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Database: UniProt
Entry: D5GIJ2_TUBMM
LinkDB: D5GIJ2_TUBMM
Original site: D5GIJ2_TUBMM 
ID   D5GIJ2_TUBMM            Unreviewed;      1407 AA.
AC   D5GIJ2;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ84335.1};
GN   ORFNames=GSTUM_00008523001 {ECO:0000313|EMBL:CAZ84335.1};
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:CAZ84335.1, ECO:0000313|Proteomes:UP000006911};
RN   [1] {ECO:0000313|EMBL:CAZ84335.1, ECO:0000313|Proteomes:UP000006911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28 {ECO:0000313|EMBL:CAZ84335.1,
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; FN430327; CAZ84335.1; -; Genomic_DNA.
DR   RefSeq; XP_002840144.1; XM_002840098.1.
DR   STRING; 656061.D5GIJ2; -.
DR   EnsemblFungi; CAZ84335; CAZ84335; GSTUM_00008523001.
DR   GeneID; 9183269; -.
DR   KEGG; tml:GSTUM_00008523001; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_002763_0_0_1; -.
DR   InParanoid; D5GIJ2; -.
DR   OMA; WHFRTEV; -.
DR   OrthoDB; 12386at2759; -.
DR   Proteomes; UP000006911; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43719:SF11; HISTIDINE KINASE G7-RELATED; 1.
DR   PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          715..992
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1280..1401
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          302..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          413..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1165..1200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..323
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..526
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1185..1199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1331
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1407 AA;  152843 MW;  F4E158E54CD2E7B7 CRC64;
     MALLTSPSPV PFADCSVHNE AGYPGGISEA LRSRELYKYY QPPSDNSPPT PPGERLDHQK
     VDVGLEVVSS EDPTLSAFAL LTANLLNCKR SMISLVDDEL VYLVAESTRS LSLTKPYTHD
     PGDGLWVGGR TTMPRGRGLC ERTISLVPPE ELNNGEECIM IFELEDMAKE PEWEHHPNVS
     NWPYLRYYAG APLRTKNGVS IGSICVVDDK THPGGLEEEE RRTMAKMAEI VMEHLERVRA
     ENEMKRGKMM GIGMSRFVAA NFLQAGAEFG DVRNDGRLRS IGGNAREEKV VEAEQLAWAD
     AIRGQEPGKQ DRGYEKRGIR RQPSMESHCS CKLDMPDQNS PGAGDSVDPL SPSEKPRPGG
     VLSNLKPSQL PLSFPSPDRE DFASPEPPRT YPPELSRKLS YCSQSTSGLA TFSGNASGFS
     GTNTTTPSAS STESLSPPIF KEPDYGYPSA PDAQPRYRDG DDVENSLLST FGRASALIRS
     SLEADGVAFV DCDLGRNYGF EANPEDVVGK RPKLADAYRD QKPSGSRRKS GLFGYATASS
     SSLTNTLEGE GFFGHRVGEA EEDLPFSVEA LSEPFLHSLV DSCPQGRIFT YGGGVDGGYE
     AVELECDIGC SEIVSTVSDS DCTSTHPGGK SVCKTQIEKL KEFLPGSRSI VFVPLYDFDG
     NLFAVGFAWS NSKTRVFCKD IEGTYMIAFG NSIMAEIGRL HSVSADRAKG DFISSVSHEL
     RSPLHGILAS AEFLSETDLD NFQRSFVDTV ESCGRTLLDT INHVLDFSKL NSFGNRWDGD
     CKGRLRYARD FSNSAADVDN LTADTDLSAI LEEVTEGVFA GYEFRGISTP GIMEDVGKVD
     DFGASGRQIV GTKNDITVIM DIDRREDGWV FRTQPGALRR IFLNLGGNAI KYTDSGWVRI
     KLRAEDLPPS LGDDDEKSLV TLVFTDSGKG ISREFLKTKL FTPFSQENPL VSGTGLGMSI
     VRQIVEMLGG EIDVKSELGK GTEVTVSLVL KKSNRRTAKP DENFGTGGRD VGDWETEIEN
     IREKGRGKKV RLFGFDSPSE ANIHAASIFY LGCSFSRYIS HWFGMTPAAE SSPCNISSDF
     IIAHEGPRVE EHLARQIRGL PGKEGGTPLI VICSNASRHE TYQSLCGIDD GGIVYFVSKP
     CGPRKLAKAL AACIEKMETT FRNGNAAPPP LTVSGVDSPR ESTVGEIPTR PTSSPKLKSS
     GPVGFGKVLW GPSNNRGSCD TELPIVEADC DSYSTSPGSI CPALLKKDEK RPETLRRGLS
     ASSVSSTISA GSTLDGTLPT ALIVEDNPVN LMLLATFMKK RGYPFEKATN GLEALRAAES
     RPGGFDIILM DLQMPIMSGI ESTRAIRRLE RQSRAKGSVI IALTGLAAAS DKVEAYEAGI
     DLFMVKPVSF KQLESTMREY SLIGGET
//
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