(data stored in SCRATCH zone)

SWISSPROT: DNLJ_SALAR

ID   DNLJ_SALAR              Reviewed;         671 AA.
AC   A9MIG0;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   11-DEC-2019, entry version 75.
DE   RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_01588};
DE            EC=6.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01588};
DE   AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] {ECO:0000255|HAMAP-Rule:MF_01588};
GN   Name=ligA {ECO:0000255|HAMAP-Rule:MF_01588}; OrderedLocusNames=SARI_00461;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA ligase that catalyzes the formation of phosphodiester
CC       linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-
CC       stranded DNA using NAD as a coenzyme and as the energy source for the
CC       reaction. It is essential for DNA replication and repair of damaged
CC       DNA. {ECO:0000255|HAMAP-Rule:MF_01588}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta-
CC         nicotinamide D-nucleotide.; EC=6.5.1.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01588};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01588};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01588};
CC   -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01588}.
DR   EMBL; CP000880; ABX20397.1; -; Genomic_DNA.
DR   RefSeq; WP_000433259.1; NC_010067.1.
DR   SMR; A9MIG0; -.
DR   PRIDE; A9MIG0; -.
DR   EnsemblBacteria; ABX20397; ABX20397; SARI_00461.
DR   KEGG; ses:SARI_00461; -.
DR   eggNOG; ENOG4105C77; Bacteria.
DR   eggNOG; COG0272; LUCA.
DR   HOGENOM; HOG000218459; -.
DR   KO; K01972; -.
DR   OMA; HDVEHEI; -.
DR   OrthoDB; 241401at2; -.
DR   BioCyc; SENT882884:G1GAH-451-MONOMER; -.
DR   Proteomes; UP000002084; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd00114; LIGANc; 1.
DR   Gene3D; 3.40.50.10190; -; 1.
DR   HAMAP; MF_01588; DNA_ligase_A; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR041663; DisA/LigA_HHH.
DR   InterPro; IPR018239; DNA_ligase_AS.
DR   InterPro; IPR033136; DNA_ligase_CS.
DR   InterPro; IPR001679; DNAligase.
DR   InterPro; IPR013839; DNAligase_adenylation.
DR   InterPro; IPR013840; DNAligase_N.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004150; NAD_DNA_ligase_OB.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR004149; Znf_DNAligase_C4.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF01653; DNA_ligase_aden; 1.
DR   Pfam; PF03120; DNA_ligase_OB; 1.
DR   Pfam; PF03119; DNA_ligase_ZBD; 1.
DR   Pfam; PF12826; HHH_2; 1.
DR   PIRSF; PIRSF001604; LigA; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM00278; HhH1; 4.
DR   SMART; SM00532; LIGANc; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   TIGRFAMs; TIGR00575; dnlj; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS01055; DNA_LIGASE_N1; 1.
DR   PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A9MIG0.
DR   SWISS-2DPAGE; A9MIG0.
KW   DNA damage; DNA repair; DNA replication; Ligase; Magnesium; Manganese;
KW   Metal-binding; NAD; Reference proteome; Zinc.
FT   CHAIN           1..671
FT                   /note="DNA ligase"
FT                   /id="PRO_0000340377"
FT   DOMAIN          593..671
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   NP_BIND         32..36
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   NP_BIND         81..82
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   ACT_SITE        115
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   METAL           408
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   METAL           411
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   METAL           426
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   METAL           432
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         113
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         136
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         173
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         290
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         314
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
SQ   SEQUENCE   671 AA;  73466 MW;  BB8A6E7EB9862897 CRC64;
     MEPIEQQLTE LRTTLRHHEY LYHVMDAPEI PDAEYDRLMR ELRALEAQRP DLITPDSPTQ
     RVGAAPLTAF NQIRHEVPML SLDNVFDEES FLAFNKRVQD RLKSTENVTW CCELKLDGLA
     VSILYENGVL VRAATRGDGT TGEDITSNVR TIRAIPLKLR GDNIPARLEV RGEVFLPQAG
     FEKINEEARR SGGKVFANPR NAAAGSLRQL DPRITAKRPL TFFCYGVGIL EGGELPDTHL
     GRLLQFKAWG LPVSDRVTLC DSPQAVLAFY HNVEEDRPTL GFDIDGVVIK VNSLALQEQL
     GFVARAPRWA VAFKFPAQEQ MTFVRDVEFQ VGRTGAITPV ARLEPVQVAG VLVSNATLHN
     ADEIDRLGLR IGDKVVIRRA GDVIPQVVNV VLSERPEETR PIVFPTHCPV CGSDVERVEG
     EAVTRCTGGL ICGAQRKESL KHFVSRRAMD VDGMGDKIID QLVEREYVHT PADLFRLTAG
     KLTGLDRMGP KSAQNVVNAL EKAKATIFAR FLYALGIREV GEATAAGLAA YFGTLEALQA
     ASIDELQKVP DVGIVVATHV FNFFAEESNR EVIGQLLAEG VHWPAPVVIN AQEIDSPFAG
     KTVVLTGSLS QMSRDDAKAR LVELGAKVAG SVSKKTDLVI AGEAAGSKLA KAQELGIDVI
     DEAEMLRLLG V
//

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