ID D2PC53_SULID Unreviewed; 143 AA.
AC D2PC53;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Ribonuclease P protein component 2 {ECO:0000256|HAMAP-Rule:MF_00755};
DE Short=RNase P component 2 {ECO:0000256|HAMAP-Rule:MF_00755};
DE EC=3.1.26.5 {ECO:0000256|HAMAP-Rule:MF_00755};
DE AltName: Full=Pop5 {ECO:0000256|HAMAP-Rule:MF_00755};
GN Name=rnp2 {ECO:0000256|HAMAP-Rule:MF_00755};
GN OrderedLocusNames=LD85_1607 {ECO:0000313|EMBL:ADB87273.1};
OS Sulfolobus islandicus (strain L.D.8.5 / Lassen #2).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=425944 {ECO:0000313|EMBL:ADB87273.1, ECO:0000313|Proteomes:UP000001404};
RN [1] {ECO:0000313|Proteomes:UP000001404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L.D.8.5 / Lassen #2 {ECO:0000313|Proteomes:UP000001404};
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC -!- FUNCTION: Part of ribonuclease P, a protein complex that generates
CC mature tRNA molecules by cleaving their 5'-ends. {ECO:0000256|HAMAP-
CC Rule:MF_00755}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00755};
CC -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein
CC subunits. {ECO:0000256|HAMAP-Rule:MF_00755}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00755}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 2 family. {ECO:0000256|HAMAP-Rule:MF_00755}.
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DR EMBL; CP001731; ADB87273.1; -; Genomic_DNA.
DR RefSeq; WP_012713725.1; NC_013769.1.
DR AlphaFoldDB; D2PC53; -.
DR SMR; D2PC53; -.
DR GeneID; 8761435; -.
DR KEGG; sii:LD85_1607; -.
DR HOGENOM; CLU_1801579_0_0_2; -.
DR Proteomes; UP000001404; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030677; C:ribonuclease P complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.3250; Ribonuclease P, Pop5 subunit; 1.
DR HAMAP; MF_00755; RNase_P_2; 1.
DR InterPro; IPR002759; Pop5/Rpp14/Rnp2-like.
DR InterPro; IPR038085; Rnp2-like_sf.
DR Pfam; PF01900; RNase_P_Rpp14; 1.
DR SUPFAM; SSF160350; Rnp2-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00755};
KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_00755};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00755};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_00755};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00755}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 143 AA; 16327 MW; BF60C86C0B1E248E CRC64;
MNSIQLIIDI ILILWLLILT VLYLRKKSLN LNIVKNKKIV RAKRYIVFYV IAESKVKSDD
LERVVRNSLK DLLGNVWLNI ANPKVVTYRE DTQEGIISTN RIGYKAVLAS LPFAKEINGN
KILIVPRRTT GSLKKAKKLI GLK
//
