CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014871
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 tRNA-splicing ligase RtcB homolog 
Protein Synonyms/Alias
 p55 
Gene Name
  
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
14DELQFLDKINKNCWRacetylation[1]
366EQHVVDGKERTLLVHubiquitination[2]
465AIRVASPKLVMEEAPubiquitination[2]
496GISKKAIKLRPIAVIacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
Functional Description
 Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'- phosphodiester. May act as a RNA ligase with broad substrate specificity, and may function toward other RNAs (By similarity). 
Sequence Annotation
 METAL 122 122 Zinc (Potential).
 METAL 227 227 Zinc (Potential).
 METAL 259 259 Zinc (Potential).  
Keyword
 ATP-binding; Complete proteome; Cytoplasm; Ligase; Metal-binding; Nucleotide-binding; Reference proteome; tRNA processing; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 505 AA 
Protein Sequence
MSRNYNDELQ FLDKINKNCW RIKKGFVPNM QVEGVFYVND ALEKLMFEEL RNACRGGGVG 60
GFLPAMKQIG NVAALPGIVH RSIGLPDVHS GYGFAIGNMA AFDMNDPEAV VSPGGVGFDI 120
NCGVRLLRTN LDESDVQPVK EQLAQAMFDH IPVGVGSKGV IPMNAKDLEE ALEMGVDWSL 180
REGYAWAEDK EHCEEYGRML QADPNKVSPR AKKRGLPQLG TLGAGNHYAE IQVVDEIFNE 240
YAAKKMGIDH KGQVCVMIHS GSRGLGHQVA TDALVAMEKA MKRDKIIVND RQLACARIAS 300
PEGQDYLKGM AAAGNYAWVN RSSMTFLTRQ AFAKVFNTTP DDLDLHVIYD VSHNIAKVEQ 360
HVVDGKERTL LVHRKGSTRA FPPHHPLIAV DYQLTGQPVL IGGTMGTCSY VLTGTEQGMT 420
ETFGTTCHGA GRALSRAKSR RNLDFQDVLD KLADMGIAIR VASPKLVMEE APESYKNVTD 480
VVNTCHDAGI SKKAIKLRPI AVIKG 505 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0072669; C:tRNA-splicing ligase complex; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003972; F:RNA ligase (ATP) activity; ISS:UniProtKB.
 GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; ISS:UniProtKB. 
Interpro
 IPR027513; RtcB_euk.
 IPR001233; RtcB_family. 
Pfam
 PF01139; UPF0027 
SMART
  
PROSITE
 PS01288; UPF0027 
PRINTS