SPM_001920


  Uniprot: A0A037UQK8
Description: NAD-dependent DNA ligase LigA
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}; ; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|SAAS:SAAS00611843};
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 116 116 N6-AMP-lysine intermediate. {ECO:0000256|HAMAP-Rule:MF_01588}.
Binding site: BINDING 114 114 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.; BINDING 137 137 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.; BINDING 170 170 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.; BINDING 286 286 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.; BINDING 310 310 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.
Calcium binding: 
DNA binding: 
Metal binding: METAL 404 404 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}.; METAL 407 407 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}.; METAL 422 422 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}.; METAL 427 427 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}.
Nucleotide binding: NP_BIND 34 38 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.; NP_BIND 83 84 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.
Site: 
Gene names (primary): ligA
Gene names (synonym): 
Mass: 76,324
Subunit structure [CC]: 
Gene ontology (GO): DNA binding [GO:0003677]; DNA ligase (NAD+) activity [GO:0003911]; metal ion binding [GO:0046872]; DNA repair [GO:0006281]; DNA replication [GO:0006260]
Gene ontology IDs: GO:0003677; 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: 
Domain [FT]: DOMAIN 588 667 BRCT. {ECO:0000259|PROSITE:PS50172}.
Motif: 
Region: 
EMBL: AGBZ02000001
ProteinModelPortal: 
MEROPS: 
EnsemblBacteria KO: KAI92791
UniPathway: 
CDD: 
Gene3D: 
HAMAP: 2.40.50.140;3.40.50.10190
InterPro: MF_01588
PANTHER: IPR001357;IPR001679;IPR013839;IPR013840;IPR003583;IPR012340;IPR004150;IPR010994;IPR004149
PIRSF: 
PRINTS: PIRSF001604
PROSITE: 
Pfam: PS50172
ProDom: PF00533;PF01653;PF03120;PF03119
SMART: 
SUPFAM: SM00292;SM00278;SM00532
TIGRFAMs: SSF47781;SSF50249;SSF52113
349730-351734(-)

