ID A0A1U7R3Y6_MESAU Unreviewed; 586 AA.
AC A0A1U7R3Y6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=ribonuclease P {ECO:0000256|ARBA:ARBA00012179};
DE EC=3.1.26.5 {ECO:0000256|ARBA:ARBA00012179};
GN Name=Kiaa0391 {ECO:0000313|RefSeq:XP_005080562.1,
GN ECO:0000313|RefSeq:XP_021088870.1, ECO:0000313|RefSeq:XP_021088871.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|RefSeq:XP_005080562.1};
RN [1] {ECO:0000313|RefSeq:XP_005080562.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (APR-2022) to UniProtKB.
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 RefSeq; XP_005080562.1; XM_005080505.3.
DR RefSeq; XP_021088870.1; XM_021233211.1.
DR RefSeq; XP_021088871.1; XM_021233212.1.
DR STRING; 10036.ENSMAUP00000021598; -.
DR GeneID; 101834490; -.
DR KEGG; maua:101834490; -.
DR CTD; 9692; -.
DR eggNOG; ENOG502QRKG; Eukaryota.
DR OrthoDB; 2969930at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
DR GO; GO:0030678; C:mitochondrial ribonuclease P complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0097745; P:mitochondrial tRNA 5'-end processing; IEA:Ensembl.
DR CDD; cd18718; PIN_PRORP; 1.
DR Gene3D; 3.40.50.11980; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR033495; MRPP3_PIN_dom.
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:UP000189706};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 339..575
FT /note="PRORP"
FT /evidence="ECO:0000259|Pfam:PF16953"
SQ SEQUENCE 586 AA; 67293 MW; E4FE3A7404343867 CRC64;
MTHLSGFRSV RKLWTNIPYF ELGPATSPVT FFLTVTRNQH RWFSVKTTSP ANSKTMNLLV
AKTRTLKKED DNNRQVSSDH YFAAGAAKKR SYLNSSPEQQ RDHAMPSVRG TIELPTTPLT
SEAWDQLQAE FNGKGSFEDR VISQMLHNHS SIDVAKSLLA WVAAKNNGIV GYNLLVKYLY
LCVSHKETSE VIDVYEILKA KYKCLESGAN SILIRGLMHS DRWREALLLL EDIKKVMIPS
KKNYDDCIRG ALFHQDVSLA WSLYQELIGH NLTPLLETLK AFFDFGKNIN DDHYSNKLLD
ILAYLRNNQL YPGEALAHSI KTWFESIPGK QWKGQFTTVQ KSGHCSSCGR ALESIHLSSE
EYEFLKEKIL RDVIDGGDQY KKTTPQELKR FENFVNSCPP FDIVIDGLNV AKMFPKSRES
QALLSVVSQL AQQSLRLLVL GRKHMLRPSS RWKKEEMEQV RKQAYCFFAD NISKDDPFLL
YATLNSGNHC KFITQDLMRD HKACLPDAHT QRLFFKWQQG HQLAIMKCSQ RSKLTFQHTL
SYDTVVQTTG DSWHIPYDED QVQRSSYEVP TKWLCLQRKT QAPALC
//
