ID A0A2T0RRR1_9RHOB Unreviewed; 1153 AA.
AC A0A2T0RRR1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=CLV78_104300 {ECO:0000313|EMBL:PRY23807.1};
OS Aliiruegeria haliotis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Aliiruegeria.
OX NCBI_TaxID=1280846 {ECO:0000313|EMBL:PRY23807.1, ECO:0000313|Proteomes:UP000239480};
RN [1] {ECO:0000313|EMBL:PRY23807.1, ECO:0000313|Proteomes:UP000239480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29328 {ECO:0000313|EMBL:PRY23807.1,
RC ECO:0000313|Proteomes:UP000239480};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PRY23807.1}.
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DR EMBL; PVTD01000004; PRY23807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0RRR1; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000239480; 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; 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; 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 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 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 Reference proteome {ECO:0000313|Proteomes:UP000239480};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..75
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1153 AA; 127761 MW; 28E576E78E46EE8C CRC64;
MSSAPRFIHL RLHTEYSLLE GAIRTKKLPG LCRDMGMPAV AVTDTNNMFA ALEFSVTAAG
AGIQPIMGCQ VDLEYEPVIP GQRQVPPAPI VLLAQDEAGY ENLLKLNSCL YLRGDHQLPH
VTADELEQYS EGVICLSGGP DGALGRMVRA GQEPKALDLL KRLAAAYPNR FYVELQRHPG
EDGLPDAETR TEKFFVETAY ALDLPLVATN DVYFPKPKFY EAHDALICIA EGAYVDQQQE
RRRLTPQHYL KTPDEMAALF ADLPEAIENT VEIAQRCWVV SERRDPILPT FAEDEVEELR
RQAHEGLEKR LAVIPHAASV EEYNDRLEFE LGIIESMGFP GYFLIVADFI KWAKEHDIPV
GPGRGSGAGS LVAYALTITN LDPLRYSLLF ERFLNPERVS MPDFDIDFCM DRREEVIHYV
QEKYGHDKVG QIITFGALLS KAAVRDIGRV LQMPFGQVDR LSKMIPVEGV KPVSIEKALA
TEERLREEAR NEEVVDRLLT YGQQVEGLLR NASTHAAGVV IGDRPLDELV PLYQDPRSDM
PATQFNMKWV EQAGLVKFDF LGLKTLTVIQ NALDLLKQRG VEIDIDHIPL DDKPTYDLYA
AAKTVAVFQV ESSGMMDALR RMKPTCIEDI VALVALYRPG PMENIPTYCE VKNGVKERES
VHPLIDHILE ETQGIIVYQE QVMQIAQVMA GYSLGGADLL RRAMGKKIKE AMDAERPKFE
KGAGENGVDK KKASEVFDLL EKFANYGFNK SHAAAYAVVS YQTAYLKANY PVEFMAGIMN
CDIHLTDKLS VYAEEVRRGL EIEIVPPCIN RSIETFSVKE GKIVYALAAL KNVGHEAMHL
IVEGRGDKAF VTLFDLARRV DLKHVGKRPL EMLARAGAFD VLDRNRQRVL KSLDALVAYS
AAIHEQRNSN QVSLFGEAGE DLPEPKLAQV VDWLPAERLG EEHVAIGFYL SGHPLDDYMG
VLKRKGIQTL AQVEELVKSG AAVVKMAGTV AAKQERKSAR GNRFAFVQLS DPSGLYEVTV
FSETLEKSRE HLEAGQNVVI TAEATYEAEQ LKLLCKGARP IDQEASSGAG GGGGLRLFIN
DSNAVSTVRS ILSRTVEAGQ VRMKGPILLT LMDPALPGEV DLEIGADLPV SPQVRGALKA
VQGVLDVEEL YSR
//
