RNZ2_MACFA
ID RNZ2_MACFA Reviewed; 826 AA.
AC Q8HY87;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Zinc phosphodiesterase ELAC protein 2;
DE EC=3.1.26.11;
DE AltName: Full=ElaC homolog protein 2;
DE AltName: Full=Ribonuclease Z 2;
DE Short=RNase Z 2;
DE AltName: Full=tRNA 3 endonuclease 2;
DE AltName: Full=tRNase Z 2;
DE Flags: Precursor;
GN Name=ELAC2;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15358515; DOI=10.1016/j.bbaexp.2004.07.001;
RA Dumont M., Frank D., Moisan A.-M., Tranchant M., Soucy P., Breton R.,
RA Labrie F., Tavtigian S.V., Simard J.;
RT "Structure of primate and rodent orthologs of the prostate cancer
RT susceptibility gene ELAC2.";
RL Biochim. Biophys. Acta 1679:230-247(2004).
CC -!- FUNCTION: Zinc phosphodiesterase, which displays mitochondrial tRNA 3'-
CC processing endonuclease activity. Involved in tRNA maturation, by
CC removing a 3'-trailer from precursor tRNA. Associates with
CC mitochondrial DNA complexes at the nucleoids to initiate RNA processing
CC and ribosome assembly. {ECO:0000250|UniProtKB:Q9BQ52}.
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:0000250|UniProtKB:Q9BQ52};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- SUBUNIT: Homodimer. Interacts with PTCD1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BQ52}.
CC Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000250|UniProtKB:Q9BQ52}. Nucleus {ECO:0000250|UniProtKB:Q9BQ52}.
CC Note=Mainly mitochondrial. {ECO:0000250|UniProtKB:Q9BQ52}.
CC -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000305}.
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DR EMBL; AY149903; AAN75377.1; -; mRNA.
DR RefSeq; NP_001306341.1; NM_001319412.1.
DR AlphaFoldDB; Q8HY87; -.
DR SMR; Q8HY87; -.
DR STRING; 9541.XP_005582987.1; -.
DR GeneID; 102127182; -.
DR CTD; 60528; -.
DR eggNOG; KOG2121; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0072684; P:mitochondrial tRNA 3'-trailer cleavage, endonucleolytic; ISS:UniProtKB.
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; 2.
PE 2: Evidence at transcript level;
KW Endonuclease; Hydrolase; Metal-binding; Mitochondrion;
KW Mitochondrion nucleoid; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome; Transit peptide; tRNA processing; Zinc.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..826
FT /note="Zinc phosphodiesterase ELAC protein 2"
FT /id="PRO_0000155829"
FT REGION 15..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
SQ SEQUENCE 826 AA; 92282 MW; B9EE064E8E624B23 CRC64;
MWALCSLLRS ATGRTMSQGR TISQGSARRQ RPPKDPLRHL RTREKRGPSG SSGGANTVYL
QVVAVGSRDA GAALYVFSEF NRYLFNCGEG VQRLMQEHKL KVARLDNIFL TRMHWSNVGG
LSGMILTLKE TGLPKCVLSG PPQLEKYLEA IKIFSGPLKG IELAVRPHSA PEYKDETMTV
YQIPIHSEQR SGKHQPWQSP ERPLGRLSPE RSSDSESNES EPHLPRGVSQ RRGVRDPSLV
VAFICKLHLK RGSFLVLKAK ELGLPVGTAA IAPIIAAVKD GKSITHEGRE ILAEELCTPP
DPGAAFVVVE CPDEGFIQPI CENATFQRYQ GKADAPVALV VHMAPESVLA DSRYQQWMER
FGPDTQHLVL NENCASVHNL RSYKIQTQLN LIHPDIFPLL TSFPRKKEGP TLSVPVVQGE
CLLKYQLRPR REWQRDAIIT CNPEEFIDEA LQLPNFQESM QEYRRSAQDG PAPAEKRSQY
PEIVFLGTGS AVPMKTRNVS ATLVNISPDT SLLLDCGEGT FGQLYRHYGD QVDRVLGSLA
AVFVSHLHAD HHTGLLNILL QRERALASLG KPFHPLLVVA PTQLKAWLQQ YHNQCQEVLH
HVSMIPAKYL QVGAEISSPA VERLISSLLR TCDLEEFQTC LVRHCRHAFG CALVHTSGWK
VVYSGDTMPC EALVQMGKDA TLLIHEATLE DGLEEEAVEK THSTTSQAIR VGMRMNAEFI
MLNHFSQRYA KVPLFSPDFN EKVGIAFDHM KVSFGDFPTV PKLIPPLKAL FAGDIEEMEE
RREKRELRQV RAALLSRALT DDLEDGEPQQ KRAHTEEPQS KKVRAQ
