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Database: UniProt
Entry: M0K3L6_9EURY
LinkDB: M0K3L6_9EURY
Original site: M0K3L6_9EURY 
ID   M0K3L6_9EURY            Unreviewed;       156 AA.
AC   M0K3L6;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Small ribosomal subunit protein uS15 {ECO:0000256|HAMAP-Rule:MF_01343};
GN   Name=rps15p {ECO:0000313|EMBL:EMA16002.1};
GN   Synonyms=rps15 {ECO:0000256|HAMAP-Rule:MF_01343};
GN   ORFNames=C442_18709 {ECO:0000313|EMBL:EMA16002.1};
OS   Haloarcula amylolytica JCM 13557.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=1227452 {ECO:0000313|EMBL:EMA16002.1, ECO:0000313|Proteomes:UP000011623};
RN   [1] {ECO:0000313|EMBL:EMA16002.1, ECO:0000313|Proteomes:UP000011623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13557 {ECO:0000313|EMBL:EMA16002.1,
RC   ECO:0000313|Proteomes:UP000011623};
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   -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01343}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS15 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01343, ECO:0000256|RuleBase:RU003919}.
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:EMA16002.1}.
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DR   EMBL; AOLW01000050; EMA16002.1; -; Genomic_DNA.
DR   RefSeq; WP_008313088.1; NZ_AOLW01000050.1.
DR   AlphaFoldDB; M0K3L6; -.
DR   GeneID; 25154603; -.
DR   PATRIC; fig|1227452.3.peg.3722; -.
DR   Proteomes; UP000011623; Unassembled WGS sequence.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00677; S15_NS1_EPRS_RNA-bind; 1.
DR   Gene3D; 4.10.860.130; -; 1.
DR   Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR   HAMAP; MF_01343_A; Ribosomal_S15_A; 1.
DR   InterPro; IPR000589; Ribosomal_uS15.
DR   InterPro; IPR023029; Ribosomal_uS15_arc_euk.
DR   InterPro; IPR012606; Ribosomal_uS15_N.
DR   InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR   PANTHER; PTHR11885:SF6; 40S RIBOSOMAL PROTEIN S13; 1.
DR   PANTHER; PTHR11885; RIBOSOMAL PROTEIN S15P/S13E; 1.
DR   Pfam; PF08069; Ribosomal_S13_N; 1.
DR   Pfam; PF00312; Ribosomal_S15; 1.
DR   SMART; SM01386; Ribosomal_S13_N; 1.
DR   SMART; SM01387; Ribosomal_S15; 1.
DR   SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 1.
DR   PROSITE; PS00362; RIBOSOMAL_S15; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01343};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01343}.
FT   DOMAIN          1..59
FT                   /note="Small ribosomal subunit protein uS15 N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01386"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   156 AA;  17751 MW;  EC4934B073F8197E CRC64;
     MARMHTRRRG SSDSDKPAAD EPPEWSDVDE DAIEERVVEL AEQGHSPSEI GLKLRDEGVQ
     GTPIPDVSLA TGKKVTEILE ENEAEPDLPE DLRNLLERAV RLRDHMDENP GDYQNKRALQ
     NTQSKIRRLI DYYRGDEVDE DFTYSYDNAV EALGLE
//
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