ID A0A165N639_9APHY Unreviewed; 933 AA.
AC A0A165N639;
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};
DE Flags: Fragment;
GN ORFNames=DAEQUDRAFT_714778 {ECO:0000313|EMBL:KZT66566.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT66566.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT66566.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT66566.1,
RC ECO:0000313|Proteomes:UP000076727};
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; KV429087; KZT66566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165N639; -.
DR STRING; 1314783.A0A165N639; -.
DR OrthoDB; 296811at2759; -.
DR Proteomes; UP000076727; 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:UP000076727};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 37..89
FT /note="tRNase Z endonuclease"
FT /evidence="ECO:0000259|Pfam:PF13691"
FT DOMAIN 631..861
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
FT REGION 173..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZT66566.1"
SQ SEQUENCE 933 AA; 103714 MW; 6720655E29E821D9 CRC64;
MFARRLCSSV DHCIFSALKQ SLYQKRDCGA MNWSAEAITA ATSDTEPSIL VSFDDRKYLF
NAGEGTSRAW LQGPRRWKRT AAIFMTGVGS RQASGLPGLL MFLADGGINK VDLIGPNGIT
HYLASMRTSL LRVGMELNAS EEPSSVTEDA MPAPAYTDDL VSIWSLPIHA ERPAGEGADE
GQMHEECSSV PAKRKRTPSP DVPSKRPTSE PATLVEEAKG DADEVEEGSE RVGSPASDPD
EIYDSDPQLW RRLMVQNMFP FKAPELQSEV KALRKQEEWN AKARRGYGLV GMPVPPALRL
KPAPLPPQFA PVRNKQLKRL PLFTHGPEGK PTLCYILVGP AARGRFDSAK AEELGIPLGP
ERKRLTEGET VTFTVKDSAG NEIERTVKPE DCLGPPEIPR AMVLLDVPTP SHIPELVKSF
TQHPFYSNFC SKAVAGDESE LLVHVVFHLC GKDVLEDERY KAFMRTFPEN THHVISSREH
GNDPIVFSST TYNQLRMNRL DPDMFPILSC ARDPLRDLSS IPDLPVRSHH LQKFSFVEMR
PPREPCLDPL SKKWEHQGYT PGKDRDVWIP SHVQRAFVKA EDKIKDMGNF KRKPRPGDDV
EIVSLGTSSS RPALYRNVSG TLVRIPGYGS VLLDAGEGSW GQLARLYGDD RQNTTTGVWE
VLRDLRCIFV SHMHGDHHFG LQKILAMRKL LNPTPTQPLY VVGLRSHLLG LQEISDLEDL
GLDQVDGHGI VFIPADDLCR RPVYKNDSPE GLSIHCSPQD IANMHNALGL RSFATVEVPH
RCKAYGAVLD HIDGWSIAYS GDCMPSKNLT KAARYATLLI HEATLADDQA EMAKEKAHST
FSQAVKVGDE MQAENILLTH FSARYPKVPP TAFLPSSPRA GASQSPNIGV AFDFQRFTIG
DMWKLRFYLP AIEANMRDIA RDDEEDIEIS AWD
//
