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Database: UniProt
Entry: D8SI62_SELML
LinkDB: D8SI62_SELML
Original site: D8SI62_SELML 
ID   D8SI62_SELML            Unreviewed;       534 AA.
AC   D8SI62;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=ribonuclease P {ECO:0000256|ARBA:ARBA00012179};
DE            EC=3.1.26.5 {ECO:0000256|ARBA:ARBA00012179};
GN   ORFNames=SELMODRAFT_117602 {ECO:0000313|EMBL:EFJ15811.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ15811.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
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; GL377621; EFJ15811.1; -; Genomic_DNA.
DR   RefSeq; XP_002983002.1; XM_002982956.1.
DR   AlphaFoldDB; D8SI62; -.
DR   STRING; 88036.D8SI62; -.
DR   EnsemblPlants; EFJ15811; EFJ15811; SELMODRAFT_117602.
DR   Gramene; EFJ15811; EFJ15811; SELMODRAFT_117602.
DR   KEGG; smo:SELMODRAFT_117602; -.
DR   eggNOG; KOG1347; Eukaryota.
DR   HOGENOM; CLU_014066_2_0_1; -.
DR   InParanoid; D8SI62; -.
DR   OMA; KPRQWIC; -.
DR   Proteomes; UP000001514; 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; IPR002885; Pentatricopeptide_rpt.
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.
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:UP000001514};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          40..245
FT                   /note="Pentacotripeptide-repeat region of PRORP"
FT                   /evidence="ECO:0000259|Pfam:PF17177"
FT   REPEAT          158..192
FT                   /note="PPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT   DOMAIN          288..524
FT                   /note="PRORP"
FT                   /evidence="ECO:0000259|Pfam:PF16953"
SQ   SEQUENCE   534 AA;  59704 MW;  E322ED7AB26E2850 CRC64;
     MPIASEVLEG DLPLRVNYLQ LETKKRAATD NTNHESKRCV QKKKKFTPDS ELRFKLESCS
     KVGDVTGALD IYDSSKDQGV KLSQYHYNVL LYLCSSAALG VILALDRGLE IYERMKLEGI
     SANEAAFTSI ARLAVAKRDG DLAFSLVKEM TTSGITPKLR SYGPALYTYF KSNQVDKAFE
     VDDHMRSFGV QPEEMELQIL LELSLKAGLD QRVYSVLHRL RRSVREVSPS TATTIERWFS
     SDAASSSGSD KKYDDEDVRR ALAAQGGGGL ELGWIGSGGW SVKRTALDAS GVCESCRHKM
     AAVDLNAEET NRFAENLAAL ACEKERDANS FKEFQEWMAE HGPFDAIVDG ANVALFNQNF
     SAGGFSFSQL NSVVTELSNQ HGKSPLVILH KRRVTGGPAA SPQSQELLKQ WTAANALYTA
     ATGSNDDWYW LYAAVTCKCL LVSNDEMRDH LFQMLGNDLF PRWKERHQVK LRALSYNPFF
     DMPPPYSTVI QECENGSWHF PISRGNDEND EAEEPRKQPR SWLCITRRGN KVIE
//
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