GenomeNet

Database: UniProt
Entry: M4BWN3_HYAAE
LinkDB: M4BWN3_HYAAE
Original site: M4BWN3_HYAAE 
ID   M4BWN3_HYAAE            Unreviewed;       425 AA.
AC   M4BWN3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=ribonuclease P {ECO:0000256|ARBA:ARBA00012179};
DE            EC=3.1.26.5 {ECO:0000256|ARBA:ARBA00012179};
OS   Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS   (Peronospora arabidopsidis).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Hyaloperonospora.
OX   NCBI_TaxID=559515 {ECO:0000313|EnsemblProtists:HpaP810934, ECO:0000313|Proteomes:UP000011713};
RN   [1] {ECO:0000313|Proteomes:UP000011713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Emoy2 {ECO:0000313|Proteomes:UP000011713};
RX   PubMed=21148394; DOI=10.1126/science.1195203;
RA   Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA   Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA   Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA   Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA   Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA   Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA   Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA   Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA   Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA   Tyler B.M.;
RT   "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT   arabidopsidis genome.";
RL   Science 330:1549-1551(2010).
RN   [2] {ECO:0000313|EnsemblProtists:HpaP810934}
RP   IDENTIFICATION.
RC   STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP810934};
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; JH598005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M4BWN3; -.
DR   STRING; 559515.M4BWN3; -.
DR   EnsemblProtists; HpaT810934; HpaP810934; HpaG810934.
DR   VEuPathDB; FungiDB:HpaG810934; -.
DR   eggNOG; KOG1347; Eukaryota.
DR   HOGENOM; CLU_014066_2_0_1; -.
DR   InParanoid; M4BWN3; -.
DR   OMA; KPRQWIC; -.
DR   Proteomes; UP000011713; 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; IPR002885; Pentatricopeptide_rpt.
DR   InterPro; IPR033443; PPR_long.
DR   InterPro; IPR031595; PRORP_C.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   NCBIfam; TIGR00756; PPR; 1.
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.
DR   PROSITE; PS51375; PPR; 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:UP000011713};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          3..175
FT                   /note="Pentacotripeptide-repeat region of PRORP"
FT                   /evidence="ECO:0000259|Pfam:PF17177"
FT   REPEAT          53..87
FT                   /note="PPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT   DOMAIN          188..418
FT                   /note="PRORP"
FT                   /evidence="ECO:0000259|Pfam:PF16953"
SQ   SEQUENCE   425 AA;  49039 MW;  06C86D7C61914569 CRC64;
     MIVASYIYNV IINLCSKAED PADCKAGACK VFEEMKLANV ATEQTKKKAV AVGEPIYSAM
     IKLCSKASDF EACEALVAEM EEAKVVPKLR TFGPLLQAHS DAGNLDKCIW VHEKLLSHEL
     ELTEDDYVAL LRVCVKTGHA EQFYAFLDRF IDEIWQPSLS TWDVLKDWFS SEAAQVDGRK
     WTITEGTVNK QGVCSVTSNQ LQSVELSPEL DEELLVKIEK LVRTDEKRIA QWDDFKQWLE
     KYGPFEVLID AANVGYCNQN FQGGGFDYGQ IKLMVQHYEA KGKKVLIVLH ERRISDEQVP
     VKHRAQIVQW GVSHNMFNCQ PGNNDDWYWL YAAVKLGKRT LLVTNDEMRD HHFQMIHNRA
     FARWKERHQV RYQVHGRRVT VDEPLPYSER PQRVGNVWHF PSREFPDQVS DSDRRWLCVE
     LQQTA
//
DBGET integrated database retrieval system