RL25_HALOH
ID RL25_HALOH Reviewed; 218 AA.
AC B8D015;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=50S ribosomal protein L25 {ECO:0000255|HAMAP-Rule:MF_01334};
DE AltName: Full=General stress protein CTC {ECO:0000255|HAMAP-Rule:MF_01334};
GN Name=rplY {ECO:0000255|HAMAP-Rule:MF_01334};
GN Synonyms=ctc {ECO:0000255|HAMAP-Rule:MF_01334};
GN OrderedLocusNames=Hore_21220;
OS Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halothermothrix.
OX NCBI_TaxID=373903;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 168 / OCM 544 / DSM 9562;
RX PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT "Genome analysis of the anaerobic thermohalophilic bacterium
RT Halothermothrix orenii.";
RL PLoS ONE 4:E4192-E4192(2009).
CC -!- FUNCTION: This is one of the proteins that binds to the 5S RNA in the
CC ribosome where it forms part of the central protuberance.
CC {ECO:0000255|HAMAP-Rule:MF_01334}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S
CC rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA. Binds to the 5S rRNA
CC independently of L5 and L18. {ECO:0000255|HAMAP-Rule:MF_01334}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL25 family. CTC
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01334}.
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DR EMBL; CP001098; ACL70867.1; -; Genomic_DNA.
DR RefSeq; WP_015923836.1; NC_011899.1.
DR AlphaFoldDB; B8D015; -.
DR SMR; B8D015; -.
DR STRING; 373903.Hore_21220; -.
DR EnsemblBacteria; ACL70867; ACL70867; Hore_21220.
DR KEGG; hor:Hore_21220; -.
DR eggNOG; COG1825; Bacteria.
DR HOGENOM; CLU_075939_2_0_9; -.
DR OMA; HVDFYEV; -.
DR OrthoDB; 1673077at2; -.
DR Proteomes; UP000000719; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0008097; F:5S rRNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00495; Ribosomal_L25_TL5_CTC; 1.
DR Gene3D; 2.170.120.20; -; 1.
DR Gene3D; 2.40.240.10; -; 1.
DR HAMAP; MF_01334; Ribosomal_L25_CTC; 1.
DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
DR InterPro; IPR029751; Ribosomal_L25.
DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR InterPro; IPR020057; Ribosomal_L25_b-dom.
DR InterPro; IPR037121; Ribosomal_L25_C.
DR InterPro; IPR001021; Ribosomal_L25_long.
DR Pfam; PF01386; Ribosomal_L25p; 1.
DR Pfam; PF14693; Ribosomal_TL5_C; 1.
DR SUPFAM; SSF50715; SSF50715; 1.
DR TIGRFAMs; TIGR00731; bL25_bact_ctc; 1.
PE 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..218
FT /note="50S ribosomal protein L25"
FT /id="PRO_1000166173"
FT REGION 186..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..218
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 218 AA; 23733 MW; 76E569616CBEFE81 CRC64;
MERYNLKAEV RKDTGKGVAR KLRRNGLIPG VIYGKTRKPQ PLAVDAKDLN KVVGGNAILD
MTLVDGDKEE KETAVVKDLQ RDPVQGNILH VDFQHISMTD KLTVSVPVHI VGNARGVVAG
GVLQQLAREI EVECLPTDIP DEIEVDITDL GLGDSLSVGD IEPPANTDFI TPEDEVIVTI
VAPSEAVEEE VPAEDEEIMP EPEVIGEEDE GDEEEPEE