Tag | Content |
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CPLM ID | CPLM-013871 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ribonuclease Y |
Protein Synonyms/Alias | RNase Y |
Gene Name | rny |
Gene Synonyms/Alias | TTHA1817 |
Created Date | July 27, 2013 |
Organism | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) |
NCBI Taxa ID | 300852 |
Lysine Modification | Position | Peptide | Type | References |
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132 | RSLQEELKEERERLK | acetylation | [1] |
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Reference | [1] Acetylome with structural mapping reveals the significance of lysine acetylation in Thermus thermophilus. Okanishi H, Kim K, Masui R, Kuramitsu S. J Proteome Res. 2013 Aug 1;. [ PMID: 23901841] |
Functional Description | Endoribonuclease that initiates mRNA decay (By similarity). |
Sequence Annotation | DOMAIN 264 327 KH. DOMAIN 391 482 HD. |
Keyword | Cell membrane; Complete proteome; Endonuclease; Hydrolase; Membrane; Nuclease; Reference proteome; RNA-binding; Transmembrane; Transmembrane helix. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 574 AA |
Protein Sequence | MSLLDLVLLL LVLGLGGVLL LRRKGEDRSA QEARELLEAA RREAREVLEA ARKEARDILE 60 AARQEAKALR QEAEARAKAQ REEVEAELRR RLEAAEAEAK KRLEEAGERL KAEREELRAE 120 RERLRSLQEE LKEERERLKA EREELRREGE RLAKRAEALD ARAARLEEAE AELVRKEEAL 180 KAEARALEER LKEVERRLYE VAGLTPEEAR RLVLERLDRE LEEEKAQRVR AALERARLEA 240 RREAQKILAQ AMQRQASETA AQLAVTVVPI PSDAMKGRII GREGRNIRAF EALTGVDLII 300 DDTPDAVLLS SFNPIRREIA RMALEELLKD GRIHPSRIEE VVEKAKQEMK TFIYERGEEA 360 ALEAGVVGLK PGLIQLLGRL HFRSSYGQNV LKHSIQVAHL AGIMAAELGL DAALARRAGL 420 LHDIGKSVDR EVEGSHVEIG IALARRFGEP KEVVDAIAHH HDPDNAETLY AVLVAAADAL 480 SAARPGARRE SLEEYLQRLE ALERIALSFP GVETAFAVQA GREVRVIVKP EKISDAKATL 540 LAREIASRIE KEMNYPGQVQ VTVVRETRAV EYAR 574 |
Gene Ontology | GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. GO:0004521; F:endoribonuclease activity; IEA:HAMAP. GO:0046872; F:metal ion binding; IEA:InterPro. GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro. GO:0003723; F:RNA binding; IEA:HAMAP. GO:0006402; P:mRNA catabolic process; IEA:HAMAP. |
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Pfam | |
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PROSITE | |
PRINTS | |