RL7A_PYRAB
ID RL7A_PYRAB Reviewed; 123 AA.
AC P62008; G8ZJD3; O59165; Q9V0W4;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=50S ribosomal protein L7Ae {ECO:0000255|HAMAP-Rule:MF_00326};
DE AltName: Full=Ribosomal protein L8e {ECO:0000255|HAMAP-Rule:MF_00326};
GN Name=rpl7ae {ECO:0000255|HAMAP-Rule:MF_00326};
GN OrderedLocusNames=PYRAB06750; ORFNames=PAB0460;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
RN [3]
RP CRYSTALLIZATION.
RX PubMed=14684904; DOI=10.1107/s090744490302239x;
RA Charron C., Manival X., Charpentier B., Branlant C., Aubry A.;
RT "Purification, crystallization and preliminary X-ray diffraction data of
RT L7Ae sRNP core protein from Pyrococcus abyssii.";
RL Acta Crystallogr. D 60:122-124(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS), AND RNA-BINDING.
RX PubMed=15342235; DOI=10.1016/j.jmb.2004.07.046;
RA Charron C., Manival X., Clery A., Senty-Segault V., Charpentier B.,
RA Marmier-Gourrier N., Branlant C., Aubry A.;
RT "The archaeal sRNA binding protein L7Ae has a 3D structure very similar to
RT that of its eukaryal counterpart while having a broader RNA-binding
RT specificity.";
RL J. Mol. Biol. 342:757-773(2004).
CC -!- FUNCTION: Multifunctional RNA-binding protein that recognizes the K-
CC turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA,
CC box C/D and box C'/D' sRNAs.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Probably part of the RNase
CC P complex. {ECO:0000255|HAMAP-Rule:MF_00326}.
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=CAB49588.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CCE70060.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ248285; CAB49588.1; ALT_INIT; Genomic_DNA.
DR EMBL; HE613800; CCE70060.1; ALT_INIT; Genomic_DNA.
DR PIR; C75109; C75109.
DR RefSeq; WP_048053601.1; NC_000868.1.
DR PDB; 1PXW; X-ray; 1.94 A; A/B=1-123.
DR PDB; 6SW9; EM; 4.20 A; 3=1-123.
DR PDB; 6SWC; EM; 3.30 A; 3=1-123.
DR PDB; 6SWE; EM; 3.10 A; 3=1-123.
DR PDBsum; 1PXW; -.
DR PDBsum; 6SW9; -.
DR PDBsum; 6SWC; -.
DR PDBsum; 6SWE; -.
DR AlphaFoldDB; P62008; -.
DR SMR; P62008; -.
DR STRING; 272844.PAB0460; -.
DR EnsemblBacteria; CAB49588; CAB49588; PAB0460.
DR GeneID; 1495573; -.
DR KEGG; pab:PAB0460; -.
DR PATRIC; fig|272844.11.peg.705; -.
DR eggNOG; arCOG01751; Archaea.
DR HOGENOM; CLU_084513_4_0_2; -.
DR OMA; KPFYVRF; -.
DR OrthoDB; 114541at2157; -.
DR PhylomeDB; P62008; -.
DR EvolutionaryTrace; P62008; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
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_0000136800"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:6SWE"
FT HELIX 13..29
FT /evidence="ECO:0007829|PDB:1PXW"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1PXW"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:1PXW"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:1PXW"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1PXW"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1PXW"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:1PXW"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1PXW"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:1PXW"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:1PXW"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1PXW"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:1PXW"
SQ SEQUENCE 123 AA; 13423 MW; 934817F40CD2D4C5 CRC64;
MAKPSYVKFE VPKELAEKAL QAVEIARDTG KIRKGTNETT KAVERGQAKL VIIAEDVDPE
EIVAHLPPLC EEKEIPYIYV PSKKELGAAA GIEVAAASVA IIEPGKARDL VEEIAMKVRE
LMK
