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Database: UniProt/TrEMBL
Entry: U5WV83_MYCKA
LinkDB: U5WV83_MYCKA
Original site: U5WV83_MYCKA 
ID   U5WV83_MYCKA            Unreviewed;       509 AA.
AC   U5WV83;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   25-OCT-2017, entry version 27.
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=ligB {ECO:0000313|EMBL:AGZ52852.1};
GN   Synonyms=lig {ECO:0000256|HAMAP-Rule:MF_00407};
GN   ORFNames=MKAN_23085 {ECO:0000313|EMBL:AGZ52852.1};
OS   Mycobacterium kansasii ATCC 12478.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=557599 {ECO:0000313|EMBL:AGZ52852.1, ECO:0000313|Proteomes:UP000017786};
RN   [1] {ECO:0000313|EMBL:AGZ52852.1, ECO:0000313|Proteomes:UP000017786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12478 {ECO:0000313|EMBL:AGZ52852.1,
RC   ECO:0000313|Proteomes:UP000017786};
RG   McGill University Mycobacterium genome consortium;
RA   Veyrier F.J., Behr M.A.;
RT   "Genome sequence of Mycobacterium kansasii.";
RL   Submitted (OCT-2013) 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; CP006835; AGZ52852.1; -; Genomic_DNA.
DR   RefSeq; WP_023372085.1; NC_022663.1.
DR   STRING; 557599.MkanA1_010100021065; -.
DR   EnsemblBacteria; AGZ52852; AGZ52852; MKAN_23085.
DR   GeneID; 29697421; -.
DR   KEGG; mkn:MKAN_23085; -.
DR   eggNOG; ENOG4107T0X; Bacteria.
DR   eggNOG; COG1793; LUCA.
DR   KO; K10747; -.
DR   OrthoDB; POG091H0BGA; -.
DR   Proteomes; UP000017786; 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:UP000017786};
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:AGZ52852.1};
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;  53881 MW;  BD8C00120346377C CRC64;
     MLLLDVATTS LDVGATSSRL SKVERIADLL RRAAPDPELV AILVAWLSGE LPQRHIGVGW
     ASLRSLPPPA GHATLTVTGV DAAFSEIGAT SGSGSQARRA QLVSELFSAA TESEQTFLFR
     LLSGELRQGA LTGIMTDAVA KAAAIRASAV QRAAMLGGDL PAVAAAGLTG GAAALDAFTL
     RVGRPVGPML AQTATGVTDA LERHYGTTIF EAKLDGARVQ IHRAGDHVTV YTRSLDDVTA
     RLPEVVEATL ALPVHELIAD GEAIAWRPDH RPHRFQVTAS RFGRSVDVAA ARATQPLSVF
     FFDILHRDGD DLLDAPTTER LAVLDAVVPV RHRVDRLITS DAAAAAAFLD ATLAAGHEGV
     MAKAPGAPYQ AGRRGAGWLK VKPVHTLDLV VLGVEWGSGR RRGKLSNIHL GARDPASGKY
     VMVGKTFKGM TDAMLDWQTA RFTGLAIGGT DGYVVQLRPE QVVEVAVDGV QGSSRYPGGV
     ALRFARVLRY RDDKSPDEAD TIDTVRALY
//
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