RL10_NATPD
ID RL10_NATPD Reviewed; 354 AA.
AC Q3INI7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=50S ribosomal protein L10 {ECO:0000255|HAMAP-Rule:MF_00280};
DE AltName: Full=Acidic ribosomal protein P0 homolog {ECO:0000255|HAMAP-Rule:MF_00280};
GN Name=rpl10 {ECO:0000255|HAMAP-Rule:MF_00280};
GN Synonyms=rplP0 {ECO:0000255|HAMAP-Rule:MF_00280};
GN OrderedLocusNames=NP_4450A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
CC -!- FUNCTION: Forms part of the ribosomal stalk, playing a central role in
CC the interaction of the ribosome with GTP-bound translation factors.
CC {ECO:0000255|HAMAP-Rule:MF_00280}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms part of the ribosomal
CC stalk which helps the ribosome interact with GTP-bound translation
CC factors. Forms a heptameric L10(L12)2(L12)2(L12)2 complex, where L10
CC forms an elongated spine to which the L12 dimers bind in a sequential
CC fashion. {ECO:0000255|HAMAP-Rule:MF_00280}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000255|HAMAP-Rule:MF_00280}.
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DR EMBL; CR936257; CAI50316.1; -; Genomic_DNA.
DR RefSeq; WP_011323931.1; NC_007426.1.
DR AlphaFoldDB; Q3INI7; -.
DR SMR; Q3INI7; -.
DR STRING; 348780.NP_4450A; -.
DR EnsemblBacteria; CAI50316; CAI50316; NP_4450A.
DR GeneID; 3703119; -.
DR KEGG; nph:NP_4450A; -.
DR eggNOG; arCOG04288; Archaea.
DR HOGENOM; CLU_053173_0_0_2; -.
DR OMA; MAHVAEW; -.
DR OrthoDB; 73593at2157; -.
DR Proteomes; UP000002698; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.1730; -; 1.
DR Gene3D; 3.90.105.20; -; 1.
DR HAMAP; MF_00280; Ribosomal_L10_arch; 1.
DR InterPro; IPR022909; 50S_L10_arch.
DR InterPro; IPR043141; Ribosomal_L10-like_sf.
DR InterPro; IPR001790; Ribosomal_L10P.
DR InterPro; IPR043164; RL10_insert_sf.
DR InterPro; IPR040637; RL10P_insert.
DR Pfam; PF00466; Ribosomal_L10; 1.
DR Pfam; PF17777; RL10P_insert; 1.
DR SUPFAM; SSF160369; SSF160369; 1.
PE 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..354
FT /note="50S ribosomal protein L10"
FT /id="PRO_1000078823"
FT REGION 286..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..347
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 354 AA; 37197 MW; 2A6D9F47D9A22727 CRC64;
MSAEARKTET IPEWKQEEID ELVAFLERYE SVGVVDITGI PSRQLQDMRR DLHGTAALRV
SRNTLMERAL NEGGDGLGEL VEHVEGQVGL IGTNDNPFGL YQQLEESKTP APINAGEVAP
NDIVIPEGDT GVDPGPFVGD LQQVGANARI EGGSIKVVED STVLSAGEEV SSDLSNVLSE
LGIEPKEVGL DLRGVSSEGV LFSPEELDID VESYRTDIES AASAARNLSV NAEYPTARTA
PSMLAKAAGE AKSVGLSAAV ESPDLADDLV SKADAQVRAL AAQIDDEEAL PEELQDVEQP
AAADSAAEAD DEDDTGNVEQ TDESDADDAD DADDADDADE EDGDGGDALG DMFG