RL1_HALSA
ID RL1_HALSA Reviewed; 212 AA.
AC P13575; P05966; Q9HQL3;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
DE AltName: Full=HL8;
GN Name=rpl1 {ECO:0000255|HAMAP-Rule:MF_01318}; OrderedLocusNames=VNG_1105G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R1 / S9;
RX PubMed=2458258; DOI=10.1111/j.1432-1033.1988.tb14281.x;
RA Itoh T.;
RT "Complete nucleotide sequence of the ribosomal 'A' protein operon from the
RT archaebacterium, Halobacterium halobium.";
RL Eur. J. Biochem. 176:297-303(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33170 / DSM 669 / NCCB 81095 / NRC 34001;
RX PubMed=2743981; DOI=10.1002/j.1460-2075.1989.tb03496.x;
RA Shimmin L.C., Dennis P.P.;
RT "Characterization of the L11, L1, L10 and L12 equivalent ribosomal protein
RT gene cluster of the halophilic archaebacterium Halobacterium cutirubrum.";
RL EMBO J. 8:1225-1235(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [4]
RP PROTEIN SEQUENCE OF 2-37.
RX PubMed=6467081; DOI=10.1139/o84-058;
RA Matheson A.T., Yaguchi M., Christensen P., Rollin C.F., Hasnain S.;
RT "Purification, properties, and N-terminal amino acid sequence of certain
RT 50S ribosomal subunit proteins from the archaebacterium Halobacterium
RT cutirubrum.";
RL Can. J. Biochem. Cell Biol. 62:426-433(1984).
CC -!- FUNCTION: Binds directly to 23S rRNA. Probably involved in E site tRNA
CC release. {ECO:0000255|HAMAP-Rule:MF_01318}.
CC -!- FUNCTION: Protein L1 is also a translational repressor protein, it
CC controls the translation of its operon by binding to its mRNA.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
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DR EMBL; X13008; CAA31430.1; -; Genomic_DNA.
DR EMBL; X15078; CAA33179.1; -; Genomic_DNA.
DR EMBL; AE004437; AAG19500.1; -; Genomic_DNA.
DR PIR; H84266; H84266.
DR PIR; S01314; R5HSLH.
DR RefSeq; WP_010902795.1; NC_002607.1.
DR AlphaFoldDB; P13575; -.
DR SMR; P13575; -.
DR STRING; 64091.VNG_1105G; -.
DR PaxDb; P13575; -.
DR EnsemblBacteria; AAG19500; AAG19500; VNG_1105G.
DR GeneID; 5954211; -.
DR GeneID; 62886622; -.
DR KEGG; hal:VNG_1105G; -.
DR PATRIC; fig|64091.14.peg.846; -.
DR HOGENOM; CLU_062853_4_0_2; -.
DR InParanoid; P13575; -.
DR OMA; GWTDVDV; -.
DR OrthoDB; 70269at2157; -.
DR PhylomeDB; P13575; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00403; Ribosomal_L1; 1.
DR Gene3D; 3.40.50.790; -; 1.
DR HAMAP; MF_01318_A; Ribosomal_L1_A; 1.
DR InterPro; IPR002143; Ribosomal_L1.
DR InterPro; IPR023674; Ribosomal_L1-like.
DR InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR InterPro; IPR023669; Ribosomal_L1_arc.
DR InterPro; IPR023673; Ribosomal_L1_CS.
DR Pfam; PF00687; Ribosomal_L1; 1.
DR PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR SUPFAM; SSF56808; SSF56808; 1.
DR PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Reference proteome; Repressor;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Translation regulation; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6467081"
FT CHAIN 2..212
FT /note="50S ribosomal protein L1"
FT /id="PRO_0000125795"
FT CONFLICT 15
FT /note="E -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="A -> V (in Ref. 2; CAA33179)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 212 AA; 23092 MW; 20C6B679D80B9D73 CRC64;
MADNDIEEAV ARALEDAPQR NFRETVDLAV NLRDLDLNDP SQRVDEGVVL PSGTGQETQI
VVFADGETAV RADDVADDVL DEDDLSDLAD DTDAAKDLAD ETDFFVAEAP MMQDIAGALG
QVLGPRGKMP TPLQPDDDVV DTVNRMKNTV QIRSRDRRTF HTRVGAEDMS AEDIASNIDV
IMRRLHANLE KGPLNVDSVY VKTTMGPAVE VA