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Database: UniProt/SWISS-PROT
Entry: DNLI_METMJ
LinkDB: DNLI_METMJ
Original site: DNLI_METMJ 
ID   DNLI_METMJ              Reviewed;         548 AA.
AC   A3CWP1;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-OCT-2017, entry version 74.
DE   RecName: Full=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=Memar_1865;
OS   Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales;
OC   Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=368407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX   PubMed=21304656; DOI=10.4056/sigs.32535;
RA   Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA   Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S.,
RA   Hauser L., Land M., Lucas S., Richardson P., Whitman W.B.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Methanoculleus marisnigri Romesser et al.
RT   1981 type strain JR1.";
RL   Stand. Genomic Sci. 1:189-196(2009).
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; CP000562; ABN57791.1; -; Genomic_DNA.
DR   RefSeq; WP_011844700.1; NC_009051.1.
DR   ProteinModelPortal; A3CWP1; -.
DR   SMR; A3CWP1; -.
DR   STRING; 368407.Memar_1865; -.
DR   EnsemblBacteria; ABN57791; ABN57791; Memar_1865.
DR   GeneID; 4846179; -.
DR   KEGG; mem:Memar_1865; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; ETVCNIG; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000002146; Chromosome.
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; IEA:UniProtKB-EC.
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-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; 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    548       DNA ligase.
FT                                /FTId=PRO_0000365255.
FT   ACT_SITE    246    246       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     244    244       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     251    251       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     266    266       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     295    295       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     334    334       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     405    405       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     411    411       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   548 AA;  61157 MW;  3544373E6F328D03 CRC64;
     MQFLEFAQVC EHLEGTPGRL DMIEQVAAVL PRLDDEELPV FVRFVMGRVF PDWSTKKLGV
     GPNLLYDAVA YVVGTKRETV REAINTTGDV GLAVEGLLAR KEQTSFFIQE LDLLDVYREL
     ERMAAAEGQR SQREKLRVAQ GLFGNARPLE GRYLARLLLE ELRIGMGEGN VRDAVAKAFE
     LDVRLVEHAH QALNDLGEVA LLARRDPDAL SGVTIEPFRP VKMMLAQAGT IAAQIEDHGE
     VAVEYKYDGS RFQFHKVGDV CRIYSRRLED VTESLPDIAN LLLEATDHDV ILDGEAVAVR
     DGKPMPFQYV IRRFRRKHEV DSMMEKIELV PMVFDILYLD GETLMDRPLA ERRKALDEVL
     GAHVAPQFPA TDAAAAEAIY AEALDLGHEG VMVKVLDSPY TPGVRGRLWV KVKPGVETLD
     LVVVGAEWGE GRRAGTFGSF LLAVQDQGRL LPVGKVATGI TDEVLAELYA LFKDRVIARS
     GKEVTLEPEV VFEVGYSEIQ TSPNYESGYA LRFPRFVRVR EDKSVDETET LDSLAERYGR
     QRNGQGSL
//
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