ID B8D5W0_DESA1 Unreviewed; 142 AA.
AC B8D5W0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Large ribosomal subunit protein uL14 {ECO:0000256|HAMAP-Rule:MF_01367};
GN Name=rpl14 {ECO:0000256|HAMAP-Rule:MF_01367};
GN OrderedLocusNames=DKAM_1165 {ECO:0000313|EMBL:ACL11491.1};
OS Desulfurococcus amylolyticus (strain DSM 18924 / JCM 16383 / VKM B-2413 /
OS 1221n) (Desulfurococcus kamchatkensis).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Desulfurococcus.
OX NCBI_TaxID=490899 {ECO:0000313|EMBL:ACL11491.1, ECO:0000313|Proteomes:UP000006903};
RN [1] {ECO:0000313|EMBL:ACL11491.1, ECO:0000313|Proteomes:UP000006903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18924 / JCM 16383 / VKM B-2413 / 1221n
RC {ECO:0000313|Proteomes:UP000006903};
RX PubMed=19114480; DOI=10.1128/JB.01525-08;
RA Ravin N.V., Mardanov A.V., Beletsky A.V., Kublanov I.V., Kolganova T.V.,
RA Lebedinsky A.V., Chernyh N.A., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Complete genome sequence of the anaerobic, protein-degrading
RT hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis.";
RL J. Bacteriol. 191:2371-2379(2009).
CC -!- FUNCTION: Binds to 23S rRNA. Forms part of two intersubunit bridges in
CC the 70S ribosome. {ECO:0000256|HAMAP-Rule:MF_01367}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC proteins L3 and L24e, part of which may contact the 16S rRNA in 2
CC intersubunit bridges. {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; CP001140; ACL11491.1; -; Genomic_DNA.
DR RefSeq; WP_012608832.1; NC_011766.1.
DR AlphaFoldDB; B8D5W0; -.
DR STRING; 490899.DKAM_1165; -.
DR GeneID; 7171251; -.
DR KEGG; dka:DKAM_1165; -.
DR eggNOG; arCOG04095; Archaea.
DR HOGENOM; CLU_095071_3_0_2; -.
DR Proteomes; UP000006903; 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; 2.40.150.20; Ribosomal protein L14; 1.
DR HAMAP; MF_01367; Ribosomal_L14; 1.
DR InterPro; IPR000218; Ribosomal_uL14.
DR InterPro; IPR019971; Ribosomal_uL14_arc.
DR InterPro; IPR019972; Ribosomal_uL14_CS.
DR InterPro; IPR036853; Ribosomal_uL14_sf.
DR NCBIfam; TIGR03673; uL14_arch; 1.
DR PANTHER; PTHR11761; 50S/60S RIBOSOMAL PROTEIN L14/L23; 1.
DR PANTHER; PTHR11761:SF8; 60S RIBOSOMAL PROTEIN L23; 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 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}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01367};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01367}.
SQ SEQUENCE 142 AA; 15407 MW; 33AF707811CC4A8C CRC64;
MGAKRAVAGK PAFSRRRVNT GLQVMSIAKA ADNSGAKEVM IIGVPGYHGR LRRVPPAGVG
DLVVVSVKKG IPEMRKKVFK AIVVRQRRPY KRPDGTWVAF EDNAVVILTP EGTPKGTEIR
GPIAREAAER WPQIANLASM IV
//