GCW_03920







Uniprot: A0A0F6CLH5
Description: DNA ligase
EC number: 6.5.1.2
Annotation score: 3 out of 5
Miscellaneous [CC]: 
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + beta-nicotinamide D-ribonucleotide + (deoxyribonucleotide)(n+m). {ECO:0000256|HAMAP-Rule:MF_01588, ECO:0000256|SAAS:SAAS00572200}.
Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-Rule:MF_01588}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-Rule:MF_01588};
Enzyme regulation: 
Function [CC]: FUNCTION: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. {ECO:0000256|HAMAP-Rule:MF_01588, ECO:0000256|SAAS:SAAS00572229}.
Pathway: 
Active site: ACT_SITE 119 119 N6-AMP-lysine intermediate. {ECO:0000256|HAMAP-Rule:MF_01588}.
Binding site: BINDING 117 117 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.; BINDING 140 140 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.; BINDING 175 175 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.; BINDING 289 289 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.; BINDING 313 313 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.
Calcium binding: 
DNA binding: 
Metal binding: METAL 407 407 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}.; METAL 410 410 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}.; METAL 425 425 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}.; METAL 430 430 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}.
Nucleotide binding: NP_BIND 37 41 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.; NP_BIND 86 87 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.
Site: 
Gene names (primary): lig
Gene names (synonym): ligA
Mass: 82,654
Subunit structure [CC]: 
Gene ontology (GO): DNA ligase (NAD+) activity [GO:0003911]; metal ion binding [GO:0046872]; DNA repair [GO:0006281]; DNA replication [GO:0006260]
Gene ontology IDs: GO:0003911; GO:0006260; GO:0006281; GO:0046872
Chain: 
Signal peptide: 
Domain [CC]: 
Sequence similarities: SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA subfamily. {ECO:0000256|HAMAP-Rule:MF_01588, ECO:0000256|SAAS:SAAS00572184}.; SIMILARITY: Contains 1 BRCT domain. {ECO:0000256|HAMAP-Rule:MF_01588}.
Protein families: NAD-dependent DNA ligase family, LigA subfamily
Coiled coil: COILED 262 289 {ECO:0000256|SAM:Coils}.
Domain [FT]: DOMAIN 8 446 LIGANc. {ECO:0000259|SMART:SM00532}.
Motif: 
Region: 
EMBL: CP006916
ProteinModelPortal: 
MEROPS: 
EnsemblBacteria KO: AHB99947
UniPathway: K01972
CDD: 
Gene3D: 
HAMAP: 2.40.50.140;3.40.50.10190
InterPro: MF_01588
PANTHER: IPR001357;IPR033136;IPR001679;IPR013839;IPR013840;IPR012340;IPR004150;IPR010994;IPR004149
PIRSF: 
PRINTS: PIRSF001604
PROSITE: 
Pfam: PS01056
ProDom: PF00533;PF01653;PF03120;PF03119
SMART: 
SUPFAM: SM00532
TIGRFAMs: SSF47781;SSF50249;SSF52113
943553-945701(-)

