RNZ4_ARATH
ID RNZ4_ARATH Reviewed; 942 AA.
AC F4J1H7; Q8GYZ2; Q8LBW8; Q9LU20;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=tRNAse Z TRZ4, mitochondrial {ECO:0000303|PubMed:16336119};
DE EC=3.1.26.11 {ECO:0000269|PubMed:19411372};
DE AltName: Full=Long tRNase Z 2 {ECO:0000303|PubMed:16336119};
DE AltName: Full=tRNase ZL2 {ECO:0000303|PubMed:16336119};
DE Short=AthTRZL2 {ECO:0000303|PubMed:16336119};
DE Flags: Precursor;
GN Name=TRZ4 {ECO:0000303|PubMed:16336119};
GN OrderedLocusNames=At3g16260 {ECO:0000312|Araport:AT3G16260};
GN ORFNames=MYA6.7 {ECO:0000312|EMBL:BAB01266.1};
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|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 435-942.
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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. Can process the mitochondrial tRNA-like
CC structures (t-elements). {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: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 -!- DISRUPTION PHENOTYPE: No visible phenotype due to the redundancy with
CC TRZ3. 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=BAB01266.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB023046; BAB01266.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75791.1; -; Genomic_DNA.
DR EMBL; AK117304; BAC41975.1; -; mRNA.
DR EMBL; AY086950; AAM67367.1; -; mRNA.
DR RefSeq; NP_188247.2; NM_112497.3.
DR AlphaFoldDB; F4J1H7; -.
DR SMR; F4J1H7; -.
DR STRING; 3702.AT3G16260.1; -.
DR iPTMnet; F4J1H7; -.
DR PaxDb; F4J1H7; -.
DR PRIDE; F4J1H7; -.
DR ProteomicsDB; 227953; -.
DR EnsemblPlants; AT3G16260.1; AT3G16260.1; AT3G16260.
DR GeneID; 820872; -.
DR Gramene; AT3G16260.1; AT3G16260.1; AT3G16260.
DR KEGG; ath:AT3G16260; -.
DR Araport; AT3G16260; -.
DR TAIR; locus:2094912; AT3G16260.
DR eggNOG; KOG2121; Eukaryota.
DR HOGENOM; CLU_006220_2_0_1; -.
DR InParanoid; F4J1H7; -.
DR OrthoDB; 454909at2759; -.
DR PRO; PR:F4J1H7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J1H7; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Calcium; Endonuclease; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Mitochondrion; Nuclease; Reference proteome; Transit peptide;
KW tRNA processing; Zinc.
FT TRANSIT 1..50
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 51..942
FT /note="tRNAse Z TRZ4, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439064"
FT REGION 38..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 678
FT /note="N -> K (in Ref. 3; BAC41975)"
FT /evidence="ECO:0000305"
FT CONFLICT 733
FT /note="Q -> H (in Ref. 4; AAM67367)"
FT /evidence="ECO:0000305"
FT CONFLICT 917
FT /note="V -> VE (in Ref. 4; AAM67367)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 942 AA; 104727 MW; 732F55B0F67167EC CRC64;
MLTSSMPQNL SLFGFSPLKS SSFALILRPF SLYPPIFASS SPAPSRRPPR TAGYRRSGPS
PPRRKWSSFE EQKRKGRSPM EKDKAISFNH SSDSFEFNKR RAEGLDKVDK PKKNLKRNTR
TLNPTNTIAY VQILGTGMDT QDTSPSVLLF FDKQRFIFNA GEGLQRFCTE HKIKLSKVDH
IFLSRVCSET AGGLPGLLLT LAGIGEQGLS VNVWGPSDLK YLVDAMRSFI PRAAMVHTRS
FGPSLNISDS APQIGLSKPK DDAYVLVDDE VVKISAILLE PSRLEESGSK PGETAVIYVC
ELPEIKGKFD PKKAMALGLR AGPKYSYLQS GQSVKSDFKD ITVHPSDVMG PSVPGPVVLL
VDCPTESHAE ELLSIPSMKT YYSCLDNSTD GAKLVNCIIH LSPASVTNSS TYRSWMKRFH
SAQHILAGHE AKNMEFPILR ASSRITARLN YLCPQFFPAP GFWSHQHDNN SINPTSLSKC
FDSNLGESIS AENLLKFTLR PHGNLGVDRS SIPSRLTALR VMDELLSEIP EISSKTEEIK
QLWNGQHNKM MIEEPWLGES TVPSCLENIR RDDMEIVLLG TGSSQPSKYR NVTAIYIDLF
SRGSILLDCG EGTLGQLKRR YGLEGADEAV RNLRCIWISH IHADHHTGLA RILARRRELL
KGLAHEPAIV VGPRSLKNFL DAYQRLEDLD MEFLDCRNTT TTSWASVETS RPEKNTSSGN
AEGSLFSKGS LMQSIYKRPS SPLTDNSSAL PFLKKLKKVL GEMGLEHLIS FPVVHCPQAF
GVSLKAAERK NIAGDEIPGW KMVYSGDTRP CPEMVEASKG ATVLIHEATF EDALVEEAVA
KNHSTTKEAI KVGSSAGVYR TVLTHFSQRY PKIPVIDESH MHNTCIAFDM MSINMADLHV
LPKILPYFKT LFRNQVVEEE EEEEETDDDS LIRDKVPSFF IN
