ID O04829_SOLTU Unreviewed; 156 AA.
AC O04829; Q41500; Q41502; Q41504;
DT 01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT 01-JUL-1997, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE SubName: Full=Ubiquitin extension protein {ECO:0000313|EMBL:ABA46785.1, ECO:0000313|EMBL:CAA71132.1, ECO:0000313|EnsemblPlants:PGSC0003DMT400011938};
GN Name=102593024 {ECO:0000313|EnsemblPlants:PGSC0003DMT400011938};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EMBL:CAA71132.1};
RN [1] {ECO:0000313|EMBL:CAA71132.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Tuber {ECO:0000313|EMBL:CAA71132.1};
RX PubMed=9085582;
RA Royo J., Sanchez-Serrano J.J.;
RT "Nucleotide sequence of a potato, Solanum tuberosum L. tuber cDNA for ubi3-
RT 2 a second copy of the potato ubiquitin-ribosomal protein ubi3.";
RL Plant Physiol. 113:1003-1003(1997).
RN [2] {ECO:0000313|EMBL:ABA46785.1}
RP NUCLEOTIDE SEQUENCE.
RA Nielsen K.L., Welinder K.G., Nielsen H.V., Emmersen J.M.G.;
RT "Full length sequences from Solanum tuberosum cv. Kuras.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [4] {ECO:0000313|EnsemblPlants:PGSC0003DMT400011938}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400011938};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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; DQ200392; ABA46785.1; -; mRNA.
DR EMBL; Y10024; CAA71132.1; -; mRNA.
DR PIR; S19803; S19803.
DR PIR; T52334; T52334.
DR RefSeq; NP_001275598.1; NM_001288669.1.
DR AlphaFoldDB; O04829; -.
DR SMR; O04829; -.
DR STRING; 4113.O04829; -.
DR PaxDb; 4113-PGSC0003DMT400011939; -.
DR EnsemblPlants; PGSC0003DMT400011938; PGSC0003DMT400011938; PGSC0003DMG400004686.
DR EnsemblPlants; PGSC0003DMT400011939; PGSC0003DMT400011939; PGSC0003DMG400004686.
DR GeneID; 102593024; -.
DR Gramene; PGSC0003DMT400011938; PGSC0003DMT400011938; PGSC0003DMG400004686.
DR Gramene; PGSC0003DMT400011939; PGSC0003DMT400011939; PGSC0003DMG400004686.
DR Gramene; RHC12H1G2658.2.1; RHC12H1G2658.2.1.cds.1; RHC12H1G2658.2.
DR Gramene; RHC12H1G2665.2.1; RHC12H1G2665.2.1.cds.1; RHC12H1G2665.2.
DR KEGG; sot:102593024; -.
DR eggNOG; KOG0004; Eukaryota.
DR HOGENOM; CLU_010412_2_0_1; -.
DR InParanoid; O04829; -.
DR OMA; GVFMAFH; -.
DR OrthoDB; 312211at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
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:0031386; F:protein tag activity; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd01803; Ubl_ubiquitin; 1.
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:SF468; POLYUBIQUITIN-LIKE; 1.
DR PANTHER; PTHR10666; UBIQUITIN; 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 2: Evidence at transcript level;
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
SQ SEQUENCE 156 AA; 17702 MW; 1FD5C770FFD64DAD CRC64;
MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
IQKESTLHLV LRLRGGAKKR KKKTYTKPKK IKHKKKKVKL AVLQFYKVDD SGKVQRLRKE
CPNAECGAGT FMANHFDRHY CGKCGLTYVY QKAGGD
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