RNZ2_ARATH
ID RNZ2_ARATH Reviewed; 354 AA.
AC Q8L633; Q8LGU8; Q9SJB8;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=tRNase Z TRZ2, chloroplastic {ECO:0000303|PubMed:16336119};
DE EC=3.1.26.11 {ECO:0000269|PubMed:12032089};
DE AltName: Full=Chloroplast ribonuclease Z {ECO:0000303|PubMed:12032089};
DE Short=Chloroplast RNase Z {ECO:0000303|PubMed:12032089};
DE AltName: Full=Short tRNase Z 2 {ECO:0000303|PubMed:16336119};
DE AltName: Full=Zinc phosphodiesterase CPZ {ECO:0000303|PubMed:12032089};
DE AltName: Full=tRNA 3 endonuclease;
DE AltName: Full=tRNase ZS2 {ECO:0000303|PubMed:16336119};
DE Short=AthTRZS2 {ECO:0000303|PubMed:16336119};
DE Flags: Precursor;
GN Name=TRZ2 {ECO:0000303|PubMed:16336119};
GN Synonyms=CPZ {ECO:0000303|PubMed:12032089};
GN OrderedLocusNames=At2g04530 {ECO:0000312|Araport:AT2G04530};
GN ORFNames=T1O3.6 {ECO:0000312|EMBL:AAD25827.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=12032089; DOI=10.1093/emboj/21.11.2769;
RA Schiffer S., Roesch S., Marchfelder A.;
RT "Assigning a function to a conserved group of proteins: the tRNA 3'
RT - processing enzymes.";
RL EMBO J. 21:2769-2777(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16336119; DOI=10.1515/bc.2005.142;
RA Vogel A., Schilling O., Spaeth B., Marchfelder A.;
RT "The tRNase Z family of proteins: physiological functions, substrate
RT specificity and structural properties.";
RL Biol. Chem. 386:1253-1264(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19411372; DOI=10.1104/pp.109.137950;
RA Canino G., Bocian E., Barbezier N., Echeverria M., Forner J., Binder S.,
RA Marchfelder A.;
RT "Arabidopsis encodes four tRNase Z enzymes.";
RL Plant Physiol. 150:1494-1502(2009).
CC -!- FUNCTION: Zinc phosphodiesterase, which displays tRNA 3'-processing
CC endonuclease activity. Involved in tRNA maturation, by removing a 3'-
CC trailer from precursor tRNA. {ECO:0000269|PubMed:12032089,
CC ECO:0000269|PubMed:19411372}.
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:12032089};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q8LGU7};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q8LGU7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8LGU7};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8LGU7};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8LGU7}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:19411372}.
CC -!- TISSUE SPECIFICITY: Highly expressed in green and actively dividing
CC tissues. {ECO:0000305|PubMed:19411372}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous.
CC {ECO:0000269|PubMed:19411372}.
CC -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25827.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ428988; CAD22099.1; -; mRNA.
DR EMBL; AC006951; AAD25827.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC05843.1; -; Genomic_DNA.
DR EMBL; AY099564; AAM20416.1; -; mRNA.
DR EMBL; BT001247; AAN65134.1; -; mRNA.
DR PIR; E84458; E84458.
DR RefSeq; NP_178532.2; NM_126484.5.
DR AlphaFoldDB; Q8L633; -.
DR SMR; Q8L633; -.
DR STRING; 3702.AT2G04530.1; -.
DR PaxDb; Q8L633; -.
DR PRIDE; Q8L633; -.
DR ProteomicsDB; 228214; -.
DR EnsemblPlants; AT2G04530.1; AT2G04530.1; AT2G04530.
DR GeneID; 814995; -.
DR Gramene; AT2G04530.1; AT2G04530.1; AT2G04530.
DR KEGG; ath:AT2G04530; -.
DR Araport; AT2G04530; -.
DR TAIR; locus:2058374; AT2G04530.
DR eggNOG; ENOG502S564; Eukaryota.
DR HOGENOM; CLU_054121_0_0_1; -.
DR InParanoid; Q8L633; -.
DR OMA; TRNNAMG; -.
DR OrthoDB; 1387038at2759; -.
DR PhylomeDB; Q8L633; -.
DR BRENDA; 3.1.26.11; 399.
DR PRO; PR:Q8L633; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8L633; baseline and differential.
DR Genevisible; Q8L633; AT.
DR GO; GO:0009507; C:chloroplast; ISS:TAIR.
DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042780; P:tRNA 3'-end processing; IDA:TAIR.
DR GO; GO:0008033; P:tRNA processing; TAS:TAIR.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 2: Evidence at transcript level;
KW Calcium; Chloroplast; Endonuclease; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Nuclease; Plastid; Reference proteome; Transit peptide;
KW tRNA processing; Zinc.
FT TRANSIT 1..68
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 69..354
FT /note="tRNase Z TRZ2, chloroplastic"
FT /id="PRO_0000030991"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 107
FT /note="G -> V (in Ref. 1; CAD22099)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="K -> R (in Ref. 1; CAD22099)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="K -> R (in Ref. 1; CAD22099)"
FT /evidence="ECO:0000305"
FT CONFLICT 242..243
FT /note="DT -> YA (in Ref. 1; CAD22099)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="D -> N (in Ref. 1; CAD22099)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="D -> N (in Ref. 1; CAD22099)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="D -> N (in Ref. 1; CAD22099)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="T -> S (in Ref. 1; CAD22099)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 39951 MW; F8374B7784C3B945 CRC64;
MQLSSSFPIS PPKIFPSTKH HKPPVITHQL AAQIQSNRRH FVSPVKVSGY FSSISRAIEE
EEEYRKARAA VNRKGVELES YAIEGISVGG HETCVIVPEL KCVFDIGRCP SRAIQQKFLF
ITHAHLDHIG GLPMYVASRG LYNLEPPKIF VPPSIKEDVE KLLEIHRTMG QVELNVELIP
LAVGETYELR NDIVVRPFAT HHVIPSQGYV IYSVRKKLQK QYAHLKGKQI EKIKKSGVEI
TDTILSPEIA FTGDTTSEYM LDPRNADALR AKVLITEATF LDESFSTEHA QALGHTHISQ
IIENAKWIRS KTVLLTHFSS RYHVEEIREA VLKLQSKVSA KVIPLTEGFR SRYS
