ID A0A2U0SIR0_9SPHN Unreviewed; 1159 AA.
AC A0A2U0SIR0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=DD559_19220 {ECO:0000313|EMBL:PVX31209.1};
OS Sphingomonas pokkalii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2175090 {ECO:0000313|EMBL:PVX31209.1, ECO:0000313|Proteomes:UP000245890};
RN [1] {ECO:0000313|EMBL:PVX31209.1, ECO:0000313|Proteomes:UP000245890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L3B27 {ECO:0000313|EMBL:PVX31209.1,
RC ECO:0000313|Proteomes:UP000245890};
RA Menon R., Kumari S., Rameshkumar N.;
RT "Description of Sphingomonas pokkalii sp nov, isolated from the rhizosphere
RT of saline tolerant pokkali rice and its draft genome analysis.";
RL Submitted (MAY-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:PVX31209.1}.
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DR EMBL; QENQ01000001; PVX31209.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U0SIR0; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000245890; 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; 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; SSF160975; AF1531-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 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1159 AA; 127026 MW; F1DC5215868168A9 CRC64;
MAHSGFVPLR VFSCYTMLEG AIDPKAIAKH AKNHGFPAIA VADRNGLYAA MSFSDAAKKA
GVQPIVGTLL AVKRSNVAEG LNVPIDWLAL YAQDQTGYEN LCHLVSQAHL DRPIEEDAHV
PFAALTGHTH GLLCLTAGAE GAIARLYAEG QDKTAEAYVA QLEALFPDRL YVEIARRNNE
VETRAEDKLI ELAYARNLPL VGTNPACFAD ADFYDAHDAM LCIANSTYLE TDDRPRSSPE
AWLKPAETMK TSFADLPEAI ENTLVVAQRC AYAAPKRKPI LPSLAGDREG EAAMLRERSW
QGLKDRLDFA GVTDPSEVEV YNQRLQFELD IIIQMGFPGY FLIVADFIQW AKSNDIPVGP
GRGSGAGSAV AWALTITDLD PLKLGLLFER FLNPERVSMP DFDIDFCETR RGEVIRYVQE
KYGRDHVAQI ITFGTMKARA VIKDVGRVLQ MSYGQVDRLA KQIPNHPTDP WTLERTLNGV
SEFLAEYSDK EDVKRLVDLS MRMEGLPRHS STHAAGVVIG DRPLAQLVPL YRDPRSDMPV
TQFDMKNVEG AGLVKFDFLG LKTLSVLKKA VVLLAKRGVD VNLDRLDWDD EGVYALLQRG
DTVGVFQLES EGMRRTLTAV RPTNFGDIVA LVSLYRPGPM DNIPMFGARK AGREPIIYPH
DLLEPILKET YGIFVYQEQV MQAAQILAGY TLGGADMLRR AMGKKVKAEM DAQRSIFVKG
CKEVNDIPAA KANELFDLID KFAGYGFNKS HAAAYALLAY QTAWLKAHHP HEFFAASMAY
DIHQTDKLAV FADDMRRLGI EATSPDINAS EADFTVQPHG EGLAVRYALG ALKGVGERAM
ELLVEEREKN GRFASLDDFA KRVDPRVLNK RQLETLASAG AFDSIEPNRA GVHAAAETIL
AVAQRDHASR MSGQGGLFGD AEPAGGGITV PKDAVWSMSD KINAEKDAFG YYFSAHPLDR
YEHLFRGQGV RDIASLPDMQ IPEGARVNAQ IAALIEDCRY RTSARGNRYL MATISDRSAQ
IQTSCFEELI AKDMEACANG TGCAILTLEL DKRPGEDTPR AAVKRVQPFD TLAGTTQLIL
EIRIEDPTVP AQLAALVGDL RGGGRGEILL HAPIEGGEAT VMLGRGFRLD TELAARIEGM
PGVQAASLMP ASMKLQAAA
//