>nucleotide sequence
TTAGTCCTCCTTATTTAATAATTGTTGAAATTCTTCTTCATTAATAATTTTAACATTTAA
TTTTTGTGCTTTTACTAATTTATTACCAGCATCAGTTCCCGCCAGTAAATAAGTGGTTTT
TGCACTAACACTTTCAGAAACTTGTCCACCATAACTTTCAATTAATTCTTTAAAGTATTC
TCGTGATTTTGATAAGACTCCAGTAATCACAAACCGATAATTTTCAAACTTCTGTGCTAA
ATGCTGATTAGTAGCAAAATACTCCATTTTAACCCCATTTTGGCGTAATAAAGCCAGTTC
TTGTTGGTTAGCTGGAATTGCAAAATAATCCACAACACTAGCTGCTACAATTGGACCAAT
ATCATTAATAATTGATAATTGTTCAATATTCATAGCAGCTAAATTATCAATTGTTTTAAA
TTGTCGTGCTAATAATTTTGCTGTTTTTTGACCAACATGACGAATTCCTAACGCAAATAA
TAGTCGTTCTAAGGAATTATTTTTTGAATTATTAATTGAAGTAATCATATTTTCAAACGA
TTTTTCACCAAAATTTTCTAATTCAATAATTTCAGCGCGGTATTGTTCTAATTGATATAA
ATCACTAAAACTTTTTAAATATTCTAATTTAAATAATCGTTCAATAATTTTTTCACTAAT
TCCTTCAATATTCATCGCATTTCGTGAACAATAATGTTCTAATCCACGTGTAATTTTTTT
GGGACAAACAGAATTAATGCAATACTGGTCAACCTCCCCTTCAACACGTTCTAATAAAGA
ATTACATTCTGGGCAATGCGTTGCTTCTTGTCACTTCTGAGCATTTTTTTGGCGACGAGC
TGCAACATAATTAATTACTTCTGGAATAATATCTCCCGCTTTTTTAACTTGGACATTATC
ACCAATCCGAATATCACGTTCAGTAATAAAATCAGCATTATGTAATGTTGCAGCTCGTAC
GATTGTTCCTGCAATACGAATTGGTTCAAGAACAGCATTATAAGTAATGCGCCCCGTTCT
CCCAACGGAAGGAAAAATATTAAGCAATTTAGTAACCACAACTTCCGCTGGAAATTTATA
AGCGATTGCTCATTTTGGATTTTTAGCAGTATAACCAATACGATTATATAAATTTAAGTT
ATTAACTTTAATCACAATTCCATCAATTTCATAACCTAACTGATGACGTTTTGGCTCATA
TTCTTGAATATATGCTCACACTGCCGCAATATTTGAGCAATAACGATATTCAGGATTTGT
TTTAAATTTCAATTGTTCTAATCTTTGTAATGCTTCGTATTGTGATTGAATCCCATCCTG
TAAAGCATTAACATAATAATATAAAAATGCATTTAACTTTCGTTTTGCAACAATTGTTGA
ATCTAATTGACGTAAAGTGCCTGCTGCTGCATTTCGAGGATTAGCAAATTCAGATTCACC
ATTTTTAACACGTTCTTCATTAATCTTATTAAACTCTTCAACTGATAAATAAACTTCTCC
CCGAACAATTAAAGTTGGTTGGTCAATTCGAAGGGGAATTGATTTAATTTGTTTAATATT
AATAGTAACATCTTCACCGGTAAGACCATCGCCCCGAGTTGCCCCCATCACTAAAAGATG
ATTATCATAAACTAATGAAATTGATAATCCATCAATTTTTAATTCACAAGTATATTCAAT
TTCTGGCAAACCAGTTAATTCTTTAATTTGCTCATCAAAATGAATTAAATCATCATAATT
AAACGCGTTTCCTAAACTTAGCATTGGACTTGTATGAACATATTTATTAAACTTTTCACT
AATTTGGCCAGAAACACGTTGCGTTGGTGAATCAATTGTAATTAATTCACTATATTGCTG
TTCAATTGCAATTAATTCTTGCATTGCTCGATCATATTCTTGGTCACTAACACTAGGGTT
ATCATTAACATAATATTCATAATTTCATTTTTCTAATTGTTCTTTTAACACTAAACTACG
TTTTTTTGCTTGCTCAAAAGTCAT


>protein sequence
MTFEQAKKRSLVLKEQLEKWNYEYYVNDNPSVSDQEYDRAMQELIAIEQQYSELITIDSP
TQRVSGQISEKFNKYVHTSPMLSLGNAFNYDDLIHFDEQIKELTGLPEIEYTCELKIDGL
SISLVYDNHLLVMGATRGDGLTGEDVTINIKQIKSIPLRIDQPTLIVRGEVYLSVEEFNK
INEERVKNGESEFANPRNAAAGTLRQLDSTIVAKRKLNAFLYYYVNALQDGIQSQYEALQ
RLEQLKFKTNPEYRYCSNIAAVWAYIQEYEPKRHQLGYEIDGIVIKVNNLNLYNRIGYTA
KNPKWAIAYKFPAEVVVTKLLNIFPSVGRTGRITYNAVLEPIRIAGTIVRAATLHNADFI
TERDIRIGDNVQVKKAGDIIPEVINYVAARRQKNAQKWQEATHCPECNSLLERVEGEVDQ
YCINSVCPKKITRGLEHYCSRNAMNIEGISEKIIERLFKLEYLKSFSDLYQLEQYRAEII
ELENFGEKSFENMITSINNSKNNSLERLLFALGIRHVGQKTAKLLARQFKTIDNLAAMNI
EQLSIINDIGPIVAASVVDYFAIPANQQELALLRQNGVKMEYFATNQHLAQKFENYRFVI
TGVLSKSREYFKELIESYGGQVSESVSAKTTYLLAGTDAGNKLVKAQKLNVKIINEEEFQ
QLLNKED






















© Fisunov Lab of Proteomics, 2016.