>nucleotide sequence
CTATTTGTTCCAGATTTCTTCTTGAATGATTGGAATATTTAGCACTTTGGCTTGGTTAAT
TTTTTTAGCTGTCGGACTGTTACCCGCTAAAACAAAATCAACGTTTTTAGACACACCACT
TACAAACTTAATTTTGTATTTTAAAGATAGTTTTTTAATAATGTCGTTTCGTGAGATACT
AAAAGAACCAGTGATTACAAACTTTTTATCATAGTAGATAGATGAACTATCAACTAAATC
ATTATTAATCCCATCTTTAGTGTTAATCGATAAAGTTTTTAATTGTTCAATTAATTCCCA
ATTTTTTTCATCTGAGAAAAAACTAAATAGTGAATTAGCAGTTATGCTGCTAATATCAGC
TAATCGCATGTAATCTTCAACAGTTAAGCTTTTAAGTTGATCAATATCGTGATATGTATT
AGCAATCGACTTCGCTGTTGCTATTCCAATATATTTAATATTAAGTGCAGCCAATAACCG
ATATAATTCTCGGTTTTTAGATTCATTAATACTGTTAATTAATTTATCAAACGATTTCTC
TTGAAATCTAAAGTTATATTTTAAAGATGATTTAGAAAACCCCTTCTTAAGCCAAGGTTT
GATAATAATCTCTTTGTATCGTTCTAATTGATAAATATCTAAAACGCTATTAACAAACGT
TTGTTCTTCATTATCTAATAACTTAAATAAACTAAGATCTTCATTAACATTTTGATTGGT
GATTAATTCATTACATTCTCTAATAACATCATTAACTTTAGTATTAAAGAATAAAGCTAA
AGTGCTTTCACTCAAACCTTCAATGTTCATTATTGGTTTAGAACAATAATAGATTAGATA
TTGCAATTGCTTTTGTTTACATTGATCATAAATACAATATCAATCAACCTCTTCAGGCTT
TTTTACTAGAGTTTGATGACAACTTGGACAGTTGTAATCAAACTCAAGTTTTTTAGCATT
ATTCGGTCGTTTATCTAGATTTACACCAATCACCTTAGGGATGATCTCAGCAGCCTTAAT
TAAATATACGTAGTCATTAATTCTGATATCTAGGTCGTTGATATACTCTAAGTTATGTAA
AGTTGCATAAGTGATAATCGAACCTTCTAATTCAATTGGGGCTAGTTGTGCAACAAAAGT
TAGTTTGCCAGTTCGACCAACGTTAAGGATAATATCTTTTAATTGGGTTTGCGCCTGAGT
AGGTGCAAACTTGTATGCGATTGCTCATTTGGGAAACTTAGAGGTGTAACCGATTGTTTC
ATAATTCTTGAAGTTGTTATATTTGATTACAGCTCCATCGATTCGATAATCTAATTTATT
CTTGTTGTTTTCTAGTTCTTTAAGACTGGTGTAAAGTTCTTTAATGTTGCTAAATAACTT
AATCTCTTTAGCAACATTAAAGCCTCATTCTTTTAACTGTTGGATCACTTGATACTGGGT
TTCAAAACCTAGTTCATAAGCGTTGGGAATATAATAAAAGAACGCATTAAGTTTACGTTT
GGCAACTTCACTAACATCAATGTTTCTTAAACTTCCAGAAGCATAGTTTCTAGAGTTCGC
AAACTTCTTATCTTCATCTCTTGAAGCATTAATTACTTCAAAGTCTTGATTGCTTACGTA
GACCTCTCCACGGATAACGATCTTTTTGATCGTTGTATTAATTTTTAATGGGATTGTTTT
AATTGTTTTGATATTAGCTATCACACTCTCACCAACAACCCCATCACCCCTAGTAAGTGC
TTCAGATAACACGCCGTCAAGATAAATTAATGAGATTGATAAACCATCAATCTTAGGTTC
TAACACGTAAGGATTATCTTCTTGTTTACTTATCTTAGCAATATTTTCATTAAAGTTAAG
CAACTCTTCAAAATTAAAGCAGTTGCCCAATGATAACATCAAGTAATCATGTTTAACTTT
AATGAACTTATTGCTAATTGATGATCCCACTCTTTGAGTGGGGGAATAACTTAAAACGTA
TTGTGGGTATTTTCTTTCATAACCTAGTAAAGTTCGATAAGTATTATCATACACTTCATC
TGAAACACTTGGGTTAGATAAAACATAATACTCATGTTCTCATTTAGTTAATTTTTTAAC
TAAATCTTCGATTATCTCTTTGATACTTTCGTTCTTCTTTTCAATCAT


>protein sequence
MIEKKNESIKEIIEDLVKKLTKWEHEYYVLSNPSVSDEVYDNTYRTLLGYERKYPQYVLS
YSPTQRVGSSISNKFIKVKHDYLMLSLGNCFNFEELLNFNENIAKISKQEDNPYVLEPKI
DGLSISLIYLDGVLSEALTRGDGVVGESVIANIKTIKTIPLKINTTIKKIVIRGEVYVSN
QDFEVINASRDEDKKFANSRNYASGSLRNIDVSEVAKRKLNAFFYYIPNAYELGFETQYQ
VIQQLKEWGFNVAKEIKLFSNIKELYTSLKELENNKNKLDYRIDGAVIKYNNFKNYETIG
YTSKFPKWAIAYKFAPTQAQTQLKDIILNVGRTGKLTFVAQLAPIELEGSIITYATLHNL
EYINDLDIRINDYVYLIKAAEIIPKVIGVNLDKRPNNAKKLEFDYNCPSCHQTLVKKPEE
VDWYCIYDQCKQKQLQYLIYYCSKPIMNIEGLSESTLALFFNTKVNDVIRECNELITNQN
VNEDLSLFKLLDNEEQTFVNSVLDIYQLERYKEIIIKPWLKKGFSKSSLKYNFRFQEKSF
DKLINSINESKNRELYRLLAALNIKYIGIATAKSIANTYHDIDQLKSLTVEDYMRLADIS
SITANSLFSFFSDEKNWELIEQLKTLSINTKDGINNDLVDSSSIYYDKKFVITGSFSISR
NDIIKKLSLKYKIKFVSGVSKNVDFVLAGNSPTAKKINQAKVLNIPIIQEEIWNK






















© Fisunov Lab of Proteomics, 2016.