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Database: UniProt
Entry: A0A291QEC9_9ACTN
LinkDB: A0A291QEC9_9ACTN
Original site: A0A291QEC9_9ACTN 
ID   A0A291QEC9_9ACTN        Unreviewed;       214 AA.
AC   A0A291QEC9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Large ribosomal subunit protein uL3 {ECO:0000256|HAMAP-Rule:MF_01325};
GN   Name=rplC {ECO:0000256|HAMAP-Rule:MF_01325};
GN   ORFNames=KY5_4795 {ECO:0000313|EMBL:ATL29813.1};
OS   Streptomyces formicae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1616117 {ECO:0000313|EMBL:ATL29813.1, ECO:0000313|Proteomes:UP000221011};
RN   [1] {ECO:0000313|EMBL:ATL29813.1, ECO:0000313|Proteomes:UP000221011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KY5 {ECO:0000313|EMBL:ATL29813.1,
RC   ECO:0000313|Proteomes:UP000221011};
RA   Holmes N.A., Devine R., Qin Z., Seipke R.F., Wilkinson B., Hutchings M.I.;
RT   "Complete Genome Sequence of Streptomyces formicae KY5, the formicamycin
RT   producer.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC       near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC       subunit. {ECO:0000256|HAMAP-Rule:MF_01325,
CC       ECO:0000256|RuleBase:RU003906}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC       proteins L14 and L19. {ECO:0000256|HAMAP-Rule:MF_01325,
CC       ECO:0000256|RuleBase:RU003906}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC       {ECO:0000256|ARBA:ARBA00006540, ECO:0000256|HAMAP-Rule:MF_01325,
CC       ECO:0000256|RuleBase:RU003905}.
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DR   EMBL; CP022685; ATL29813.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A291QEC9; -.
DR   KEGG; sfk:KY5_4795; -.
DR   Proteomes; UP000221011; 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; 3.30.160.810; -; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   HAMAP; MF_01325_B; Ribosomal_L3_B; 1.
DR   InterPro; IPR000597; Ribosomal_uL3.
DR   InterPro; IPR019927; Ribosomal_uL3_bac/org-type.
DR   InterPro; IPR019926; Ribosomal_uL3_CS.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   NCBIfam; TIGR03625; L3_bact; 1.
DR   PANTHER; PTHR11229:SF8; 39S RIBOSOMAL PROTEIN L3, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11229; 50S RIBOSOMAL PROTEIN L3; 1.
DR   Pfam; PF00297; Ribosomal_L3; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000221011};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01325};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01325};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01325,
KW   ECO:0000256|RuleBase:RU003906};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01325,
KW   ECO:0000256|RuleBase:RU003906}.
FT   REGION          133..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   214 AA;  22654 MW;  3E5F18DF660202C9 CRC64;
     MTKQIKGILG EKLGMTQVWD ENNRVVPVTV VKAGPCVVTQ VRTNDSDGYE SVQIAFGEID
     PRKVNKPLKG HFAKADVTPR RHLVEIRTAG ASEYVLGQEL TAETFEAGIK VDVTGKSKGK
     GFAGVMKRHN FAGGKASHGA HRVHRKPGSI GGCATPGRVF KGQRMAGRMG SERVTTQNLT
     VHAVDAEKGL LLIKGAVPGP NGGLVLVRTA AKGA
//
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