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Database: UniProt/TrEMBL
Entry: X7Y6W4_MYCKA
LinkDB: X7Y6W4_MYCKA
Original site: X7Y6W4_MYCKA 
ID   X7Y6W4_MYCKA            Unreviewed;       509 AA.
AC   X7Y6W4;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-SEP-2017, entry version 25.
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=I547_0544 {ECO:0000313|EMBL:EUA02952.1};
OS   Mycobacterium kansasii 824.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1299328 {ECO:0000313|EMBL:EUA02952.1, ECO:0000313|Proteomes:UP000022044};
RN   [1] {ECO:0000313|EMBL:EUA02952.1, ECO:0000313|Proteomes:UP000022044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=824 {ECO:0000313|EMBL:EUA02952.1,
RC   ECO:0000313|Proteomes:UP000022044};
RA   Brown-Elliot B., Wallace R., Lenaerts A., Ordway D., DeGroote M.A.,
RA   Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N.,
RA   Fraser C.M., Hine E., Shefchek K.A., Das S.P., Tettelin H.;
RL   Submitted (DEC-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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EUA02952.1}.
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DR   EMBL; JANY01000001; EUA02952.1; -; Genomic_DNA.
DR   RefSeq; WP_023372085.1; NZ_JANY01000001.1.
DR   EnsemblBacteria; EUA02952; EUA02952; I547_0544.
DR   GeneID; 29697421; -.
DR   KEGG; mki:LH54_22970; -.
DR   PATRIC; fig|1299328.3.peg.527; -.
DR   KO; K10747; -.
DR   Proteomes; UP000022044; Unassembled WGS sequence.
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; 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:UP000022044};
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:EUA02952.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000022044}.
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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