ID A0A2A4CVI4_9RHOB Unreviewed; 1172 AA.
AC A0A2A4CVI4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=CLN94_01855 {ECO:0000313|EMBL:PCD78074.1};
OS Pseudothioclava arenosa.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudothioclava.
OX NCBI_TaxID=1795308 {ECO:0000313|EMBL:PCD78074.1, ECO:0000313|Proteomes:UP000243507};
RN [1] {ECO:0000313|EMBL:PCD78074.1, ECO:0000313|Proteomes:UP000243507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAU 1312 {ECO:0000313|EMBL:PCD78074.1,
RC ECO:0000313|Proteomes:UP000243507};
RA Liu Y., Shao Z.;
RT "A multilocus sequence analysis scheme for characterization of bacteria in
RT the genus Thioclava.";
RL Submitted (SEP-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 -!- 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:PCD78074.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NTJD01000001; PCD78074.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4CVI4; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000243507; 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 Reference proteome {ECO:0000313|Proteomes:UP000243507};
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 1172 AA; 129218 MW; 400ECE46D1615C9B CRC64;
MPDPRFIHLR LHTEYSLLEG AVPVKKLIKL CEGAKIPAVA VTDTNALFAA LEFSVLAQGA
GVQPIIGCQV SVAYDPAAPG EKPRLPAPLV LLAQNEAGYE NLMKLSTCLY VDKPGGMIEV
TVDELAAHSE GLICLSGGAD GALGRLIRAG QPGKARLLME RLATIYPNRL YVELQRHPGE
GGALPEAERA TERPFIEMAY DLHLPLVATN DVYFPKSDMF EAHDALICIA EGAYVDQQEP
RRRLTPQHYF KSEGEMCALF ADLPEALENT VEIAKRCSFA AYKRKPILPR FAEDEVEELR
RQSWEGLRAR LAVIPHAAPV EEYEERLKFE LGIIEQMGFP GYFLIVADFI KWAKDHGIPV
GPGRGSGAGS LVAYALTITD LDPLRYSLLF ERFLNPERVS MPDFDIDFCM DRREEVIHYV
QEKYGREKVA QIITFGALLS KAAVRDVGRV LQMSYGQVDR LSKMIPVEGV KPVSIEKALA
DEPRLREAAR AEEVVERLLT YAKQVEGLLR NASTHAAGVV IGDRPLDALV PLYQDPRSDM
PATQFNMKWV EQAGLVKFDF LGLKTLTVIQ SAMELIFKSG RPLHVAADGT ELYEPAEGAE
NQINAIPLDD AKTYRLYADA RTVAVFQVES SGMMNALRQM KPTCIEDVVA LVALYRPGPM
DNIPTYCEVK HGTRPLESLH PTIDPILKET QGIIVYQEQV MQIAQVMAGY SLGGADLLRR
AMGKKIAEEM AKERPKFLEG AKATHNVDAK KAGEVFDLLE KFANYGFNKS HAAAYAVVSY
QTAWLKANHP VEFMAGVMNC DIHLTDKLAI YLNEVRRGLD IEVVPPCVNR SLASFDVVDQ
KLVYALGALK NVGLDAMRLI VEARQVDGRD VPFASLTDFA RRCDLKRIGK RPLEMLARAG
AFDQIDPNRK RVFESLESLM AWSAAVLEAR ASAQVSLFGD AGDDLPPPRL ADTDDWLPAE
RLSEEHKAIG FYLSAHPIED YLPALRRKKV MSFEEIEKKA AADGPFVCKV AGELASMRER
KSAKGNRFAF IAFSDASGPF EVTFWSDALD GARAHLENGR LLVMTVRAEP EGESVRLVAQ
GVQPIDQVTA DAGGAGLLIH LETPEAVPSV AAILERLAAE GKVRSRGPVA FNVFDAERGC
QYKIDTGSQF PVNPQVKGAI RALRGVSMVE EI
//
