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Database: UniProt
Entry: F9YSV6_CAPCC
LinkDB: F9YSV6_CAPCC
Original site: F9YSV6_CAPCC 
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
//
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