ID A0A2T5BUK2_9RHOB Unreviewed; 1166 AA.
AC A0A2T5BUK2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=C8N32_10338 {ECO:0000313|EMBL:PTN03196.1};
OS Rhodovulum imhoffii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=365340 {ECO:0000313|EMBL:PTN03196.1, ECO:0000313|Proteomes:UP000243859};
RN [1] {ECO:0000313|EMBL:PTN03196.1, ECO:0000313|Proteomes:UP000243859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18064 {ECO:0000313|EMBL:PTN03196.1,
RC ECO:0000313|Proteomes:UP000243859};
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 (APR-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:PTN03196.1}.
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DR EMBL; QAAA01000003; PTN03196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5BUK2; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000243859; 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 Reference proteome {ECO:0000313|Proteomes:UP000243859};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1166 AA; 128325 MW; F493314F3D4FE0A6 CRC64;
MTQPRFIHLR LHTEYSLLEG AVRLKKLPAL CEAAAMPAVA VTDTNNLFAA LEFSVLASNS
GIQPIIGCQV DVAYDPPALG ERPRPPAPVV LLAQNEAGYL NLMKLNSHLY VDKNGQLPQV
TLEELETHSA GLICLTGGPD GPVGRLLRAG HPARAKALMK RLAAACPGRL YVELQRHPGE
GGTCPEAETT TERPHIEMAY AMGLPLVATN DVYFPKTDMY VAHDALLCIR DGAYVDQATP
RRRLTPQHYF KTPEEMAALF ADLPEALENT VEIARRCAFK AEKRKPILPR FAADEVEELR
RQAHEGLAAR LAVIPHAAPV EEYEKRLRFE LDIIEGMGFP GYFLIVADFI KWAKDHDIPV
GPGRGSGAGS LVAYALTITD LDPLRYSLLF ERFLNPERVS MPDFDIDFCM DRREEVIGYV
QRKYGREKVA QIITFGALLS KAAVRDVGRV LQMPYGQVDK LSKLIPVEGV KPVSIAKALE
EEPRLREAAR AEEVVERLLT YGQQVEGLLR NASTHAAGVV IGDRPLDELV PLYRDPRSDM
PATQFNMKWV EQAGLVKFDF LGLKTLTVIR NAIEQIHAAG RNLHEGADGT RLYDPAEGAE
NDIGHIPLDD EKTYDLYASA KTVAVFQVES SGMMDALRRM KPTCIEDIVA LVALYRPGPM
ENIPKYCEVK NGLSERDRLH PLIDDILDET QGIIVYQEQV MQIAQKMAGY SLGGADLLRR
AMGKKIKEAM DAERPKFIDG ARKNGVDDAK ALEVWNLLEK FANYGFNKSH AAAYAVVSYQ
TAWLKANHPV EFMAGVMNCD IHLTDKLAVY AEEVRRGLKT GIVPPCVNRS AATFGVEAGR
LVYALGALKN VGVDAMKTIV AARADKPFAT LYDFARRVDM KRVGKRPLEM LARAGAFDEL
DRNRRRVFDS LDVLSAYSAA VHDQRASNQV SLFGEAGADL PEPRLPPVTD WLPNERLAEE
HKAVGFYLSG HPLDDYMPAL RRKKVSTLAE VAEAVKSGPR VTKIAGAVSG RQERKSARGN
RFAFAQLSDP TGLYEVTIFS DVLEASRDLL EAGTNVVLVV EATYESEQIK LLARGVQPID
QEVADAGGAG LRVFVENEPA VAEVAKLLIR TKGESGLRGR GPVYFCLLAP DLPGEVEMAL
PGQFPVTPQI RGAIKSLPGV VAVEEF
//
