ID J3TEY5_9ENTR Unreviewed; 151 AA.
AC J3TEY5;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 08-NOV-2023, entry version 41.
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 ORFNames=A359_01030 {ECO:0000313|EMBL:AFP84507.1};
OS secondary endosymbiont of Ctenarytaina eucalypti.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts.
OX NCBI_TaxID=1199245 {ECO:0000313|EMBL:AFP84507.1, ECO:0000313|Proteomes:UP000003936};
RN [1] {ECO:0000313|EMBL:AFP84507.1, ECO:0000313|Proteomes:UP000003936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ceuc_S {ECO:0000313|EMBL:AFP84507.1};
RX PubMed=22821013; DOI=10.1093/molbev/mss180;
RA Sloan D.B., Moran N.A.;
RT "Genome reduction and co-evolution between the primary and secondary
RT bacterial symbionts of psyllids.";
RL Mol. Biol. Evol. 29:3781-3792(2012).
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; CP003546; AFP84507.1; -; Genomic_DNA.
DR RefSeq; WP_014887805.1; NC_018419.1.
DR AlphaFoldDB; J3TEY5; -.
DR STRING; 1199245.A359_01030; -.
DR KEGG; sect:A359_01030; -.
DR PATRIC; fig|1199245.3.peg.120; -.
DR HOGENOM; CLU_078938_4_1_6; -.
DR OrthoDB; 9788336at2; -.
DR Proteomes; UP000003936; 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 Reference proteome {ECO:0000313|Proteomes:UP000003936};
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 151 AA; 16088 MW; F6D91F7A88B750C5 CRC64;
MQVILLDKVT NLGGFGDQVN VKAGYARNYL VPKGKAVPAT KKNVAYFQAR HAELKAKMAD
VQAKAKARAE KINTLGSITI TSKSGEKGKL FGSIGARDIA EALSIATGMN VAKSEVRLQN
GVLRTTGNHD VSIQVHSDVF ATLNVLILPE V
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