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Database: UniProt
Entry: A0A257KCY8_9FLAO
LinkDB: A0A257KCY8_9FLAO
Original site: A0A257KCY8_9FLAO 
ID   A0A257KCY8_9FLAO        Unreviewed;      1018 AA.
AC   A0A257KCY8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=CFE24_03315 {ECO:0000313|EMBL:OYU85166.1};
OS   Flavobacterium sp. BFFFF2.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2015558 {ECO:0000313|EMBL:OYU85166.1, ECO:0000313|Proteomes:UP000216176};
RN   [1] {ECO:0000313|EMBL:OYU85166.1, ECO:0000313|Proteomes:UP000216176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFFFF2 {ECO:0000313|EMBL:OYU85166.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) 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:OYU85166.1}.
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DR   EMBL; NKJD01000006; OYU85166.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257KCY8; -.
DR   Proteomes; UP000216176; 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; cd07431; PHP_PolIIIA; 1.
DR   Gene3D; 1.10.150.870; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR011708; DNA_pol3_alpha_NTPase_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   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   Reference proteome {ECO:0000313|Proteomes:UP000216176};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..68
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
FT   REGION          993..1018
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1018 AA;  117273 MW;  636DB7A084CE3927 CRC64;
     MYLNCHSFHS LRFGTIPLDD LVAQAVGYGV TAMALTDLNT VTGIYDFIKA CKKVGIKPLV
     GIDFRNNGKQ LYIGLAKNRA GLAEMNRLVT KHHFENTLLP EVAPPFDHVF VIYPFNNVPD
     ELKEHEFIGI GADQLPKLYN YVWKRRISKM VILHSVTYRT KKEFNLHKIL RAIDLNIIGS
     KLTEADYCKV SEVMIPIDQL LQRFNDFPQI IQNTEAIIAG CHFEYDFYTP KNKKHFTGNS
     QDDMELLTKL AYEGMIRRYG AEHAEAKARV EKELKVIHEL AFSGYFLITW DIIQYSLNKG
     FLHIGRGSGA NSIIAYCLDI TNICPLELDL YFERFLNVNR KTPPDFDIDW SWRERDTILT
     YIFDKYGQDH VAFCGTNVEF KYRSIFREVG KVFGLPKEEL DELAKKPMKK HHKNNVVMMV
     QDYGMMLEKY PNQRSMHSCG IIISEEPITH FTALEMPPKG FPIVQFDMHV AEDIGFDKFD
     ILSQRGIGHI DDTVKLIREN QGIEVDIRDT SISKDEPTCN ELLSQGKTIG CFYIESPAMR
     GLLRRLKCDN YKVLVAASSI IRPGVAQSGM MKEYIFRHNH PDRFEYFHEV FKEQLGETYG
     IMVYQEDVIK IALHYGGLPA ADGDILRRAM SGKGRSKAAL QKVKDDFFTS CAKQGHPLAL
     SQEIYRQIES FAGYSFCKAH SASYAVESYQ SLYLKTYYPI EFMTAVINNF GGFYRTEVYI
     HEARMSGAKI NSPCVNKSDY QTKVYGKNIY LGFQHLKSLE SKTAELITKE RAENGPFNSL
     EDFINRIPIG IEAIQILIFI GAFRFTRKPK NELLIIARLI LINFRPENRD LLLLQEPVKE
     YQLPVLERSP FEDAFDEIEL LDFPVSVTPF NLLQTRYRGD VMAKDLTKHH KKTVKMLAYL
     ISRKHVPTKR GDMFFGTWID AEGAFFDTAH FTDSLQKYPF KGGGCYLLLG QVEVDYHFPT
     VTISKMEKMP FIPDPRYSAT DEKRFQTQQQ IREDVSLTHR APYPQEHEIG LPRQKMKP
//
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