CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005920
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Exoribonuclease 2 
Protein Synonyms/Alias
 Exoribonuclease II; RNase II; Ribonuclease II 
Gene Name
 rnb 
Gene Synonyms/Alias
 b1286; JW1279 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
31GVVKATEKGFGFLEVacetylation[1]
68IAVIHSEKERESAEPacetylation[1]
107VPDHPLLKDAIPCRAacetylation[1]
123RGLNHEFKEGDWAVAacetylation[1]
172LARHNLEKEAPDGVAacetylation[1]
359HNHALVFKDRPDYRFacetylation[1]
371YRFILGEKGEVLDIVacetylation[1]
501TWTSPIRKYGDMINHacetylation[1, 2]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 
Functional Description
 Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction. 
Sequence Annotation
 DOMAIN 561 643 S1 motif.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 644 AA 
Protein Sequence
MFQDNPLLAQ LKQQLHSQTP RAEGVVKATE KGFGFLEVDA QKSYFIPPPQ MKKVMHGDRI 60
IAVIHSEKER ESAEPEELVE PFLTRFVGKV QGKNDRLAIV PDHPLLKDAI PCRAARGLNH 120
EFKEGDWAVA EMRRHPLKGD RSFYAELTQY ITFGDDHFVP WWVTLARHNL EKEAPDGVAT 180
EMLDEGLVRE DLTALDFVTI DSASTEDMDD ALFAKALPDD KLQLIVAIAD PTAWIAEGSK 240
LDKAAKIRAF TNYLPGFNIP MLPRELSDDL CSLRANEVRP VLACRMTLSA DGTIEDNIEF 300
FAATIESKAK LVYDQVSDWL ENTGDWQPES EAIAEQVRLL AQICQRRGEW RHNHALVFKD 360
RPDYRFILGE KGEVLDIVAE PRRIANRIVE EAMIAANICA ARVLRDKLGF GIYNVHMGFD 420
PANADALAAL LKTHGLHVDA EEVLTLDGFC KLRRELDAQP TGFLDSRIRR FQSFAEISTE 480
PGPHFGLGLE AYATWTSPIR KYGDMINHRL LKAVIKGETA TRPQDEITVQ MAERRRLNRM 540
AERDVGDWLY ARFLKDKAGT DTRFAAEIVD ISRGGMRVRL VDNGAIAFIP APFLHAVRDE 600
LVCSQENGTV QIKGETVYKV TDVIDVTIAE VRMETRSIIA RPVA 644 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0008408; F:3'-5' exonuclease activity; IGI:EcoCyc.
 GO:0008859; F:exoribonuclease II activity; IEA:HAMAP.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0006402; P:mRNA catabolic process; IEA:HAMAP.
 GO:0016078; P:tRNA catabolic process; IGI:EcoCyc. 
Interpro
 IPR011129; Cold_shock_prot.
 IPR012340; NA-bd_OB-fold.
 IPR003029; Rbsml_prot_S1_RNA-bd_dom.
 IPR022967; RNA-binding_domain_S1.
 IPR013223; RNase_B_OB_dom.
 IPR011804; RNase_II.
 IPR001900; RNase_II/R.
 IPR022966; RNase_II/R_CS.
 IPR004476; RNase_II/RNase_R. 
Pfam
 PF08206; OB_RNB
 PF00773; RNB
 PF00575; S1 
SMART
 SM00357; CSP
 SM00955; RNB
 SM00316; S1 
PROSITE
 PS01175; RIBONUCLEASE_II
 PS50126; S1 
PRINTS