ID M0CGT8_9EURY Unreviewed; 149 AA.
AC M0CGT8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Large ribosomal subunit protein eL19 {ECO:0000256|HAMAP-Rule:MF_01475};
GN Name=rpl19e {ECO:0000256|HAMAP-Rule:MF_01475,
GN ECO:0000313|EMBL:ELZ21848.1};
GN ORFNames=C476_07573 {ECO:0000313|EMBL:ELZ21848.1};
OS Natrinema limicola JCM 13563.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1230457 {ECO:0000313|EMBL:ELZ21848.1, ECO:0000313|Proteomes:UP000011615};
RN [1] {ECO:0000313|EMBL:ELZ21848.1, ECO:0000313|Proteomes:UP000011615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13563 {ECO:0000313|EMBL:ELZ21848.1,
RC ECO:0000313|Proteomes:UP000011615};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000256|HAMAP-Rule:MF_01475}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01475}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL19 family.
CC {ECO:0000256|ARBA:ARBA00011082, ECO:0000256|HAMAP-Rule:MF_01475,
CC ECO:0000256|RuleBase:RU000574}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELZ21848.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AOIT01000030; ELZ21848.1; -; Genomic_DNA.
DR RefSeq; WP_008011527.1; NZ_AOIT01000030.1.
DR AlphaFoldDB; M0CGT8; -.
DR STRING; 1230457.C476_07573; -.
DR PATRIC; fig|1230457.4.peg.1520; -.
DR eggNOG; arCOG04089; Archaea.
DR OrthoDB; 11624at2157; -.
DR Proteomes; UP000011615; Unassembled WGS sequence.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:InterPro.
DR GO; GO:0070180; F:large ribosomal subunit 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 CDD; cd01418; Ribosomal_L19e_A; 1.
DR Gene3D; 1.10.1200.60; -; 1.
DR Gene3D; 1.10.1650.10; -; 1.
DR Gene3D; 1.20.5.560; Single Heli x bin; 1.
DR HAMAP; MF_01475; Ribosomal_L19e; 1.
DR InterPro; IPR035970; 60S_ribosomal_eL19_sf.
DR InterPro; IPR039547; Ribosomal_eL19.
DR InterPro; IPR033936; Ribosomal_eL19_arc.
DR InterPro; IPR023638; Ribosomal_eL19_CS.
DR InterPro; IPR000196; Ribosomal_eL19_dom.
DR InterPro; IPR015972; Ribosomal_eL19_dom1.
DR InterPro; IPR015973; Ribosomal_eL19_dom2.
DR InterPro; IPR015974; Ribosomal_eL19_dom3.
DR PANTHER; PTHR10722; 60S RIBOSOMAL PROTEIN L19; 1.
DR PANTHER; PTHR10722:SF0; 60S RIBOSOMAL PROTEIN L19; 1.
DR Pfam; PF01280; Ribosomal_L19e; 1.
DR SMART; SM01416; Ribosomal_L19e; 1.
DR SUPFAM; SSF48140; Ribosomal protein L19 (L19e); 1.
DR PROSITE; PS00526; RIBOSOMAL_L19E; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000011615};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01475};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01475};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01475}; rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01475}.
FT DOMAIN 3..146
FT /note="Large ribosomal subunit protein eL19"
FT /evidence="ECO:0000259|SMART:SM01416"
FT REGION 46..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 149 AA; 17241 MW; 428342EF3BC53D86 CRC64;
MTDLSAQKRL AADVLDVGEN RVWLDPEAQG DIAEAITRDE IRELVDDGRI QADEPSGNSR
GRARERNAKR SYGHQKGHGK RRGKKGARQN EKEDWQNKIR AQRRKLRELR DKGELTPTQY
RELYKKAGGG EFRSVRYLLN YIDDNYGDQ
//