ID   A0A1M6KE09_9FLAO        Unreviewed;      1461 AA.
AC   A0A1M6KE09;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=SAMN04487911_12545 {ECO:0000313|EMBL:SHJ57184.1};
OS   Arenibacter nanhaiticus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Arenibacter.
OX   NCBI_TaxID=558155 {ECO:0000313|EMBL:SHJ57184.1, ECO:0000313|Proteomes:UP000184231};
RN   [1] {ECO:0000313|EMBL:SHJ57184.1, ECO:0000313|Proteomes:UP000184231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.8863 {ECO:0000313|EMBL:SHJ57184.1,
RC   ECO:0000313|Proteomes:UP000184231};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FQYX01000025; SHJ57184.1; -; Genomic_DNA.
DR   RefSeq; WP_072765367.1; NZ_FQYX01000025.1.
DR   STRING; 558155.SAMN04487911_12545; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000184231; 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: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:UP000184231};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..192
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00479"
FT   DOMAIN          262..350
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1461 AA;  166163 MW;  4EF674C5CDC5D5AC CRC64;
     MYLIFDTETT GLPKRWDAPY TDTENWPRCI QIAWQLHDSM GNLVESQDYL VQPDGFNIPY
     DAEKIHGIST ELAKEQGVPM AEVLEKFNIA LSRSKFVVGQ NVGFDLNIMG AEFHRFQMAN
     SLHDLPVLDT CTEHTAQLCQ IPGGRGGKFK LPTLTELHQY LFGEPFGEAH NATADVEATT
     RCFLELIRRK EYTIEQLDVA PDYFKNFSEA NPKEIQLIGL KHINLKKASK KIADKLWAQD
     TEAPSKEEIR ENLQSLKETQ FAHLHNHSQF SVLQSTISIS DLVNAAAKDN MPAVALTDHA
     NMMGAFHFVR AVINYNKSVQ AENEAAIAEG KEPEKNEITP IVGCEFFVCE DRLDKTRKDN
     GYQIVLLAKN KKGYHNLAKL SSSAFTEGFY YVPRVDKKII EQYKEDLIVL TGNLYGEVPS
     KVLNVGENQA EEALLWWKEQ FGEDLYVEIM RHNQEDENRV NPVLISLAQK HQVKLVATNN
     TYYVDKKDAN AHDILLCVRD GEKQSTPIGR GRGYRYGLPN QEYYFKSSEE MKSLFKDIPE
     AISNIQEVIG KIETYELARD VLLPKFDIPE EFQHPEDELD GGKRGENAFL RHITYKGAKI
     RYGEITPDIA ERLDFELDVI ENTGYPGYFL IVEDFIREAR KMDVSVGPGR GSAAGSVVAY
     CLWITNIDPI KYNLLFERFL NPDRVSMPDI DIDFDDEGRG RVMDYVIKKY GSNQVAQIIT
     YGTMAAKSSI RDTARVLDLP LFDADRIAKL IPNMSKLNKI FGLDEKGLKE KFRAEELEKV
     HELISLAEGN NLEADTLNLA RRLEGSVRNT GIHACGVIIT PDDITKFVPV ALAKDSDLYV
     TQFDNSVVED AGLLKMDFLG LKTLTLIKDT VKIVKAKHGI LLDPENFPLD DVKTYELFQR
     GETVGVFQYE SPGMQKHMKD LKPTVFDDLI AMNALYRPGP MEYIPSFVRR KHGGEEIEYD
     LPAMEEYLKE TYGITVYQEQ VMLLSQKLAD FTKGEADVLR KAMGKKQIAV LDKMKPKFID
     QASAKGHDAV KLEKIWKDWE AFASYAFNKS HSTCYAWIAY QTAYLKAHYP AEYMAAVLSN
     NMNDIKQVTF FMEECKRMGL EVLGPDVNES FYKFAVNNEG AVRFGMGAVK GVGRGAVETI
     VANREKDGHY RSVFDMAKRI DLRAANKKAF ENLALAGGFD SFGDTHRAQY FHDEGDGVTF
     LEKIMKYGSK YQENENSSQV SLFGDSSDVQ IPEPVIPPAE EWGTMGKLRR EKEVVGIYIS
     GHPLDDFKTE IKAFCNANIT AVANMEEHVG RELSFAGVIS DVQHRVSKNG KGWASFIVED
     YTDSLEFRMF GEEYLRFRHF LTINSFVYFK VFIKEGWMNR DTGKKGEPRM QFNTVMMLQD
     IMEAYAKKLT IKIDITQLKE EGVRDLKNIM DAHQGSHPLS FIVYEMEEKI KVNLSCRKQK
     IQISSELLLQ LNEKDVHYKL N
//