GenomeNet

Database: UniProt
Entry: G3EAC3_MESVI
LinkDB: G3EAC3_MESVI
Original site: G3EAC3_MESVI 
ID   G3EAC3_MESVI            Unreviewed;       132 AA.
AC   G3EAC3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Ubiquitin extension protein {ECO:0000313|EMBL:ADU04751.1};
DE   Flags: Fragment;
OS   Mesostigma viride (Green alga).
OC   Eukaryota; Viridiplantae; Streptophyta; Mesostigmatophyceae;
OC   Mesostigmatales; Mesostigmataceae; Mesostigma.
OX   NCBI_TaxID=41882 {ECO:0000313|EMBL:ADU04751.1};
RN   [1] {ECO:0000313|EMBL:ADU04751.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIES-296 {ECO:0000313|EMBL:ADU04751.1}, and SAG 50-1
RC   {ECO:0000313|EMBL:ADU04750.1};
RX   PubMed=21621456; DOI=10.1016/j.protis.2011.04.003;
RA   Hua J., Smith D.R., Borza T., Lee R.W.;
RT   "Similar relative mutation rates in the three genetic compartments of
RT   mesostigma and chlamydomonas.";
RL   Protist 163:105-115(2012).
CC   -!- FUNCTION: Component of the 40S subunit of the ribosome.
CC       {ECO:0000256|ARBA:ARBA00002225}.
CC   -!- SUBUNIT: Part of the 40S ribosomal subunit.
CC       {ECO:0000256|ARBA:ARBA00035123}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC       ribosomal protein eS31 family. {ECO:0000256|ARBA:ARBA00009891}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family.
CC       {ECO:0000256|ARBA:ARBA00008373}.
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DR   EMBL; HQ668000; ADU04750.1; -; Genomic_DNA.
DR   EMBL; HQ668001; ADU04751.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3EAC3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IEA:UniProt.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 6.20.50.150; -; 1.
DR   InterPro; IPR002906; Ribosomal_eS31.
DR   InterPro; IPR038582; Ribosomal_eS31_euk-type_sf.
DR   InterPro; IPR011332; Ribosomal_zn-bd.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   PANTHER; PTHR10666; UBIQUITIN; 1.
DR   PANTHER; PTHR10666:SF506; UBIQUITIN-40S RIBOSOMAL PROTEIN S27A-3; 1.
DR   Pfam; PF01599; Ribosomal_S27; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM01402; Ribosomal_S27; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   3: Inferred from homology;
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1..56
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADU04751.1"
FT   NON_TER         132
FT                   /evidence="ECO:0000313|EMBL:ADU04751.1"
SQ   SEQUENCE   132 AA;  15179 MW;  336194EFF69499CD CRC64;
     DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN IQKESTLHLV LRLRGGAKKR
     KKKTYTKPKK NKHKKKKVKL AVLQYYKVDD SGKVQRLRKE CPNPDCGAGC FMASHKDRHY
     CGKCGLTYVY QK
//
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