ID Q6FIT8_CANGA Unreviewed; 177 AA.
AC Q6FIT8;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Ribonuclease P/MRP protein subunit POP5 {ECO:0000256|ARBA:ARBA00044198, ECO:0000256|PIRNR:PIRNR023803};
DE EC=3.1.26.5 {ECO:0000256|PIRNR:PIRNR023803};
GN OrderedLocusNames=CAGL0M11836g {ECO:0000313|CGD:CAL0136697,
GN ECO:0000313|EMBL:CAG62836.1};
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG62836.1, ECO:0000313|Proteomes:UP000002428};
RN [1] {ECO:0000313|EMBL:CAG62836.1, ECO:0000313|Proteomes:UP000002428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC {ECO:0000313|Proteomes:UP000002428};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380959; CAG62836.1; -; Genomic_DNA.
DR RefSeq; XP_449856.1; XM_449856.1.
DR AlphaFoldDB; Q6FIT8; -.
DR STRING; 284593.Q6FIT8; -.
DR EnsemblFungi; CAGL0M11836g-T; CAGL0M11836g-T-p1; CAGL0M11836g.
DR GeneID; 2891251; -.
DR KEGG; cgr:CAGL0M11836g; -.
DR CGD; CAL0136697; CAGL0M11836g.
DR VEuPathDB; FungiDB:CAGL0M11836g; -.
DR eggNOG; KOG4639; Eukaryota.
DR HOGENOM; CLU_086710_1_2_1; -.
DR InParanoid; Q6FIT8; -.
DR OMA; IVRCPRA; -.
DR Proteomes; UP000002428; Chromosome M.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; IEA:EnsemblFungi.
DR GO; GO:0000172; C:ribonuclease MRP complex; IEA:EnsemblFungi.
DR GO; GO:0000171; F:ribonuclease MRP activity; IEA:EnsemblFungi.
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:0034965; P:intronic box C/D RNA processing; IEA:EnsemblFungi.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IEA:EnsemblFungi.
DR GO; GO:0000294; P:nuclear-transcribed mRNA catabolic process, RNase MRP-dependent; IEA:EnsemblFungi.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:EnsemblFungi.
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; PTHR48326; RIBONUCLEASE P_MRP PROTEIN SUBUNIT POP5; 1.
DR PANTHER; PTHR48326:SF1; RIBONUCLEASE P_MRP PROTEIN SUBUNIT POP5; 1.
DR Pfam; PF01900; RNase_P_Rpp14; 1.
DR PIRSF; PIRSF023803; Ribonuclease_P_prd; 2.
DR SUPFAM; SSF160350; Rnp2-like; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR023803}.
SQ SEQUENCE 177 AA; 20534 MW; 4C78E274BEFF56A5 CRC64;
MVRLKSRYVL FEIIYPPESM AEAELDRMDD VMMGFHKSTR NYHEINSKTI LQEIRRVVQY
NFGDLGSGQL TSLLHLKYFS NATSTGILRC HREDLNILLT TLALVNKIGD CEGIILNPVK
VSGTIKKLEQ YAIRRNHNFI NALKRFELNK MKISEMNMES STFENEIRDI PMDSEDN
//
