ID   RNZ2_GORGO              Reviewed;         826 AA.
AC   Q9GL73;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 85.
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   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11175785; DOI=10.1038/84808;
RA   Tavtigian S.V., Simard J., Teng D.H.F., Abtin V., Baumgard M., Beck A.,
RA   Camp N.J., Carillo A.R., Chen Y., Dayananth P., Desrochers M., Dumont M.,
RA   Farnham J.M., Frank D., Frye C., Ghaffari S., Gupte J.S., Hu R., Iliev D.,
RA   Janecki T., Kort E.N., Laity K.E., Leavitt A., Leblanc G.,
RA   McArthur-Morrison J., Pederson A., Penn B., Peterson K.T., Reid J.E.,
RA   Richards S., Schroeder M., Smith R., Snyder S.C., Swedlund B., Swensen J.,
RA   Thomas A., Tranchant M., Woodland A.-M., Labrie F., Skolnick M.H.,
RA   Neuhausen S., Rommens J., Cannon-Albright L.A.;
RT   "A candidate prostate cancer susceptibility gene at chromosome 17p.";
RL   Nat. Genet. 27:172-180(2001).
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; AF308694; AAG24916.1; -; mRNA.
DR   RefSeq; NP_001266674.1; NM_001279745.1.
DR   AlphaFoldDB; Q9GL73; -.
DR   SMR; Q9GL73; -.
DR   STRING; 9593.ENSGGOP00000015469; -.
DR   GeneID; 101145069; -.
DR   KEGG; ggo:101145069; -.
DR   CTD; 60528; -.
DR   eggNOG; KOG2121; Eukaryota.
DR   InParanoid; Q9GL73; -.
DR   OrthoDB; 454909at2759; -.
DR   Proteomes; UP000001519; 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; IBA:GO_Central.
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   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_0000155827"
FT   REGION          15..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..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        207..230
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        805..826
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;  92260 MW;  D323B5F3D8B294A6 CRC64;
     MWALCSLLRS AAGRTMSQGR TISQAPARRE RPRKDPLRHL RTREKRGPSG CSGGPNTVYL
     QVVAAGSRDS GAALYVFSEF NRYLFNCGEG VQRLMQEHKL KVVRLDNIFL TRMHWSNVGG
     LSGMILTLKE TGLPKCVLSG PPQLEKYLEA IKIFSGPLKG IELAVRPHSA PEYEDETMTV
     YQIPIHSEQR RGRHQPWQSP ERPLSRLSPE RSSDSESNEN EPHLPHGVSQ RRGVRDSSLV
     VAFICKLHLK RGNFLVLKAK EMGLPVGTAA IAPIIAAVKD GKSITHEGRE ILAEELCTPP
     DPGAAFVVVE CPDESFIQPI CENATFQRYQ GKADAPVALV VHMAPESVLV DSRYQQWMER
     FGPDTQHLVL NENCASVHNL RSHKIQTQLN LIHPDIFPLL TSFPCKKEGP TLSVPMVQGE
     CLLKYQLRPR REWQRDAIIT CNPEEFIVEA LQLPNFQQSV QEYRRSVQDV PAPAEKRSQY
     PEIIFLGTGS AIPMKIRNVS ATLVNISPDT SLLLDCGEGT FGQLCRHYGD QVDRVLGTLA
     AVFVSHLHAD HHTGLLNILL QREQALASLG KPLHPLLVVA PSQLKAWLQQ YHNQCQEVLH
     HISMIPAKCL QEGAEISSPA VERLISSLLR TCDLEEFQTC LVRHCKHAFG CALVHTSGWK
     VVYSGDTMPC EALVRMGKDA TLLIHEATLE DGLEEEAVEK THSTTSQAIS VGMRMNAEFI
     MLNHFSQRYA KVPLFSPNFN EKVGVAFDHM KVCFGDFPTM PKLIPPLKAL FAGDIEEMEE
     RREKRELRQV RAALLSGELA GGLEDGEPQQ KRAHTEEPQA KKVRAQ