Basic Information
Name | Ribonuclease Z (RNase Z) (EC 3.1.26.11) (tRNA 3 endonuclease) (tRNase Z) |
Uniprot ID | P36159 |
Systematic gene name | YKR079C |
Standard gene name | TRZ1 |
Gene names | TRZ1 YKR079C |
Description from SGD | YKR079C TRZ1 SGDID:S000001787, Chr XI from 589305-586789, Genome Release 64-3-1, reverse complement, Verified ORF, "tRNA 3'-end processing endonuclease tRNase Z; also localized to mitochondria and interacts genetically with Rex2 exonuclease; homolog of the human candidate prostate cancer susceptibility gene ELAC2" |
Protein length | 838 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MFTFIPITHP TSDTKHPLLL VQSAHGEKYF FGKIGEGSQR SLTENKIRIS
KLKDIFLTGE LNWSDIGGLP GMILTIADQG KSNLVLHYGN DILNYIVSTW
RYFVFRFGID LNDHIMKDKE VYKDKIIAVK SFNVLKNGGE DRLGVFDSFQ
KGVLRSIVAK MFPKHAPTDR YDPSSDPHLN VELPDLDAKV EVSTNYEISF
SPVRGKFKVE EAIKLGVPKG PLFAKLTKGQ TITLDNGIVV TPEQVLENER
HFAKVLILDI PDDLYLNAFV EKFKDYDCAE LGMVYYFLGD EVTINDNLFA
FIDIFEKNNY GKVNHMISHN KISPNTISFF GSALTTLKLK ALQVNNYNLP
KTDRVFSKDF YDRFDTPLSR GTSMCKSQEE PLNTIIEKDN IHIFSQNKTV
TFEPFRMNEE PMKCNINGEV ADFSWQEIFE EHVKPLEFPL ADVDTVINNQ
LHVDNFNNSA EKKKHVEIIT LGTGSALPSK YRNVVSTLVK VPFTDADGNT
INRNIMLDAG ENTLGTIHRM FSQLAVKSIF QDLKMIYLSH LHADHHLGII
SVLNEWYKYN KDDETSYIYV VTPWQYHKFV NEWLVLENKE ILKRIKYISC
EHFINDSFVR MQTQSVPLAE FNEILKENSN QESNRKLELD RDSSYRDVDL
IRQMYEDLSI EYFQTCRAIH CDWAYSNSIT FRMDENNEHN TFKVSYSGDT
RPNIEKFSLE IGYNSDLLIH EATLENQLLE DAVKKKHCTI NEAIGVSNKM
NARKLILTHF SQRYPKLPQL DNNIDVMARE FCFAFDSMIV DYEKIGEQQR
IFPLLNKAFV EEKEEEEDVD DVESVQDLEV KLKKHKKN
KLKDIFLTGE LNWSDIGGLP GMILTIADQG KSNLVLHYGN DILNYIVSTW
RYFVFRFGID LNDHIMKDKE VYKDKIIAVK SFNVLKNGGE DRLGVFDSFQ
KGVLRSIVAK MFPKHAPTDR YDPSSDPHLN VELPDLDAKV EVSTNYEISF
SPVRGKFKVE EAIKLGVPKG PLFAKLTKGQ TITLDNGIVV TPEQVLENER
HFAKVLILDI PDDLYLNAFV EKFKDYDCAE LGMVYYFLGD EVTINDNLFA
FIDIFEKNNY GKVNHMISHN KISPNTISFF GSALTTLKLK ALQVNNYNLP
KTDRVFSKDF YDRFDTPLSR GTSMCKSQEE PLNTIIEKDN IHIFSQNKTV
TFEPFRMNEE PMKCNINGEV ADFSWQEIFE EHVKPLEFPL ADVDTVINNQ
LHVDNFNNSA EKKKHVEIIT LGTGSALPSK YRNVVSTLVK VPFTDADGNT
INRNIMLDAG ENTLGTIHRM FSQLAVKSIF QDLKMIYLSH LHADHHLGII
SVLNEWYKYN KDDETSYIYV VTPWQYHKFV NEWLVLENKE ILKRIKYISC
EHFINDSFVR MQTQSVPLAE FNEILKENSN QESNRKLELD RDSSYRDVDL
IRQMYEDLSI EYFQTCRAIH CDWAYSNSIT FRMDENNEHN TFKVSYSGDT
RPNIEKFSLE IGYNSDLLIH EATLENQLLE DAVKKKHCTI NEAIGVSNKM
NARKLILTHF SQRYPKLPQL DNNIDVMARE FCFAFDSMIV DYEKIGEQQR
IFPLLNKAFV EEKEEEEDVD DVESVQDLEV KLKKHKKN
Legend
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[148, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[201, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[366, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[369, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[377, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[551, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[551, Phos] | Holt, L.J., Tuch, B.B., Villén, J., Johnson, A.D., Gygi, S.P., Morgan, D.O. (2009). Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325(5948): 1682-1686. (Publication) (All modifications) |
[551, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[824, Phos] | Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications) |
[824, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[824, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[824, Phos] | Albuquerque, C.P., Smolka, M.B., Payne, S.H., Bafna, V., Eng, J., Zhou, H. (2008). A multidimensional chromatography technology for in-depth phosphoproteome analysis. Molecular and Cellular Proteomics 7(7):1389-1396. (Publication) (All modifications) |
[824, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |