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Database: UniProt/TrEMBL
Entry: L0IW00_9MYCO
LinkDB: L0IW00_9MYCO
Original site: L0IW00_9MYCO 
ID   L0IW00_9MYCO            Unreviewed;       515 AA.
AC   L0IW00;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   25-OCT-2017, entry version 36.
DE   RecName: Full=Probable DNA ligase {ECO:0000256|HAMAP-Rule:MF_00407};
DE            EC=6.5.1.1 {ECO:0000256|HAMAP-Rule:MF_00407};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000256|HAMAP-Rule:MF_00407};
DE   Flags: Precursor;
GN   Name=lig {ECO:0000256|HAMAP-Rule:MF_00407};
GN   ORFNames=Mycsm_02145 {ECO:0000313|EMBL:AGB22502.1};
OS   Mycobacterium sp. JS623.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB22502.1, ECO:0000313|Proteomes:UP000010844};
RN   [1] {ECO:0000313|Proteomes:UP000010844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A.,
RA   Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL   Submitted (OCT-2011) 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:0000256|HAMAP-Rule:MF_00407}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|HAMAP-Rule:MF_00407,
CC       ECO:0000256|RuleBase:RU000617}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00407};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00407, ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; CP003078; AGB22502.1; -; Genomic_DNA.
DR   RefSeq; WP_015306084.1; NC_019966.1.
DR   EnsemblBacteria; AGB22502; AGB22502; Mycsm_02145.
DR   KEGG; msa:Mycsm_02145; -.
DR   PATRIC; fig|710686.3.peg.2162; -.
DR   KO; K10747; -.
DR   OrthoDB; POG091H0BGA; -.
DR   Proteomes; UP000010844; 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; -; 2.
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 {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010844};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617, ECO:0000313|EMBL:AGB22502.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617}.
FT   DOMAIN      292    416       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    215    215       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     213    213       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     220    220       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     235    235       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     264    264       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     304    304       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     376    376       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     382    382       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   515 AA;  54837 MW;  5B83E7CE1D17DCFE CRC64;
     MQLIDVAAAS AEVGATSARL AKIARIADLL RHAGAEEDAK LVAVVVSWLS GELPQRQIGV
     GWAALRSLPS PAAEPSLTVR QVDASFSEIG LVAGKGSQAR RAELVNAVFA AATEPEQTFL
     RRLLSGELRQ GALVGVMADA VAKAANIAAS VVRRAAMLGG DLPAVAAAAL TGDETALEQF
     TLKVGQPVGP MLAQTATGVG EALERLGGTA VLEAKLDGAR VQIHRAGDAV SIYTRSLDDV
     TERLPEVVEA TLALPVTDLI ADAEAIALRP DGRPHRFQET ASRFGRRVDI AKARETQPLS
     VFVFDLLHLD GEDLLDRPAS ERVAALDAIV PKAHRVDRLI TDDAEAAQRF LDITLDAGHE
     GVMAKSLTAP YEAGRRGAGW LKVKPVHTLD LVVLGVEWGS GRRTGKLSNI HLGARDPATG
     GFVMLGKTFK GMTDAMLEWQ TTRFMELADG PTDGYVVKVR PEQVVEIAFD GVQGSTRYPG
     GMALRFARVL RYRDDKSPAE ADTIDTVRAF YERGS
//
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