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Database: UniProt
Entry: Q8STU1_ENCCU
LinkDB: Q8STU1_ENCCU
Original site: Q8STU1_ENCCU 
ID   Q8STU1_ENCCU            Unreviewed;       118 AA.
AC   Q8STU1;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=Ribonuclease P/MRP protein subunit POP5 {ECO:0000256|PIRNR:PIRNR023803};
DE            EC=3.1.26.5 {ECO:0000256|PIRNR:PIRNR023803};
GN   OrderedLocusNames=ECU09_0630 {ECO:0000313|EMBL:CAD27036.1};
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813 {ECO:0000313|EMBL:CAD27036.1, ECO:0000313|Proteomes:UP000000819};
RN   [1] {ECO:0000313|EMBL:CAD27036.1, ECO:0000313|Proteomes:UP000000819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1 {ECO:0000313|EMBL:CAD27036.1,
RC   ECO:0000313|Proteomes:UP000000819};
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
CC   -!- FUNCTION: Component of ribonuclease P, a protein complex that generates
CC       mature tRNA molecules by cleaving their 5'-ends.
CC       {ECO:0000256|PIRNR:PIRNR023803}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC         from tRNA precursor.; EC=3.1.26.5;
CC         Evidence={ECO:0000256|PIRNR:PIRNR023803};
CC   -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC       component 2 family. {ECO:0000256|ARBA:ARBA00010800,
CC       ECO:0000256|PIRNR:PIRNR023803}.
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DR   EMBL; AL590451; CAD27036.1; -; Genomic_DNA.
DR   RefSeq; XP_955617.1; XM_950524.1.
DR   AlphaFoldDB; Q8STU1; -.
DR   STRING; 284813.Q8STU1; -.
DR   VEuPathDB; MicrosporidiaDB:ECU09_0630; -.
DR   HOGENOM; CLU_162874_0_0_1; -.
DR   InParanoid; Q8STU1; -.
DR   OMA; HENNIFV; -.
DR   OrthoDB; 1343653at2759; -.
DR   Proteomes; UP000000819; Chromosome IX.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0030677; C:ribonuclease P complex; IEA:InterPro.
DR   GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR   GO; GO:0033204; F:ribonuclease P RNA binding; IEA:InterPro.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IEA:InterPro.
DR   Gene3D; 3.30.70.3250; Ribonuclease P, Pop5 subunit; 1.
DR   InterPro; IPR002759; Pop5/Rpp14/Rnp2-like.
DR   InterPro; IPR016819; RNase_P/MRP_POP5.
DR   InterPro; IPR038085; Rnp2-like_sf.
DR   PANTHER; PTHR15441; RIBONUCLEASE P PROTEIN SUBUNIT P14; 1.
DR   PANTHER; PTHR15441:SF2; RIBONUCLEASE P/MRP PROTEIN SUBUNIT POP5; 1.
DR   Pfam; PF01900; RNase_P_Rpp14; 1.
DR   PIRSF; PIRSF023803; Ribonuclease_P_prd; 1.
DR   SUPFAM; SSF160350; Rnp2-like; 1.
PE   3: Inferred from homology;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000819};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW   ECO:0000256|PIRNR:PIRNR023803}.
SQ   SEQUENCE   118 AA;  13374 MW;  DD64AC4D3F14B09F CRC64;
     MVRIKARYIV VKLRFEGNGS MPGREMLGSV IRSRVCTDYG IHVLSMVGSL VVVEYLPHNQ
     VAVVRCDAPA CKYVLFTIAT IGEVSDLKCS MSVLWVSGIL KRAMRRILRY VEKERVRK
//
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