ID A0A238J593_9RHOB Unreviewed; 1148 AA.
AC A0A238J593;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-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 Name=dnaE1 {ECO:0000313|EMBL:SMX25054.1};
GN ORFNames=BOA8489_03188 {ECO:0000313|EMBL:SMX25054.1};
OS Boseongicola aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Boseongicola.
OX NCBI_TaxID=1470561 {ECO:0000313|EMBL:SMX25054.1, ECO:0000313|Proteomes:UP000201838};
RN [1] {ECO:0000313|EMBL:SMX25054.1, ECO:0000313|Proteomes:UP000201838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8489 {ECO:0000313|EMBL:SMX25054.1,
RC ECO:0000313|Proteomes:UP000201838};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) 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 -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC subfamily. {ECO:0000256|ARBA:ARBA00009496}.
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DR EMBL; FXXQ01000012; SMX25054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238J593; -.
DR Proteomes; UP000201838; 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; 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 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:SMX25054.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000201838};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SMX25054.1}.
FT DOMAIN 2..155
FT /note="PHP"
FT /evidence="ECO:0000259|Pfam:PF02811"
FT DOMAIN 276..540
FT /note="Bacterial DNA polymerase III alpha subunit NTPase"
FT /evidence="ECO:0000259|Pfam:PF07733"
FT DOMAIN 543..723
FT /note="DNA polymerase III alpha subunit finger"
FT /evidence="ECO:0000259|Pfam:PF17657"
FT DOMAIN 798..884
FT /note="DNA polymerase helix-hairpin-helix motif"
FT /evidence="ECO:0000259|Pfam:PF14579"
SQ SEQUENCE 1148 AA; 127078 MW; 206091339A56FCF7 CRC64;
MRLKKLPGLC EKAGMPAVAV TDTNNMFAAL EFSVSALDAG IQPIVGCQVD LAYETPAPGE
KPLRPAPLVL LAQTRAGYEC LMKLNSALYL READYPHVTL DELAEFSEGL ICLTGGPDGP
VGRLLRAGQK PKAQGLMTQL AATFGDRLYV ELQRHPTENG QVPEAEKLTE TPQIEMAYAM
DLPLVATNDV YFTDQKMYEA HDALICIAEG AYVDQQAPRR RLTPQHYFKT PAEMATLFAD
LPEALENTVE IARRCAFAVE RHDPILPKFA DDEIEELRRQ SFEGLKNRLA VIEAVAPVEE
YEKRLEFELG IIEGMGFPGY FLIVADFIKW AKDHHIPVGP GRGSGAGSLV AYALTITDLD
PLRYSLLFER FLNPERVSMP DFDIDFCMDR REEVIRYVQE KYGRDKVGQI ITFGALLSKA
AVRDVGRVLQ MPYGQVDRLS KLIPVEGVKP VSIEKALADE PRLREEAKAE EVVARLLDYG
QQVEGLLRNA STHAAGVVIG DRPLDKLVPL YRDPRSEMPA TQFNMKWVEQ AGLVKFDFLG
LKTLTVIQNA IDQILASGRS LDVAADGTRL YEPDPGTEND IGLIPLDDEK SYELYAKART
VAVFQVESSG MMDALRRMRP TCIEDIVALV ALYRPGPMEN IPQYCDVKNA RAERERLHPS
IDHILDETQG IIVYQEQVMQ IAQEMAGYSL GGADLLRRAM GKKIQEAMDA ERPKFLEGAA
KNGVDKKKAM EVWNLLDKFA NYGFNKSHAA AYAVVSYQTA WLKANHPVEF MAGVMNCDLH
LTEKLDVYAN EVRRGLEIEI VPPCVNRSEA VFSVRDQKLV YALGALKNVG VEAMKLIVEA
RGDKPFVNVF DLARRVDLKR VGKRPMEMLA RAGAFDQLDP NRRRIFQSLD GLTAYSAAIH
EQRASAQVSL FGEAGDDLPE PRLSPVEDWL PNERLDQEQT AIGFYLSGHP LDDYAPALKR
KGLMNLADLQ VKAEADGAAI ARVGVVVTAL QERKSGRGTR FFRMNISDPT GQVSGMALFP
DDFETVRKVF EQTTQVVMTL EARFNEGQFD PIARSVAPID GIVDAATAGL NVMIDDEGAV
QMVQSVLERF KVDQSIRTRG EVCLTALAVP LPGALQDVTV SIGDGWPVSP QIKGALKSLP
GVVLVEDI
//
