ID A0A2T6ZKZ7_TUBBO Unreviewed; 1377 AA.
AC A0A2T6ZKZ7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE RecName: Full=GAF domain-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=B9Z19DRAFT_991453 {ECO:0000313|EMBL:PUU76169.1};
OS Tuber borchii (White truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=42251 {ECO:0000313|EMBL:PUU76169.1, ECO:0000313|Proteomes:UP000244722};
RN [1] {ECO:0000313|EMBL:PUU76169.1, ECO:0000313|Proteomes:UP000244722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tbo3840 {ECO:0000313|EMBL:PUU76169.1,
RC ECO:0000313|Proteomes:UP000244722};
RG DOE Joint Genome Institute;
RA Murat C., Kuo A., Barry K.W., Clum A., Dockter R.B., Fauchery L., Iotti M.,
RA Kohler A., Labutti K., Lindquist E.A., Lipzen A., Ohm R.A., Wang M.,
RA Grigoriev I.V., Zambonelli A., Martin F.M.;
RT "Draft genome sequence of Tuber borchii Vittad., a whitish edible
RT truffle.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PUU76169.1}.
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DR EMBL; NESQ01000198; PUU76169.1; -; Genomic_DNA.
DR STRING; 42251.A0A2T6ZKZ7; -.
DR Proteomes; UP000244722; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; 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; 3.30.450.270; -; 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 Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013654; PAS_2.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR001294; Phytochrome.
DR InterPro; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043150; Phytochrome_PHY_sf.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08446; PAS_2; 1.
DR Pfam; PF00360; PHY; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR01033; PHYTOCHROME.
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; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00022543};
KW Reference proteome {ECO:0000313|Proteomes:UP000244722};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 401..563
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 777..1021
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1193..1324
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1173
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1244
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1377 AA; 152558 MW; 4167AF9A4255DFA8 CRC64;
MGDKQAENVD DPLEIDTFSE SRDEQAPFSP SPTHQRPSSE SLPFYFHHRG LITPGSSAAG
TGSGGDFGPP PPDGRDIVYP IRSVVSISRP PPGLGSPAPG VRSGDAREEL SETRSESQSR
SQKTLTIANP DRKSPIASPV GGKRESGNSS GIPTSRQSLL PSTTKEGSDE RYVTARFKHL
VTNEGHMVVT GVSGSGSIQR CEDEPIHIPG AVQGFGVLIA LKEDMEGRLG VKIVSENSEQ
IIGYSPAALF ALESFCNILS EEQIENLHEH LDFVRDYASD PVHSGPDVFP LAVTSPNSTE
VKLWCAIHIA EKNPDLLICE FELEDDHIYP LFSPTEEETP SLPEDTLNSS PSEQDLLEST
LSASRPLRVL RNARKRRGQA AAMEVFSLMS QIQEQLSSAS TLDVFLKVLV GIVKELTGFH
RVMIYRFDEV WNGQVVTELV DPRATKDLYK GLHFPASDIP KQARDLYLLN KVRLLYDRDQ
ATARLVCKSK EYLDDPLDMT HSYLRAMSPI HIKYLRNMAV RASTSISLTA FDELWGLISC
HSYGQKGMRV SFPIRKMCRL IGETASRSIE RLSYASRLQA RKLINTVPTE QNPSGYIVAS
SDDLLKIFNA DFGLLSIREE TKVLGQLEYS QESLAMLEYL RERKFTSVLT SQNLSVDFPD
LNYDPGFSII AGLLLVPLSV GGQDFIVFFR KGQLWKVNWA GNPYEKNVKK GTQEYLEPRK
SFKIWSETVV GKSRDWTEEQ VETAAVLCLI YGKFIEVWRQ KEAALQTSQL TRLLLANASH
EVRTPLNAII NYLEIALESP LDSETRDNLM RSHSASKSLI YVINDLLDLT RTEAGQSLIM
EEAFDLSETI RDATERYKSG AERKNITFEV VEYEGLPRFV KGDQARLRQA VSNIAGNAVK
HTSEGGVRVD IWMSQVADGR CQIEIVVQDT GVGMSSEKLE ALFREFEQVH TEEDVMDRPE
ARENESPPLS FNAVSKIPGQ KILGLGLAVV ARIVRNMNGQ LRLKSEWGKG SRFTISFPLS
LASEAELDSE QKKRVVERQK SPSPQPPSVT PAPGEILLID SQNCRPQDMT RRNSGASMNN
SGSLGGAKSG ESETDEFVHT TSSPHLSTVS NSPPVRRGAD IRAKSFLDTM GLATPQQRPN
REIREGSAAP IKGPRAPDES SSPTPPPAAD TAPMKIPPIA DTNLPIEPSE KYEILVAEDD
PINSKIIKKR LEKMGHGVAL TVNGEECADL YTKHGQKYDI VLMDMQMPIM DGGTSTTRIR
QFEGTDLGRC VPRRHRINLR VPIFAVSASL AEERRTEYAD LGFDGWILKP IDFKRLKLLL
DGIRDPAIRA KSAYEPGHWE KGGWFFGTPG EIKSSPPEHE DIPPAALKTK DEGPDGI
//
