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Database: UniProt
Entry: A0A0G1T1H2_9BACT
LinkDB: A0A0G1T1H2_9BACT
Original site: A0A0G1T1H2_9BACT 
ID   A0A0G1T1H2_9BACT        Unreviewed;       230 AA.
AC   A0A0G1T1H2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   08-NOV-2023, entry version 33.
DE   RecName: Full=Large ribosomal subunit protein bL25 {ECO:0000256|HAMAP-Rule:MF_01334};
DE   AltName: Full=General stress protein CTC {ECO:0000256|HAMAP-Rule:MF_01334};
GN   Name=rplY {ECO:0000256|HAMAP-Rule:MF_01334};
GN   Synonyms=ctc {ECO:0000256|HAMAP-Rule:MF_01334};
GN   ORFNames=UX68_C0023G0039 {ECO:0000313|EMBL:KKU48063.1};
OS   Parcubacteria group bacterium GW2011_GWA2_46_9.
OC   Bacteria.
OX   NCBI_TaxID=1618838 {ECO:0000313|EMBL:KKU48063.1, ECO:0000313|Proteomes:UP000034480};
RN   [1] {ECO:0000313|EMBL:KKU48063.1, ECO:0000313|Proteomes:UP000034480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:0000256|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:0000256|HAMAP-Rule:MF_01334}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL25 family. CTC
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01334}.
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:KKU48063.1}.
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DR   EMBL; LCND01000023; KKU48063.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1T1H2; -.
DR   Proteomes; UP000034480; 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: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; Ribosomal protein L25, beta domain; 1.
DR   HAMAP; MF_01334; Ribosomal_L25_CTC; 1.
DR   InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR   InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR   InterPro; IPR020057; Ribosomal_bL25_b-dom.
DR   InterPro; IPR037121; Ribosomal_bL25_C.
DR   InterPro; IPR001021; Ribosomal_bL25_long.
DR   InterPro; IPR029751; Ribosomal_L25_dom.
DR   NCBIfam; TIGR00731; bL25_bact_ctc; 1.
DR   PANTHER; PTHR33284; RIBOSOMAL PROTEIN L25/GLN-TRNA SYNTHETASE, ANTI-CODON-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR33284:SF1; RIBOSOMAL PROTEIN L25/GLN-TRNA SYNTHETASE, ANTI-CODON-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01386; Ribosomal_L25p; 1.
DR   Pfam; PF14693; Ribosomal_TL5_C; 1.
DR   SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01334};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01334};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01334};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01334}.
FT   DOMAIN          5..91
FT                   /note="Large ribosomal subunit protein bL25 L25"
FT                   /evidence="ECO:0000259|Pfam:PF01386"
FT   DOMAIN          99..184
FT                   /note="Large ribosomal subunit protein bL25 beta"
FT                   /evidence="ECO:0000259|Pfam:PF14693"
FT   REGION          184..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..230
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   230 AA;  25282 MW;  EE912CA499302224 CRC64;
     MTYSLQVATR TLVGKKNKLL RGQGLIPGVV YGHGETNRSV EIKKVPFEKL FQSAGESSLV
     DLNIDEDASL KVLIHDIQRH PVTGQIIHVD FYQVKMTEKL TADVPLVFIG EAKAVKELGG
     VLVKTLDHVK VECLPQDLVH ELKVNLSSLE TFDDAIHVKD IVVPTGINVL SSIDDMVVSV
     QPPRTEEEAK IEGAEAPVDV SEVEVEKEKK DKEVKGSGEE VRAEGKKEKS
//
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