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Database: UniProt
Entry: A0A1H3ZIY0_9RHOB
LinkDB: A0A1H3ZIY0_9RHOB
Original site: A0A1H3ZIY0_9RHOB 
ID   A0A1H3ZIY0_9RHOB        Unreviewed;       208 AA.
AC   A0A1H3ZIY0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=SAMN05444370_103554 {ECO:0000313|EMBL:SEA23548.1};
OS   Rubrimonas cliftonensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rubrimonas.
OX   NCBI_TaxID=89524 {ECO:0000313|EMBL:SEA23548.1, ECO:0000313|Proteomes:UP000198703};
RN   [1] {ECO:0000313|EMBL:SEA23548.1, ECO:0000313|Proteomes:UP000198703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15345 {ECO:0000313|EMBL:SEA23548.1,
RC   ECO:0000313|Proteomes:UP000198703};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNQM01000003; SEA23548.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3ZIY0; -.
DR   STRING; 89524.SAMN05444370_103554; -.
DR   OrthoDB; 9788336at2; -.
DR   Proteomes; UP000198703; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198703};
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          185..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          37..71
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          146..173
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   208 AA;  22546 MW;  B54893FCD66511B2 CRC64;
     MQVVLLERVE RLGQIGDIVT VRAGFGRNFL LPQGKALRAT KANMVRFEEQ RAQLEARNLE
     LKREAEAVAA KLDGQIFVVI RQASDGGALY GSVTARDAAD AATAGGFSLD RGQVRLDRPV
     KDLGLHPMRV VLHPEVSATI RVNVARTAEE AELQAAGKTV AELRAEAEAA EQADFDVQRL
     FETDDEEEAG ARAAPAGMEV IDGDDDRR
//
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