ID F9YSV6_CAPCC Unreviewed; 175 AA.
AC F9YSV6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Ribosome maturation factor RimM {ECO:0000256|HAMAP-Rule:MF_00014};
GN Name=rimM {ECO:0000256|HAMAP-Rule:MF_00014};
GN OrderedLocusNames=Ccan_18350 {ECO:0000313|EMBL:AEK23951.1};
OS Capnocytophaga canimorsus (strain 5).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=860228 {ECO:0000313|EMBL:AEK23951.1, ECO:0000313|Proteomes:UP000008895};
RN [1] {ECO:0000313|EMBL:AEK23951.1, ECO:0000313|Proteomes:UP000008895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5 {ECO:0000313|Proteomes:UP000008895};
RX PubMed=21914877; DOI=10.1128/JB.05853-11;
RA Manfredi P., Pagni M., Cornelis G.R.;
RT "Complete genome sequence of the dog commensal and human pathogen
RT Capnocytophaga canimorsus strain 5.";
RL J. Bacteriol. 193:5558-5559(2011).
CC -!- FUNCTION: An accessory protein needed during the final step in the
CC assembly of 30S ribosomal subunit, possibly for assembly of the head
CC region. Essential for efficient processing of 16S rRNA. May be needed
CC both before and after RbfA during the maturation of 16S rRNA. It has
CC affinity for free ribosomal 30S subunits but not for 70S ribosomes.
CC {ECO:0000256|HAMAP-Rule:MF_00014}.
CC -!- SUBUNIT: Binds ribosomal protein uS19. {ECO:0000256|HAMAP-
CC Rule:MF_00014}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00014}.
CC -!- DOMAIN: The PRC barrel domain binds ribosomal protein uS19.
CC {ECO:0000256|HAMAP-Rule:MF_00014}.
CC -!- SIMILARITY: Belongs to the RimM family. {ECO:0000256|HAMAP-
CC Rule:MF_00014}.
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DR EMBL; CP002113; AEK23951.1; -; Genomic_DNA.
DR RefSeq; WP_013997935.1; NC_015846.1.
DR AlphaFoldDB; F9YSV6; -.
DR STRING; 860228.Ccan_18350; -.
DR KEGG; ccm:Ccan_18350; -.
DR eggNOG; COG0806; Bacteria.
DR HOGENOM; CLU_077636_4_1_10; -.
DR OrthoDB; 9810331at2; -.
DR Proteomes; UP000008895; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.30.240; PRC-barrel domain; 1.
DR Gene3D; 2.40.30.60; RimM; 1.
DR HAMAP; MF_00014; Ribosome_mat_RimM; 1.
DR InterPro; IPR027275; PRC-brl_dom.
DR InterPro; IPR011033; PRC_barrel-like_sf.
DR InterPro; IPR011961; RimM.
DR InterPro; IPR002676; RimM_N.
DR InterPro; IPR036976; RimM_N_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR02273; 16S_RimM; 1.
DR PANTHER; PTHR33692; RIBOSOME MATURATION FACTOR RIMM; 1.
DR PANTHER; PTHR33692:SF1; RIBOSOME MATURATION FACTOR RIMM; 1.
DR Pfam; PF05239; PRC; 1.
DR Pfam; PF01782; RimM; 1.
DR SUPFAM; SSF50346; PRC-barrel domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00014};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00014};
KW Reference proteome {ECO:0000313|Proteomes:UP000008895};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW Rule:MF_00014};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_00014}.
FT DOMAIN 9..88
FT /note="RimM N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01782"
FT DOMAIN 98..169
FT /note="PRC-barrel"
FT /evidence="ECO:0000259|Pfam:PF05239"
SQ SEQUENCE 175 AA; 19845 MW; 555651D51E50DF7D CRC64;
MNLKDCFFIG TIVSKFSFKG EVLVKLDSDD PEIYENMESV FIALGGKPVP FFIEKCSLHK
SDLLRIKFED VSSEADAEAL MKHKLYLPLS FLPKLSGNQF YFHEVIGFTV KDVHYGEVGT
IVGVNDTTSQ ALFEIERDGK QILIPMNDDF LVEVNRKNKT IVVQTPEGLI DLYLE
//