CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015050
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Polyribonucleotide nucleotidyltransferase 
Protein Synonyms/Alias
 Polynucleotide phosphorylase; PNPase 
Gene Name
 pnp 
Gene Synonyms/Alias
 RPA0432 
Created Date
 July 27, 2013 
Organism
 Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) 
NCBI Taxa ID
 258594 
Lysine Modification
Position
Peptide
Type
References
304VFKELEAKIVRWNILacetylation[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
 Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3'- to 5'-direction (By similarity). 
Sequence Annotation
 DOMAIN 554 613 KH.
 DOMAIN 623 691 S1 motif.  
Keyword
 Complete proteome; Cytoplasm; Nucleotidyltransferase; RNA-binding; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 722 AA 
Protein Sequence
MFNIHSVEID WGGRPLKLET GKVARQADGA VVATYGETVV LATVVAAKAP REGVDFLPLT 60
VDYQEKAYAA GRIPGGYFKR EGRPTEKETL VSRLIDRPIR PLFADGWRNE TQVIVTVLSH 120
DMENDPDVLA MVAASAALTL SGVPFKGPIG AARVGFINDE YVLNPVLDEM AETQLELVVA 180
GTADAVLMVE SEAKELSEEI MLGAVMFGHR HFQPVIDAII DLAEKAAKEP RELTVVDDSE 240
IEKEMLGLVE QELRAAYAIP VKQDRYAAVG KVKEKAIAHF FPEGQEPKYD KLRIAGVFKE 300
LEAKIVRWNI LDTGKRIDGR DSKTVRNILA QVGVLPRTHG SALFTRGETQ AMVVTTLGTG 360
EDEQYVDSLS GTYKETFLLH YNFPPYSVGE TGRLGGTKRR EIGHGKLAWR AIHPVLPPHH 420
EFPYTIRVVS EITESNGSSS MASVCGASLA LMDAGVPLKR PTAGIAMGLI LEGERFAVLS 480
DILGDEDHLG DMDFKVAGTE AGITSLQMDI KIAGITEEIM KVALGQAKDG RIHILGEMSK 540
ALDRARAELG EHAPRIETFK IPTDKIREVI GTGGKVIREI VEKTGAKVNI EDDGTVKVAS 600
SDGESIKAAI KWIKSIASDP EVGEIYEGTV VKVMEFGAFV NFFGAKDGLV HISQLAAGRV 660
QKTSDVVKEG DKVKVKLLGF DDRGKTRLSM KVVDQTTGED LEAKQKAEAK AEGEAPAQAA 720
GE 722 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro.
 GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:HAMAP.
 GO:0003723; F:RNA binding; IEA:HAMAP.
 GO:0006402; P:mRNA catabolic process; IEA:HAMAP.
 GO:0006396; P:RNA processing; IEA:InterPro. 
Interpro
 IPR001247; ExoRNase_PH_dom1.
 IPR015847; ExoRNase_PH_dom2.
 IPR004087; KH_dom.
 IPR004088; KH_dom_type_1.
 IPR012340; NA-bd_OB-fold.
 IPR012162; PNPase.
 IPR027408; PNPase/RNase_PH_dom.
 IPR015848; PNPase_PH_RNA-bd_bac/org-type.
 IPR003029; Rbsml_prot_S1_RNA-bd_dom.
 IPR020568; Ribosomal_S5_D2-typ_fold.
 IPR022967; RNA-binding_domain_S1. 
Pfam
 PF00013; KH_1
 PF03726; PNPase
 PF01138; RNase_PH
 PF03725; RNase_PH_C
 PF00575; S1 
SMART
 SM00322; KH
 SM00316; S1 
PROSITE
 PS50084; KH_TYPE_1
 PS50126; S1 
PRINTS