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Database: UniProt/TrEMBL
Entry: J9R234_RIEAN
LinkDB: J9R234_RIEAN
Original site: J9R234_RIEAN 
ID   J9R234_RIEAN            Unreviewed;      1550 AA.
AC   J9R234;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=B739_1256 {ECO:0000313|EMBL:AFR35854.1};
OS   Riemerella anatipestifer RA-CH-1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Riemerella.
OX   NCBI_TaxID=1228997 {ECO:0000313|EMBL:AFR35854.1, ECO:0000313|Proteomes:UP000006276};
RN   [1] {ECO:0000313|EMBL:AFR35854.1, ECO:0000313|Proteomes:UP000006276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA-CH-1 {ECO:0000313|EMBL:AFR35854.1,
RC   ECO:0000313|Proteomes:UP000006276};
RA   Chun C.A., Shu W.M., Kang Z.D., Jia W.X.;
RT   "Riemerella anatipestifer vaccine strains.";
RL   Submitted (SEP-2012) 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};
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DR   EMBL; CP003787; AFR35854.1; -; Genomic_DNA.
DR   RefSeq; WP_014938188.1; NC_018609.1.
DR   STRING; 34085.AB406_0520; -.
DR   KEGG; rag:B739_1256; -.
DR   PATRIC; fig|1228997.3.peg.1252; -.
DR   HOGENOM; CLU_001600_1_0_10; -.
DR   Proteomes; UP000006276; Chromosome.
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; cd06127; DEDDh; 1.
DR   CDD; cd04485; DnaE_OBF; 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   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
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; PF00929; RNase_T; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-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:UP000006276};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..191
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00479"
FT   DOMAIN          249..349
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1550 AA;  177013 MW;  5F8C81121DC038DE CRC64;
     MYLIFDTETT GLPKNFNAPL SDSDNWPRMV QIAWQLHDEE GNLVENQDYI IKPEGYDIPF
     NATRIHGIST KMAHEQGRDL VEVLEEFREV LKKTKIVAGH NIEFDYNIVG AEFYRKSIEN
     VLEKIPSADT MALGTDYCQL GGGRNGKYKP PKLEELYEKL YGEKFDEAHN AAADVNATAQ
     VFFEMMRVGI IPAETLKISE EQLKVYQENH PSPIRPFAIV IRRQVEDFNK KKKRTDFGDI
     SEIELGDYFN FHNHSIFSSL QSTTSIGDLI DKAKNNQFPA VGMVDLGNMM GAFKFVSDVE
     KYNSGVKKAH QEYLVNKQKA EEEGADFNEN APESKELMAV LGCEFYISDR PEQKQFTKDD
     PDRRTNVVLL AKNFNGYKNL AKLSSLGYVN GFYFGVPRVS REMVAQYKED VIAVTSGIYG
     DIPDAILNFG EQKGEERFKW WKETFGGDFY VQLQNHGLQE EEHLNEVLLD FADKYDVKIL
     AQNETFYTDK SDANIQDIVS CIKDGEKLST PVGKGFGKRK GLRSQEFYIK DAEELKQCFR
     QYPDAFEAYT ELLSKFEPYT LKRDVLLPKF DIPKEFQSEE DLKDGGKRGE NAYLRYLTYE
     GAKKRYDEIT DDIRERLDFE LEIIANTGYP GYFLIVQDFC NEARKMGVWV GPGRGSAAGS
     AVAYCIGITN VDPIKYDLLF ERFLNPERIS MPDIDIDFDD EGRDRIIKWV IDKYGKSNVA
     QIITYSVLGG KSAIKDAGRV LDVPIPETNN IAKLVPSVPG MNIAKALSKY DKLKDEDKVL
     VDEMKAVLDN PNDQRFPVLD SAKKMEGCIR NTGIHACGVI ITPEDISNLV PISIAAKDAD
     ILVSQFDNSV AESAGLLKMD FLGLRTLTII KDALKLVKER HGIDINPDEI SLDDAKTYQL
     FKEGRTIGIF QYESPGMQKY MRELKPTVFA DLIAMNALYR PGPIKYIPNF INRKHGIEEI
     IYDLPETEEY LKETYGITVY QEQVMLLSQK LANFTKGEAD TLRKAMGKKQ IDVLNKMYPK
     FIEGGKKNNL DEEKLNKIWN DWKAFAEYAF NKSHSTCYAL IAYQTAFLKA NYPAEYMASV
     MSNNINNTAQ ITMFMEDCRA MGVDVLGPDV NESQYKFSVN DKGQIRFGLG AIKGIGEGPS
     EAISQERVKG KFKNIYDFFE RVTPSQVNKR VVESLVMAGA FDEVDTYHRA QYFDIDNSGK
     TNIEKLIRYG QSFQESKNEV ENSLFADFAE EIQIEQPKIA PAMEWQNMHK LNKEKEIIGF
     YLSAHPLDEY KYQFRFIQGE LSKKEVLSQK DEILEELQSI PKESVLIEDT EDEPDLAVDL
     DLVEGEDGEI MEEEVKNVEP KGSFNFLNLD EVEAFKDSIA GSINPNLFSE KEAWKELRKI
     NDAAKEYTVA GLITEYTIRD GKNSGEKIAF LTLEDYSGSY GFRLGDRDYM RLREKLALQR
     FVIVKIKMVI SKDGRVFVNI NEVIDLKDAF EKYAKSLSIV ADITDIRRAD IDFFQNDLLS
     HQGEHKLSFY LKNPNDETEL ELPSIQKKIN ISAELLYKIQ QYNKYQIFLN
//
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