ID A0A133VMW8_9EURY Unreviewed; 126 AA.
AC A0A133VMW8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Large ribosomal subunit protein eL8 {ECO:0000256|HAMAP-Rule:MF_00326};
GN Name=rpl7ae {ECO:0000256|HAMAP-Rule:MF_00326,
GN ECO:0000313|EMBL:KXB07770.1};
GN ORFNames=AKJ51_00235 {ECO:0000313|EMBL:KXB07770.1};
OS candidate division MSBL1 archaeon SCGC-AAA382A20.
OC Archaea; Euryarchaeota; candidate division MSBL1.
OX NCBI_TaxID=1698280 {ECO:0000313|EMBL:KXB07770.1, ECO:0000313|Proteomes:UP000070263};
RN [1] {ECO:0000313|EMBL:KXB07770.1, ECO:0000313|Proteomes:UP000070263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC-AAA382A20 {ECO:0000313|EMBL:KXB07770.1};
RX PubMed=26758088; DOI=10.1038/srep19181;
RA Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W., Anthony Kamau A.,
RA Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V., Stingl U.;
RT "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT pools of the Red Sea.";
RL Sci. Rep. 6:19181-19181(2016).
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. {ECO:0000256|HAMAP-Rule:MF_00326}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Probably part of the RNase
CC P complex. {ECO:0000256|HAMAP-Rule:MF_00326}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00326}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC {ECO:0000256|ARBA:ARBA00007337, ECO:0000256|HAMAP-Rule:MF_00326}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXB07770.1}.
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DR EMBL; LHYE01000001; KXB07770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133VMW8; -.
DR PATRIC; fig|1698280.3.peg.63; -.
DR Proteomes; UP000070263; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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: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; Ribosomal_eL30-like_sf.
DR InterPro; IPR004038; Ribosomal_eL8/eL30/eS12/Gad45.
DR InterPro; IPR018492; Ribosomal_eL8/Nhp2.
DR InterPro; IPR022481; Ribosomal_eL8_arc.
DR NCBIfam; TIGR03677; eL8_ribo; 1.
DR PANTHER; PTHR11843; 40S RIBOSOMAL PROTEIN S12; 1.
DR PANTHER; PTHR11843:SF0; 40S RIBOSOMAL PROTEIN S12; 1.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR PRINTS; PR00881; L7ARS6FAMILY.
DR PRINTS; PR00884; RIBOSOMALHS6.
DR SUPFAM; SSF55315; L30e-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00326};
KW Reference proteome {ECO:0000313|Proteomes:UP000070263};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_00326};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_00326};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00326};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_00326};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00326}.
FT DOMAIN 20..110
FT /note="Ribosomal protein eL8/eL30/eS12/Gadd45"
FT /evidence="ECO:0000259|Pfam:PF01248"
SQ SEQUENCE 126 AA; 13988 MW; CABD03E467E6B83A CRC64;
MAENSIYVRF EVSRGLPDRI FEIVEAARDT DKVKKGTNET IKAIERNNAK LVVMAEDVDP
PEILAYVPPL CEEKDVPYGY VSDKIELGYA AGIDVQAASV AFIDPGEAKD ELRSVIDELE
EIKEEA
//
