ID A0A031K1M7_9SPHN Unreviewed; 1200 AA.
AC A0A031K1M7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=BV97_01041 {ECO:0000313|EMBL:EZP83851.1};
OS Novosphingobium resinovorum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=158500 {ECO:0000313|EMBL:EZP83851.1, ECO:0000313|Proteomes:UP000024329};
RN [1] {ECO:0000313|EMBL:EZP83851.1, ECO:0000313|Proteomes:UP000024329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KF1 {ECO:0000313|EMBL:EZP83851.1,
RC ECO:0000313|Proteomes:UP000024329};
RA Gan H.M., Gan H.Y., Chew T.H., Savka M.A.;
RT "Whole genome sequence of Novosphingobium resinovorum KF1.";
RL Submitted (MAR-2014) 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:EZP83851.1}.
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DR EMBL; JFYZ01000002; EZP83851.1; -; Genomic_DNA.
DR RefSeq; WP_008829737.1; NZ_JFYZ01000002.1.
DR AlphaFoldDB; A0A031K1M7; -.
DR STRING; 158500.BES08_07730; -.
DR PATRIC; fig|158500.4.peg.1070; -.
DR eggNOG; COG0587; Bacteria.
DR Proteomes; UP000024329; 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 1200 AA; 131780 MW; FDEC3F92B37B7234 CRC64;
MPHAPFVPLR IFSSFTMLDG AIDPKAIAKL AKERKFPAAG LCDRNGLYAA PIFAGAAKGA
GVQPIVGTFL AVARPGAAKQ GQERAIDWLA LFAQNEAGWL NLCDHVSRAH LGRPLELDPH
VELESLRGHT DGLICLTGGN EGALARLFAA GRHEQAESYC DTLQSLFGDR LYIEITRTGE
PEEDESEEDL IALAYTRDIP LVGTNPAQFS DRSFHAAHDA LLCIANSTQV DAADRPRSSS
ERWVKPAAEM AELFADLPEA LANTLVVAQR CAYVPPRRKP LLPSLAGDRE GEARMLADDS
RRGLAARLAP YWPEVTEQEL DEAMALTGDE RRAAYEILRE KGVTEDFLEY AERLDFEVNI
IVGMGFPGYF LIVADFIKWA GDNGIPVGPG RGSGAGSLVA WALTITGLDP LKLGLLFERF
LNPERVSMPD FDIDFCETRR GEVIRYVQKK YGHDHVAQII TFGKMKARAV LRDCGRILQM
GYGRVDSLCK MVPNHPTDPW TLTETIQGRK AHGVTKDPPV AEFKREYDND REVRRLVDLA
VQLEGLPRNS STHAAGVVIG DRPLAQLVPL YRDPRSDMPV TQFDMKYVED TGLVKFDFLG
LKTLSVLRKA CDLLERRGIT INLSTLAWDD PGVYELLKRG DTVGVFQLES EGMRRTLAAV
KPTNFGDIIA LVSLYRPGPM DNIPLFGQRK NGLAPIEYPH DKLAGILGET YGIFVYQEQV
MQAAQILAGY SLGDADLLRR AMGKKVQAEM DKQRQRFVDG CKEVSGIEAA KANELFDLID
KFAGYGFNKS HAAAYALLAY HTAWFKAHYP HEFYAAAMCF DMHQSEKLAI FVDDARRNGI
ELAAPDINKS EAEFIVEETA ESHAVRYALA GIRNVGEKAM DAIVAEREAN GPFVDLDDVF
RRAPAGSMNR RQLESLAAAG AFDALEPNRA KVLANADTLL AEADRSSRER NSTQGGLFGG
EDHVEQGLRL VEADKWDRAD QMAKERETFG FYFAAHPVEA YRAVASANGA RTYSSLMAGG
GGGGRTGAVM AAMVENVQKR KTRKGKDFVM ADFSDSSGNF SASCFEESLV ENFVKWAKEG
ACILLNVELD SPSPDEPPRI TVRGGKPLNE VKADARMVLK LDIDRVEAVQ ELALLMRPGE
RGAGEVIATL HLGDGRTQKV RLGRDFALDG EFAEHLQSVE GITNVSLTAK RGPERVAMAA
//
