RNZ2_SCHPO
ID RNZ2_SCHPO Reviewed; 678 AA.
AC P87168;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Ribonuclease Z 2, mitochondrial;
DE Short=RNase Z 2;
DE EC=3.1.26.11;
DE AltName: Full=tRNA 3 endonuclease 2;
DE AltName: Full=tRNase Z 2;
DE Flags: Precursor;
GN Name=trz2; ORFNames=SPBC3D6.03c;
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: Mitochondrion {ECO:0000269|PubMed:21208191}.
CC Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000305}.
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DR EMBL; CU329671; CAB09123.1; -; Genomic_DNA.
DR PIR; T40362; T40362.
DR RefSeq; NP_595514.1; NM_001021423.2.
DR AlphaFoldDB; P87168; -.
DR SMR; P87168; -.
DR STRING; 4896.SPBC3D6.03c.1; -.
DR MaxQB; P87168; -.
DR PaxDb; P87168; -.
DR PRIDE; P87168; -.
DR EnsemblFungi; SPBC3D6.03c.1; SPBC3D6.03c.1:pep; SPBC3D6.03c.
DR GeneID; 2540985; -.
DR KEGG; spo:SPBC3D6.03c; -.
DR PomBase; SPBC3D6.03c; trz2.
DR VEuPathDB; FungiDB:SPBC3D6.03c; -.
DR eggNOG; KOG2121; Eukaryota.
DR HOGENOM; CLU_422817_0_0_1; -.
DR InParanoid; P87168; -.
DR OMA; YNPWSAT; -.
DR PhylomeDB; P87168; -.
DR BRENDA; 3.1.26.11; 5613.
DR PRO; PR:P87168; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; 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:0072684; P:mitochondrial tRNA 3'-trailer cleavage, endonucleolytic; IDA:PomBase.
DR GO; GO:0031426; P:polycistronic mRNA processing; 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 SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Mitochondrion; Nuclease;
KW Reference proteome; Transit peptide; tRNA processing; Zinc.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 38..678
FT /note="Ribonuclease Z 2, mitochondrial"
FT /id="PRO_0000315962"
SQ SEQUENCE 678 AA; 75987 MW; 6C10654707315B78 CRC64;
MKASLLVPRR ALLFGQLLPP KYSWYSVKRW QSQLTFRNKS KRNTNRIMLS VVSSLNPDSL
IAPLLCVSLD NRKYLIGSMG ELTQMKFRSQ ASNYGGKSVS VFLMPPSLQS LNAWGITAGL
FGYLQSSGIQ NTWGLHAPKP VISIIKKSHH LFSGSPLRLD LNSFSSEDNA DATNSFYLDE
PEFCTIKGNI YSNWSFLSFN SKEAAGVFNA DKALALGVPF GPSNGKLCAG EAVLSKDGTT
WIYPHQVVGP PRKRQYFYVL GCSSLSALNQ MSKHVDSFSD VYPTCIIHIL EKGIWGPEYI
KFLSHPKFSR AQHFISCIEL ASNNPVFQRN KGRNVLPACR DFAAFDIKPS TLDTQTQLPE
NTYVLKEETS MVLYDEQCKI SESPSYSPVK LAKKFSSFNP LPFENEGYTL DVLGTSATCP
TWRRSLSSYS VAIDGTVIML DCGEGAISQF FRQYGTNTEP MLRKLKAIFI THLHSDHYLG
LLNVLQAWNK ANTNNSMHIN IIGPKFLWQW LQRLKSPANL QALLNRIIFI IAKETVTTPL
QLTSDLSISS VPSIHINDSY SCIISHTKYG KLVYSGDTRP NEKLVKAGIG ASLLLHESTF
EDDLKHEAIQ RQHSTASEAL SVAQSMKAKA LILTHFSQRS YDADFLPPDW TIYPKSKTIY
ANDGLQWQQF QSKQRETI