ID A7TRK3_VANPO Unreviewed; 167 AA.
AC A7TRK3;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 03-MAY-2023, entry version 63.
DE RecName: Full=Ribonuclease P/MRP protein subunit POP5 {ECO:0000256|PIRNR:PIRNR023803};
DE EC=3.1.26.5 {ECO:0000256|PIRNR:PIRNR023803};
GN ORFNames=Kpol_1071p8 {ECO:0000313|EMBL:EDO15101.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO15101.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480481; EDO15101.1; -; Genomic_DNA.
DR RefSeq; XP_001642959.1; XM_001642909.1.
DR AlphaFoldDB; A7TRK3; -.
DR STRING; 436907.A7TRK3; -.
DR GeneID; 5543147; -.
DR KEGG; vpo:Kpol_1071p8; -.
DR eggNOG; KOG4639; Eukaryota.
DR HOGENOM; CLU_086710_1_2_1; -.
DR InParanoid; A7TRK3; -.
DR OMA; IVRCPRA; -.
DR OrthoDB; 2787248at2759; -.
DR PhylomeDB; A7TRK3; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
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; 2.
DR SUPFAM; SSF160350; Rnp2-like; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000000267};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR023803}.
SQ SEQUENCE 167 AA; 19404 MW; 4778FC421111E19D CRC64;
MVRLKSRYIL FEILYPNSDE NGKMIESKSS LRKDILLRQH RVSPPEISIK TIIQEIRRSL
QLNFGDYGSG KVSSLLQSKY FSNMTSTGII RCHREDCDTL IMALFFINKI GDIDNLIINP
VKVSGTIKKI EEYSIRRNKK LANIMDRDQK SFIDDYHSVS DDEPRED
//