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Database: UniProt
Entry: A0A3S0AGJ4_9FLAO
LinkDB: A0A3S0AGJ4_9FLAO
Original site: A0A3S0AGJ4_9FLAO 
ID   A0A3S0AGJ4_9FLAO        Unreviewed;      1478 AA.
AC   A0A3S0AGJ4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   13-SEP-2023, entry version 21.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=EHW67_01490 {ECO:0000313|EMBL:RTE55266.1};
OS   Arenibacter aquaticus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Arenibacter.
OX   NCBI_TaxID=2489054 {ECO:0000313|EMBL:RTE55266.1, ECO:0000313|Proteomes:UP000267585};
RN   [1] {ECO:0000313|EMBL:RTE55266.1, ECO:0000313|Proteomes:UP000267585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GUO666 {ECO:0000313|EMBL:RTE55266.1,
RC   ECO:0000313|Proteomes:UP000267585};
RA   Guo J., Sun J.;
RT   "Arenibacter aquaticus sp.nov., a marine bacterium isolated from surface
RT   seawater in the South China Sea.";
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:RTE55266.1}.
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DR   EMBL; RQPJ01000001; RTE55266.1; -; Genomic_DNA.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000267585; 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; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
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   ECO:0000313|EMBL:RTE55266.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RTE55266.1}.
FT   DOMAIN          1..192
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00479"
FT   DOMAIN          262..367
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1478 AA;  167728 MW;  CCAAE10674F63A42 CRC64;
     MYLIFDTETT GLPKRWDAPY TDTDNWPRCI QIAWQLHDDM GRVIESQDYL VQPDGFNIPY
     DAEQIHGIST ELAQQDGVPI GEVLEKFNAA LSKTKFVVGQ NVGFDLNIMG AEFHRYEVEN
     SLQELPVLDT CTEHTAQLCQ IPGGRGGKFK LPTLTELHQY LFGEPFGEAH NATADVEATT
     RCFLELVRRK EYTAEQLDVG PDYFKNFSEA NPQEIQLIGL KHINLKKASK KIADALWEKD
     TGGISKEEIK ENLATLETAN FAHLHNHTQF SILQSTMSIP ALISATAKAK MPAVAMTDHA
     NMMGAFHFVN GVINHNKGVV ARNEENLKRY EATKNGTLEE GQEPLEELPE PEVEITPIIG
     CEFQVCEDHT NKSQKDNGYQ IVMLAKNKRG YLNLAKMSSI AFVDGKYYVP RIDKKVIEQY
     KEDIIVLTGN LYGEVPSKVL NVGENQAEEA LIWWKETFGD DLYIEIMRHG QEDEDRVNQV
     LLKFAEKHNV KLVATNNTYY QEKADAHAHD ILLCVKDGEK QATPIGRGRG YRYGLPNQEY
     YFKSSEEMKE LFKDIPEAIT NIQEVIDKVE TFTLARDVLL PAFDIPEEFR FEEDKLDGGK
     RGENKYLRHI TYEGAKKRYG EITPEIDERL DFELKVIEKT GYPGYFLIVE DFIRAAREMD
     VSVGPGRGSA AGSAVAYCLW ITNLDPIKYD LLFERFLNPD RVSMPDIDID FDDEGRGRVM
     DYVIDKYGAN QVAQIITYGT MAAKSSIRDT ARALDLPLGD ADRMAKLIPN MSKLKKIIGV
     DEKKLKEKFN SEEIAKINEL LAISEGDDLE SETLNQAYVL EGSVRNTGIH ACGVIITPDD
     ITKFVPVALA KDSDMYCTQF DNSVVESAGL LKMDFLGLKT LTLIKDTVKI VKAKHGVELD
     PENFPLDDQK TYELFQRGET VGVFQYESPG MQKHMRSLKP TVFADLIAMN ALYRPGPMEY
     IPSFIARKHG TEEIVYDLEA CEEYLAETYG ITVYQEQVML LSQKLADFTK GEADVLRKAM
     GKKQKHVLDK MKPKFIEQAS KKGHAVDKLE KIWKDWEAFA AYAFNKSHST CYAWIAYQTA
     YCKAHYPAEY MAAVLSNNMN DIKQVTFFME ECKRMGLDVL GPDVNESYYK FAVNDAGAVR
     FGMGAVKGVG RGAVETIVEN RKEGGPFKSV FDLAKRIDLR AANKKAFENL AVAGGFDSFG
     DTHRAQYFYE EGDGITFLEK AMKYGAKFQE NENSSQVSLF GEASEVQIPE PVVPPCEEWG
     TMEKLRREKE VVGIYISGHP LDDFNAEIKA FCNASLSNLN DLEAIVNREV SFAGVITDVQ
     HRVSKNGKGW AMFTMEDYTD SFEFRMFGEE YLKYRHFLMI NSFAYVKVFV REGWVNRDTG
     KKGDPRMQFN MIMMLQDVME TFAKKLTIKL DIAQLREENI LELKDTLVSH QGNHPLSFVV
     YEMEEQIKVN MTSRKQKIHI SSELLLELNK QDVLYKLN
//
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