ID A0A1I4MXI6_9BACI Unreviewed; 1095 AA.
AC A0A1I4MXI6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=SAMN04487943_107178 {ECO:0000313|EMBL:SFM08034.1};
OS Gracilibacillus orientalis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX NCBI_TaxID=334253 {ECO:0000313|EMBL:SFM08034.1, ECO:0000313|Proteomes:UP000198565};
RN [1] {ECO:0000313|EMBL:SFM08034.1, ECO:0000313|Proteomes:UP000198565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.4250 {ECO:0000313|EMBL:SFM08034.1,
RC ECO:0000313|Proteomes:UP000198565};
RA de Groot N.N.;
RL Submitted (OCT-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOTR01000007; SFM08034.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4MXI6; -.
DR STRING; 334253.SAMN04487943_107178; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000198565; 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; 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 5..72
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1095 AA; 126049 MW; 3DF4C0C46441BF59 CRC64;
MSNSSALQIK SGYSLMNSTI QIAPLVNQAK NYGYHHLALT DEGIMHGAIP FYQACKKAGI
NPIIGLSYQV EINERFVEVI ALAKNVTGYQ HLLQISTALQ HDEKVTIKML ENYDESLFTI
LPAEQWPLEQ METTIQQIRT NHQLNNVYLG LSENMVNYRN ILEQLDIPKV ALPDVKYLNK
QEVIAYSCLR AIDQGVKWDK TMVDEIEGTY LKTPDELEIA FQSWPELLSN ADQLAEQCHI
DLPLEQRLLP KYPVPGDMHA DQFLEELCEK SLSEKYPDVT DEVAERLHYE IDVIQSMGFS
DYFLIVWDFV HYAKESQIMV GPGRGSAAGS LVAYLLGITD VDPIKYDLLF ERFLNPDRVT
MPDIDIDFAD EKRDQVIRYV VEKYGTDHVA QIITFGTFAA RSLLRELFKV LDISDNDQNY
ILKSLPKDSN STLAALLRQT SELTEYVKQS EQLKRLFKIA NQLEGLPRHV STHAAGVIIS
DQEMTSHVAT MPSQSNVALT QYPMNDLEKI GLLKIDFLGL RNLTLIEKIL KQMTYHYKKS
ISLETIPFND ENTYRLLQKG ETNGIFQLES QGMQKVLREL RPTNFEDIVA VNALYRPGPM
EFIPTYIERK HRKKEIPHLH PDLASILEKT YGVLVYQEQI MQIVHTMAGF TYGEADIFRR
AVSKKDKTLL MDNKQKFISG SLEKGYNNRT AEEVFDWIVR FSNYGFNRSH AVAYSVIAYQ
LAYLKANYPI AFFIEMLSMH MGNAEKIQIY LREAKNRHIE ILPPSINHSI GKFKAEQAGI
RIGLNIIKGI GFQAVQTILE ARKNQRFKNL FDFCLRVPLQ KINRTIIESL ILAGAFDELH
DNRATLLASL DEAMEQGELF REFDDQIHFF ESDLALDVSY TEIEPYPIMK QLMMEKEVIG
FFVSTHPLAQ VRDKIREYGY ISIQQTQHLK QKKIKMAAVV QSLKVIRTKK GETMAFVTIS
DESGELDTVL FPKIFRQVNH WLEEDSFVFV EGKLEERNEK KQLIVNDIQP YQLEEKQLTN
DSVYIKVEDE KEVSLEKLKE IATKFPGSAT IYLYQENQRQ LFKLSSSYNL DSAWNVVKEL
KQYFGEDNVV LRHSS
//
