ID A0A133VBF9_9EURY Unreviewed; 260 AA.
AC A0A133VBF9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Large ribosomal subunit protein uL4 {ECO:0000256|HAMAP-Rule:MF_01328};
GN Name=rpl4lp {ECO:0000313|EMBL:KXB03786.1};
GN Synonyms=rpl4 {ECO:0000256|HAMAP-Rule:MF_01328};
GN ORFNames=AKJ45_00415 {ECO:0000313|EMBL:KXB03786.1};
OS candidate division MSBL1 archaeon SCGC-AAA261F19.
OC Archaea; Euryarchaeota; candidate division MSBL1.
OX NCBI_TaxID=1698275 {ECO:0000313|EMBL:KXB03786.1, ECO:0000313|Proteomes:UP000070565};
RN [1] {ECO:0000313|EMBL:KXB03786.1, ECO:0000313|Proteomes:UP000070565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC-AAA261F19 {ECO:0000313|EMBL:KXB03786.1};
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: Forms part of the polypeptide exit tunnel.
CC {ECO:0000256|HAMAP-Rule:MF_01328}.
CC -!- FUNCTION: One of the primary rRNA binding proteins, this protein
CC initially binds near the 5'-end of the 23S rRNA. It is important during
CC the early stages of 50S assembly. It makes multiple contacts with
CC different domains of the 23S rRNA in the assembled 50S subunit and
CC ribosome. {ECO:0000256|HAMAP-Rule:MF_01328}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01328}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC {ECO:0000256|ARBA:ARBA00010528, ECO:0000256|HAMAP-Rule:MF_01328}.
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:KXB03786.1}.
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DR EMBL; LHXZ01000003; KXB03786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133VBF9; -.
DR PATRIC; fig|1698275.3.peg.226; -.
DR Proteomes; UP000070565; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1370.10; -; 1.
DR HAMAP; MF_01328_A; Ribosomal_L4_A; 1.
DR InterPro; IPR002136; Ribosomal_uL4.
DR InterPro; IPR023574; Ribosomal_uL4_dom_sf.
DR InterPro; IPR013000; Ribosomal_uL4_euk/arc_CS.
DR InterPro; IPR045240; Ribosomal_uL4_euk/arch.
DR InterPro; IPR019970; Ribosomall_uL4-arc.
DR NCBIfam; TIGR03672; rpl4p_arch; 1.
DR PANTHER; PTHR19431; 60S RIBOSOMAL PROTEIN L4; 1.
DR PANTHER; PTHR19431:SF0; 60S RIBOSOMAL PROTEIN L4; 1.
DR Pfam; PF00573; Ribosomal_L4; 1.
DR SUPFAM; SSF52166; Ribosomal protein L4; 1.
DR PROSITE; PS00939; RIBOSOMAL_L1E; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000070565};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01328};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01328}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01328};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01328}.
FT REGION 40..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 260 AA; 28812 MW; 6191DE0455C75053 CRC64;
MKVKVYSIEG EPGTQVELPQ IFEEKFRPDV IRRAVLAAQS ARVQPWGADP RAGKRTTAET
PQKGTGLTRV KRIKGRRHHA AGRSAFAPFT SGGRRAHPPK PNQKRKEKIN RKERRLAIRS
AISATKEGGL VRSRGHEVDD IKEFPVVIEE EVERIKKTTE AKELFKKLGV WRDVERVKEG
KKISSGKGKM RGRKYRKAIG PLLVIAEDRG VVRAARNLPG VDIVPVEKLN AELLAPGGDP
ARLTLWAKSA VDSLAGGMFS
//
