ID A0A0R3S834_HYMDI Unreviewed; 548 AA.
AC A0A0R3S834;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=ribonuclease P {ECO:0000256|ARBA:ARBA00012179};
DE EC=3.1.26.5 {ECO:0000256|ARBA:ARBA00012179};
GN ORFNames=HDID_LOCUS266 {ECO:0000313|EMBL:VDL14471.1};
OS Hymenolepis diminuta (Rat tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000026501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HDID_0000026501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL14471.1, ECO:0000313|Proteomes:UP000274504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000928};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the PPR family. P subfamily.
CC {ECO:0000256|ARBA:ARBA00007626}.
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DR EMBL; UYSG01000033; VDL14471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3S834; -.
DR STRING; 6216.A0A0R3S834; -.
DR WBParaSite; HDID_0000026501-mRNA-1; HDID_0000026501-mRNA-1; HDID_0000026501.
DR Proteomes; UP000046397; Unplaced.
DR Proteomes; UP000274504; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.11980; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR031595; PRORP_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13547:SF1; MITOCHONDRIAL RIBONUCLEASE P CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR13547; UNCHARACTERIZED; 1.
DR Pfam; PF16953; PRORP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000274504};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 291..535
FT /note="PRORP"
FT /evidence="ECO:0000259|Pfam:PF16953"
SQ SEQUENCE 548 AA; 63646 MW; F8259F951C843EBD CRC64;
MLQRHCVRHF LSNSTKEFRM LKTYYNSCFI HFNANDALKS RQQIDAYFKH LDNSFLERSR
LQTMQEILDL PTTDKYFKVH FWPKFISSTI INGKDKILQS LILFVLEKAE AHSTPTLISI
LKTLASQHRF EEFESLYILI KSRLSPTDTI AYSVDLSGAL CFSPFYKEAM TYLQLSLKHN
LPIVSFTHIL TAAATFGPLD EAISLLHEFH SMGLKPNSEF YTTFIKRLDE SDGEQLMVSL
LETVRKYNYA LTNFVALLIK EWFERLGWKG TMGVNLSRYV HYFLIDSARL SCPSCLKYLD
KVHLDSETCN QLAEIFFNNV LKGKTSDELF LTTTPKELES FLIFLKTNKT LRFDCVIDLP
NYLHSVTHRK LSKMSIEEQV GLLSDLISIL HRTYHFKRIC LVGKERAIVK RKQFWDVIKT
LGNRTGINVQ TFLVDHNNDD AFMIYMALWS GPDCYLLSID EFRQHRYTIG PEGADLLAQW
QTARQISVKN THPLSFNDPV VCDSRIQGNM KDGWHIPYDS GEPRLSYLPP TTWLCLRPPT
RLLLNNFQ
//
