ID I3R7Q8_HALMT Unreviewed; 248 AA.
AC I3R7Q8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Large ribosomal subunit protein uL4 {ECO:0000256|HAMAP-Rule:MF_01328};
GN Name=rpl4LP {ECO:0000313|EMBL:AFK20268.1};
GN Synonyms=rpl4 {ECO:0000256|HAMAP-Rule:MF_01328}, rpl4lp
GN {ECO:0000313|EMBL:AHZ23638.1}, rpl4p {ECO:0000313|EMBL:QCQ76297.1};
GN OrderedLocusNames=HFX_2587 {ECO:0000313|EMBL:AFK20268.1};
GN ORFNames=BM92_13740 {ECO:0000313|EMBL:AHZ23638.1}, C439_14729
GN {ECO:0000313|EMBL:ELZ99123.1}, E6P09_13845
GN {ECO:0000313|EMBL:QCQ76297.1};
OS Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=523841 {ECO:0000313|EMBL:AFK20268.1, ECO:0000313|Proteomes:UP000006469};
RN [1] {ECO:0000313|EMBL:AFK20268.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.2087 {ECO:0000313|EMBL:AFK20268.1};
RX PubMed=22247127; DOI=10.1128/AEM.07114-11;
RA Cai S., Cai L., Liu H., Liu X., Han J., Zhou J., Xiang H.;
RT "Identification of the haloarchaeal phasin (PhaP) that functions in
RT polyhydroxyalkanoate accumulation and granule formation in Haloferax
RT mediterranei.";
RL Appl. Environ. Microbiol. 78:1946-1952(2012).
RN [2] {ECO:0000313|EMBL:AFK20268.1, ECO:0000313|Proteomes:UP000006469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC R-4 {ECO:0000313|Proteomes:UP000006469}, and CGMCC 1.2087
RC {ECO:0000313|EMBL:AFK20268.1};
RX PubMed=22843593; DOI=10.1128/JB.00880-12;
RA Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA Zhou J., Hu S., Xiang H.;
RT "Complete genome sequence of the metabolically versatile halophilic
RT archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT hydroxyvalerate) producer.";
RL J. Bacteriol. 194:4463-4464(2012).
RN [3] {ECO:0000313|Proteomes:UP000011603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC R-4 {ECO:0000313|Proteomes:UP000011603};
RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA Eisen J.A., Facciotti M.T.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:ELZ99123.1, ECO:0000313|Proteomes:UP000011603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 {ECO:0000313|EMBL:ELZ99123.1}, and ATCC 33500 / DSM
RC 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000313|Proteomes:UP000011603};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [5] {ECO:0000313|EMBL:AHZ23638.1, ECO:0000313|Proteomes:UP000027075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 {ECO:0000313|EMBL:AHZ23638.1}, and ATCC 33500 / DSM
RC 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000313|Proteomes:UP000027075};
RA Bautista V.;
RT "Transcriptional profiles of Haloferax mediterranei on the basis of
RT nitrogen availability.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:AFK20268.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.2087;
RA Wang L., Yang H., Xiang H.;
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:QCQ76297.1, ECO:0000313|Proteomes:UP000299011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 {ECO:0000313|EMBL:QCQ76297.1}, and ATCC 33500 / DSM
RC 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000313|Proteomes:UP000299011};
RA DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA Roberts R.J.;
RT "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT mediterranei.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP001868; AFK20268.1; -; Genomic_DNA.
DR EMBL; CP007551; AHZ23638.1; -; Genomic_DNA.
DR EMBL; AOLO01000012; ELZ99123.1; -; Genomic_DNA.
DR EMBL; CP039139; QCQ76297.1; -; Genomic_DNA.
DR RefSeq; WP_004060048.1; NZ_CP039139.1.
DR AlphaFoldDB; I3R7Q8; -.
DR STRING; 523841.HFX_2587; -.
DR PaxDb; 523841-HFX_2587; -.
DR GeneID; 40157520; -.
DR KEGG; hme:HFX_2587; -.
DR PATRIC; fig|523841.21.peg.2971; -.
DR eggNOG; arCOG04071; Archaea.
DR HOGENOM; CLU_026535_0_0_2; -.
DR OrthoDB; 10737at2157; -.
DR Proteomes; UP000006469; Chromosome.
DR Proteomes; UP000011603; Unassembled WGS sequence.
DR Proteomes; UP000027075; Chromosome.
DR Proteomes; UP000299011; Chromosome.
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 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 44..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 248 AA; 26980 MW; 75BE32AB7B312C12 CRC64;
MQATIRDLNG DDAGSIDLPE VFETAYRPDL IKRAVIAAQA NRKQPYGADP YAGLRTPAES
MGSGRGMSHD PRQNGVARRV PHAVSGRRAH PPKAEKDQGK EINTKERKLA VRSALAATTD
SELVAERGHR FDDDLELPLV VSDDFEDLVK TKEVVDLLQT LGVYDDIERS EDNKKVKGGQ
GKLRGRKYTR PKSILFVTAE EPSKAARNLA GVDVATAANV SAEDLAPGTH AGRLTLFTES
AIEEVAER
//