CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-045495
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 tRNA-splicing ligase RtcB homolog 
Protein Synonyms/Alias
  
Gene Name
  
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
284EKAMKRDKIIVNDRQacetylation[1]
365EQHVVDGKERTLLVHubiquitination[2]
464AIRVASPKLVMEEAPubiquitination[2]
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 121 121 Zinc (By similarity).
 METAL 226 226 Zinc (By similarity).
 METAL 258 258 Zinc (By similarity).  
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
MSRNYNDDLQ FLDKINKNCW RIKKGFVPNM QVEGVFYVND ALEKLMFEEL RNACRGGGIG 60
GFLPAMQIGN VAALPGIVHR SIGLPDVHSG YGFAIGNMAA FDMNDPEAVV SPGGVGFDIN 120
CGVRLLRTNL DESDVQPVKE QLAQAMFDHI PVGVGSKGVI PMNAKDLEEA LEMGVDWSLR 180
EGYAWAEDKE HCEEYGRMLQ ADPNKVSPRA KKRGLPQLGT LGAGNHYAEI QVVDEIFNEY 240
AAKKMGIDHK GQVCVMIHSG SRGLGHQIAT DALVAMEKAM KRDKIIVNDR QLACARIASP 300
EGQDYLKGMA AAGNYAWVNR SSMTFLTRQA FAKVFNTTPD DLDLHVIYDV SHNIAKVEQH 360
VVDGKERTLL VHRKGSTRAF PPHHPLIAVD YQLTGQPVLI GGTMGTCSYV LTGTEQGMTE 420
TFGTTCHGAG RALSRAKSRR NLDFQDVLDK LGDMGIAIRV ASPKLVMEEA PESYKNVTDV 480
MNTCHDAAIS KKAIKLRSIA VIKGL 505 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0072669; C:tRNA-splicing ligase complex; IEA:HAMAP.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003972; F:RNA ligase (ATP) activity; IEA:HAMAP.
 GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IEA:HAMAP. 
Interpro
 IPR027513; RtcB_euk.
 IPR001233; RtcB_family. 
Pfam
 PF01139; UPF0027 
SMART
  
PROSITE
 PS01288; UPF0027 
PRINTS