CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008585
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Decapping nuclease RAI1 
Protein Synonyms/Alias
 RAT1-interacting protein 
Gene Name
 RAI1 
Gene Synonyms/Alias
 YGL246C; NRE387 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
281PRIIYGFKDDHYVLKacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919
Functional Description
 Ribonuclease that specifically degrades pre-mRNAs with a defective 5' end cap and is part of a pre-mRNA capping quality control. Has decapping and pyrophosphohydrolase activities. Has decapping activity toward incomplete 5' end cap mRNAs such as unmethylated 5' end-capped RNA to release GpppN and 5' end monophosphate RNA. Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5' end triphosphate to release pyrophosphates. Stimulates exoribonuclease activity of RAT1, allowing it to degrade RNAs with stable secondary structure more effectively. Required for the processing of nuclear mRNA and rRNA precursors. May promote termination of transcription by RNA polymerase II. 
Sequence Annotation
 REGION 273 387 Interaction with RAT1.
 METAL 172 172 Divalent metal cation (By similarity).
 METAL 223 223 Divalent metal cation (By similarity).
 METAL 241 241 Divalent metal cation (By similarity).
 METAL 242 242 Divalent metal cation; via carbonyl
 BINDING 105 105 Substrate (By similarity).
 BINDING 221 221 Substrate (By similarity).
 BINDING 267 267 Substrate (By similarity).
 MOD_RES 198 198 Phosphoserine.  
Keyword
 Complete proteome; Direct protein sequencing; Hydrolase; Metal-binding; mRNA processing; Nuclease; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; RNA-binding; rRNA processing; Transcription; Transcription regulation; Transcription termination. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 387 AA 
Protein Sequence
MGVSANLFVK QRGSTTALKQ PKEIGFYSRT KDEEYLISDD TNLNYYYLPD AELDRKLDLS 60
SGFQKFKDYY KDFEDRCSLR GLLETIESSE RHKGKKINAD IITFRGIARK LISCAFDSPS 120
FNTVDLRIVS FNGQLFIKEV PEAVNAAKAS SATEAGRNIN QDLNVFTGYK FETLATLSNP 180
LQYTPREVIE KRTKRIVSHG DEYISVVRTG VGNCKLILGA EVDCIFDFKE NGRDNLKHYA 240
ELKCTQQVAN ISDTHKFERK LFRTWLQCFL VGIPRIIYGF KDDHYVLKTV EEFSTEEVPV 300
LLKNNNPQVG SACLEAIKWY GLLTEWLLKM IPRDEDPHSQ IRAFKLVFEN NHLRLSEIEE 360
SDEEYSGLID GEHILSNGFK EWRKSLK 387 
Gene Ontology
 GO:0005829; C:cytosol; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0030234; F:enzyme regulator activity; IDA:SGD.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0016462; F:pyrophosphatase activity; IDA:SGD.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
 GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:SGD.
 GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; IMP:SGD. 
Interpro
 IPR013961; RAI1. 
Pfam
 PF08652; RAI1 
SMART
  
PROSITE
  
PRINTS