ID A0A0W1KMR1_9ACTO Unreviewed; 1190 AA.
AC A0A0W1KMR1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:KTF04830.1};
GN ORFNames=AQZ59_00130 {ECO:0000313|EMBL:KTF04830.1};
OS Trueperella bernardiae.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Trueperella.
OX NCBI_TaxID=59561 {ECO:0000313|EMBL:KTF04830.1, ECO:0000313|Proteomes:UP000054404};
RN [1] {ECO:0000313|EMBL:KTF04830.1, ECO:0000313|Proteomes:UP000054404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCDC 89-0504 {ECO:0000313|EMBL:KTF04830.1,
RC ECO:0000313|Proteomes:UP000054404};
RA Bernier A.-M., Bernard K.;
RT "Draft Genome Sequence of the Type Strain Trueperella bernardiae LCDC 89-
RT 0504T, Isolated from Blood Culture.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KTF04830.1}.
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DR EMBL; LNIZ01000001; KTF04830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W1KMR1; -.
DR STRING; 59561.AQZ59_00130; -.
DR PATRIC; fig|59561.3.peg.130; -.
DR Proteomes; UP000054404; 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; cd12113; PHP_PolIIIA_DnaE3; 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 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 4: Predicted;
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:KTF04830.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054404};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KTF04830.1}.
FT DOMAIN 16..83
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1190 AA; 131816 MW; ADB8E54F954E99FD CRC64;
MPEALARLNP MAKNFAHLHV HTDYSLLDGA AKIGRLVKEV AALGQPAVAI TDHGNLHGAY
ELYKAANGAG IKPIIGLEAY MTPGTSRHDK TRVFWGTEAQ RKDDVSARGS YTHMTLLAET
TEGMHNLFRM QSLASIEGTL GKAARIDREL LEKYHHGLIG TAGCPSGEIQ TRLRLGQFDE
ALKAAGEFQD IFGKENFYFE LMDHGLDIER RVKDDLLAIA RQIGAPLLAT NDSHYVTQDQ
STVQDAMLAL NSGSTLMDPD RFRFEGTGYY IRSSEDMWNS FGHLEGACEN TLEIVERCNV
HFDTTADGVN YMPKFPVPSG EDEKSWFVRE VNDGLHRRYG DVIPDDVRKR ADYEMDVILQ
MDFPGYFLVV SDYIRWARRH GIRVGPGRGS GAGSMVAYAL EITQLDPIKH DLLFERFLNP
ERISMPDLDI DFDDSRRDEV IEYVEDKYGK DKVSQVVTFG TIKAKQSLKD ASRVLGYPFE
MGDRLTKAMP PSVMGKDIPV NDLFNKDHPR YAEAGEIREL IDNDPDCKKV YDLACGLEGM
TRQTGMHACA VIMSSKPLTD VIPVMMRQQD GAILTQFEYP ECEELGLIKM DFLGLSNLTV
IEAALANIRV NGKDAPDIDA IPLDDPKTYE LLARGDTLGI FQLDGAGMRT LLRQMKMDSF
ADISAVSALY RPGPMGANSH TNYALRKNGL QEKTPIHPEL EEGLEDILGV THGLIVFQEQ
VMRIAQKLAG FTLGQADILR KAMGKKKAEV LQQQFASFSQ GMRDNGFSQE SIDTLWDILL
PFSSYAFNKS HSEAYALVSY QTAYLKSHFP AEFMAALLTS KMSDKTKVAT YLAECRRMGI
KVQVPDVNSS LADYTAVGDE IRVGLRAVRN VGANVVDGII KAREEKGPFT SFQDFLDKIP
LSACNKRSIE CLIKAGGFDS LGECRRALVA IVEEAIDAVI PVKRNEAAGQ FDLFGDLGVG
GSDGFDVAIP DIPEWDKREK LNFEREMLGL YVSDHPLSGM ENFLNRAADT TVVDLLESDN
VRDGQMVTIA GLISAVQTKI TKKSGKAWAI ATIEDRTGPI DVNFFPATYQ QVSSILIPDA
VVIVEARAQI EDEGPVKLSA RTMTLPPAGE IELDHPIDIK IDERACSAVK MDQLAEILAR
YPGQSPVRLH VWRAAPNKTV VAEVASNFWV SPEPSLYTEL KVLLGRDCVV
//
