ID A0A1W2CAR7_9FLAO Unreviewed; 1443 AA.
AC A0A1W2CAR7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, 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=SAMN06296427_109139 {ECO:0000313|EMBL:SMC82293.1};
OS Moheibacter sediminis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Moheibacter.
OX NCBI_TaxID=1434700 {ECO:0000313|EMBL:SMC82293.1, ECO:0000313|Proteomes:UP000192393};
RN [1] {ECO:0000313|EMBL:SMC82293.1, ECO:0000313|Proteomes:UP000192393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12708 {ECO:0000313|EMBL:SMC82293.1,
RC ECO:0000313|Proteomes:UP000192393};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-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};
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DR EMBL; FWXS01000009; SMC82293.1; -; Genomic_DNA.
DR STRING; 1434700.SAMN06296427_109139; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000192393; 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:UP000192393};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..191
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT DOMAIN 252..325
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1443 AA; 163663 MW; 549E364ED9E8EBB3 CRC64;
MYLIYDTETT GLPNNFNAPV TDSDNWPRMV QIAWQLHDEM GRLLENDNII VKPEGYDIPF
NAAKIHGITT EKANAEGIPL IEALEKFQTV LQKSKVIVGH NINFDQNIVG AEFFRKEFDY
EELNLPLVDT MNVSVDFCAI PGGRGGGFKF PKLGELHEKL FDEKFDEAHN ASADVNATAR
SFMELLRLGI ISQENSGLDT DNYLKFKEIN PNPFKPFAIQ IDKQVADFNQ NLSNELNKLN
IKSGSLTDSP YFHFHNHTSY SILTATTSVE ALIQKAIDEK MPAVGMTDMG NLMAAFKFVS
AIKKANSGLE KPIIPIIGCE LYVAENYTQT KFTKDSPDRR FTQVLLAKNK SGYKNLSKIS
STGYIDGFYS GFPRVGKEVI LNFKENLIAT TGSITGEIPN LILNVGEIQA EEAFVWWKEQ
FGDDFYVELI RHGLDEEEHV NQVLIKFAQK HNVKVIAQNN TFYIKKEDAY AHDILLCVRD
GEKKDTEIGR GRGTRFGFPN DEFYFKSQEQ MKKLFHEIPE AIDNLSELLS KIEPYDLASD
VLLPKFDIPE EFKHAEDEVD NGTRGEMAFL RHITFEGARK RYKEITPDIE ERLTFELDTI
ERTGYPGYFL IVQDFTTQAR NMGVSVGPGR GSAAGSAVAY CVGITNVDPI KYNLLFERFL
NPDRVSLPDI DIDFDDRGRD AIIKWVVDKY GKNQVAQIIT YGTMAGKSAI RDTGRVLNLP
LSDTDRIAKK THLKLNRLLK MEEKALKSGL GSDEFADSME IRKMAEQDTL EGRTIQQACV
IEGSVRNTGI HACGVIITPK DIKELVPVAV SKDAELLVTQ FDNSVVESAG LLKMDFLGLR
TLTIIDDAIR LIEKNHGIKL HPDDIPLDDL KTYELFQKAQ TVAIFQYESP GMQKHMRALK
PDKFDDLIAM NALYRPGPLQ YIPNFIARKN GSEEIIYDLP EMEENLAETY GITVYQEQVM
LLSQKLANFT KGEADVLRKA MGKKQRDVLD KMKPKFLEGG EANNHPVKTL EKIWNDWEAF
AEYAFNKSHS TCYALIGYHT GYLKAHYPAE FMSAVLSNNM SNIKSVTFFM EECRSMGIPV
LGPDVNESEY MFSVNDQGAI RFGMGAVKGV GGGAVESIIR EREENGKYES VFDFVQRIDL
RQANKRTLEN LALAGGFDQY EFHRAQFFYQ EDSTSNLEKL IRYGAAFQEA KDSAQTSLFG
EMAGEIEIVK PHLPDCEEWN SVQKLNKEKE VVGIYISSHP LDDFKDELKF FQGVSLKQLK
ENEDKFVGRE VSIGGMITSA QHKVSAKDGR EFGSFIFEDY ESQYEFVLFG EDYLKFKYFL
QANMFVVLKI MVSERIFKDQ MGNVTMKKRY VNVTRMQLLS DVLESMANKL TIQLNVEDLN
EEIFKDLAEL FSKYQGEKSV LVQLDDVQSQ TKLNVPARNI KVSITKELLS DIREIPNLQF
KLN
//
