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Database: UniProt
Entry: A0A285F4W1_9ACTN
LinkDB: A0A285F4W1_9ACTN
Original site: A0A285F4W1_9ACTN 
ID   A0A285F4W1_9ACTN        Unreviewed;       208 AA.
AC   A0A285F4W1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=SAMN05421748_101546 {ECO:0000313|EMBL:SNY05754.1};
OS   Actinoplanes atraurantiacus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1036182 {ECO:0000313|EMBL:SNY05754.1, ECO:0000313|Proteomes:UP000219612};
RN   [1] {ECO:0000313|EMBL:SNY05754.1, ECO:0000313|Proteomes:UP000219612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.6857 {ECO:0000313|EMBL:SNY05754.1,
RC   ECO:0000313|Proteomes:UP000219612};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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: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}.
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DR   EMBL; OBDY01000001; SNY05754.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285F4W1; -.
DR   OrthoDB; 5242980at2; -.
DR   Proteomes; UP000219612; 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   Reference proteome {ECO:0000313|Proteomes:UP000219612};
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          6..94
FT                   /note="Large ribosomal subunit protein bL25 L25"
FT                   /evidence="ECO:0000259|Pfam:PF01386"
FT   DOMAIN          102..181
FT                   /note="Large ribosomal subunit protein bL25 beta"
FT                   /evidence="ECO:0000259|Pfam:PF14693"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   208 AA;  21713 MW;  003AE0AB597D9503 CRC64;
     MSEVKISAEP RTEFGKGGAR RTRRAGLVPA VLYGHGEKPQ HIALPAREFA AAIRHGGLNQ
     VFTIDIQGAS AATLALPKAI QRDPIKDTYE HVDLIIVKRG EKVQVDVPVN LTGEAARNTL
     VVHESNTLAV VADALHLPGG LDVSIEGLEA GSQITAGDVT LPNGVELAVE PDFVLAIVSQ
     AQTAEQLEGE SAEGAEAPAE GEEAPAAE
//
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