RNZ_YEAST
ID RNZ_YEAST Reviewed; 838 AA.
AC P36159; D6VXD9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Ribonuclease Z;
DE Short=RNase Z;
DE EC=3.1.26.11;
DE AltName: Full=tRNA 3 endonuclease;
DE AltName: Full=tRNase Z;
GN Name=TRZ1; OrderedLocusNames=YKR079C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP ENZYME ACTIVITY.
RX PubMed=12711671; DOI=10.1093/nar/gkg337;
RA Takaku H., Minagawa A., Takagi M., Nashimoto M.;
RT "A candidate prostate cancer susceptibility gene encodes tRNA 3' processing
RT endoribonuclease.";
RL Nucleic Acids Res. 31:2272-2278(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-824, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-824, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'-
CC processing endonuclease activity. Probably involved in tRNA maturation,
CC by removing a 3'-trailer from precursor tRNA.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing extra 3' nucleotides
CC from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy
CC group is left at the tRNA terminus and a 5'-phosphoryl group is left
CC at the trailer molecule.; EC=3.1.26.11;
CC Evidence={ECO:0000269|PubMed:12711671};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2710 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z28304; CAA82158.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09229.1; -; Genomic_DNA.
DR PIR; S38156; S38156.
DR RefSeq; NP_013005.1; NM_001179869.1.
DR PDB; 5MTZ; X-ray; 2.99 A; A/B=2-838.
DR PDBsum; 5MTZ; -.
DR AlphaFoldDB; P36159; -.
DR SMR; P36159; -.
DR BioGRID; 34210; 28.
DR DIP; DIP-5339N; -.
DR IntAct; P36159; 4.
DR MINT; P36159; -.
DR STRING; 4932.YKR079C; -.
DR iPTMnet; P36159; -.
DR MaxQB; P36159; -.
DR PaxDb; P36159; -.
DR PRIDE; P36159; -.
DR EnsemblFungi; YKR079C_mRNA; YKR079C; YKR079C.
DR GeneID; 853954; -.
DR KEGG; sce:YKR079C; -.
DR SGD; S000001787; TRZ1.
DR VEuPathDB; FungiDB:YKR079C; -.
DR eggNOG; KOG2121; Eukaryota.
DR GeneTree; ENSGT00730000111191; -.
DR HOGENOM; CLU_006220_0_0_1; -.
DR InParanoid; P36159; -.
DR OMA; MSHCKHT; -.
DR BioCyc; YEAST:G3O-32043-MON; -.
DR BRENDA; 3.1.26.11; 984.
DR PRO; PR:P36159; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36159; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990180; P:mitochondrial tRNA 3'-end processing; IDA:SGD.
DR GO; GO:0072684; P:mitochondrial tRNA 3'-trailer cleavage, endonucleolytic; IBA:GO_Central.
DR GO; GO:0042780; P:tRNA 3'-end processing; IDA:SGD.
DR GO; GO:0034414; P:tRNA 3'-trailer cleavage, endonucleolytic; IDA:SGD.
DR Gene3D; 3.60.15.10; -; 2.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR027794; tRNase_Z_dom.
DR Pfam; PF13691; Lactamase_B_4; 1.
DR SUPFAM; SSF56281; SSF56281; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW Nucleus; Phosphoprotein; Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..838
FT /note="Ribonuclease Z"
FT /id="PRO_0000155837"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:5MTZ"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:5MTZ"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 125..137
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 192..200
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 281..288
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:5MTZ"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 330..342
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 358..363
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:5MTZ"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 425..432
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 443..447
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 460..464
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 467..472
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 486..494
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 500..509
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 513..520
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 523..531
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 533..537
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 543..546
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 549..560
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 568..571
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 574..587
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 589..593
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 601..603
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 604..607
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 619..621
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 641..644
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 648..658
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 660..667
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 669..671
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 675..682
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 691..696
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 704..711
FT /evidence="ECO:0007829|PDB:5MTZ"
FT TURN 712..714
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 716..721
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 726..728
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 729..735
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 740..750
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 753..758
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 778..783
FT /evidence="ECO:0007829|PDB:5MTZ"
FT STRAND 788..791
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 792..794
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 796..801
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 802..807
FT /evidence="ECO:0007829|PDB:5MTZ"
FT HELIX 810..816
FT /evidence="ECO:0007829|PDB:5MTZ"
SQ SEQUENCE 838 AA; 96816 MW; 473A69D9C10167AB CRC64;
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
