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Database: UniProt
Entry: A0A1I7AME4_9FLAO
LinkDB: A0A1I7AME4_9FLAO
Original site: A0A1I7AME4_9FLAO 
ID   A0A1I7AME4_9FLAO        Unreviewed;      1453 AA.
AC   A0A1I7AME4;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=SAMN05216474_2225 {ECO:0000313|EMBL:SFT76045.1};
OS   Lishizhenia tianjinensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Crocinitomicaceae; Lishizhenia.
OX   NCBI_TaxID=477690 {ECO:0000313|EMBL:SFT76045.1, ECO:0000313|Proteomes:UP000236454};
RN   [1] {ECO:0000313|EMBL:SFT76045.1, ECO:0000313|Proteomes:UP000236454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7005 {ECO:0000313|EMBL:SFT76045.1,
RC   ECO:0000313|Proteomes:UP000236454};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FPAS01000003; SFT76045.1; -; Genomic_DNA.
DR   STRING; 477690.SAMN05216474_2225; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000236454; 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:UP000236454};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..192
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00479"
FT   DOMAIN          257..345
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1453 AA;  165504 MW;  4AEC742977AB7DC3 CRC64;
     MYIIFDTETT GLPRNWNAPI TDTDNWPRCI QIAWQLHDDM GRLIEAKDYL VKPDGFDIPY
     DAERIHGIST ELAMEQGEDL DMVLKEFNVA LSKAKFVVGQ NVGFDVNIMG CEFYRQSVDS
     PMAEMPVLDT CTEITANLCK IPGGRGGKFK LPTLTELHEF LFQQPFAEAH NATADVEATT
     RCFFELIRRE VFTEEELQVE RNYFDNFITV NPNMIEGVGL THLNLKEESA KLKTDTSSVS
     KAEIKEGLEK LEGVNFTHLH NHSQFSILQS TTDIKGLIAK AASLDMPAVA LTDTGNMMAA
     FHFEKYITEH NNKIKAERAA AEEKGEPYTK TELMPIIGCE FNVCRDHLDK SNKDNGYQIV
     LLAKNKRGYH NLAKMASIAF TDGMYYVPRI DKNVVEKYKG DIICLTGNLY GEVPSKILNV
     GEAQAEEALV WWKEQFQDDF YIELMRHGQE DEDRVNETLL KFAETHDVKV VATNNTFYLE
     KEDAKSHDIL LCVKDGELRD TPKGRGRGFR FGLDNDEYYF KTADEMKEVF ADIPEAIINT
     NEIVAKIEHY HLAMDVLLPA FDIPEEFLDE RDKEDGGKRG ENNYLRHLTY EGAKQRYEEI
     TDEIRERLDF ELSIIAKTGY PGYFLIVQDF CNASREMGVS VGPGRGSAAG SAVAYCTGIT
     NVDPIKYDLL FERFLNPDRV SMPDIDIDFD DEGRGRVIQW VIDKYGANQV AQIITYGTMA
     AKSAVRDTSR VMDLSLFDAD RIAKLIPDLS LAKMFNLTDE QLAEKLKNNQ EDIQRVMEFR
     ALAEGNDLTG EVIQQARKLE GTIRNTGIHA CGVIITPSDI TDYVPVARAK DSELYCTQYD
     NSVAEEAGLL KMDFLGLKTL TLIKDAIRHV KDRHGIDLVA DDFPLDDEKT YELFQRGETV
     GVFQYESPGM QKYMKDLKPT VFADLIAMNA LYRPGPLEYI PSFIRRKHGE EEIVYDLDAC
     KEYLEETYGI TVYQEQVMLL SQSLAGFTKG EADTLRKAMG KKKLDLLAKL KPKFLDQGNE
     RGHDRDKLDK IWRDWEAFAS YAFNKSHSTC YAWVAYQTAY LKAHYPAEYM ASVLSNNMND
     LKQVTFFMEE CKRMGVEVLG PDINESDYKF TVNKQGAIRF GLGAIKGVGS GPVNAIKTER
     EENGPFRDIF DLTKRINLRL CNKKAFESLA LAGGFDSFKN IHRAQYFIED NGKTFLETAI
     KFGANYQENE NSAQASLFGE ASGTEIPAPQ VPHAEEWTSM YKLNREREVV GIFISGHPLD
     DYRLDIESFC NGNVGMLNEM EKHANKEVSI ACIITECEER RTKRNDPFGT LLIEDYNDSH
     KLFLWREDFL KWKSFMTNGL FVCIKGNIVP HRYRAGEFNF QISAIEMLSE MRKKKAKSLD
     LRISTKSVDQ RLIDEVYKLF NDNVGTTPIK FKIYDTAHNM EVEMPSRSVR VDLTDELVKS
     LKEYDMEVTL SDK
//
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