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Database: UniProt/SWISS-PROT
Entry: DNLI_MYCUA
LinkDB: DNLI_MYCUA
Original site: DNLI_MYCUA 
ID   DNLI_MYCUA              Reviewed;         513 AA.
AC   A0PTC0;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   07-JUN-2017, entry version 81.
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=MUL_3413;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L.,
RA   Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C.,
RA   Jones L.M., Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
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; CP000325; ABL05589.1; -; Genomic_DNA.
DR   ProteinModelPortal; A0PTC0; -.
DR   SMR; A0PTC0; -.
DR   EnsemblBacteria; ABL05589; ABL05589; MUL_3413.
DR   KEGG; mul:MUL_3413; -.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG091H0BGA; -.
DR   Proteomes; UP000000765; 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; 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; 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    513       Probable DNA ligase.
FT                                /FTId=PRO_0000365233.
FT   ACT_SITE    217    217       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     215    215       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     222    222       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     237    237       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     266    266       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     378    378       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     384    384       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   513 AA;  53686 MW;  E9004DEE06F58F4C CRC64;
     MLLIDIASTS LNVGGTSSRL AKVARIAEPL RAAAPDPELV AIVVAWLSGE LRQRQIGVGW
     ATLRSPPAAA GSPALTVTGT DAAFSEIGAV SGKGSAARRR ELITRLFAAS TETEQAFLVR
     LLSGELRQGA LAGIMVDAVA RAAEVPATAV QRAAMLGGDL PTVAAACLAA GSSGAAGALD
     SFTLRVGRPI GPMLAQSAGS ITDALERHGG ATIFEAKLDG ARVQIHRTGD EVTVYTRSLD
     DVTARLPEVV QATLALPVSD LVADGEAIAL QPDGRPHRFQ VTASRFGRSV NVAAAQAKQP
     LSVFFSDILH RDGRDLLDAP TTDRLAALDA VVPARHRVDR LTTADAAAAT DFLRATLAAG
     HEGVMAKSPT APYLAGRRGA GWLKVKPVHT LDLVVLAVEW GSGRRRGKLS NIPLGARDAA
     TGEFVMLGKT FKSMTDAMLD WQTARFTELA VGGTDGYVVA LRPEQVVEVA FDGVQASSRY
     PGGLALRFAR VVRYRDDKGP ADADTIDTVR ALY
//
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