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RL31_ALISL
ID   RL31_ALISL              Reviewed;          72 AA.
AC   B6EMM4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=50S ribosomal protein L31 {ECO:0000255|HAMAP-Rule:MF_00501};
GN   Name=rpmE {ECO:0000255|HAMAP-Rule:MF_00501}; OrderedLocusNames=VSAL_I2744;
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238;
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
CC   -!- FUNCTION: Binds the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00501}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00501};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00501};
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00501}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL31 family.
CC       Type A subfamily. {ECO:0000255|HAMAP-Rule:MF_00501}.
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DR   EMBL; FM178379; CAQ80428.1; -; Genomic_DNA.
DR   RefSeq; WP_012551187.1; NC_011312.1.
DR   AlphaFoldDB; B6EMM4; -.
DR   SMR; B6EMM4; -.
DR   STRING; 316275.VSAL_I2744; -.
DR   EnsemblBacteria; CAQ80428; CAQ80428; VSAL_I2744.
DR   KEGG; vsa:VSAL_I2744; -.
DR   eggNOG; COG0254; Bacteria.
DR   HOGENOM; CLU_114306_4_3_6; -.
DR   OMA; WYPDAKV; -.
DR   OrthoDB; 2014569at2; -.
DR   Proteomes; UP000001730; Chromosome 1.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 4.10.830.30; -; 1.
DR   HAMAP; MF_00501; Ribosomal_L31_1; 1.
DR   InterPro; IPR034704; L28p-like.
DR   InterPro; IPR002150; Ribosomal_L31.
DR   InterPro; IPR027491; Ribosomal_L31_A.
DR   InterPro; IPR042105; Ribosomal_L31_sf.
DR   PANTHER; PTHR33280; PTHR33280; 1.
DR   Pfam; PF01197; Ribosomal_L31; 1.
DR   PRINTS; PR01249; RIBOSOMALL31.
DR   SUPFAM; SSF143800; SSF143800; 1.
DR   TIGRFAMs; TIGR00105; L31; 1.
DR   PROSITE; PS01143; RIBOSOMAL_L31; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; Zinc.
FT   CHAIN           1..72
FT                   /note="50S ribosomal protein L31"
FT                   /id="PRO_1000126556"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00501"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00501"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00501"
FT   BINDING         41
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00501"
SQ   SEQUENCE   72 AA;  7979 MW;  767757DC6AF799B5 CRC64;
     MKVGIHPEYK AVKATCSCGN EFEFKSALGK DTIHLDVCGE CHPFYTGKQR IVDTGGRVDR
     FNKRFGAIGS KK
 
 
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