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Database: UniProt/SWISS-PROT
Entry: DNLI_DICT6
LinkDB: DNLI_DICT6
Original site: DNLI_DICT6 
ID   DNLI_DICT6              Reviewed;         582 AA.
AC   B5YD88;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   10-OCT-2018, entry version 66.
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=DICTH_0616;
OS   Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12).
OC   Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX   NCBI_TaxID=309799;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35947 / DSM 3960 / H-6-12;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Dictyoglomus thermophilum strain ATCC
RT   35947 / DSM 3960 / H-6-12.";
RL   Submitted (AUG-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; CP001146; ACI19645.1; -; Genomic_DNA.
DR   RefSeq; WP_012548277.1; NC_011297.1.
DR   ProteinModelPortal; B5YD88; -.
DR   SMR; B5YD88; -.
DR   STRING; 309799.DICTH_0616; -.
DR   PRIDE; B5YD88; -.
DR   EnsemblBacteria; ACI19645; ACI19645; DICTH_0616.
DR   KEGG; dth:DICTH_0616; -.
DR   eggNOG; ENOG4107TRG; Bacteria.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG091H09SJ; -.
DR   BioCyc; DTHE309799:G1GCP-594-MONOMER; -.
DR   Proteomes; UP000001733; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-UniRule.
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; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
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; IPR036599; DNA_ligase_N_sf.
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.
FT   CHAIN         1    582       Probable DNA ligase.
FT                                /FTId=PRO_0000365219.
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;  66791 MW;  5AB0045336097A03 CRC64;
     MLFGELAQYF ERIEKTTKRN EMMEILADLF RKVDKEEIDK IIYLLNGRVA PDYEKIEFGM
     SDKLVLRAMA LALKIPLLEL ERSYKEVGDL GELVVKYSKN EGKDLTVVET FNTLYDIANL
     SGEGSVDAKV NRLAFLINSL TPQGGKYLVR IVLGKLRLGV GEPTIMDALS FAKVKDKGLR
     PFIERAFNIT SDLGYVAKVF WEGGVEALKR IKVQVGRPIR MALAERVSRA EEIIKRLGKC
     AVEPKFDGFR CQIHKKENSV RIFSRNLEDN TYMFPDLVEA VLKQFPDRDV IIEGEAISYN
     PETGEFYPFQ VTVQRKRKYN ISEMVELYPL QLFAFDILYL DGEDTTSLPY IRRRQKLEEA
     LVEGEKISIT KNIITNDPKE IQSFFEECIT EGLEGIVAKR LDAPYQAGMR NFNWIKLKRS
     YQGHLADTVD CVILGYFKGR GHRAKFGIGA LLVGVYDDER DLFKTIAKIG TGPTEEEWVK
     FREILDEIKV EKRPNNVESF IEPDVWVEPK YVVVVQADEI TRSPVHTCGR ELDGLGYALR
     FPRVQGFVRE DKGPYDATTV KEILEMFRNQ KKEKVEEDSD LL
//
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