ID B2W9G6_PYRTR Unreviewed; 1347 AA.
AC B2W9G6;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Phytochrome E {ECO:0000313|EMBL:EDU49544.1};
GN ORFNames=PTRG_06624 {ECO:0000313|EMBL:EDU49544.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU49544.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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DR EMBL; DS231620; EDU49544.1; -; Genomic_DNA.
DR RefSeq; XP_001936957.1; XM_001936922.1.
DR STRING; 426418.B2W9G6; -.
DR EnsemblFungi; EDU49544; EDU49544; PTRG_06624.
DR GeneID; 6344887; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_50_4_1; -.
DR InParanoid; B2W9G6; -.
DR OMA; MEVRASM; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000001471; 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:UP000001471};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 438..600
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 814..981
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1120..1250
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1275..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1171
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1347 AA; 148933 MW; B54C7BD5E540CE6A CRC64;
MSQSPYQTPD AGPPAQDDHR YTFSTVSPVQ EETCSPLDAA TKPLHSTSPP RKSANTGPST
PVGPLSPSAT DRVFPIRSAI SVDPSPTPKG AQSQGDYFHP YSRTNDPRLT SDRRASQGSA
TSQSSHASQR GWPMRHSASK ADPGRGNGSK RATSQLPPAQ LFNDISSTRS TGTGSVQENS
RSPSFKVDRP PSVSAASAKS GISSLDMGGL VAHRFKHVVT DGGHMVITGR EGDTLQRCED
EPIHLPGAVQ GFGLLVALQD DSEGSLLVRI VSENSRRILG RTPKELFALE SFTDILSEEQ
ADNLLDHIDF IKDEDSDVTS NGPEVFTMSI KVAGHSRTRK LWCAIHINET NPGLVICEFE
LEEDPLYPLV PPNDLTPELP EDTLSSQPTA EELLESTEIK SKPLRVLRSA RKRKGEAAAM
EVFNIMSQVQ EQLAAAPSLE KFLKVLVGVV KELTGFHRVM IYQFDQTFNG RVVTELVDPR
ATKDLYKGLN FPASDIPKQA RELYKLNKVR MLYDRDQQTA RLVCRTAEDL ETPLDLTHSY
LRAMSPIHLK YLNNMAVRSS MSISINAFNE LWGLIACHSY GPRGMRVSFP IRKMCRMVGD
AASRNIERLS YASRLQARKL INTVPTQHNP SGYIIASSDD LLKLFDADFG LLSIRDETKI
LGTLENSQEA LAMLEYLRMR KIQAVMTSTD IVSDFPDLRY PPGFHVIAGM LIVPLSVDGE
DFIVFFRKGQ LKEVKWAGNP YEKFIKEGTE GYLEPRKSFK TWSETVVGKC REWTEEEIET
ASVLCLVYGK FIEVWRQKEA ALQSSQLTRL LLANSAHEVR TPLNAIINYL EIALEGALDT
ETRENLSRSH SASKSLIYVI NDLLDLTKTE EGGPLIKGES FDFQETIKEA TDMFRNDAKR
KSIKYEVIEH PGLPKHCIGD QRRIRQAISN ITANAIQHTT QGTVKVEIYV TGQPSVDHVD
VEVAVSDTGA GMSQKKLDQL FYDLEQVHSE PTSMIEDALL PDQKHIAKQD PDSAASRKRS
KSLEHISTQS IVPPHQRSME SGGPGEENIF GSNAPVTALK MPDEGGDSPI GLRRSGSILG
EVKSESPPGP TPQTQPTPPT DATQPSPEPE PANLSPNNMR VLVAEDDPVN SRIVKKRLEK
LGHQVHLTVN GEECSSAFCD NSQETDIILM DMQMPIVDGL TSTKMIRSFE KLHQNIYSPR
AAICGRVPII AVSASLIERD RQTYIDAGFD AWILKPISFD RLNKLMTAVV DKEIRNDCLY
QPGAWEKGGW FHTGKHSAGE VDTKPSGEAP VTNPSEEMEE AIIRDDDPMA GEKKEEGDIP
EEQERLLENQ AEGKTEPPED SAEKPPA
//
