ID D5G3U0_TUBMM Unreviewed; 637 AA.
AC D5G3U0;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 03-MAY-2023, entry version 60.
DE SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ79183.1};
GN ORFNames=GSTUM_00003803001 {ECO:0000313|EMBL:CAZ79183.1};
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:CAZ79183.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ79183.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ79183.1,
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).
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DR EMBL; FN429986; CAZ79183.1; -; Genomic_DNA.
DR RefSeq; XP_002835062.1; XM_002835016.1.
DR AlphaFoldDB; D5G3U0; -.
DR STRING; 656061.D5G3U0; -.
DR EnsemblFungi; CAZ79183; CAZ79183; GSTUM_00003803001.
DR GeneID; 9187121; -.
DR KEGG; tml:GSTUM_00003803001; -.
DR eggNOG; KOG1173; Eukaryota.
DR HOGENOM; CLU_011751_4_1_1; -.
DR InParanoid; D5G3U0; -.
DR OMA; DPFHNNA; -.
DR OrthoDB; 1215698at2759; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0005680; C:anaphase-promoting complex; IEA:EnsemblFungi.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:EnsemblFungi.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IEA:EnsemblFungi.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IEA:EnsemblFungi.
DR GO; GO:0032297; P:negative regulation of DNA-templated DNA replication initiation; IEA:EnsemblFungi.
DR GO; GO:1901970; P:positive regulation of mitotic sister chromatid separation; IEA:EnsemblFungi.
DR GO; GO:0016567; P:protein ubiquitination; IEA:EnsemblFungi.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR12558; CELL DIVISION CYCLE 16,23,27; 1.
DR PANTHER; PTHR12558:SF9; CELL DIVISION CYCLE PROTEIN 16 HOMOLOG; 1.
DR Pfam; PF12895; ANAPC3; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 313..346
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 415..448
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 100..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 71644 MW; D730EE09290908CA CRC64;
MEEFLKSWRQ DALNKHQYDA AIYIGDKLLA LTGDPKDAFW LAQVHFSTGH YSRAQTFLTR
NDLISRSTSC RYLAALCLIK QSKYDEALNI LGDKDPTHLF SGSTSTTNGR RRAAAGGRSS
KDREEHVGNV KFEAAMCYLR GLVYAKQNSF DKAKECYKHA VLIDVKCFEA FDQLMRNALM
SPDEEWAFLE SLDFESLGAD GEEPGEQAEF VKMLYTTRLS KYKNPAYFNK ATEILSETYN
LAQNADMILS QAELLFTQCK FKECLALCKK VIDDDNYNFS IYPLYLACLH ELDEKNTLFL
ISHDMADNYP EEPVTWLSVG VYYLTIGKIA ESRRFFSKAS MMDPHFGPAW IGFAHTFAAE
GEHDQAISAY STAARLFQGT HLPQLFLGMQ HLQLNNITLA DEYLNNAFTL CKSDPLLLNE
LGVVFYHKDH LKESVQLFTK ALDIAEEIES DPKAWIATRA NLAHAYRRLE FFDKALEQFL
IVKRTGEGKD SNVYSAIGLC QMQLRRPWEA VVSLHEALAV SPQDPIATEL LEKALQENSS
SNLLFQSSVM SADGEIIIQD DEEVEAIINQ RLKGKSKSRQ RYGNDGESSS RALRTTSRSV
GRSVATAGDA GGGGGRKRLG DVTSNYQEGM EISDDDL
//
