ACL_RS06670


  Uniprot: A9NHW0
Description: DNA ligase (NAD(+)) 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:0000255|HAMAP-Rule:MF_01588}.
Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01588}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01588}.
Pathway: 
Active site: ACT_SITE 111 111 N6-AMP-lysine intermediate. {ECO:0000255|HAMAP-Rule:MF_01588}.
Binding site: BINDING 109 109 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.; BINDING 132 132 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.; BINDING 166 166 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.; BINDING 281 281 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.; BINDING 305 305 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
Calcium binding: 
DNA binding: 
Metal binding: METAL 398 398 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.; METAL 401 401 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.; METAL 416 416 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.; METAL 421 421 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.
Nucleotide binding: NP_BIND 31 35 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.; NP_BIND 80 81 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
Site: 
Gene names (primary): ligA
Gene names (synonym): 
Mass: 74,009
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: CHAIN 1 659 DNA ligase. /FTId=PRO_0000340321.
Signal peptide: 
Domain [CC]: 
Sequence similarities: SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA subfamily. {ECO:0000255|HAMAP-Rule:MF_01588}.; SIMILARITY: Contains 1 BRCT domain. {ECO:0000255|HAMAP-Rule:MF_01588}.
Protein families: NAD-dependent DNA ligase family, LigA subfamily
Coiled coil: 
Domain [FT]: DOMAIN 581 659 BRCT. {ECO:0000255|HAMAP-Rule:MF_01588}.
Motif: 
Region: 
EMBL: CP000896
ProteinModelPortal: A9NHW0
MEROPS: 
EnsemblBacteria KO: ABX81940
UniPathway: K01972
CDD: 
Gene3D: 
HAMAP: 2.40.50.140;3.40.50.10190
InterPro: MF_01588
PANTHER: IPR001357;IPR018239;IPR033136;IPR001679;IPR013839;IPR013840;IPR003583;IPR012340;IPR004150;IPR010994;IPR004149
PIRSF: 
PRINTS: PIRSF001604
PROSITE: 
Pfam: PS50172;PS01055;PS01056
ProDom: PF00533;PF01653;PF03120;PF03119
SMART: 
SUPFAM: SM00292;SM00278;SM00532
TIGRFAMs: SSF47781;SSF50249;SSF52113
1407905-1409885(-)

