ID A0A134AGH9_9FIRM Unreviewed; 234 AA.
AC A0A134AGH9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=HMPREF1863_00875 {ECO:0000313|EMBL:KXB66823.1};
OS Peptoniphilus coxii.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=755172 {ECO:0000313|EMBL:KXB66823.1, ECO:0000313|Proteomes:UP000070442};
RN [1] {ECO:0000313|Proteomes:UP000070442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00729 {ECO:0000313|Proteomes:UP000070442};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2016) 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}.
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:KXB66823.1}.
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DR EMBL; LSDG01000024; KXB66823.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A134AGH9; -.
DR STRING; 755172.HMPREF1863_00875; -.
DR PATRIC; fig|755172.3.peg.833; -.
DR Proteomes; UP000070442; 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:UP000070442};
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 26..111
FT /note="Large ribosomal subunit protein bL25 L25"
FT /evidence="ECO:0000259|Pfam:PF01386"
FT DOMAIN 120..205
FT /note="Large ribosomal subunit protein bL25 beta"
FT /evidence="ECO:0000259|Pfam:PF14693"
FT REGION 198..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..234
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 234 AA; 25877 MW; 34E63849FC1B6587 CRC64;
MAILGILMYN MLLIRRRRRL MKTIHLNLQK REELGTSGAK KVRAKGLVPG VFYAENEEPV
AVAAKANELQ KVVEQAGTSA LVDIELDGKT TKILFKEIQN HPFKNQILHF DAYGVNLKEK
LRLSIPVVLE NRDEIHAQPS VLLQLLEEVE VECLPTNLPS EALVDVQNME IGDTLTVADL
DVSSIEGIDV LTDAEEAVAS LQEPREEAIE EDDEADAADV PTVGETEGEG EDEE
//
