ID A0A1W0E3Z9_9MICR Unreviewed; 610 AA.
AC A0A1W0E3Z9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ribonuclease Z {ECO:0000256|ARBA:ARBA00012477};
DE EC=3.1.26.11 {ECO:0000256|ARBA:ARBA00012477};
GN ORFNames=EHP00_2248 {ECO:0000313|EMBL:OQS53958.1};
OS Ecytonucleospora hepatopenaei.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC Ecytonucleospora.
OX NCBI_TaxID=646526 {ECO:0000313|EMBL:OQS53958.1, ECO:0000313|Proteomes:UP000192758};
RN [1] {ECO:0000313|EMBL:OQS53958.1, ECO:0000313|Proteomes:UP000192758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH1 {ECO:0000313|EMBL:OQS53958.1,
RC ECO:0000313|Proteomes:UP000192758};
RX PubMed=28345194; DOI=10.1111/1462-2920.13734;
RA Wiredu Boakye D., Jaroenlak P., Prachumwat A., Williams T.A., Bateman K.S.,
RA Itsathitphaisarn O., Sritunyalucksana K., Paszkiewicz K.H., Moore K.A.,
RA Stentiford G.D., Williams B.A.;
RT "Decay of the glycolytic pathway and adaptation to intranuclear parasitism
RT within Enterocytozoonidae microsporidia.";
RL Environ. Microbiol. 19:2077-2089(2017).
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:OQS53958.1}.
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DR EMBL; MNPJ01000023; OQS53958.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W0E3Z9; -.
DR STRING; 646526.A0A1W0E3Z9; -.
DR VEuPathDB; MicrosporidiaDB:EHP00_2248; -.
DR Proteomes; UP000192758; 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 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; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000192758};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 15..51
FT /note="tRNase Z endonuclease"
FT /evidence="ECO:0000259|Pfam:PF13691"
FT DOMAIN 375..558
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
SQ SEQUENCE 610 AA; 71942 MW; 7A281FB408654DC7 CRC64;
MQINATILTN KDEYSLLLKI EDKLYVFNMF EGFQRKCFEH KISISKLSAV FSPYIENMAG
LTGTYLTLAD AGVVFCDFIS EYIIDHSTLY TIAYRPSFKF LENQKNVFSD THISVKCITV
NKKTSFTIDF KKVAGKFQIE KLSALFPKNK IKNLKNKEKV NINGIMYDGK DYCEDDILVS
SIFVCFSKKY HTVFKESVLN CDLFFCYNKK LYKKFERIKK KQYKLTNINH NNLKNNSCKN
NNNLNYHNNI IWKIFYFKKE FQIEFLKQYE ELLENKSDIK PITKTSKESL ISKEFNLYKN
CMYNQMSFYF NKQSPFIFSD VNKQTIKNYQ VSEHNKNEKN YFPKDFLLFL GTGCAVPSKT
RNVSSLLFYT EKTSLLFDCG EDTFGQAYRC DPTLNIISNL NCILLSHSHA DHILGTCKII
KYIYKKHKRR IHILCSQNVN NFIQQYVTEY VFIDVMDYVN SKKDIILHEY TIKVEKSDHF
MDSVFYSVYI QNFHVTYSGD CRPSCKFIEM SKNCDVMVHE ATYNTEKDLA EKRKHSTEEE
AKEVFYKSKG KYLILTHFSN RNTSYNNNIN NNNNNNNINN ITNNNNNITN NNNNIKYAYD
YYLFDLSKNI
//
