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Database: UniProt
Entry: M7Y1J4_9BACT
LinkDB: M7Y1J4_9BACT
Original site: M7Y1J4_9BACT 
ID   M7Y1J4_9BACT            Unreviewed;      1428 AA.
AC   M7Y1J4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=C943_02659 {ECO:0000313|EMBL:EMS31086.1};
OS   Mariniradius saccharolyticus AK6.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Mariniradius.
OX   NCBI_TaxID=1239962 {ECO:0000313|EMBL:EMS31086.1, ECO:0000313|Proteomes:UP000010953};
RN   [1] {ECO:0000313|EMBL:EMS31086.1, ECO:0000313|Proteomes:UP000010953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK6 {ECO:0000313|EMBL:EMS31086.1,
RC   ECO:0000313|Proteomes:UP000010953};
RA   Vaidya B., Khatri I., Tanuku N.R.S., Subramanian S., Pinnaka A.;
RT   "Genome assembly of Mariniradius saccharolyticus AK6.";
RL   Submitted (JAN-2013) 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:EMS31086.1}.
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DR   EMBL; AMZY02000023; EMS31086.1; -; Genomic_DNA.
DR   RefSeq; WP_008631618.1; NZ_AMZY02000023.1.
DR   STRING; 1239962.C943_02659; -.
DR   eggNOG; COG0587; Bacteria.
DR   InParanoid; M7Y1J4; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000010953; 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   CDD; cd12113; PHP_PolIIIA_DnaE3; 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:UP000010953};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..191
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00479"
FT   DOMAIN          246..313
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1428 AA;  161003 MW;  5D8561829D545892 CRC64;
     MYIIFDTETT GLPRNYDAPM EDLDNWPRLV QIAWQLHDAR GKLLSNHNYI VKPEGFTIPY
     NAEKVHGIST ARALKEGHDL EKVLGIFDED LKKATYVVGH NIGFDINVVG SEFLRKKLPM
     KLRDRKELDT KDLSTDFCAI PGGKGGKFKW PTLTELHHKL FGNGFADAHD AAYDVDATAK
     CFFGLITQRV IQPEKGIPLA EVVYEPPRLD AANFANAKDD TKTAAKEILK AAGTADISQM
     QDLPFTHLHV HTQYSVLQAT SEIPSLIALA KSMNMPAIAM TDHGNMMGAF HFVKEAFSKG
     IKPIIGCEFN LCKDRKNKSQ KDDGYQTVLI AKNKGGYHNL AKLASYANIE GYYYVPRIDK
     ELLVQYKSDL IATTGGLWSE IPYLILNVGD TQAEEAFIWW KEQFGEDFYV ELNRHGIPEE
     EKVNEVLLHF AKKYGVKFFA ANNAYYNQKV DAKAHDILLC VKDGELVEKP KKYIGKRGRE
     FRFGFPNDEF YIKSPEEMKK LFADLPEAIA CTDEIVQKIE SYKLERPVLL PKFDIPDEFK
     DPQDEIDGGK RGENAYLRYL TYEGAKKRYP DLTDEIKERL DFELATIEKT GYPGYFLIVQ
     DFTGEARKMG VSVGPGRGSA AGSAVAYCTG ITNVDPIAYD LLFERFLNPD RVSLPDIDID
     FDDEGRDKVI KYVIDKYGSN QVAQIITYGT MAAKSAIRDT ARVLNLPLAE ADKLAKLVPD
     IKLKALFDLS KDRAKLADKL KGNGEDLSKA EELIRISKGQ DELSKTVNQA TVLEGSVRNT
     GIHACGVIIT PDDITNFVPV ALAKDSDMVC TQFDNSVVES AGLLKMDFLG LKTLTLIKDA
     VKIVKERHGI DLDPDNFPID DAKTYELFQR GETVGIFQYE SPGMQKYMRD LKPTVFADLI
     AMNALYRPGP LEYIPSFVRR KHGQEPITYD LDDMKEYLEE TYGITVYQEQ VMLLSQKLAG
     FTKGEADVLR KAMGKKQKDV LDKMKPKFVE QASAKGHDAQ KLEKIWKDWE AFASYAFNKS
     HSTCYAWIAY QTAYLKAHYP AEYMASVLSN NMNDITQVTF FMEECKRMGI SVLGPDVNES
     KSGFTVNKDG QIRFGLAAIK GAGAAAVEAI IVEREKSGRY QTIFDFCKRV NSRALNKKTL
     EALAMAGSFD CFPQHHRRQY LEAPEGDVTL LEKAVKYAQK VQQESESNQV SLFGGGSGME
     VSLPTVASME PFSQLQQLNI EKEVVGLYIS GHPLDQFRVE IDAFTNTPLP EFADIENLRK
     KSDIKAAGIV TSFAHRTTKT GKPFGTLSME DYHGAHTFFL FGDDYIKFKG YFMTGWFLYL
     SGSVHPNKFK ENEFEFKINM IMLLNEVRGK MVKGLRVNID LDDLSFELME KLEAITQRYR
     GDAKLYINII DSKENITLDL MSKRFTVDPS NEMIKELGRI PEVVYEIV
//
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