ID A0A397PBN9_9SPHN Unreviewed; 1201 AA.
AC A0A397PBN9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=DFR49_1561 {ECO:0000313|EMBL:RIA46996.1};
OS Hephaestia caeni.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Hephaestia.
OX NCBI_TaxID=645617 {ECO:0000313|EMBL:RIA46996.1, ECO:0000313|Proteomes:UP000266568};
RN [1] {ECO:0000313|EMBL:RIA46996.1, ECO:0000313|Proteomes:UP000266568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25527 {ECO:0000313|EMBL:RIA46996.1,
RC ECO:0000313|Proteomes:UP000266568};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
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:RIA46996.1}.
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DR EMBL; QXDC01000002; RIA46996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397PBN9; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000266568; 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; SSF160975; AF1531-like; 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:UP000266568};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 823..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1201 AA; 130440 MW; 544F5A1CF0D30DD5 CRC64;
MPHSAFVPLR IFSSYTMLDG AIEPKQIAKR AQEMGFPAAA LTDRNGLYAA MAFSDACKAS
GVQPIIGTML GVCRPDMPEG VEAPLDWLAL YAQDKTGYDN LCALVSRAHL DRPIEQPAHV
SFDDLQGHTQ GLIALTAGRE GALARLFAEE QHDRALAYAD RLQALFGDRL YVELTRRLDE
IEGRAEPLLL DLAYDRGLPL VATNPCCFAD KDFSEAHDAL LCIASSSYVA SDDRPRSSPD
AWMKPAREMR ELFADLPEAI ANTMVVAQRC AVAAPRRKPI LPSLAGDREG EAAKLREDAR
AGLEMRLAKI EALAGQPLTP EEREAYFTRL EFEVGIIIQM GFPGYFLIVA DFIKWAKDHD
IPVGPGRGSG AGSVVAWSLT ITDLDPLKLG LLFERFLNPE RVSMPDFDID FCETRRGEVI
RYVQEKYGRD QVAQIITFGK LKARAVLKDT GRVLQMSYGQ VDRLAKLVPN LPADPWTLER
ALNGVSELAA EYKGDEGVRH LLDLAMKLEG LPRHSSTHAA GVVIGDRPLS ELVPLYRDPR
SDMPVTQFDM KYVEGAGLVK FDFLGLKTLS VLKMAVELLA KRGIAVDLEA LSWDDPKVFA
LLQRGDTVGV FQVESEGMRR TLSAVKPTVF EDIIALNALY RPGPMDNIPM FGRRKNGHEE
IEYPHPLLEG ILKETYGIFV YQEQVMQAAQ ILAGYSLGGA DLLRRAMGKK IKAEMDAQRA
IFVEGCAKTN DIPEAKANEL FDLIDKFAGY GFNKSHAAAY ALLTYQTAWL KAHHAPEFYA
ASMSFDMALT DKLSVFVDDM RRLGVACLAP DLNASEADFS VEATTASSPS PSGEGLGRGS
AAGDALGETS PTPNPSPEGE GQTFTVRYAL AALKGVGERA MEELVAERRA GGPFTSLSDL
ARRVDPRLLN KRQLETLAAG GAFDSIDPNR PGIAAVAETV LATAARLHEQ RASGQGGLFG
GEGAVAEAEI RPLATARWTL AERMEQEKEA FGFYFSAHPV DRHRLLAKMH GARNYAALGE
LPIAEGQRTG ATMAALVEDA RWRTSARGRR YLMATLSDAT GQFIATCFDD AVAADLEAAA
KSGGCGLLTV ELDRRAGEET PRVTVKRLQP FASLATTARM TIECVIDDPA VIRQLAELVA
GARGGRGEIR VRTSLPGGGS ATVLLGRDFL LDTELAGDLE AMHGIAALVF KTSEARLALA
G
//