>nucleotide sequence
TTATTCATTAATCTTCACCTTGAATGTAGCCTCATCCATAACTTCTATACCCAGTTCTAA
TGCTTTGGTCAGTTTAGAACCAGCCTCTTTACCTGCTAAAACATAATCTGTCTTTTTAGA
AACAGATCCACTAACCTTGCCACCTAATTTTTCAATGATATCACTTGCCTCAGTTCTTGA
AAAATCATCTAACGTACCTGTAACAACAAATGTCTTACCATTAAATGGATGTGTTGTAAC
AACATCTATTTTGTAAGTCATTTGTAGTCCTAAGTTTTTTAATTCTTCTAACATATGTTG
GTTTGATTCATTAGAAAAATAAGTTGTTACACTATCTGCAATTTCTGGACCAATATCAGG
TATTTGAATTAAATCCTCATACTTCGCATCAGCTAATAACGTGATGGATGGATAATGATT
TAATAATGTTTTAGCTACTTTGGCACCTACATTCTTAATACCCAATCCAAAGATAAGTCT
ATCTAAGGTTTGCATCTTAGATGCTTCAATGGCATTAAGCAGTTTTTCTACCTTCTTTTT
ACCAAATCCAGGTAGTTCTTCTAATTGATCTTTAAAGGTATGTAATTTATAGATATCTGG
TATGGTTTGAAGATAGGTTTGGTCATGTAAGAGTTCAACAACTTTTTCTCCTAATGTATC
AATATCCATAGCAGCTCTACTTGCAAAATGAATAAGCCCAAATACATTTTTACCTGGACA
ATTATCATTTGCACAATAATAGTCTGCTTCACCTTGTTTTCTAACTAAATTAGATTCACA
GGCTGGACAATGTTTAACCATTTCAAATGGTGCTTGATTGGTTCTACTACCTAGTACAAC
TTCAATCACCTCAGGTATAATTTCACCTGCTTTATGAACTAATACTTGATCATCAATTCG
AATGTCTTTATTTAATATATAATCTTCGTTATGTAGTGTAGCTCTAGATACTAAAGAACC
TGATATAAATACTGGTGTTAATACAGCCACCGGTGTAATTACACCAGTACGCCCTACTTG
AAAGATAATATCTTCAACTTTAGTAATTTGTTTTTCAGCCTCAAACTTATATGCGCCTGC
ATACTTAGGATATTTAGCCGTGTAACCAATCGTTTCATAATGTTCAAACTGATTGACTTT
AATAACTACACCATCTGTATCATAAGGTAATGTTTTTCTTAAAATGTCATAGTTATCAAT
AGCATCTGATAATGCATCTAAATTATCAACAAGTTTATAATGAGGATTTACTGGAAAACC
TAGTTCTGATAAAAACTCTAAGGTTTCTTTTTGTGTGCTATTAAAATTACTTGCACCTAC
TACAGTGTAGGTAAAGAGATCCAACCTTCTTTTAGCAACCACTTTAGAATCTAGTTGTCT
GACTGTACCGGCTGCTGCATTTCTAGGATTTACAAATAAATCTAGATTGCTATTAGCACG
TTCTAAATTCACTTCTTTAAATGTCTTATGAGACATATAAATTTCACCACGTACTTCAAT
ATCTAAAGGTTTAGATAATTGTAGTGGTAAGGTTTTAATGGTCTTAACATTTTCAGTAAT
ATCTTCACCCACCACACCATTACCACGAGTCGCTGCCTTTTTAAATATACCTTTTTCATA
AATAAGCGTTACTGCTAAACCATCTATTTTAAGCTCTGTTGTAAAACTAGTGTTTGGTAT
AACTTTTTGAATTCTATCATAAAAGACCTTTAACTCTTCTTTGTTAAAGATATTAGATAA
ACTCATCATTGGTACCGTATGTGTATGCTTTTTAAAGGCATCTAAAACAACACCACCAAT
TTTTTTAGTTGGAGATGTTTCATCATCATATTCTGGATATTTAGTTTCAAGTTCAATCAA
TTCACGCATTAATCCATCATAGACAAAATCACTAATAATCGGTTGATCTTTTGTATGATA
TAGGTAGTTTGCTTCATTGATTTGTTTTCTTAGCTCTTTGATTCTAGTCTGTATGTCCAT


>protein sequence
MDIQTRIKELRKQINEANYLYHTKDQPIISDFVYDGLMRELIELETKYPEYDDETSPTKK
IGGVVLDAFKKHTHTVPMMSLSNIFNKEELKVFYDRIQKVIPNTSFTTELKIDGLAVTLI
YEKGIFKKAATRGNGVVGEDITENVKTIKTLPLQLSKPLDIEVRGEIYMSHKTFKEVNLE
RANSNLDLFVNPRNAAAGTVRQLDSKVVAKRRLDLFTYTVVGASNFNSTQKETLEFLSEL
GFPVNPHYKLVDNLDALSDAIDNYDILRKTLPYDTDGVVIKVNQFEHYETIGYTAKYPKY
AGAYKFEAEKQITKVEDIIFQVGRTGVITPVAVLTPVFISGSLVSRATLHNEDYILNKDI
RIDDQVLVHKAGEIIPEVIEVVLGSRTNQAPFEMVKHCPACESNLVRKQGEADYYCANDN
CPGKNVFGLIHFASRAAMDIDTLGEKVVELLHDQTYLQTIPDIYKLHTFKDQLEELPGFG
KKKVEKLLNAIEASKMQTLDRLIFGLGIKNVGAKVAKTLLNHYPSITLLADAKYEDLIQI
PDIGPEIADSVTTYFSNESNQHMLEELKNLGLQMTYKIDVVTTHPFNGKTFVVTGTLDDF
SRTEASDIIEKLGGKVSGSVSKKTDYVLAGKEAGSKLTKALELGIEVMDEATFKVKINE






















© Fisunov Lab of Proteomics, 2016.