RNP1_ARCFU
ID RNP1_ARCFU Reviewed; 102 AA.
AC O28362;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Ribonuclease P protein component 1 {ECO:0000255|HAMAP-Rule:MF_00754};
DE Short=RNase P component 1 {ECO:0000255|HAMAP-Rule:MF_00754};
DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00754};
DE AltName: Full=Rpp29 {ECO:0000255|HAMAP-Rule:MF_00754};
DE AltName: Full=aRpp29;
GN Name=rnp1 {ECO:0000255|HAMAP-Rule:MF_00754}; OrderedLocusNames=AF_1917;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP CHARACTERIZATION, AND STRUCTURE BY NMR.
RX PubMed=14622001; DOI=10.1021/bi030170z;
RA Sidote D.J., Hoffman D.W.;
RT "NMR structure of an archaeal homologue of ribonuclease P protein Rpp29.";
RL Biochemistry 42:13541-13550(2003).
CC -!- FUNCTION: Part of ribonuclease P, a protein complex that generates
CC mature tRNA molecules by cleaving their 5'-ends.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00754};
CC -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein
CC subunits. {ECO:0000255|HAMAP-Rule:MF_00754}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00754}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 1 family. {ECO:0000255|HAMAP-Rule:MF_00754}.
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DR EMBL; AE000782; AAB89336.1; -; Genomic_DNA.
DR PIR; D69489; D69489.
DR RefSeq; WP_010879410.1; NC_000917.1.
DR PDB; 1PC0; NMR; -; A=17-77.
DR PDB; 1TS9; X-ray; 1.70 A; A=1-102.
DR PDB; 1TSF; X-ray; 1.70 A; A=1-102.
DR PDBsum; 1PC0; -.
DR PDBsum; 1TS9; -.
DR PDBsum; 1TSF; -.
DR AlphaFoldDB; O28362; -.
DR BMRB; O28362; -.
DR SMR; O28362; -.
DR STRING; 224325.AF_1917; -.
DR EnsemblBacteria; AAB89336; AAB89336; AF_1917.
DR GeneID; 24795661; -.
DR KEGG; afu:AF_1917; -.
DR eggNOG; arCOG00784; Archaea.
DR HOGENOM; CLU_107020_2_1_2; -.
DR OMA; PHERIKK; -.
DR OrthoDB; 124913at2157; -.
DR PhylomeDB; O28362; -.
DR BRENDA; 3.1.26.5; 414.
DR EvolutionaryTrace; O28362; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR DisProt; DP00382; -.
DR Gene3D; 2.30.30.210; -; 1.
DR HAMAP; MF_00754; RNase_P_1; 1.
DR InterPro; IPR036980; RNase_P/MRP_Rpp29_sf.
DR InterPro; IPR023538; RNP1.
DR InterPro; IPR023534; Rof/RNase_P-like.
DR InterPro; IPR002730; Rpp29/RNP1.
DR Pfam; PF01868; RNase_P-MRP_p29; 1.
DR SMART; SM00538; POP4; 1.
DR SUPFAM; SSF101744; SSF101744; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Nuclease;
KW Reference proteome; tRNA processing.
FT CHAIN 1..102
FT /note="Ribonuclease P protein component 1"
FT /id="PRO_0000128425"
FT HELIX 6..12
FT /evidence="ECO:0007829|PDB:1TS9"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:1TS9"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:1TS9"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:1TS9"
FT STRAND 42..57
FT /evidence="ECO:0007829|PDB:1TS9"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:1TS9"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1TS9"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1TS9"
FT HELIX 83..96
FT /evidence="ECO:0007829|PDB:1TS9"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1TS9"
SQ SEQUENCE 102 AA; 11806 MW; DF427B08A4543567 CRC64;
MRGRLQGVEL IARDWIGLMV EVVESPNHSE VGIKGEVVDE TQNTLKIMTE KGLKVVAKRG
RTFRVWYKGK IMRIKGDLIN FRPEDRIKRG LMMLKRAKGV WI
