ID A0A3A1P6J2_9SPHN Unreviewed; 1188 AA.
AC A0A3A1P6J2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=D2V17_08395 {ECO:0000313|EMBL:RIV87403.1};
OS Aurantiacibacter xanthus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=1784712 {ECO:0000313|EMBL:RIV87403.1, ECO:0000313|Proteomes:UP000265366};
RN [1] {ECO:0000313|EMBL:RIV87403.1, ECO:0000313|Proteomes:UP000265366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AB 2015396 {ECO:0000313|EMBL:RIV87403.1,
RC ECO:0000313|Proteomes:UP000265366};
RA Fang C., Wu Y.-H., Sun C., Wang H., Cheng H., Meng F.-X., Wang C.-S.,
RA Xu X.-W.;
RT "Erythrobacter zhengii sp.nov., a bacterium isolated from deep-sea
RT sediment.";
RL Submitted (AUG-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:RIV87403.1}.
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DR EMBL; QXFM01000074; RIV87403.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A1P6J2; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000265366; 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 ECO:0000313|EMBL:RIV87403.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000265366};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RIV87403.1}.
FT DOMAIN 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1188 AA; 130140 MW; 2BC6FACDA0951BF0 CRC64;
MPYAPFVPLR VFSSFSMLEA AIDPKQIAKL AKERGFPAVA ICDRNGLYGS SAFAGACKGE
GVQPLIGTLL GVARDETGEV VDYLPLFAQG EEGWNNLCHL VSRAHLDRPL ERDPHVQMTD
LKGHTGDLIA LTGAGEGALA RLLADGKAAR AGELLDRLQA LFPGKLYIEL ARRGDPVEEA
AEGALIDLAY ARDLPLVATN PAHYGEPHMH KAHDAMLCIA NSSQLDSADR PTSNAETYIK
PASMMEELFA DLPEALANTL VVAQRCAFAP PKRKPILPSL AGDQEGEARM LEEDARDGLI
ARLKPLYPEA AQAELVEALS FSSAEALEKE EQSFDKLRTS GIWDEVLEYK KRLDFEVGII
KRMGFPGYFL IVADFIKWAK SQGIPVGPGR GSGAGSLVAW ALTITDLDPI RLGLLFERFL
NPERVSMPDF DIDFCETRRG EVIRYVQAKY GHDHVAQIIT FGKMKARAVL RDCGRILQMP
YGQVDRLTKM VPNHPTDPWT LPRTLNGAAD FKREYSNDNE VKRLVDLAMQ LEGFPRNSST
HAAGVVIGDR PLSQLVPLYR DPRSDMPVTQ FDMKHVEDSG LVKFDFLGLK TLSVLRKAVD
LLARRGIAVE LDKLAWDDPA VFELLKRGDT VGVFQLESEG MRRTLTAVKP TKFEDIIALV
SLYRPGPMDN IPSFGRRKAG EEEIIYPHEK LKGILEETYG IFVYQEQVMQ AAQILAGYSL
GDADLLRRAM GKKIQAEMDA QRLRFCEGCK EVSGIEKAEA NALFDLIDKF AGYGFNKSHA
AAYALLAYQT AWLKAHYPEE FYAGSMCFDM HQSEKLAVFV DDLRRNGLKL LGPCINHSEA
EFHVEQTDEG YAVRFALAGL RNVGEKAMEQ VVAEREARGA FTSLTDVFER MPAGAMNRRQ
LESLAASGAF DVLEPNRAKV LANADMLMAV ADAASRERSS GQAGLFGGDD HAEPEVRLVE
AKPWPRAEQM AAERENFGFY FAAHPVEQFR HAASAQGART YASLMTGGVR GGRENAVVAA
MVEGASKGRT KRGAEFIRAD FSDSTGNFSA ACFEEGLVES FQRWASEGTC VLLNVELDSP
SPDEPPRVTV RGAKPLAEVT GSAKMILRAD VYDEAGLATL RAMLEPGQVG HGEVLVRLRI
GEEQEPSVLL GRDFALDGSL VDKLANVAGL GGVSLAPIRG IGHLRLVA
//