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Database: UniProt/SWISS-PROT
Entry: DNLI_MYCSK
LinkDB: DNLI_MYCSK
Original site: DNLI_MYCSK 
ID   DNLI_MYCSK              Reviewed;         520 AA.
AC   A1UDY9;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-OCT-2017, entry version 82.
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=Mkms_1846;
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=189918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Miller C.D., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) 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: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; CP000518; ABL91047.1; -; Genomic_DNA.
DR   RefSeq; WP_011559199.1; NC_008705.1.
DR   ProteinModelPortal; A1UDY9; -.
DR   SMR; A1UDY9; -.
DR   EnsemblBacteria; ABL91047; ABL91047; Mkms_1846.
DR   GeneID; 32421237; -.
DR   KEGG; mkm:Mkms_1846; -.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG091H0BGA; -.
DR   Proteomes; UP000000638; 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; 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; Cell cycle; Cell division; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    520       Probable DNA ligase.
FT                                /FTId=PRO_0000365229.
FT   ACT_SITE    215    215       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     213    213       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     220    220       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     235    235       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     264    264       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     300    300       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     372    372       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     378    378       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   520 AA;  54705 MW;  AC030FF721DFE324 CRC64;
     MLLVDVATAS VDVGAMSSRL AKTARIADLL SRAGTEQDAR LVAVTVAWLS GELPQRQIGV
     GWAALRSLPA PAAAPTLTVT AVDAVFSEIG AVAGKGSQAR RAGLIAELFA AATDVEQTFL
     RRLLTGELRQ GALIGVMADA VAKAADVPAA RVRRAAMLAG DLPAVAAAVL AGGDAALARF
     TLQVGRPVGP MLAQTATGVA DALDRLGGTA VFEAKLDGAR VQIHRRGSDV SVYTRSLDDV
     TARLPEVVEA ALALPVTDLI ADAEAIALRP DGRPHRFQVT ASRFGRAAAR ATQPLSVFMF
     DLLHVDGADL LDQPTSDRVR VLDDLVPAAH RVDRLVTDDG AAAQRFLEAT LAAGHEGVMA
     KSPNAPYEAG RRGAGWLKVK PVHTLDLVVL AVEWGSGRRT GKLSNIHLGA RDPATGGFVM
     LGKTFKGMTD AMLDWQTARF LELADPAAQP ATSGRDPTDG HTVKVRPEQV VEIAFDGVQG
     STRYPGGMAL RFARVLRYRD DKSPAEADTV DTVRAFYEHG
//
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