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
//