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}.
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; 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
//