ID A0A0J6Y7S3_COCIT Unreviewed; 220 AA.
AC A0A0J6Y7S3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=CIRG_02420 {ECO:0000313|EMBL:KMP02728.1};
OS Coccidioides immitis RMSCC 2394.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP02728.1, ECO:0000313|Proteomes:UP000054565};
RN [1] {ECO:0000313|Proteomes:UP000054565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; DS028094; KMP02728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J6Y7S3; -.
DR STRING; 404692.A0A0J6Y7S3; -.
DR Proteomes; UP000054565; 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 tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR023803}.
FT REGION 200..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 220 AA; 24459 MW; 0162D330CCCE8675 CRC64;
MVRLKHRYLL VNILYPPTSS SAVPGAKSRA LGKDAPDTQF HLQVCRPTPD CLTAQLLARM
IRETVSDMFG DWGMGRLGGA GAGSVSVKYL SPATSTAIIR CPRASYRLVW AALTYMSRLP
EPKEKRPGIG KSAFPRDSSF KSQKQQLDCV FRVVRVSGTM KKAEQEAIRR ARLEVVRLSK
KWEEEGKDVL QEMFPSGALK EHRMGIGVES DEDEDEDSDG
//
