ID A0A221NY21_9ACTN Unreviewed; 122 AA.
AC A0A221NY21;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Large ribosomal subunit protein uL14 {ECO:0000256|HAMAP-Rule:MF_01367};
GN Name=rplN {ECO:0000256|HAMAP-Rule:MF_01367};
GN ORFNames=LK07_13365 {ECO:0000313|EMBL:ASN24867.1};
OS Streptomyces pluripotens.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1355015 {ECO:0000313|EMBL:ASN24867.1, ECO:0000313|Proteomes:UP000031501};
RN [1] {ECO:0000313|EMBL:ASN24867.1, ECO:0000313|Proteomes:UP000031501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 137 {ECO:0000313|EMBL:ASN24867.1,
RC ECO:0000313|Proteomes:UP000031501};
RA Ser H.-L., Lee L.-H.;
RT "Genome sequence of Streptomyces pluripotens MUSC 137T.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds to 23S rRNA. Forms part of two intersubunit bridges in
CC the 70S ribosome. {ECO:0000256|HAMAP-Rule:MF_01367,
CC ECO:0000256|RuleBase:RU003950}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC proteins L3 and L19. In the 70S ribosome, L14 and L19 interact and
CC together make contacts with the 16S rRNA in bridges B5 and B8.
CC {ECO:0000256|HAMAP-Rule:MF_01367}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL14 family.
CC {ECO:0000256|HAMAP-Rule:MF_01367, ECO:0000256|RuleBase:RU003949}.
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DR EMBL; CP022433; ASN24867.1; -; Genomic_DNA.
DR RefSeq; WP_003998823.1; NZ_CP022433.1.
DR AlphaFoldDB; A0A221NY21; -.
DR SMR; A0A221NY21; -.
DR STRING; 1355015.LK06_012235; -.
DR GeneID; 79931266; -.
DR OrthoDB; 9806379at2; -.
DR Proteomes; UP000031501; Chromosome.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
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; 2.40.150.20; Ribosomal protein L14; 1.
DR HAMAP; MF_01367; Ribosomal_L14; 1.
DR InterPro; IPR000218; Ribosomal_uL14.
DR InterPro; IPR005745; Ribosomal_uL14_bac-type.
DR InterPro; IPR019972; Ribosomal_uL14_CS.
DR InterPro; IPR036853; Ribosomal_uL14_sf.
DR NCBIfam; TIGR01067; rplN_bact; 1.
DR PANTHER; PTHR11761; 50S/60S RIBOSOMAL PROTEIN L14/L23; 1.
DR PANTHER; PTHR11761:SF3; 54S RIBOSOMAL PROTEIN L38, MITOCHONDRIAL; 1.
DR Pfam; PF00238; Ribosomal_L14; 1.
DR SMART; SM01374; Ribosomal_L14; 1.
DR SUPFAM; SSF50193; Ribosomal protein L14; 1.
DR PROSITE; PS00049; RIBOSOMAL_L14; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000031501};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01367};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01367};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01367,
KW ECO:0000256|RuleBase:RU003950};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01367,
KW ECO:0000256|RuleBase:RU003950}.
SQ SEQUENCE 122 AA; 13372 MW; CBFA71D6EC1CB98A CRC64;
MIQQESRLRV ADNTGAKEIL CIRVLGGSGR RYAGIGDVIV ATVKDAIPGG NVKKGDVVKA
VIVRTVKERR RPDGSYIRFD ENAAVILKND GDPRGTRIFG PVGRELREKK FMKIISLAPE
VL
//