ID H3H2L4_PHYRM Unreviewed; 485 AA.
AC H3H2L4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=ribonuclease P {ECO:0000256|ARBA:ARBA00012179};
DE EC=3.1.26.5 {ECO:0000256|ARBA:ARBA00012179};
OS Phytophthora ramorum (Sudden oak death agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra84631, ECO:0000313|Proteomes:UP000005238};
RN [1] {ECO:0000313|Proteomes:UP000005238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [2] {ECO:0000313|EnsemblProtists:Phyra84631}
RP IDENTIFICATION.
RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra84631};
RG EnsemblProtists;
RL Submitted (JUN-2015) 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 EMBL; DS566115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3H2L4; -.
DR STRING; 164328.H3H2L4; -.
DR EnsemblProtists; Phyra84631; Phyra84631; Phyra84631.
DR VEuPathDB; FungiDB:PSURA_84631; -.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_014066_2_0_1; -.
DR InParanoid; H3H2L4; -.
DR OMA; KPRQWIC; -.
DR Proteomes; UP000005238; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004526; F:ribonuclease P activity; IBA:GO_Central.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IBA:GO_Central.
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:UP000005238};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 31..245
FT /note="Pentacotripeptide-repeat region of PRORP"
FT /evidence="ECO:0000259|Pfam:PF17177"
FT DOMAIN 259..475
FT /note="PRORP"
FT /evidence="ECO:0000259|Pfam:PF16953"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 55213 MW; 93EA6F1883BD4DCB CRC64;
MATLAGTKRP AEAAPATEGA EPARKLTKAQ RRRERKQTPA EKTENQFRIQ VQICAQQDDA
ARALEVYEQM KREAVNVAPY LYNMIINVCS KADDPAAFKA GAYAVYQDMK QAAISANQKI
GVSEPIYSAM LKLCSKAQDF GACETLIAEM EAANVNPKLR TFGSLLQAHS DAGHLEKCVW
VHEKFLSHEL EPTEDDYVAL LRVCVKTGHA ERFYAFLDMF IEDVWQPSLS TWDVLKDWFN
SEAAQVDGRK WKITEGTVSE EGVCSVTGDQ LQSLELEAEL EAELLAKVEK LVRTDEKRTA
QWDAFKQWLG EFGPFDVIID AANVGYCNQN FDGGGFNYAQ IELMVQHYEA RGNKPLLVLH
ERRTWDEQVP AEHRAQVAQW RASHKMFNCQ PGNNDDWYWL YAAVKLGGRT LMISNDEMRD
HHFQMIHNRA FGRWKERHQV HYQVHGDRVT VDEPLPYSAR PQRVGDVWHF PAAADPRWLA
VELAP
//