RL7A_PYRHO
ID RL7A_PYRHO Reviewed; 123 AA.
AC P62009; O59165; Q9V0W4;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=50S ribosomal protein L7Ae {ECO:0000255|HAMAP-Rule:MF_00326};
DE AltName: Full=Ribonuclease P protein component Rpp38;
DE Short=RNase P component Rpp38;
DE AltName: Full=Ribosomal protein L8e {ECO:0000255|HAMAP-Rule:MF_00326};
GN Name=rpl7ae {ECO:0000255|HAMAP-Rule:MF_00326}; OrderedLocusNames=PH1496;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=16829535; DOI=10.1093/jb/mvj144;
RA Terada A., Honda T., Fukuhara H., Hada K., Kimura M.;
RT "Characterization of the archaeal ribonuclease P proteins from Pyrococcus
RT horikoshii OT3.";
RL J. Biochem. 140:293-298(2006).
RN [3]
RP RNA-BINDING.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=22790959; DOI=10.1271/bbb.120272;
RA Oshima K., Nakashima T., Kakuta Y., Tsumoto K., Kimura M.;
RT "Thermodynamic analysis of a multifunctional RNA-binding protein, PhoRpp38,
RT in the hyperthermophilic archaeon Pyrococcus horikoshii OT3.";
RL Biosci. Biotechnol. Biochem. 76:1252-1255(2012).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), PUTATIVE FUNCTION IN RNASE P
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND RNA-BINDING.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=16574071; DOI=10.1016/j.bbrc.2006.02.192;
RA Fukuhara H., Kifusa M., Watanabe M., Terada A., Honda T., Numata T.,
RA Kakuta Y., Kimura M.;
RT "A fifth protein subunit Ph1496p elevates the optimum temperature for the
RT ribonuclease P activity from Pyrococcus horikoshii OT3.";
RL Biochem. Biophys. Res. Commun. 343:956-964(2006).
CC -!- FUNCTION: Multifunctional RNA-binding protein that recognizes the K-
CC turn motif in ribosomal RNA, box H/ACA, box C/D and box C'/D' sRNAs (By
CC similarity). When added to reconstituted ribonuclease P (RNase P) it
CC increases the optimum temperature to that of the partially purified
CC enzyme and causes a 5-fold increase in apparent Vmax. Binds the RNase P
CC catalytic RNA. {ECO:0000250, ECO:0000269|PubMed:16829535}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 72-76 degrees Celsius for RNase P
CC reconstituted with this protein as well as protein subunits Rnp1-4.
CC {ECO:0000269|PubMed:16574071};
CC -!- SUBUNIT: Part of the 50S ribosomal subunit (By similarity). May be part
CC of the RNase P complex. Reconstituted enzyme missing individual protein
CC subunits is suboptimally active, showing each subunit contributes to
CC optimization of activity. {ECO:0000250, ECO:0000269|PubMed:16574071,
CC ECO:0000269|PubMed:16829535}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00326}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC {ECO:0000255|HAMAP-Rule:MF_00326}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA30604.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000001; BAA30604.1; ALT_INIT; Genomic_DNA.
DR PIR; D71025; D71025.
DR RefSeq; WP_048053601.1; NC_000961.1.
DR PDB; 2CZW; X-ray; 1.90 A; A=1-123.
DR PDB; 5DCV; X-ray; 3.40 A; A/C=1-123.
DR PDB; 5XTM; X-ray; 2.10 A; A/C=1-123.
DR PDB; 5Y7M; X-ray; 3.10 A; A/C=1-123.
DR PDBsum; 2CZW; -.
DR PDBsum; 5DCV; -.
DR PDBsum; 5XTM; -.
DR PDBsum; 5Y7M; -.
DR AlphaFoldDB; P62009; -.
DR SMR; P62009; -.
DR STRING; 70601.3257921; -.
DR EnsemblBacteria; BAA30604; BAA30604; BAA30604.
DR GeneID; 1495573; -.
DR KEGG; pho:PH1496; -.
DR eggNOG; arCOG01751; Archaea.
DR OMA; KPFYVRF; -.
DR OrthoDB; 114541at2157; -.
DR BRENDA; 3.1.26.5; 5244.
DR EvolutionaryTrace; P62009; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:InterPro.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0004526; F:ribonuclease P activity; IDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:UniProtKB.
DR Gene3D; 3.30.1330.30; -; 1.
DR HAMAP; MF_00326; Ribosomal_L7Ae_Arch; 1.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR InterPro; IPR018492; Ribosomal_L7Ae/L8/Nhp2.
DR InterPro; IPR022481; Ribosomal_L7Ae_arc.
DR InterPro; IPR004037; Ribosomal_L7Ae_CS.
DR InterPro; IPR000948; Ribosomal_L7Ae_prok.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR PRINTS; PR00881; L7ARS6FAMILY.
DR PRINTS; PR00884; RIBOSOMALHS6.
DR SUPFAM; SSF55315; SSF55315; 1.
DR TIGRFAMs; TIGR03677; eL8_ribo; 1.
DR PROSITE; PS01082; RIBOSOMAL_L7AE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; tRNA processing.
FT CHAIN 1..123
FT /note="50S ribosomal protein L7Ae"
FT /id="PRO_0000136803"
FT HELIX 13..29
FT /evidence="ECO:0007829|PDB:2CZW"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:2CZW"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:2CZW"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:2CZW"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:2CZW"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2CZW"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:2CZW"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:2CZW"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:2CZW"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:2CZW"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:2CZW"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:2CZW"
SQ SEQUENCE 123 AA; 13423 MW; 934817F40CD2D4C5 CRC64;
MAKPSYVKFE VPKELAEKAL QAVEIARDTG KIRKGTNETT KAVERGQAKL VIIAEDVDPE
EIVAHLPPLC EEKEIPYIYV PSKKELGAAA GIEVAAASVA IIEPGKARDL VEEIAMKVRE
LMK
