; 133234 MW; 4505FCFF78084530 CRC64;
MTQISQNTCG FVHLHNHTEF SLLDGAARIK NLVQRAVELE MSALAITDHG VMYGVIDFYK
ACKQAGIKPI IGCEVYVAPN KRTDKIQGKD DANYHLVLLA ENEQGYRNLI KLVSMAHIEG
FYYKPRVDKE ILRKHSEGII ALSACLAGEV AEHLVQEQLE MAVQSALEYE EIFGKGNFFL
EIQDHGIEEQ RKVIIGMWKI HERTGIPMVA TNDVHYVKRE DAFVQDALLC IQTGKTLDDT
ARMRFSSQEF FLKSEQEMSL LFGEHPEVLT NTSLIAERCH MDFHFGDNFL PVFEVPPGYT
LDDYLEAECR KAFPHFYPQM TERERERLDY ELHVIFQTGF SGYFLIVADF CRFARDNGVV
VGPGRGSAAA SMVAYLLGIT SVEPLRFDLL FERFLNPERI SMPDIDIDFD PEGRERVIRY
VTQKYGADKV CQIITFGTMG AKAAIRDGGR VLAIPLFRVD KVAKAIPSDL GMTLEKALDV
SPDLARMVEE DEEIKRLYTL AKSLEGMTRH ASTHAAGVVI SKDPLMNYLP LQRTSEDFVM
TQFPMKAVEE IGLLKMDFLG LRNLTILQEA VLRIEETHGL KLDLPTLTLD DPKTYELLAS
GNSTGIFQLE SGGMRAILKD LKPTCFEDII AVVALYRPGP MEQIPEFIRR KRGGNITYLH
PKLEPILKST YGIIVYQEQV MQIARDLGGY SLGRADLLRR AMGKKKKEIM AEERQNFIHG
LQDTDGKWII PGALRIGLTL KDAEEIFDLM AKFAEYGFNK GHATAYAVIS YQTAYLKANY
PLEFMAALLS TVMGSSDKIS FYIQDARTGG IEVLPPDVQY SQVGFSIEEK AIRFGFGAIR
NVGVNVVEKI LDARQDGPFK SLDDFCLRVD QKVLNRRVLE SLIRSGAFGS ICTRAQALAV
IDQVLETTGR RQKDRLSGQF SLFDLDEEMD EGITLPQLPD FKEREILDME KEYLGLYLSG
HPLSSVLPQI KDYISSDILT CLEGEEEKKV ALGGLVTGFR QNVTKKGEMM ASFVLEDLTS
GIEVLVFPRV YAQTNTFAND DVIVVSGRYN IRDDEKKIFA EKITKLEDLK PSGNNKQTRP
AAISEEVPSS ITRSNSSQAV AKRLFLRFSN EESDLMQTVL SILQRFPGSQ PVYFYFEDSQ
KTLEGKRKFW VNDRDELTSA LWEVMDQQNV VWRPAKYFA
//
