ID A0A2S0MT36_9RHOB Unreviewed; 1171 AA.
AC A0A2S0MT36;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=dnaE {ECO:0000313|EMBL:AVO39044.1};
GN ORFNames=C6Y53_15895 {ECO:0000313|EMBL:AVO39044.1};
OS Pukyongiella litopenaei.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pukyongiella.
OX NCBI_TaxID=2605946 {ECO:0000313|EMBL:AVO39044.1, ECO:0000313|Proteomes:UP000237655};
RN [1] {ECO:0000313|Proteomes:UP000237655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH-1 {ECO:0000313|Proteomes:UP000237655};
RA Kim Y.-S., Kim S.-E., Kim K.-H.;
RT "Genomic analysis of the strain SH-1 isolated from shrimp intestine.";
RL Submitted (MAR-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 ---------------------------------------------------------------------------
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; CP027665; AVO39044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0MT36; -.
DR KEGG; thas:C6Y53_15895; -.
DR Proteomes; UP000237655; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0003676; F:nucleic acid binding; IEA:InterPro.
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; IPR004365; NA-bd_OB_tRNA.
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 Pfam; PF01336; tRNA_anti-codon; 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:AVO39044.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000237655};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AVO39044.1}.
FT DOMAIN 8..75
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1171 AA; 129024 MW; 2F08BECFF263BC4E CRC64;
MSSDPRFIHL RVHTEYSLLE GAVRLKALPA ICRRHGMPAV AVTDTNNMFS ALEFSVAASG
AGIQPILGCQ VDLAAQDQRP GERAAPPAPL VLLAQSEAGY ENLMKLNSCL YLGGDGDGEG
DAQVPQVTLA QLHDHGAGLI CLSGGPDGPV GRLLQAGQRE AAEALVDRLA SIYPDRLYIE
LQRHPGENGA PRAERLTERG HVEIAYARGL PLVATNDVYF PGPEMYEAHD ALICISDGAY
VDQQAERRRL TAQHYFKSPQ EMATLFADLP EAIENTVEIA RRCAFMASRR APILPKFADD
EVEELRRQAN AGLQARLAVI PHAVTPEAYQ ERLDFELGII EGMGFPGYFL IVADFIKWAK
DHDIPVGPGR GSGAGSLVAY ALTITDLDPL RYSLLFERFL NPERVSMPDF DIDFCMDRRE
EVIRYVQEKY GRDRVGQIIT FGALLSKAAV RDVGRVLQMP YGQVDRLSKL IPVEGVKPVS
IEQALADEPR LREEARNEEV VERLLRYGQQ VEGLLRNAST HAAGVVIGDR PLDELVPLYR
DPRSDMPATQ FNMKWVEQAG LVKFDFLGLK TLTVIQNAVD LIRKTGRGLH EAADGTRLYD
PPEGAENEIN AIPLDDAATY RLYAQARTVA VFQVESTGMM DALKRMRPTC IEDIVALVAL
YRPGPMENIP TYCEVKNGKR DISSVHPLID HILEETQGII VYQEQVMQIA QVMAGYSLGG
ADLLRRAMGK KIAEEMAKER PKFEKGAMEN GVDKAKASEV FDLLEKFANY GFNKSHAAAY
AVVSYQTAWL KANQPVEFMA GVMNCDIHLT DKLAIYFEEL RKGMNLPWVP PCVNRSQAGF
DVVDGALVYG LGALKNVGSD AMRLVVEGRG DAPFVNLFDF ARRVDLKRIG KRPLEMMARA
GAFDELDRNR RRVLESLDAL VAWSAAIHEQ RGSAQVSLFG EAGDDLPEPR LSQSPDWLPA
ERLAEEHKAI GFYLSGHPLD DYRVSLKRRD VLMLDDLIER ARQGPLVAKM AGVVAGRQER
KNARGNRFGF AQLSDPTGAY EVMLFSEALE NCREHLETGT QVVITVEATM EADKLRLLAR
SVAPIDSVVA QGESTGLMVY LAQPDALETV ARVLEDAAAA KNGGRGPVVF CLMDPDLPGE
VEIDAGRDFP VGPRIKGAIR SLEGVLEVEE L
//
