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Database: UniProt
Entry: D5GAD1_TUBMM
LinkDB: D5GAD1_TUBMM
Original site: D5GAD1_TUBMM 
ID   D5GAD1_TUBMM            Unreviewed;       980 AA.
AC   D5GAD1;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ81485.1};
GN   ORFNames=GSTUM_00005242001 {ECO:0000313|EMBL:CAZ81485.1};
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:CAZ81485.1, ECO:0000313|Proteomes:UP000006911};
RN   [1] {ECO:0000313|EMBL:CAZ81485.1, ECO:0000313|Proteomes:UP000006911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28 {ECO:0000313|EMBL:CAZ81485.1,
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the TFP11/STIP family.
CC       {ECO:0000256|ARBA:ARBA00010900}.
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DR   EMBL; FN430075; CAZ81485.1; -; Genomic_DNA.
DR   RefSeq; XP_002837294.1; XM_002837248.1.
DR   AlphaFoldDB; D5GAD1; -.
DR   STRING; 656061.D5GAD1; -.
DR   EnsemblFungi; CAZ81485; CAZ81485; GSTUM_00005242001.
DR   GeneID; 9181893; -.
DR   KEGG; tml:GSTUM_00005242001; -.
DR   eggNOG; KOG2184; Eukaryota.
DR   HOGENOM; CLU_007977_0_0_1; -.
DR   InParanoid; D5GAD1; -.
DR   OMA; QNEFNPH; -.
DR   OrthoDB; 3060898at2759; -.
DR   Proteomes; UP000006911; Unassembled WGS sequence.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000390; P:spliceosomal complex disassembly; IEA:InterPro.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR022783; GCFC_dom.
DR   InterPro; IPR022159; STIP/TFIP11_N.
DR   InterPro; IPR045211; TFP11/STIP/Ntr1.
DR   PANTHER; PTHR23329:SF1; TUFTELIN-INTERACTING PROTEIN 11; 1.
DR   PANTHER; PTHR23329; TUFTELIN-INTERACTING PROTEIN 11-RELATED; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF07842; GCFC; 1.
DR   Pfam; PF12457; TIP_N; 1.
DR   SMART; SM00443; G_patch; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
PE   3: Inferred from homology;
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW   Spliceosome {ECO:0000256|ARBA:ARBA00022728}.
FT   DOMAIN          294..340
FT                   /note="G-patch"
FT                   /evidence="ECO:0000259|PROSITE:PS50174"
FT   REGION          1..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          253..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..110
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   980 AA;  108747 MW;  67BD33893FDAD888 CRC64;
     MGKRKVEKWE CSSDSDSSED EIEFPDPTDD HERFSSGHQR KRRWAGGDTK ERAALGIFGS
     DGEDEGARGG KGWSSKGLRN KGMGFVKSSE IVGGEDDEDS EGDEDDEDEY TGAVRMAQKV
     EEEIEGDDRT VGGLGSVSDA TAGFAGLGSW SSKGDEEESD TGPRLGLGRK PLSSRKFTRA
     GLGAGSQNNS GTSTPRSLDA HVGLGFKASA ISRMGPTESP PPESPTGQQY STPLGRGFVS
     SFTAASVGMP SLDPEFPVSQ SENIVPRPSF FTSEPSRGKG GGRANDTSQP KANPESFAAR
     MMAKMGYVEG QGLGKKGEGI LAPIEVKLRP QGVGVGAIRE KTDQARKEAK RAAALRGEVI
     SDSEDEERKK KAKRKAGSGS MGSTPGGTPL RARKERTKFR TVEEISAAAK GLDVPSVLKN
     IIDFTGKERK LLTSSSGVMS KDPSVEDESF KIARMARKDL ESFAGEWASL QDRKTYINKE
     ERRLNLEMDE ETKQIGRLKD MVDMAKSLQS LTLNIEDPKA SIEAIVTQLE VLQLEYQNEI
     EDHDLTGVAV AALHPLFKRE LSRWSPLKDP FLLFESFRRL RRILHIRSKE DVEAEYAKKG
     FVERSKSTTH YESMMFSLWL PKVRSAINND WNVHKPAPVL KVLDVWTSLL PSFIHANILD
     QLVLPKLRAA VADWNPRVSK GNKARQPPHL WVFQWLPHLG PHMDDLLREV RRGFGIVLDT
     WDVSRGTVEG LEAWKEVFGP SQLEDLLIRH LLPRLALRLR DDFDVNPGDQ VLEPLEDVFK
     WIPFFRISTF AQLVEAEFFP KWLNVLYQWL TAEPIFTEIQ EWYMFWQDVF PEGLRSAPAI
     RSGFKKGLDM MNNALDLGQD APIKLAPPPV EPLRPTKPEA IAPKSVPVKA NNTPVPVGAT
     FRDAVEDWCA DHNLLLIPLR KAHEASGRPM FRMTASASGS GGSVVYFQGD VVWAQDKKNR
     ELWEPLGLEE LLERIEGSMR
//
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