GenomeNet

Database: UniProt
Entry: H3H2L4_PHYRM
LinkDB: H3H2L4_PHYRM
Original site: H3H2L4_PHYRM 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system