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Database: UniProt
Entry: A0A176W9V6_MARPO
LinkDB: A0A176W9V6_MARPO
Original site: A0A176W9V6_MARPO 
ID   A0A176W9V6_MARPO        Unreviewed;       177 AA.
AC   A0A176W9V6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   08-NOV-2023, entry version 24.
DE   RecName: Full=30S ribosomal protein S13, chloroplastic {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AXG93_773s1680 {ECO:0000313|EMBL:OAE29928.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE29928.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE29928.1, ECO:0000313|Proteomes:UP000077202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC   TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE29928.1};
RA   Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA   Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT   "Mechanisms controlling the formation of the plant cell surface in tip-
RT   growing cells are functionally conserved among land plants.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit.
CC       {ECO:0000256|ARBA:ARBA00011458}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS13 family.
CC       {ECO:0000256|ARBA:ARBA00008080}.
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:OAE29928.1}.
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DR   EMBL; LVLJ01001380; OAE29928.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176W9V6; -.
DR   OrthoDB; 297269at2759; -.
DR   Proteomes; UP000077202; 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:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 1.10.8.50; -; 1.
DR   Gene3D; 4.10.910.10; 30s ribosomal protein s13, domain 2; 1.
DR   HAMAP; MF_01315; Ribosomal_S13_S18; 1.
DR   InterPro; IPR027437; Rbsml_uS13_C.
DR   InterPro; IPR001892; Ribosomal_uS13.
DR   InterPro; IPR010979; Ribosomal_uS13-like_H2TH.
DR   InterPro; IPR019980; Ribosomal_uS13_bac-type.
DR   InterPro; IPR018269; Ribosomal_uS13_CS.
DR   NCBIfam; TIGR03631; uS13_bact; 1.
DR   PANTHER; PTHR10871; 30S RIBOSOMAL PROTEIN S13/40S RIBOSOMAL PROTEIN S18; 1.
DR   PANTHER; PTHR10871:SF1; 37S RIBOSOMAL PROTEIN SWS2, MITOCHONDRIAL; 1.
DR   Pfam; PF00416; Ribosomal_S13; 1.
DR   SUPFAM; SSF46946; S13-like H2TH domain; 1.
DR   PROSITE; PS00646; RIBOSOMAL_S13_1; 1.
DR   PROSITE; PS50159; RIBOSOMAL_S13_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730}.
FT   REGION          157..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   177 AA;  19449 MW;  2761623F8FF5C00F CRC64;
     MAVSLASAMS NVSLGAPSCS GLRTASSSTP SVSLALPSTG YKRVQGLPYL SIRCARVGGV
     EVPNAKRIEI SLQYIHGIGK TTARQILLDV ELENKHTRDL SEEELTKLRD EVSKYMIEGD
     LRRFNTLAIK RLKDIQCYRG KRHIMGLPCR GQHTKCNART RRGKKVTVAG KKKAPGK
//
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