ID L0AAU1_CALLD Unreviewed; 147 AA.
AC L0AAU1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=Calag_0476 {ECO:0000313|EMBL:AFZ70242.1};
OS Caldisphaera lagunensis (strain DSM 15908 / JCM 11604 / ANMR 0165 /
OS IC-154).
OC Archaea; Thermoproteota; Thermoprotei; Acidilobales; Caldisphaeraceae;
OC Caldisphaera.
OX NCBI_TaxID=1056495 {ECO:0000313|EMBL:AFZ70242.1, ECO:0000313|Proteomes:UP000010469};
RN [1] {ECO:0000313|Proteomes:UP000010469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15908 / JCM 11604 / IC-154
RC {ECO:0000313|Proteomes:UP000010469};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete genome of Caldisphaera lagunensis DSM 15908.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00010800, ECO:0000256|HAMAP-
CC Rule:MF_00755}.
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DR EMBL; CP003378; AFZ70242.1; -; Genomic_DNA.
DR AlphaFoldDB; L0AAU1; -.
DR STRING; 1056495.Calag_0476; -.
DR KEGG; clg:Calag_0476; -.
DR eggNOG; arCOG01365; Archaea.
DR HOGENOM; CLU_1763779_0_0_2; -.
DR InParanoid; L0AAU1; -.
DR OMA; RYIVFAI; -.
DR Proteomes; UP000010469; 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 PANTHER; PTHR15441; RIBONUCLEASE P PROTEIN SUBUNIT P14; 1.
DR PANTHER; PTHR15441:SF2; RIBONUCLEASE P/MRP PROTEIN SUBUNIT POP5; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000010469};
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..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 147 AA; 17277 MW; 376EC8967A9C38FC CRC64;
MDLYLLYFII VSILVSLLTT YLLNMYFIKK IENKFLLIPR KMKIKKPRRR YLIFEIASIK
DIDPGLLENS IKEEFKNLFG ITSLADSYLK LIYFDNKTKR GILRIKHIYL SHLITAIALI
RKIDNDELLI IPIRTSGTIN KAKKLLS
//