ID A0A0N9UCV7_SPHMC Unreviewed; 209 AA.
AC A0A0N9UCV7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=AN936_12735 {ECO:0000313|EMBL:ALH81202.1};
OS Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=33050 {ECO:0000313|EMBL:ALH81202.1, ECO:0000313|Proteomes:UP000058074};
RN [1] {ECO:0000313|EMBL:ALH81202.1, ECO:0000313|Proteomes:UP000058074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EY-1 {ECO:0000313|EMBL:ALH81202.1,
RC ECO:0000313|Proteomes:UP000058074};
RX PubMed=26634754;
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete Genome Sequence of Polypropylene Glycol- and Polyethylene Glycol-
RT Degrading Sphingopyxis macrogoltabida Strain EY-1.";
RL Genome Announc. 3:0-0(2015).
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; CP012700; ALH81202.1; -; Genomic_DNA.
DR RefSeq; WP_054588471.1; NZ_CP012700.1.
DR AlphaFoldDB; A0A0N9UCV7; -.
DR KEGG; smag:AN936_12735; -.
DR PATRIC; fig|33050.5.peg.2627; -.
DR OrthoDB; 9788336at2; -.
DR Proteomes; UP000058074; 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:UP000058074};
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 REGION 172..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 209 AA; 22604 MW; A551FA6732A51950 CRC64;
MEIILLERIE KLGGIGDVVT VKNGFARNFL LPNNKALRAN DANRKLFEAN RSKIEADNAE
RRTDAEGRAK DIDGKQVVLI RQASNTGQLY GSVSVRDIVD ALIEDGVTGV TKAMVELERP
IKALGLVDVK VKLHPEVAVT VGVNVARSPD EAEMQKQGID VIAAMFEEEQ AEAVASALEP
DSEDEFEEAT PPSEVAAEEA PPADEDEEA
//
