ID I2F406_9BACT Unreviewed; 151 AA.
AC I2F406;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=Theba_0953 {ECO:0000313|EMBL:AFK06659.1};
OS Mesotoga prima MesG1.Ag.4.2.
OC Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae; Mesotoga.
OX NCBI_TaxID=660470 {ECO:0000313|EMBL:AFK06659.1, ECO:0000313|Proteomes:UP000002881};
RN [1] {ECO:0000313|EMBL:AFK06659.1, ECO:0000313|Proteomes:UP000002881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mesG1.Ag.4.2 {ECO:0000313|Proteomes:UP000002881};
RX PubMed=22798451;
RA Zhaxybayeva O., Swithers K.S., Foght J., Green A.G., Bruce D., Detter C.,
RA Han S., Teshima H., Han J., Woyke T., Pitluck S., Nolan M., Ivanova N.,
RA Pati A., Land M.L., Dlutek M., Doolittle W.F., Noll K.M., Nesbo C.L.;
RT "Genome Sequence of the Mesophilic Thermotogales Bacterium Mesotoga prima
RT MesG1.Ag.4.2 Reveals the Largest Thermotogales Genome To Date.";
RL Genome Biol. Evol. 4:700-708(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; CP003532; AFK06659.1; -; Genomic_DNA.
DR RefSeq; WP_014730680.1; NC_017934.1.
DR AlphaFoldDB; I2F406; -.
DR STRING; 660470.Theba_0953; -.
DR KEGG; mpg:Theba_0953; -.
DR eggNOG; COG0359; Bacteria.
DR HOGENOM; CLU_078938_3_0_0; -.
DR Proteomes; UP000002881; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000002881};
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"
FT COILED 37..74
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 151 AA; 16789 MW; EABDDBD94864ED1B CRC64;
MKVILLKDLS NVGKAGEVKN VSDGYGRNFL IPKGFAVEAN AKEMAKLKQT QKQKEEKEER
IRKASEELLH ELQKHHFTIK AKSGVSGKLF GAVTSGDISN HIRSVIGVDI DKREIDLEDH
IKQTGEYKVD VKLPGNVKGK IALKVEGLEE E
//
