RNZ1_SCHPO
ID RNZ1_SCHPO Reviewed; 809 AA.
AC Q10155;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Ribonuclease Z 1;
DE Short=RNase Z 1;
DE EC=3.1.26.11;
DE AltName: Full=tRNA 3 endonuclease 1;
DE AltName: Full=tRNase Z 1;
GN Name=trz1; ORFNames=SPAC1D4.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21208191; DOI=10.1042/bj20101619;
RA Gan X., Yang J., Li J., Yu H., Dai H., Liu J., Huang Y.;
RT "The fission yeast Schizosaccharomyces pombe has two distinct tRNase Z(L)s
RT encoded by two different genes and differentially targeted to the nucleus
RT and mitochondria.";
RL Biochem. J. 435:103-111(2011).
CC -!- FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'-
CC processing endonuclease activity. May be involved in tRNA maturation,
CC by removing a 3'-trailer from precursor tRNA.
CC {ECO:0000269|PubMed:21208191}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:21208191}. Cytoplasm.
CC -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000305}.
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DR EMBL; CU329670; CAA93219.1; -; Genomic_DNA.
DR PIR; T38051; T38051.
DR RefSeq; NP_593023.1; NM_001018422.2.
DR AlphaFoldDB; Q10155; -.
DR SMR; Q10155; -.
DR STRING; 4896.SPAC1D4.10.1; -.
DR MaxQB; Q10155; -.
DR PaxDb; Q10155; -.
DR EnsemblFungi; SPAC1D4.10.1; SPAC1D4.10.1:pep; SPAC1D4.10.
DR GeneID; 2542457; -.
DR KEGG; spo:SPAC1D4.10; -.
DR PomBase; SPAC1D4.10; trz1.
DR VEuPathDB; FungiDB:SPAC1D4.10; -.
DR eggNOG; KOG2121; Eukaryota.
DR HOGENOM; CLU_006220_0_0_1; -.
DR InParanoid; Q10155; -.
DR OMA; YICQLKP; -.
DR PhylomeDB; Q10155; -.
DR BRENDA; 3.1.26.11; 5613.
DR PRO; PR:Q10155; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1902375; P:nuclear tRNA 3'-trailer cleavage, endonucleolytic; IMP:PomBase.
DR GO; GO:0042779; P:tRNA 3'-trailer cleavage; IMP:PomBase.
DR Gene3D; 3.60.15.10; -; 2.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR027794; tRNase_Z_dom.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR Pfam; PF13691; Lactamase_B_4; 1.
DR SUPFAM; SSF56281; SSF56281; 2.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..809
FT /note="Ribonuclease Z 1"
FT /id="PRO_0000155836"
FT REGION 74..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 809 AA; 90603 MW; 350FBE7B05FBF880 CRC64;
MSKTVNFRAT KNFYLQFVSV SSRDTSCIPC IHLFFDSKRY VFGSVGEGCQ RAILSQQLRL
SKIKDVFLMQ GSSISSPDTY DSSSSSSTTS VSDMLQLDDR DKVIVSERNS MCSTVNYPTW
WDSCGGFPGF LLSLNDISEP GETGEASPFV LHGPSEVHQF LSSMRHFTYH TNVNLTVQGY
TSAEAPVFVD ENICVTPVVV SLVKNSFKKR KHENINRGTN ARPLKEDRAN TSPHWYSHVS
NDTSFVVENA MYNTPAPLEP DKPELFISYI VQSHPTPGKF DAAKAKSLGI TKGLDCGRLA
RGEPVTLENG KTVYPKEVIG PSIPGSSFFI IHCPNELVID LVIENHKWTN APKPVCVIHS
VTPEVYKNPR YQSWISSFPS EVSHLIASTE VNEVINYPRS AVAIATLNLL DSKVFPLGFN
CYEVKNVQKN NRIAFAKPKL RFAFGKKTGI DDSEVGVSIE ELKDKILKEK PDYKSFVEEA
QKYVSDKPKA PSFAGSDIQI CTLGTGSAMP SLYRNVSSTY VRIPVDKKCM EDSAISMKNI
LLDCGEGTLG RLSRQYGDNL KYEIASLRWI YISHMHADHH AGVIGVLKAW TKYSDGRSKL
FITAPPQFEF WLLEYSRIDY LPLSNIVFIS NSALRTDRKP SALESSRLSS LFKEFDLVSF
RTVPAIHCPY SYCMEITNSS GWKIAYSGDT RPSEDFANIA KDSTLLIHEA TLEDSMHEIA
IKKQHSTYSE ALEVAKKAGT KNVILTHFSQ RYPKLPDIDI STEDLHIALA FDGMTLKISD
ISLFRYFGKP LAYLFNEENL KEESDPLKF
