RNZ3_ARATH
ID RNZ3_ARATH Reviewed; 890 AA.
AC Q8VYS2; Q8H140; Q9M819;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=tRNase Z TRZ3, mitochondrial {ECO:0000303|PubMed:16336119};
DE EC=3.1.26.11 {ECO:0000269|PubMed:19411372};
DE AltName: Full=Long tRNase Z 1 {ECO:0000303|PubMed:16336119};
DE AltName: Full=tRNase ZL1 {ECO:0000303|PubMed:16336119};
DE Short=AthTRZL1 {ECO:0000303|PubMed:16336119};
DE Flags: Precursor;
GN Name=TRZ3 {ECO:0000303|PubMed:16336119};
GN OrderedLocusNames=At1g52160 {ECO:0000312|Araport:AT1G52160};
GN ORFNames=F9I5.1 {ECO:0000312|EMBL:AAF29402.1};
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 {ECO:0000312|EMBL:AAL49818.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP 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).
RN [6]
RP FUNCTION.
RX PubMed=19420328; DOI=10.1104/pp.109.137968;
RA Barbezier N., Canino G., Rodor J., Jobet E., Saez-Vasquez J.,
RA Marchfelder A., Echeverria M.;
RT "Processing of a dicistronic tRNA-snoRNA precursor: combined analysis in
RT vitro and in vivo reveals alternate pathways and coupling to assembly of
RT snoRNP.";
RL Plant Physiol. 150:1598-1610(2009).
CC -!- FUNCTION: Zinc phosphodiesterase, which displays tRNA 3'-processing
CC endonuclease activity (PubMed:19411372). Involved in tRNA maturation,
CC by removing a 3'-trailer from precursor tRNA (PubMed:19411372). Can
CC process the mitochondrial tRNA-like structures (t-elements)
CC (PubMed:19411372). Involved in the processing of small nucleolar RNAs
CC (snoRNAs) (PubMed:19420328). {ECO:0000269|PubMed:19411372,
CC ECO:0000269|PubMed:19420328}.
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:19411372};
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: Mitochondrion {ECO:0000269|PubMed:19411372}.
CC Nucleus {ECO:0000269|PubMed:19411372}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype due to the redundancy with
CC TRZ4. Trz3 and trz4 double mutants are lethal.
CC {ECO:0000269|PubMed:19411372}.
CC -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29402.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC022354; AAF29402.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32764.1; -; Genomic_DNA.
DR EMBL; AY070061; AAL49818.1; -; mRNA.
DR EMBL; AY117303; AAM51378.1; -; mRNA.
DR EMBL; BT000791; AAN31930.1; -; mRNA.
DR PIR; F96561; F96561.
DR RefSeq; NP_175628.2; NM_104097.6.
DR AlphaFoldDB; Q8VYS2; -.
DR SMR; Q8VYS2; -.
DR STRING; 3702.AT1G52160.1; -.
DR PaxDb; Q8VYS2; -.
DR PRIDE; Q8VYS2; -.
DR ProteomicsDB; 226811; -.
DR EnsemblPlants; AT1G52160.1; AT1G52160.1; AT1G52160.
DR GeneID; 841647; -.
DR Gramene; AT1G52160.1; AT1G52160.1; AT1G52160.
DR KEGG; ath:AT1G52160; -.
DR Araport; AT1G52160; -.
DR TAIR; locus:2037430; AT1G52160.
DR eggNOG; KOG2121; Eukaryota.
DR HOGENOM; CLU_006220_2_0_1; -.
DR InParanoid; Q8VYS2; -.
DR OMA; HEAMQIS; -.
DR OrthoDB; 454909at2759; -.
DR PhylomeDB; Q8VYS2; -.
DR BRENDA; 3.1.26.11; 399.
DR PRO; PR:Q8VYS2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VYS2; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0072684; P:mitochondrial tRNA 3'-trailer cleavage, endonucleolytic; IBA:GO_Central.
DR GO; GO:0042780; P:tRNA 3'-end processing; IDA:TAIR.
DR Gene3D; 3.60.15.10; -; 2.
DR HAMAP; MF_01818; RNase_Z_BN; 1.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR013471; RNase_Z/BN.
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 Calcium; Endonuclease; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Mitochondrion; Nuclease; Nucleus; Reference proteome; Transit peptide;
KW tRNA processing; Zinc.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 45..890
FT /note="tRNase Z TRZ3, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439063"
FT REGION 46..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 890 AA; 98640 MW; 91F6FB2A2B4763F2 CRC64;
MINSMPYLHK NLRLLRLLSS KSSPFPLSLR PFSPRSFSLS TLFSSSSSSS SMENNEATNG
SKSSSNSFVF NKRRAEGFDI TDKKKRNLER KSQKLNPTNT IAYAQILGTG MDTQDTSSSV
LLFFDKQRFI FNAGEGLQRF CTEHKIKLSK IDHVFLSRVC SETAGGLPGL LLTLAGIGEE
GLSVNVWGPS DLNYLVDAMK SFIPRAAMVH TRSFGPSSTP DPIVLVNDEV VKISAIILKP
CHSEEDSGNK SGDLSVVYVC ELPEILGKFD LEKAKKVFGV KPGPKYSRLQ SGESVKSDER
DITVHPSDVM GPSLPGPIVL LVDCPTESHA AELFSLKSLE SYYSSPDEQT IGAKFVNCII
HLSPSSVTSS PTYQSWMKKF HLTQHILAGH QRKNMAFPIL KASSRIAARL NYLCPQFFPA
PGFWPSQLTD NSIIDPTPSN KCSSSNLAES ISAENLLKFN LRPVAIRGID RSCIPAPLTS
SEVVDELLSE IPEIKDKSEE IKQFWNKQHN KTIIEKLWLS ECNTVLPNCL EKIRRDDMEI
VILGTGSSQP SKYRNVSAIF IDLFSRGSLL LDCGEGTLGQ LKRRYGLDGA DEAVRKLRCI
WISHIHADHH TGLARILALR SKLLKGVTHE PVIVVGPRPL KRFLDAYQRL EDLDMEFLDC
RSTTATSWAS LESGGEAEGS LFTQGSPMQS VFKRSDISMD NSSVLLCLKN LKKVLSEIGL
NDLISFPVVH CPQAYGVVIK AAERVNSVGE QILGWKMVYS GDSRPCPETV EASRDATILI
HEATFEDALI EEALAKNHST TKEAIDVGSA ANVYRIVLTH FSQRYPKIPV IDESHMHNTC
IAFDLMSINM ADLHVLPKVL PYFKTLFRDE MVEDEDADDV AMDDLKEEAL
