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Database: UniProt/SWISS-PROT
Entry: DNLI_MYCA1
LinkDB: DNLI_MYCA1
Original site: DNLI_MYCA1 
ID   DNLI_MYCA1              Reviewed;         526 AA.
AC   A0QJL0;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-OCT-2017, entry version 84.
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=MAV_3937;
OS   Mycobacterium avium (strain 104).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=243243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-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; CP000479; ABK65463.1; -; Genomic_DNA.
DR   ProteinModelPortal; A0QJL0; -.
DR   SMR; A0QJL0; -.
DR   PRIDE; A0QJL0; -.
DR   EnsemblBacteria; ABK65463; ABK65463; MAV_3937.
DR   KEGG; mav:MAV_3937; -.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   Proteomes; UP000001574; 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   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.
FT   CHAIN         1    526       Probable DNA ligase.
FT                                /FTId=PRO_0000365221.
FT   ACT_SITE    230    230       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     228    228       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     235    235       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     250    250       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     279    279       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     319    319       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     391    391       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     397    397       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   526 AA;  54705 MW;  6AE14C9A8237CD2C CRC64;
     MSPSHAKLAT VLLFDVATAS ADVGGTPSRL TKVARIADLL RRAAPDAALV AIVVSWLSGE
     LRQRQIGVGW AALRSRPPAA AHPTLTVVAV DAAFAEIGAV AGKGAQARRA ALLNALFAAA
     TETEQTFLLR LLGGELRQGA LAGIMADAVA RAAGIPAAAV QRAAMLGGDL PAVAAAALSG
     EAAALSGEAS ALDAFTLRVG RPVAPMLAQT AAGVAEAIER HGGQAIFEAK LDGARVQIHR
     AGDQVTVYTR SLDDVTARLP EVVTATLALP VEALIADGEA IALRPDNSPQ RFQVTASRFG
     RSVDVAAAVA AQPLSVFFFD ILHCDGVDLL DAPTTDRLAA LDALVPPAQR VDQLLTADPD
     AAGRFLEATL AAGHEGVMAK APGAPYQAGR RGAGWLKVKP VHTLDLVVLA VEWGSGRRRG
     KLSNIHLGAR DPATGEFVMV GKTFKGMTDA MLDWQTARFT ELAVGGTDGY VVRVRPEQVV
     EVAVDGVQKS SRYPGGLALR FARVLRYRDD KGPAEADTID AVRALY
//
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