ID D5GGQ0_TUBMM Unreviewed; 153 AA.
AC D5GGQ0;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ83672.1};
GN ORFNames=GSTUM_00007461001 {ECO:0000313|EMBL:CAZ83672.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ83672.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ83672.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ83672.1,
RC ECO:0000313|Proteomes:UP000006911};
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
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; FN430275; CAZ83672.1; -; Genomic_DNA.
DR RefSeq; XP_002839481.1; XM_002839435.1.
DR AlphaFoldDB; D5GGQ0; -.
DR STRING; 656061.D5GGQ0; -.
DR EnsemblFungi; CAZ83672; CAZ83672; GSTUM_00007461001.
DR GeneID; 9185594; -.
DR KEGG; tml:GSTUM_00007461001; -.
DR eggNOG; KOG0004; Eukaryota.
DR HOGENOM; CLU_010412_2_0_1; -.
DR InParanoid; D5GGQ0; -.
DR OMA; GVFMAFH; -.
DR OrthoDB; 312211at2759; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
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; UBIQUITIN; 1.
DR PANTHER; PTHR10666:SF480; UBIQUITIN-LIKE DOMAIN-CONTAINING PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
SQ SEQUENCE 153 AA; 17452 MW; 5685CA953BB16E11 CRC64;
MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGGKKR KKKVYTTPKK IKHKRKKTKL AVLKYYKVDG DGKIERLRRE
CPTEGCGAGV FMAVMTNRQY CGKCHLTYVF DDA
//
