ID Q6BJN2_DEBHA Unreviewed; 183 AA.
AC Q6BJN2;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 2.
DT 27-MAR-2024, entry version 89.
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=DEHA2G01188g {ECO:0000313|EMBL:CAG90035.2};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG90035.2, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAG90035.2, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
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; CR382139; CAG90035.2; -; Genomic_DNA.
DR RefSeq; XP_461589.2; XM_461589.1.
DR AlphaFoldDB; Q6BJN2; -.
DR STRING; 284592.Q6BJN2; -.
DR GeneID; 2904450; -.
DR KEGG; dha:DEHA2G01188g; -.
DR eggNOG; KOG4639; Eukaryota.
DR HOGENOM; CLU_086710_1_2_1; -.
DR InParanoid; Q6BJN2; -.
DR OMA; IVRCPRA; -.
DR OrthoDB; 2787248at2759; -.
DR Proteomes; UP000000599; Chromosome G.
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 HAMAP; MF_00755; RNase_P_2; 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; 2.
DR SUPFAM; SSF160350; Rnp2-like; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR023803}.
SQ SEQUENCE 183 AA; 20323 MW; 76B101C363BC6BD7 CRC64;
MVRLKQRYIL FDILYPPSSD TGGSQENLED FVNFSKSRQN TLLTLHRTSP SNISQKTLTQ
AIRTVIQDHY GDFGAGTAGM QFAIKYFSNK TSTGIIRCGR SSFQIVVAAL ALMNKLGDED
VIVRCIHVSG TIKKCEEYSI KRNRDLMSVL KSGSGKANLN SIISNFENED DIIGVTDDEA
NMD
//
