ID F9Q668_9PAST Unreviewed; 149 AA.
AC F9Q668;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, 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 ECO:0000313|EMBL:EGV07451.1};
GN ORFNames=HMPREF9952_2127 {ECO:0000313|EMBL:EGV07451.1};
OS Haemophilus pittmaniae HK 85.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=1035188 {ECO:0000313|EMBL:EGV07451.1, ECO:0000313|Proteomes:UP000006235};
RN [1] {ECO:0000313|EMBL:EGV07451.1, ECO:0000313|Proteomes:UP000006235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK 85 {ECO:0000313|EMBL:EGV07451.1,
RC ECO:0000313|Proteomes:UP000006235};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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:EGV07451.1}.
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DR EMBL; AFUV01000004; EGV07451.1; -; Genomic_DNA.
DR AlphaFoldDB; F9Q668; -.
DR STRING; 1035188.HMPREF9952_2127; -.
DR Proteomes; UP000006235; 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: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 149 AA; 15625 MW; AE050D1361D3E488 CRC64;
MQVILLDKIV HLGNVGDQVN VKSGFARNFL IPQGKAVMAT KANIEHFEAR RAELEAAAAA
SLAAAQARAA QVTALGSVTI TSKAGDEGRL FGAITTRDVA EAVTAAGVEI AKSEVRLPNG
PIRTLGDHDV RFQLHGEVFA TLDVIVVAE
//
