ID E4KY45_9FIRM Unreviewed; 1141 AA.
AC E4KY45;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=HMPREF9286_1454 {ECO:0000313|EMBL:EFR33164.1};
OS Peptoniphilus harei ACS-146-V-Sch2b.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=908338 {ECO:0000313|EMBL:EFR33164.1, ECO:0000313|Proteomes:UP000003705};
RN [1] {ECO:0000313|EMBL:EFR33164.1, ECO:0000313|Proteomes:UP000003705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-146-V-Sch2b {ECO:0000313|EMBL:EFR33164.1,
RC ECO:0000313|Proteomes:UP000003705};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (OCT-2010) 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:EFR33164.1}.
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DR EMBL; AENP01000012; EFR33164.1; -; Genomic_DNA.
DR RefSeq; WP_005956070.1; NZ_AENP01000012.1.
DR AlphaFoldDB; E4KY45; -.
DR eggNOG; COG0587; Bacteria.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000003705; 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:EFR33164.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003705};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFR33164.1}.
FT DOMAIN 5..72
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1141 AA; 130714 MW; B48C7E8BEC35C617 CRC64;
MNNFVHLHLH SEYSLLDGST RISLLPQRVK DLGMDAVALT DHGNMYGAIA FYKACKDAGV
KPILGCEVYI SEKDMTVKDR TNKRYHLILL AENNEGFKNI MKIVSTGYVD GYYYKPRVDK
EVLKKYSKGV IATSACLGGE VQKALLNRDK EAAKKAALEY RDIFGEGNFF LELQDHGMPE
QARVNRELVL LSEELDLPLT ASNDVHYLMK EDSKSHDVLL CIQTGKTVND TDRMKFPSDE
FYLKSPDEMA ALFPENPEAL ENTVKIAERC NVEIKFHDLH LPEFIVPDGY SHEEYLKKLA
LEGMIKRYEN VTDEIKERFE FEFNTIKNMG YVDYFLIVWD FIRYARKHEI QVGPGRGSAA
GSMVSYCLGI TDVDPLEFDL LFERFLNPER VSMPDIDIDF CYERREEVID YVNRKYGDSH
VAQIVTFGTM AARNAIRDVG RALDMSYAKV DYIAKQVPQA LNMTIEKALE VSETFKGIYD
GEEDSRLLID MALKLEGLPR HTSTHAAGVV ISKDELTEYV PLTRNDKIIA TQFNMIELEE
LGLLKMDFLG LRTLTVIRDA INLIKENQGK TINFDNFNYN DPEVLKMFAK SETLGVFQFE
SSGMRAFLKE LKPDEFSDLV AANALFRPGP MKQIPKFVGS KHDKSTISYI HPKLEPILKS
TYGCIVYQEQ VMQIVQQIGG YSLGRADIVR RAISKKKMKV MEEERKNFIY GNKEEGVCGA
IANGVDEKSA NEIYDLIIDF ADYAFNKSHS VAYSVVAYRT AWLKYYYPRE FMAAQISTYT
NDIKQVSLYI EEIKRLGIEI LPPNINYSYK NFTVEDNKIR FGLKAVKNVG DNLIDVIVRT
RDKGPYKSLK DFVDRINALD KSALNKRAVE SLIRCGAMDD FRGNRAQYLA IYEGILSSSS
NTAKNNVMGQ FSLFEEADLQ EDLPRLRDFP QKDKLDMEKE VIGMYISGHP LDPYRELIEK
NSSINTNQIF EKYRENLLRR SKVKVGGILK SKKTMITKTN KMMAFAALED LFGTIELVIF
PNVYSRYKDL IEDENVVVVE GHFQESEIEE PKILVDSISR LKMPTKNKLY ISVDSMKNES
VNEIRKILKD YEGSTPVVFF EEETRRAFGT DSSLWIDNKS FDEIQNKLIA YTKSRDKIIL
K
//
