※ dbPPT Protein Information
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UniProt Accession | |||||||||||||||||||||||||||||||
Theoretical PI | 5.94 | ||||||||||||||||||||||||||||||
Molecular Weight | 117058.43 | ||||||||||||||||||||||||||||||
Genbank Protein ID | |||||||||||||||||||||||||||||||
Genbank Nucleotide ID | |||||||||||||||||||||||||||||||
Protein Name | DIS3-like exonuclease 2 | ||||||||||||||||||||||||||||||
Gene Name | BRADI3G58790 | ||||||||||||||||||||||||||||||
Created Date | 2012-06-13 | ||||||||||||||||||||||||||||||
Organism | Brachypodium distachyon(Purple false brome Trachynia distachya) | ||||||||||||||||||||||||||||||
NCBI Taxa ID | 15368 | ||||||||||||||||||||||||||||||
Phosphorylation Sites |
Functional Description 3'-5'-exoribonuclease that specifically recognizes RNAs polyuridylated at their 3' end and mediates their degradation. Component of an exosome-independent RNA degradation pathway that mediates degradation of cytoplasmic mRNAs that have been deadenylated and subsequently uridylated at their 3' (By similarity). Sequence Annotation Keyword Complete proteome,Cytoplasm,Exonuclease,Hydrolase,Magnesium,Manganese,Nuclease,Reference proteome,RNA-binding Sequence Source UniProt Protein Sequence MRATEEHTAT APTHAAPPPQ TEEDAEKERR RRRRPARRAK QQAAPPVAAP QAAPQVDMAG 60 PRPSRSMPPP MRVGNRFDAL AVAEPEPAAG TSRSCPLLPA PFPGAVAQAR AAPVVGMGVG 120 GAPRRLYFPP YWPDQVVEEA IQAYCTIDGI PVDVLMTGPA QNRAIEGDTV AITLDPVVQW 180 TRMKGPNSTC NPATGGVSVV REVSETNGNH SSKRGQADTS CRFENCSNGL SVSDRMHNHH 240 KNSGFSQAVK CENGHAIVPE SYEDLNEGKT EAAIALQRIC SVIYSHPSRR PTGKVVSVIK 300 MSSRRGAVVG FLAPLSEFPD GEPHRNQMNV QGSKRMNHIA SSFVTGLVHL LPTDPKFPLM 360 IVSVSTLPDS IRQSLKEGNI AIEKEIVAAC IDEWNEESPF PWARVVKFLG KGGQVESHMD 420 AILFENSISD AEFSPESMAC LPDVCWKIPQ EELEARKDLR NVLTFTIDPP TASDLDDAIS 480 IEILPEGIVR VGVHIADVSY FVHPETALDA EAQIRSTSVY TLRRKVSMLP SRLSAELVSL 540 NPGADKLAFS VIWDIDPHGS IVNRWIGRTI IFSCCKLSYD LVQDLISSDV SQFGSVAASL 600 QVHGMFEQGD IIKSLRCLYE ITKNLKEIRF KGGALSLDTA KPMILFDEDG APCDSYRYKR 660 NDACFIVEEL MLLANMSAAE VISNAFPDCA LLRRHPEPNP RKLKEFEAFC ARNGFELDSS 720 SSGQLHLSIS RMKEKLQNDP VMFDILMFYA SKQMQSAEYF CTGDLISKND DWAHYALSVP 780 LYTHFTSPLR RYPDIIVHRT LNAVIEAEQM YLKQKKVSTV RNGVKAKSCE MMDRCFTGLQ 840 FSKDAAESKE GREALSAAAK KFKFPSSDDL GEAAEHCNER KWASRRAEEA GQKLYMWALL 900 KRNEIKVSNA RVLGLGPRFM SVYVPKLSME RRIYYDEVEG LSIEWLEATG TLVVDACRNK 960 PAQRRGSQFK CSRAIEEVAV VVNPSELMLS EDKDESGATG TGDPTADSVL LSDDAVEAQV 1020 APAVLPLVIR YLSDIPVVLH AIGGEDCQVD IGVRLYISSY FK 1062 Gene Ontology GO:0000932; C: cytoplasmic mRNA processing body; IEA: UniProtKB-SubCell GO:0000175; F: 3'-5'-exoribonuclease activity; IEA: UniProtKB-HAMAP GO:0003723; F: RNA binding; IEA: UniProtKB-KW GO:0010587; P: miRNA catabolic process; IEA: UniProtKB-HAMAP GO:0034427; P: nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IEA: InterPro GO:1990074; P: polyuridylation-dependent mRNA catabolic process; IEA: UniProtKB-HAMAP Interpro Pfam SMART PROSITE PS01175; RIBONUCLEASE_II PRINTS |