ID A0A1X4NMP2_9RHOB Unreviewed; 1166 AA.
AC A0A1X4NMP2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-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=MGEO_08480 {ECO:0000313|EMBL:OSQ51482.1};
OS Marivita geojedonensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Marivita.
OX NCBI_TaxID=1123756 {ECO:0000313|EMBL:OSQ51482.1, ECO:0000313|Proteomes:UP000193926};
RN [1] {ECO:0000313|EMBL:OSQ51482.1, ECO:0000313|Proteomes:UP000193926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPG-138 {ECO:0000313|EMBL:OSQ51482.1,
RC ECO:0000313|Proteomes:UP000193926};
RA Lai Q., Shao Z.;
RT "The draft genome sequence of Marivita geojedonensis KCTC 23882.";
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:OSQ51482.1}.
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DR EMBL; JFKC01000005; OSQ51482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X4NMP2; -.
DR STRING; 1123756.MGEO_08480; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000193926; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000193926};
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 1166 AA; 128756 MW; 0E364AA33247A178 CRC64;
MADPRFIHLR VHSEYSLLEG AVRLKKLPDL CMTKGMPAVA LTDTNNLFAA LEFSVSASGA
GIQPIIGCQV DLRVAEPAPG ERAKPPAPVV LLAQTETGYE HLMKLNSCLY LRRDGELPHV
TLDELAQHSE DVICLSGGPE GAVGRILQQG NRGAAEAVMH RLAEIFGDRL YVELQRHPGE
NGLPESERLT ERGFVEIAYA MGLPLVATND VYFPKSDMYE AHDALICIAE GAYVDQQEPR
RRLTPQHYFK SPQEMVTLFA DLPEAIENTV EIARRCAFMA YRRDPILPKF ADDEVEELKR
QAREGLKERL AVIPHAAPVE EYEKRLEFEL GIIEGMGFPG YFLIVADFIK WAKDHDIPVG
PGRGSGAGSL VAYALTITDL DPLRYQLLFE RFLNPERVSM PDFDIDFCMD RREEVIRYVQ
DKYGKDRVGQ IITFGALLSK AAVRDVGRVL QMPYGQVDRL SKMIPVEGVK PVSIEKALKD
EPRLREASRE EEVVDRLLTY GQQVEGLLRN ASTHAAGVVI GDRPLDELVP LYQDPRSEMP
ATQFNMKWVE QAGLVKFDFL GLKTLTVIQY ALDMIAKAGR PLHMAADGRQ LYEPAPGAEN
DIGHIPLDDE ESYKLYAAAK TVAVFQVESS GMMDALKRMK PTCIEDIVAL VALYRPGPME
NIPTYCEVKN GLRERESVHP LIDHILEETQ GIIVYQEQVM QIAQVMAGYS LGGADLLRRA
MGKKIKEAMD AERPKFEKGA AENGVEAKKA SEVFDLLEKF ANYGFNKSHA AAYAVVSYQT
AWLKANHPVE FMAGVMNCDI HLTDKLATYF EEVKKGLGLP WVPPCVNRSQ AMFDVQDGAL
VYALGALKNV GVDAMKLITE ARGEKPFVNL FDVARRVDLK RVGKRPLEML ARSGAFDRLD
PNRRRVFESL DALVAYSAAI HDQRASAQVS LFGEAGDDLP EPRLSPVTDW LPAERLSEEF
KAVGFYLSGH PLDDYMTALK RKGAMTLDDV LAKAQNGPCV VKMAGVVAGR QERKSARGNR
FAFAQLSDPT GAYEVTLFSD TLEAARDHLE TGSKVMVTAE ATMESDQLKL LGRSVAPVDI
AVADAVSMGL RIFVDEVEVV PHVASVLTRA ADQLPKAGKG PIRICCLNAP GLPGEVDVAL
SQEFPVTPEI KGAIKSLGGV LDVEEL
//
