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RL25_DEHMB
ID   RL25_DEHMB              Reviewed;         218 AA.
AC   A5FPN6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=DehaBAV1_1255;
OS   Dehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 /
OS   BAV1).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=216389;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Lowry S., Clum A.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Ritalahti K.M., Loeffler F., Richardson P.;
RT   "Complete sequence of Dehalococcoides sp. BAV1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000688; ABQ17834.1; -; Genomic_DNA.
DR   RefSeq; WP_011309806.1; NC_009455.1.
DR   AlphaFoldDB; A5FPN6; -.
DR   SMR; A5FPN6; -.
DR   KEGG; deb:DehaBAV1_1255; -.
DR   PATRIC; fig|216389.18.peg.1324; -.
DR   HOGENOM; CLU_075939_2_0_0; -.
DR   OMA; HVDFYEV; -.
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   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..218
FT                   /note="50S ribosomal protein L25"
FT                   /id="PRO_1000086624"
FT   REGION          197..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..218
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   218 AA;  24286 MW;  D99B49E1315BEC00 CRC64;
     MTGISLALKP RQVFGNKNKL IRAQGLTPVH IFGHGLKSLA LQADTLELES TINRAGSSHL
     VNIKLDTDKK TRKVFIREIQ RNPIKGYLEH VDFYQINLKE KVTAEIPIHF SGESSLLKEK
     GHKLIAPFTH LTVEALPDDL PPEIHIDLSQ FDTLEKDLYI KDIILPGGAK ILNEADLLVA
     KVSEVHLKVE TTVAVNPAEE SGEKPVAHIE EKESTEKE
 
 
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