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Database: UniProt/TrEMBL
Entry: J9WI19_MYCIP
LinkDB: J9WI19_MYCIP
Original site: J9WI19_MYCIP 
ID   J9WI19_MYCIP            Unreviewed;       509 AA.
AC   J9WI19;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   28-MAR-2018, entry version 32.
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};
GN   Name=lig {ECO:0000256|HAMAP-Rule:MF_00407};
GN   ORFNames=MIP_05705 {ECO:0000313|EMBL:AFS15833.1};
OS   Mycobacterium indicus pranii (strain DSM 45239 / MTCC 9506).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1232724 {ECO:0000313|EMBL:AFS15833.1, ECO:0000313|Proteomes:UP000007329};
RN   [1] {ECO:0000313|EMBL:AFS15833.1, ECO:0000313|Proteomes:UP000007329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MTCC 9506 {ECO:0000313|EMBL:AFS15833.1};
RX   PubMed=17912347; DOI=10.1371/journal.pone.0000968;
RA   Ahmed N., Saini V., Raghuvanshi S., Khurana J.P., Tyagi A.K.,
RA   Tyagi A.K., Hasnain S.E.;
RT   "Molecular analysis of a leprosy immunotherapeutic bacillus provides
RT   insights into Mycobacterium evolution.";
RL   PLoS ONE 2:E968-E968(2007).
RN   [2] {ECO:0000313|EMBL:AFS15833.1, ECO:0000313|Proteomes:UP000007329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45239 / MTCC 9506 {ECO:0000313|Proteomes:UP000007329};
RX   PubMed=22965120; DOI=10.1093/nar/gks793;
RA   Saini V., Raghuvanshi S., Khurana J.P., Ahmed N., Hasnain S.E.,
RA   Tyagi A.K., Tyagi A.K.;
RT   "Massive gene acquisitions in Mycobacterium indicus pranii provide a
RT   perspective on mycobacterial evolution.";
RL   Nucleic Acids Res. 40:10832-10850(2012).
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; CP002275; AFS15833.1; -; Genomic_DNA.
DR   RefSeq; WP_014942709.1; NC_018612.1.
DR   EnsemblBacteria; AFS15833; AFS15833; MIP_05705.
DR   KEGG; mid:MIP_05705; -.
DR   PATRIC; fig|1232724.3.peg.3870; -.
DR   KO; K10747; -.
DR   BioCyc; MIND1232724:G1HA1-3864-MONOMER; -.
DR   Proteomes; UP000007329; 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 {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:UP000007329};
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:AFS15833.1};
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      290    414       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    213    213       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     211    211       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     218    218       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     233    233       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     262    262       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     302    302       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     374    374       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     380    380       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   509 AA;  53533 MW;  CCBD8ABDD5DF5F4D CRC64;
     MLLLDVAKAS TDVGSTSSRL RKVAHIADLL ARAAPDPALV MIVVSWLSGE LRQRQIGVGW
     AALRSRPPPA SHATLTVGAV DATFSEIGAV SGKGAQARRA ALLTTLFAAA AEAEQTFLLR
     LLGGELRQGA LAGIMADAVA KAAGIPAAAV QRAAMLGGDL PAVAAAALSG EPAALQAFTL
     RVGRPVGPML AQTAPSVADA IERHGGRAIF EAKLDGARVQ IHRSGDQVTV YTRSLDDVTA
     RVPEVVEATL ALPVNDLIAD GEAIALRPDN RPQRFQVTAS RFGRSVDVAA AVAAQPLSVF
     FFDILHRDGV DLLDAPTTDR LAALDALVPP AQRVDRLLTS DPVEAGAFLD ATLAVGHEGV
     MAKAPDAQYQ AGRRGAGWLK VKPVHTLDLV VLAVEWGSGR RRGKLSNIHL GARDPDSGEF
     VMVGKTFKGM TDAMLDWQTA RFTDLAIGGT DGYVVHVRPE QVVEVALDGV QKSSRYPGGL
     ALRFARVVRY RDDKGPAEAD TIDAVRALY
//
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