CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015028
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA ligase 
Protein Synonyms/Alias
 Polydeoxyribonucleotide synthase [NAD(+)] 
Gene Name
 ligA 
Gene Synonyms/Alias
 RPA3517 
Created Date
 July 27, 2013 
Organism
 Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) 
NCBI Taxa ID
 258594 
Lysine Modification
Position
Peptide
Type
References
225AAGSLRQKDVTVTASacetylation[1]
Reference
 [1] System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases.
 Crosby HA, Pelletier DA, Hurst GB, Escalante-Semerena JC.
 J Biol Chem. 2012 May 4;287(19):15590-601. [PMID: 22416131
Functional Description
 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 (By similarity). 
Sequence Annotation
 DOMAIN 637 715 BRCT.
 NP_BIND 47 51 NAD (By similarity).
 NP_BIND 96 97 NAD (By similarity).
 ACT_SITE 130 130 N6-AMP-lysine intermediate (By
 METAL 435 435 Zinc (By similarity).
 METAL 438 438 Zinc (By similarity).
 METAL 453 453 Zinc (By similarity).
 METAL 459 459 Zinc (By similarity).
 BINDING 128 128 NAD (By similarity).
 BINDING 151 151 NAD (By similarity).
 BINDING 188 188 NAD (By similarity).
 BINDING 306 306 NAD (By similarity).
 BINDING 330 330 NAD (By similarity).  
Keyword
 Complete proteome; DNA damage; DNA repair; DNA replication; Ligase; Magnesium; Manganese; Metal-binding; NAD; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 715 AA 
Protein Sequence
MTAKTKPAPD IATLTKPKAK VELMRLRLEI EGHDKAYYQD DAPKISDADY DALRRRLEAI 60
EQKFPELVNA SSPTQTVGAA PARGFAKVQH AVPMLSLGNA FADDEVAEFA LRVQRFLKLD 120
DVPAIVAEPK IDGLSLSLRY ENGELVRAAT RGDGFTGEDV TANVRTIKDV PNTLKGKHIP 180
ATCELRGEVY MLKQDFLALN KRQEEANETV FANPRNSAAG SLRQKDVTVT ASRPLKFFAY 240
AWGEMSDYPM EEPTQHKMLQ WLDHAGFVVN PEITLCHSVE DALAFYRRIG EKRASLPYDI 300
DGVVYKVDRL DYQERLGFVS RSPRWAIAHK FAAEQATTVL EKIDIQVGRT GAMTPVARLQ 360
PVTVGGVVVQ NATLHNEDYI KGIGNDGEPI RDGVDIREGD TVVVQRAGDV IPQIVSVVME 420
KRPAGAEPYH FPHKCPVCGS HAVREEGEAV WRCTGALICP AQAVERLKHF VSRLAFDIDG 480
LGEKQIELFH ERGWVQEPAD IFTLKARNAE LKLEQLEGYG ETSVRNLFAA IDARRSIELH 540
RLVFALGIRH VGEGNAKLLA RHYGTLDAFL SAMRAAADAQ TEEGNTSEAY QDLDNIAGIG 600
DVVAEAVVEF FAEERNIKAL DALLAELTEV LPAEQARRDT AVAGKTVVFT GSLSKFTRDE 660
AKAAAERLGA KVAGSVSKKT DYVVAGEDAG SKLTKAKDLG VTVLTEDEWL ALIGN 715 
Gene Ontology
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003911; F:DNA ligase (NAD+) activity; IEA:HAMAP.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0006260; P:DNA replication; IEA:UniProtKB-KW. 
Interpro
 IPR001357; BRCT_dom.
 IPR018239; DNA_ligase_AS.
 IPR004150; DNA_ligase_OB.
 IPR001679; DNAligase.
 IPR013839; DNAligase_adenylation.
 IPR013840; DNAligase_N.
 IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
 IPR012340; NA-bd_OB-fold.
 IPR010994; RuvA_2-like.
 IPR004149; Znf_DNAligase_C4. 
Pfam
 PF00533; BRCT
 PF01653; DNA_ligase_aden
 PF03120; DNA_ligase_OB
 PF03119; DNA_ligase_ZBD 
SMART
 SM00292; BRCT
 SM00278; HhH1
 SM00532; LIGANc 
PROSITE
 PS50172; BRCT
 PS01055; DNA_LIGASE_N1
 PS01056; DNA_LIGASE_N2 
PRINTS