ID   A0A165GL05_9APHY        Unreviewed;       889 AA.
AC   A0A165GL05;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=ribonuclease Z {ECO:0000256|ARBA:ARBA00012477};
DE            EC=3.1.26.11 {ECO:0000256|ARBA:ARBA00012477};
GN   ORFNames=LAESUDRAFT_810112 {ECO:0000313|EMBL:KZT10496.1};
OS   Laetiporus sulphureus 93-53.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Laetiporus.
OX   NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT10496.1, ECO:0000313|Proteomes:UP000076871};
RN   [1] {ECO:0000313|EMBL:KZT10496.1, ECO:0000313|Proteomes:UP000076871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-53 {ECO:0000313|EMBL:KZT10496.1,
RC   ECO:0000313|Proteomes:UP000076871};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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}.
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DR   EMBL; KV427609; KZT10496.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165GL05; -.
DR   STRING; 1314785.A0A165GL05; -.
DR   InParanoid; A0A165GL05; -.
DR   OrthoDB; 296811at2759; -.
DR   Proteomes; UP000076871; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; 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   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:UP000076871};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          6..58
FT                   /note="tRNase Z endonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF13691"
FT   DOMAIN          571..818
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF12706"
FT   REGION          152..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   889 AA;  98652 MW;  4DA1514B13CD8ABD CRC64;
     MNWSVSVVST ATSDTEPTII VTFDNGKYVF NAGENTGRTW TQSRRHWRKS KGLFVTSVGT
     QQCAGLTGVL MFFADGLMKG LDVVGPQGLT HYLASMRHHM FRSGFSVKCV EIPPAPSSSA
     DTEPAAPVPV FKDENVTVYG IPIYPTPPDA IVSTSSAKRK RSPLPSKRPA MAGIQYKSPL
     PGVDAQEYRR LTVENMFPRL VQPPGGGPPK DPDEQKQGKG KRHKQQVDAK SAKMVAGPEP
     PPPLMEVYNE AYAHKNKYLP PFEEYGLDMS KKMTACYVLV GPRTRGKFDA KKAETLGVFR
     TDRAKLIKGQ TVTITIKDAD GNEIQRIVKP EDCIAQSEIP KVMLLLDVPT PTHIPQVVAT
     FTENPFYSRF HSKSENDQSE YRVHIIYHLC GPGVLEDERY KAFMRGFANH VNHQISSREH
     GPDPVTFTSA AFSQLRLHQL DADMFPLPQF SLVARRDLSS VTGLPAKAEL LSPNRIVMMR
     PLTDPCDDEE IAKYDLFHPV ITSGMPVSLP ESISNEFAAA KARVQRHVDE RAQDKKPGDD
     VEVIPLGTSS AVPSKYRNVS STLIRIPNWG NILLDAGEGT WGQLTRMFGD DIDNHTTGAW
     DVLRNLKFIF LSHMHGDHHV GTAKLLAMRK LLKPSPNQAL FIVGNRNHEV YLRDQSSLED
     LGLSGPGRNG VIFMQSGFFH WFPPEERKEL MENDTFQRFE IARKLLNSSW AEPSLKSGKE
     MCRALGLESF QTLRVNHGGG CYAVILKHQD GWSIVYSADT PPDAVLAAAG ENCKLLIHEA
     TLADGQEDLA LAKKHSTFSQ ARKIGEQMKA ENLLLTHFSA RFPKIMLGDD GKIDELPHPT
     LALAVDHVRF VIGDMWKLGV YSRAVEGTIF ETNAEEGGDE DDELPSGPW
//