ID A0A3P1WMY0_9ACTN Unreviewed; 1172 AA.
AC A0A3P1WMY0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=EII42_01365 {ECO:0000313|EMBL:RRD47924.1};
OS Tessaracoccus sp. OH4464_COT-324.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=2491059 {ECO:0000313|EMBL:RRD47924.1, ECO:0000313|Proteomes:UP000274803};
RN [1] {ECO:0000313|EMBL:RRD47924.1, ECO:0000313|Proteomes:UP000274803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH4464_COT-324 {ECO:0000313|EMBL:RRD47924.1,
RC ECO:0000313|Proteomes:UP000274803};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) 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:RRD47924.1}.
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DR EMBL; RQYZ01000001; RRD47924.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1WMY0; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000274803; 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:RRD47924.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000274803};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RRD47924.1}.
FT DOMAIN 6..73
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1172 AA; 130514 MW; C4B6265E191CCA57 CRC64;
MGKQFVHLHC HTEFSMLDGA ARVKDLFENA ERMGMPALAV TDHGNLFGAY EFYKTSKNYN
VKPIIGLEAY LTPRTHRSER KRVQFGDGTG DDVASKGAYT HMTMWALNRE GMHNLFRLST
RSSLEGFFYK PRADRELLNE YGKGLIGTTG CPSGEVQTFL RLGQYDNALA SAAEFRDIFG
VGNFYVELMD HGLSIENRVR KDLLRIARDL DLPLVATNDL HYVHAHDADA HDTLLCVSAG
ARKAQNDRFK FDGSGYYLKS PEEMHSLFSE LPEACDNTLA IAERIETSFE EGMGVYMPKF
PVPDGETEET WFHREVQRGL EYRYPGGIPA EVQERADFES SIISQMGFNG YFLVVADFIN
WAKDNGIWVG PGRGSGAGSM CAYALRITDL DPIEHGLFFE RFLNPERVSM PDFDIDFDDR
RRGEVIEYVT RKYGQENVAQ IVTYGSIKAK AAVKDAARVL DMPFSVGEQI TKAMPPDVMG
KGVPLPQLFD PDHKRFAEGN EFRELYNSNA DVKTVVDTAM GLEGLKRQWG VHAAGVIMSR
SPLIDIIPLM KRESDGAIIT QFDYPGCESL GLIKMDFLGL RNLTILGDAV DNIKRNQGID
VDLENLALDD KQTYELLATG ETLGVFQLDG GPMRALLRSM QPDSFSDISA VVALYRPGPM
GADSHNKYAR RKTGKEEVEP IHPELAEPLA DILDETYGLI VYQEQVMAIA QRVAGYTLGG
ADMLRRAMGK KKKEELDKQF ATFSSGMTER GYSADAVRTL WEILVPFSDY AFNKSHSAAY
GLVSYWTAYL KAHYPTEYMA ALLQSVRDDK DKLSIYLAEC RHMGIHVLLP DINSSEIAFT
PVGKDIRFGL GAIRNVGDKV VSAWIEERDK LGPAKDFNDF LDKAPLLMCS KRVVESLIRA
GAFDELGHTR RALISIFEAA VDSIIDIKRN SANGQDDLFG FAAEPGDQPE HVVVPAIEEW
DRKTKLGFER EMLGLYVSDH PLNGLEHIIA EHSDRAIAST VGEDSYEGPA TLCGLITSVN
RRVNKNGQVY ATVTLEDLTT GIEVTVFPKL YEQVSALLEP DALVAVDGTV ERGEDRGRMR
AKHVSTPHYN LDGSVGPVII NLAESRCTPA LVKRLKAVLE SYPGSAEVHV EVRGNRRLTT
YRVNDRYSVQ LASPLFADLK ALLGPTSVRV MR
//
