ID A0A0D2JUG8_9CHLO Unreviewed; 416 AA.
AC A0A0D2JUG8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=ribonuclease P {ECO:0000256|ARBA:ARBA00012179};
DE EC=3.1.26.5 {ECO:0000256|ARBA:ARBA00012179};
GN ORFNames=MNEG_5451 {ECO:0000313|EMBL:KIZ02508.1};
OS Monoraphidium neglectum.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Monoraphidium.
OX NCBI_TaxID=145388 {ECO:0000313|EMBL:KIZ02508.1, ECO:0000313|Proteomes:UP000054498};
RN [1] {ECO:0000313|EMBL:KIZ02508.1, ECO:0000313|Proteomes:UP000054498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 48.87 {ECO:0000313|EMBL:KIZ02508.1,
RC ECO:0000313|Proteomes:UP000054498};
RX PubMed=24373495; DOI=10.1186/1471-2164-14-926;
RA Bogen C., Al-Dilaimi A., Albersmeier A., Wichmann J., Grundmann M.,
RA Rupp O., Lauersen K.J., Blifernez-Klassen O., Kalinowski J., Goesmann A.,
RA Mussgnug J.H., Kruse O.;
RT "Reconstruction of the lipid metabolism for the microalga Monoraphidium
RT neglectum from its genome sequence reveals characteristics suitable for
RT biofuel production.";
RL BMC Genomics 14:926-926(2013).
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; KK101032; KIZ02508.1; -; Genomic_DNA.
DR RefSeq; XP_013901527.1; XM_014046073.1.
DR AlphaFoldDB; A0A0D2JUG8; -.
DR STRING; 145388.A0A0D2JUG8; -.
DR GeneID; 25738328; -.
DR KEGG; mng:MNEG_5451; -.
DR OrthoDB; 47419at2759; -.
DR Proteomes; UP000054498; 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 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; IPR033443; PPR_long.
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; PF17177; PPR_long; 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:UP000054498};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..143
FT /note="Pentacotripeptide-repeat region of PRORP"
FT /evidence="ECO:0000259|Pfam:PF17177"
FT DOMAIN 169..359
FT /note="PRORP"
FT /evidence="ECO:0000259|Pfam:PF16953"
SQ SEQUENCE 416 AA; 44818 MW; 73BE0DC3D849513C CRC64;
MQAAGQAPDE TIFTHLARAA AARGDPDAAL SFAREVVAAE RGGGGGGGGK MVARLRTFQP
ALVGLALAGR ADEALAVADE LAALGRDYLD LTESEYALLL EAVARGGSYA QFAALLGRMQ
ADLNQLRPST LALVERFFAT PGAAAAFAEG GPMAGRGVGW EAARWVAVDR SGFSADAGEP
LGCIDLSPAG WQSLLGTIFD AMGAARHGTE QARRDFEAWL SCHGPYEAII DGANAALFGR
HDPPHTLDLG QVRAVWDAVQ LRFPDLRPLV VLSSGKRREV AARDPSDADA AWLLRLQRER
RLYVTPRDCH DDWFWLYAAV RAGEKGVLVT NDELRDHIYA LLRPKHFFRW KERHIARFTL
PQRPAAAPGR AGAAAAAWLH LPSPFTPCVQ QLPGSGAWMV PAADRDDWLL IRPRAG
//
