ID A0A3P1YWY5_9BACT Unreviewed; 1285 AA.
AC A0A3P1YWY5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=EII14_08525 {ECO:0000313|EMBL:RRD75469.1};
OS Alloprevotella sp. OH1205_COT-284.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Alloprevotella.
OX NCBI_TaxID=2491043 {ECO:0000313|EMBL:RRD75469.1, ECO:0000313|Proteomes:UP000272376};
RN [1] {ECO:0000313|EMBL:RRD75469.1, ECO:0000313|Proteomes:UP000272376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH1205_COT-284 {ECO:0000313|EMBL:RRD75469.1,
RC ECO:0000313|Proteomes:UP000272376};
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 -!- 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:RRD75469.1}.
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DR EMBL; RQYI01000040; RRD75469.1; -; Genomic_DNA.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000272376; 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; 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; 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 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:RRD75469.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000272376};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RRD75469.1}.
FT DOMAIN 5..127
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1285 AA; 146321 MW; 3BFC625898531A0B CRC64;
MIPYVHLHVH SHYSILDGQA TIERLVDKAI KDGMKGMALT DHGNMMGIKD FFNYTQKLKG
KAQKTLKTCD AKLKALREGT YKTKEGDKSD VGKTTEQLIA ECEKEMEKAQ RVVDFKAIFG
CEMYCARRKK ELKEGRQDQS GWHLVVLAKN KKGYHNLIKL VSRSWIDGFY MRPRTDKHDL
ERFSEGLIVS SACLGGEIPR KILTNDAEGA EEAVLWFKRV FGEDYYLELQ RHEVKDPAVR
ANRGTYPLQI ESNQALIELA KKHGIKYICT NDSHFVDEEN AESHDRLICL STNRFLSDST
RMLYTKQEWF KTQAEMNEVF ADLPEALQNT IEICDKVETY SIDHGPIMPN FEIPEDFGTE
EEYRARFTEE QLFDEFTQDE NGNVVMSREE GEEKIKKLGG YDKLYRIKLE ADYLAKLAYE
GAHWRYGNPL DKETDERIRF ELHIMKTMGF PGYFLIVQDY IKVAREQLDV SVGPGRGSAA
GSAVAYCLRI TDIDPIKYDL LFERFLNPDR ISLPDIDVDF DDDGRGKVLQ WVTEKYGAEK
VAHIITYGTM ATKSALKDVA RVQQLPLNEA NRLCKLIPDK LPEGPDGKSP KMNLNNAIAC
IPELRDAETS ADPLLRDTIR YAKMLEGNVR NTGVHACGII ICRDDISDWV PISTAEDKET
GEKLRCTQYE GSVIEETGLI KMDFLGLKTL SIIREAVENI RFSLGIELDI DNVDIEDPAT
YQLYCDGQTV GTFQFESPGM QKYLRELHPT TFEDLIAMNA LYRPGPMAYI PQFIKRKHGI
EPITYDLDCM EKYLKDTYGI TVYQEQVMLL SRRIADFTRG ESDNLRKAMG KKLIDKLNQM
YPKFVKGGQA NGHDPQVLEK IWEDWKAFAS YAFNKSHATC YSWVAYQTAY LKANFPSQYM
AAVMSRSLNN ITDLTKFLDE CKAMNISCLG PDVNESYHKF SVSHLGNIRF GLGGIKGVGE
NAVQTIIDER NRAGLFVSVY DFFERVNLYV CNRKNLECLA LAGAFDSFGT VSRERFFAET
ETGVTYLETL ITYGQRFQID KEESVNSLFG GEDTVEISKP KPPVSFERWS DLEKLNKERD
LIGIYISGHP LDEYSIVVNH LCTLKMPEIA DLSSWMDQNI TFGGIVTQVE ERISKRGAAF
GRVRMEDYAG GGEFAIFGDE WAQFKGYFAP GNSLFVTAQV TPRRWGNGDP DLHIGKVDWL
SEVKDRKIQS ITIKASLNEL DNRLVTEMID LIQSTHGETV LNFQIVDADS SNHVTLSSPQ
TRINVTKELI RYLNSHQSSL SYTIN
//
