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Database: UniProt
Entry: A0A1A6HVU5_NEOLE
LinkDB: A0A1A6HVU5_NEOLE
Original site: A0A1A6HVU5_NEOLE 
ID   A0A1A6HVU5_NEOLE        Unreviewed;       775 AA.
AC   A0A1A6HVU5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Zinc phosphodiesterase ELAC protein 2 {ECO:0000256|ARBA:ARBA00013357};
DE            EC=3.1.26.11 {ECO:0000256|ARBA:ARBA00012477};
DE   AltName: Full=ElaC homolog protein 2 {ECO:0000256|ARBA:ARBA00032616};
DE   AltName: Full=Ribonuclease Z 2 {ECO:0000256|ARBA:ARBA00030729};
DE   AltName: Full=tRNA 3 endonuclease 2 {ECO:0000256|ARBA:ARBA00032104};
DE   AltName: Full=tRNase Z 2 {ECO:0000256|ARBA:ARBA00030689};
GN   ORFNames=A6R68_23875 {ECO:0000313|EMBL:OBS82135.1};
OS   Neotoma lepida (Desert woodrat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Neotominae; Neotoma.
OX   NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS82135.1, ECO:0000313|Proteomes:UP000092124};
RN   [1] {ECO:0000313|EMBL:OBS82135.1, ECO:0000313|Proteomes:UP000092124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=417 {ECO:0000313|EMBL:OBS82135.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:OBS82135.1};
RA   Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT   "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT   lepida.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000402};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the RNase Z family.
CC       {ECO:0000256|ARBA:ARBA00007823}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBS82135.1}.
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DR   EMBL; LZPO01008206; OBS82135.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A6HVU5; -.
DR   STRING; 56216.A0A1A6HVU5; -.
DR   Proteomes; UP000092124; Unassembled WGS sequence.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
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   CDD; cd07718; RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold; 1.
DR   CDD; cd16296; RNaseZ_ELAC2-N-term-like_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 2.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR047151; RNZ2-like.
DR   InterPro; IPR027794; tRNase_Z_dom.
DR   PANTHER; PTHR12553; ZINC PHOSPHODIESTERASE ELAC PROTEIN 2; 1.
DR   PANTHER; PTHR12553:SF49; ZINC PHOSPHODIESTERASE ELAC PROTEIN 2; 1.
DR   Pfam; PF12706; Lactamase_B_2; 1.
DR   Pfam; PF13691; Lactamase_B_4; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092124};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          55..114
FT                   /note="tRNase Z endonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF13691"
FT   DOMAIN          466..672
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF12706"
FT   REGION          15..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          742..775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        751..775
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   775 AA;  86494 MW;  5E9E1F9E8DD4AC1A CRC64;
     MWTLRSLLRP IGLRTMSQGS ARRPRPPKDP LRHLRTREKR GPSWGPRSPN TVYLQVVAAG
     GRDAGAALYV FSEYNRYLFN CGEGVQRLMQ EHKLKVARLD NIFLTRMHWS NVGGLCGMIL
     TLKETGLPKC VLSGPPQLEK YLEAIKIFSG PLKGIELAVR PHSAPEYEDE TMTVHQVPIY
     CVNRKAGGRD PSLVVAFVCK LHLRKGTFLV LKAKELGLPV GTAAIAPIIA AVKDGQSITY
     GGREIAPEEL CTPSDPGPVF IVVECPDEGF IQPICDNDTF KRYQGEADAP VALVVHIAPE
     PVLTDSRYQQ WMESFGPDTQ HLILNENCPS VHNLRSHKIQ TQLSLIHPDI FPRLTSFYSK
     EEGSALSMPT VRGECLLKYQ LRPKREWQRD TTLTCNTDEF IAEALELPNF QESVQEYNKG
     MQESPAPEEK RSQYPEIVFL GTGSAIPMKI RNVSSTLINL SPDKSVLLDC GEGTFGQLCR
     HYGQQIDRVL CNLAAVFVSH LHADHHTGLL NILLQREHAL VSEAPDIVLT EALYPMTVAT
     VSAADSTRVN MIPAKCLQKG AEVSSPPVER LISLLLETCD LEEFQTCLVR HCKHAFGCAL
     VHSSGWKVVY SGDTMPCEAL VQMGKDANLL IHEATLEDGM EEEAVEKTHS TTSQAINVGM
     RMNADFIMLN HFSQRYAKIP LFSPDFNEKV GIAFDHMKVC FGDFPTVPKL IPPLKALFAD
     DIEEMVERKE KRELRQVRAA LLAQQADSPE DTELQQKRAL TEEPHSPQSK KVRTQ
//
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