ID   D5GAF3_TUBMM            Unreviewed;       881 AA.
AC   D5GAF3;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   06-MAR-2013, entry version 19.
DE   SubName: Full=Whole genome shotgun sequence assembly, scaffold_18, strain Mel28;
GN   ORFNames=GSTUM_00005262001;
OS   Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=656061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28;
RX   PubMed=20348908; DOI=10.1038/nature08867;
RA   Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M.,
RA   Jaillon O., Montanini B., Morin E., Noel B., Percudani R., Porcel B.,
RA   Rubini A., Amicucci A., Amselem J., Anthouard V., Arcioni S.,
RA   Artiguenave F., Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A.,
RA   Buee M., Cantarel B., Chevalier G., Couloux A., Da Silva C.,
RA   Denoeud F., Duplessis S., Ghignone S., Hilselberger B., Iotti M.,
RA   Marcais B., Mello A., Miranda M., Pacioni G., Quesneville H.,
RA   Riccioni C., Ruotolo R., Splivallo R., Stocchi V., Tisserant E.,
RA   Viscomi A.R., Zambonelli A., Zampieri E., Henrissat B., Lebrun M.H.,
RA   Paolocci F., Bonfante P., Ottonello S., Wincker P.;
RT   "Perigord black truffle genome uncovers evolutionary origins and
RT   mechanisms of symbiosis.";
RL   Nature 464:1033-1038(2010).
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; FN430075; CAZ81496.1; -; Genomic_DNA.
DR   RefSeq; XP_002837305.1; XM_002837259.1.
DR   UniGene; Tme.5151; -.
DR   ProteinModelPortal; D5GAF3; -.
DR   EnsemblFungi; CAZ81496; CAZ81496; GSTUM_00005262001.
DR   GeneID; 9182531; -.
DR   KEGG; tml:GSTUM_00005262001; -.
DR   KO; K11228; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.150.50; -; 1.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000159; Ras-assoc.
DR   InterPro; IPR013761; SAM/pointed.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50200; RA; 1.
PE   4: Predicted;
KW   ATP-binding; Complete proteome; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
SQ   SEQUENCE   881 AA;  96402 MW;  4A70378EDEB056E6 CRC64;
     MRVIFRVCFI RGHEPNDVII STGEALLECD HSVLKELGIK KVGDRVRIFV AIKALRTKAY
     GNGKKRNRDT LAALDNMNGM PPYRTPTQSP YHPSPSQSNK RYSRALQNDI SSTLNSSSYS
     RPDSPSDSEY PRSYPRNGSA RNVISPPLES GRSNFGPPTP ASGSSSHPTK TPRTPHDYSK
     PPQAVANSPH HMKPTHRQSP SLDKGIMVLI LAQQDAIKVI GDGGQYRVIN ISDCNTPETL
     MRKIIKKFGI NDHWPSWGIY SIVDENGKDA ARCLSDTELL RIAHDVNRPE RTRLILGKKV
     APPLPLSSEF RVAQQIAREQ QDMAQKNSSA EAVYGNANNS KVKAPFGSDL RDIPSSPMST
     SSQLSPASPT ATDPASPRSR DSGPSRKASK KITAFFGQRP PSELISSNLA EYFPDHEHKV
     LERTVRNSMR RSARMSRYNN RFSVATTRSY ASSLSDAPPV PSVGDAWLNA ASPIMSNVPS
     RVPRPLSIRK SFLPSTSFSE NRDSLGAVPE DGESSPMGSE RKSYMSFDSA KEDSIRDSVN
     VIVTDTDTGS TMESYLDTHS NASTPATEVD PHAASMLGQF LSAGESEEEE EDGEEEYQED
     SWGGLRWMKG ALIGAGSFGS VFLALNALTG ELMAVKQVEM ASGGKEDARK RSMVEALQRE
     IELLKDLQHP NIVQYLGSSD EDDSLNIFLE YVPGGSVAAL LNTYGPQKEP LIRNFVRQIL
     TGLAYLHNKD IIHRDIKGAN VLVDNKGGIK ISDFGISKKV EAGLLTSSSH RPSLQGSVFW
     MAPEVVKQTS YTLKADIWSL GCLIVEMFTG THPYPDCSQL QAIFKIGTGG SAPAIPSKCS
     AEAKQFLSRT FELDHVKRPT ADELLLNPFL NPMVGQGPIG E
//