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Database: UniProt
Entry: B8DZX8
LinkDB: B8DZX8
Original site: B8DZX8 
ID   DNLI_DICTD              Reviewed;         582 AA.
AC   B8DZX8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 57.
DE   RecName: Full=Probable DNA ligase {ECO:0000255|HAMAP-Rule:MF_00407};
DE            EC=6.5.1.1 {ECO:0000255|HAMAP-Rule:MF_00407};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000255|HAMAP-Rule:MF_00407};
GN   Name=lig {ECO:0000255|HAMAP-Rule:MF_00407};
GN   OrderedLocusNames=Dtur_0780;
OS   Dictyoglomus turgidum (strain Z-1310 / DSM 6724).
OC   Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX   NCBI_TaxID=515635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z-1310 / DSM 6724;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Mead D.;
RT   "Complete sequence of Dictyoglomus turgidum DSM 6724.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC       {ECO:0000255|HAMAP-Rule:MF_00407}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000255|HAMAP-Rule:MF_00407}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00407};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00407}.
DR   EMBL; CP001251; ACK42061.1; -; Genomic_DNA.
DR   RefSeq; WP_012583146.1; NC_011661.1.
DR   RefSeq; YP_002352675.1; NC_011661.1.
DR   SMR; B8DZX8; -.
DR   STRING; 515635.Dtur_0780; -.
DR   EnsemblBacteria; ACK42061; ACK42061; Dtur_0780.
DR   GeneID; 7082068; -.
DR   KEGG; dtu:Dtur_0780; -.
DR   eggNOG; ENOG4107TRG; Bacteria.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   InParanoid; B8DZX8; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG091H09SJ; -.
DR   Proteomes; UP000007719; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IBA:GO_Central.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   HAMAP; MF_00407; DNA_ligase; 1.
DR   InterPro; IPR022865; DNA_ligae_ATP-dep_bac/arc.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    582       Probable DNA ligase.
FT                                /FTId=PRO_1000189919.
FT   ACT_SITE    245    245       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     243    243       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     250    250       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     265    265       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     295    295       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     335    335       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     410    410       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     416    416       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   582 AA;  66609 MW;  8F52513B1C69AED3 CRC64;
     MLFGELAQYF EKIEKTTKRN EMMEILADLF KRVDKEEIEK IIYLLNGRVA PDYEKIEFGM
     SEKLVLRAMA LALKVPIFDL EKVYKEVGDL GELIIKYSQN EGKDLTVVET FNTLFEIANL
     SGEGSVDAKV NRLAFLINSL TPQGGKYLVR IVLGKLRLGV GEPTVMDALS FAKVKDKSLR
     PFIERAFNIT SDLGYVAKVF WEGGIEALKK IKVEVGKPIR MALAERVSKV EEIVKRLGKC
     AIEPKFDGFR CQIHKKENNV RIFSRNLEDN THMFPDLVEA VLKQFSDKNV IIEGEAISYN
     PETGEFYPFQ VTVQRKRKYN ISEMVELYPL QLFAFDILYL NGEDITSLPY IRRRQKLEEA
     ISEGEKIFVT KNIITNDPKE IQAFFEECIT EGLEGIVAKR LDAPYQAGIR NFNWIKLKRS
     YQGHLADTVD CVILGYFKGR GHRAKFGIGA LLVGVYDDER DLFKTVAKIG TGPTEEEWVR
     FREVLDEIKL ESKPNNVESL IEPDVWVEPK YVVVIQADEI TRSPVHTCGR ELDGLGYALR
     FPRVIGFVRE DKGPYDATTV KEILEMFRGQ KKEKVEEDSD NL
//
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