ID A0A0P1GTF0_9RHOB Unreviewed; 1170 AA.
AC A0A0P1GTF0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=dnaE1 {ECO:0000313|EMBL:CUH86116.1};
GN ORFNames=PH5382_00022 {ECO:0000313|EMBL:CUH86116.1};
OS Phaeobacter sp. CECT 5382.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1712645 {ECO:0000313|EMBL:CUH86116.1, ECO:0000313|Proteomes:UP000050782};
RN [1] {ECO:0000313|EMBL:CUH86116.1, ECO:0000313|Proteomes:UP000050782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5382 {ECO:0000313|EMBL:CUH86116.1,
RC ECO:0000313|Proteomes:UP000050782};
RG Swine Surveillance;
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; CYSG01000001; CUH86116.1; -; Genomic_DNA.
DR RefSeq; WP_058332323.1; NZ_CYSG01000001.1.
DR AlphaFoldDB; A0A0P1GTF0; -.
DR STRING; 1712645.PH5382_00022; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000050782; Unassembled WGS sequence.
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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd07433; PHP_PolIIIA_DnaE1; 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; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR049821; PolIIIA_DnaE1_PHP.
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 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:CUH86116.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050782};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CUH86116.1}.
FT DOMAIN 8..75
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1170 AA; 129652 MW; 121991BDF0D197BA CRC64;
MTNAPRFIHL RSHTEYSLLE GALRLKKLPD LCKKHDMPAI AVTDSNNLFS ALEFSVSASG
AGVQPIIGCQ VDLRYTEPAP GERPVPPAPL VLLAQSERGY EHLMKLNSCL YLRQGSELPH
VTLEELAEHS EDIICLSGGP DGPVGRLLRQ GQRPAAEELM QSLKQIFADR LYVELQRHPG
EDGQPEAEKL SERGHVEMAY AMDLPLVATN DVYFPNTEMY EAHDAMICIA EGAYVDQSEP
RRRLTAQHYF KSQEEMVALF ADLPEAIENT VEIAKRCAFK AYLRDPILPK FADDEVSELR
RIANEGLQQR LAVIPHAVSV AEYQERLDFE LGIIEGMGFP GYFLIVADFI QWAKDHNIPV
GPGRGSGAGS LVAYALTVTD LDPLRYSLLF ERFLNPERVS MPDFDIDFCM DRREEVIKYV
QEKYGRDKVG QIITFGALLS KAAVRDMGRV LQMPYGQVDR LSKLIPVEGV KPMSIVDSLK
EEPRLQEEAK NEPVVDRLLK YGMQVEGLLR SAGTHAAGVV IGDRPLDALV PLYRDPRSDM
PATQFNMKWV EQAGLVKFDF LGLKTLTVIQ NAVDLIKQSG RDLHTGADGT PLYEPPEGAV
NEINAIPLDD KPTYDLYSSA KTVAVFQVES TGMMDALKRM KPTCIEDIVA LVALYRPGPM
ENIPTYCEVK NGLKKIESVH PLIDHILEET QGIIVYQEQV MQIAQVMAGY SLGGADLLRR
AMGKKIKEAM DAERPKFEKG AAENGVPAKK ASEVFDLLEK FANYGFNKSH AAAYAVVSYQ
TGWLKANHPV EFMAGVMNCD IHLTDKLAVY FEEVKKGLGL PYVPPCVNRS LATFNVVNGE
LVYALGALKN VGLDVMRLVA EARQEDGREH PFVNIFDFAR RVNLKKVGKR PLEMLTRAGA
FDQLDRNRRR IFDSLEGLVN YSAAIHEQKN SNQVSLFGEA GDDLPEPRLT NTPDWLPAER
LSEEFKAIGF YLSGHPLDDY MPALKRKDVM TLDEVMVKAE RGPFMAKMAG VVAGRQERKS
ARGNRFAFAQ LSDTTGGYEV TIFSDVLEKS REFLETGSKV VITAEATMES DQLKLLMRSA
GPVDSAIADA GRSSLRIYLD DAAAVATVAT VLEDAKSAAR NASAGDVFLY LQDPGLPGDV
EMDLGQAFPI NPQIKGAIKS LEGVMEVEEI
//
