ID T0QVB0_AERSA Unreviewed; 148 AA.
AC T0QVB0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Large ribosomal subunit protein bL9 {ECO:0000256|ARBA:ARBA00035292, ECO:0000256|HAMAP-Rule:MF_00503};
GN Name=rplI {ECO:0000256|HAMAP-Rule:MF_00503,
GN ECO:0000313|EMBL:ATP08183.1};
GN ORFNames=Asalp_09600 {ECO:0000313|EMBL:ATP08183.1};
OS Aeromonas salmonicida subsp. pectinolytica 34mel.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1324960 {ECO:0000313|EMBL:ATP08183.1, ECO:0000313|Proteomes:UP000222916};
RN [1] {ECO:0000313|Proteomes:UP000222916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34mel {ECO:0000313|Proteomes:UP000222916};
RX PubMed=29304740; DOI=10.1186/s12864-017-4301-6;
RA Pfeiffer F., Zamora-Lagos M.A., Blettinger M., Yeroslaviz A., Dahl A.,
RA Gruber S., Habermann B.H.;
RT "The complete and fully assembled genome sequence of Aeromonas salmonicida
RT subsp. pectinolytica and its comparative analysis with other Aeromonas
RT species: investigation of the mobilome in environmental and pathogenic
RT strains.";
RL BMC Genomics 19:20-20(2018).
CC -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000256|HAMAP-Rule:MF_00503}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family.
CC {ECO:0000256|ARBA:ARBA00010605, ECO:0000256|HAMAP-Rule:MF_00503}.
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DR EMBL; CP022426; ATP08183.1; -; Genomic_DNA.
DR RefSeq; WP_005313386.1; NZ_CP022426.1.
DR AlphaFoldDB; T0QVB0; -.
DR SMR; T0QVB0; -.
DR GeneID; 79878252; -.
DR OrthoDB; 9788336at2; -.
DR Proteomes; UP000222916; Chromosome.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.430.100; Ribosomal protein L9, C-terminal domain; 1.
DR Gene3D; 3.40.5.10; Ribosomal protein L9, N-terminal domain; 1.
DR HAMAP; MF_00503; Ribosomal_L9; 1.
DR InterPro; IPR000244; Ribosomal_bL9.
DR InterPro; IPR009027; Ribosomal_bL9/RNase_H1_N.
DR InterPro; IPR020594; Ribosomal_bL9_bac/chp.
DR InterPro; IPR020069; Ribosomal_bL9_C.
DR InterPro; IPR036791; Ribosomal_bL9_C_sf.
DR InterPro; IPR020070; Ribosomal_bL9_N.
DR InterPro; IPR036935; Ribosomal_bL9_N_sf.
DR NCBIfam; TIGR00158; L9; 1.
DR PANTHER; PTHR21368:SF18; 39S RIBOSOMAL PROTEIN L9, MITOCHONDRIAL; 1.
DR PANTHER; PTHR21368; 50S RIBOSOMAL PROTEIN L9; 1.
DR Pfam; PF03948; Ribosomal_L9_C; 1.
DR Pfam; PF01281; Ribosomal_L9_N; 1.
DR SUPFAM; SSF55658; L9 N-domain-like; 1.
DR SUPFAM; SSF55653; Ribosomal protein L9 C-domain; 1.
DR PROSITE; PS00651; RIBOSOMAL_L9; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_00503};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_00503};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00503};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_00503}.
FT DOMAIN 13..40
FT /note="Ribosomal protein L9"
FT /evidence="ECO:0000259|PROSITE:PS00651"
SQ SEQUENCE 148 AA; 15329 MW; 8F0594554222C769 CRC64;
MQVILLDKIA KLGGLGDQVA VKAGYARNYL IPQGKAVMAT KANIETFDAR RAELEAKLAA
GKAAAEERAA KLGELAAVVI ASKAGDEGKL FGSIGTRDVA DAITAAGVAV AKSEVRMGNV
LRNTGEYEVV VQLHADVKAT VQVQVVAL
//
