ID A0A423WXI4_9PEZI Unreviewed; 1494 AA.
AC A0A423WXI4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE RecName: Full=Phytochrome {ECO:0008006|Google:ProtNLM};
GN ORFNames=VMCG_03111 {ECO:0000313|EMBL:ROW08244.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROW08244.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROW08244.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROW08244.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) 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:ROW08244.1}.
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DR EMBL; LKEA01000006; ROW08244.1; -; Genomic_DNA.
DR STRING; 356882.A0A423WXI4; -.
DR Proteomes; UP000283895; 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:UP000283895};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 465..627
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 841..1065
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1306..1437
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1357
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1494 AA; 166170 MW; 94BB8993C9DC5364 CRC64;
MDADQDERSS LSQASPTYEE RDFAYDNELQ EPYPRVRSPT PVHLAAGIQA SLDTNIPLVG
GHTSYHVKSP SVQSSWSAAS DRQLGHGGHD PSDRVFPIRS VISVDPQNMS SPDQEYFSRM
ASDNQATPRP SNNRNDTTKN PRQRAASITS DSLHSVGSSA LSPGPRDFGQ ESRRGYAAGA
KSTVQADAER HGSRPLPLFV DEGSDDEGSN ASGDMPPSPT ADSAGQGTNS PPESTLDSHM
TTRFKHVTTD DGHLVITGRD GTLQRCEDEP IHTPGAVQAF GLMLAIREEP DGRFTVRYAS
ENSKRFIGYS PLDLFRLHNF TDILTEEQAD NLLDHIDFIR DEDADPAING PEVFSMSVIR
PKKRATKLWC AIHIHRAHPE LIICEFELDD DPDFPLRPED ENTPDVPEDT LHSNPTMEEL
AESTEITSKP LRVLRSARKR KGEAGAMQVF DIMSQVQEQL ASAPNLERFL KVLVGIIKEL
TGFHRVMVYQ FDSSFNGKVV TELVDPTHTR DLYNGLHFPA SDIPKQAREL YKINKVRLLY
DRDQETARLV CRSKEDLEVP LDMTHSYLRA MSPIHLKYLG NMAVRSSMSI SINAFNELWG
LIACHSYGPK GMRVSFPIRK MCRLVGDTVS RNIERLSYSS RLQARKLINT VPTDKNPSGY
IIASSDDLLK LFSADFGMLC IKGETKIMGK FEHSQEALAM LEYLRLRRFT SVLTTQDINQ
DFPDLRYPPG FHFIAGFLYV PLSVGGHDFI VFFRKGQVRE VKWAGNPYEK IVQEGTQDYL
EPRRSFQVWH ETVLGKCREW SEEQIETAAV LCLVYGKFIE VWRQKEAALE GSRLTRLLLA
NSAHEVRTPL NAIINYLEIA LEGSLDNETR DNLSKSHSAS KSLIYVVTEE GNDLVTDEVF
EFPACITEAT EPFKNDAKRK GISYEVIEHP GLPKYVYGDQ RKVRQAVANI TANAVQHTTD
GFVRIELYSA EVQGNKVRVE IVVQDTGRGM KPDQLDALFR DLEQVSTDTD ESQPEKEEKD
KEEPRTLGLG LAMVARIVRN MDGQLRLKSE EGKGSRFVIQ LPFDMPPNDS PGPPEDVGPD
ASTTDSIAAS VSTTLPPADD GEVMLVDRGS TNSAYKQATA PLKGNFDDNI SIGTHPSVAS
RCSAKSSRSD ADRLIDAIKT PLGVGEPETE EASIQRRSLQ AVYQDTSSRS GVTRSLSPKR
PYGRPGDLTR SLSSPGKSHG QDGEVTVPEE PVGMAYVTDS KTPIRPVKVP DEYHDQPERP
AQPNETSGIL FEVGDSPQPG MRVSSTATTN DGNVHKAGQP TSAKLQVLIA EDDPINMKVL
RKRLEKAGHT VHHTVNGEDC AAVYREGSDK YDVVLMDMQM PIVDGLTSTK MIREIERSGE
HHKLSAIASN HGRIPIFAVS ASLMERERKT YTSAGFDGWI LKPIDFKRLE TLLFGIIDDK
VRNDAVYVTG EWERGGWFRK RLELPPDEKA EEAAALRDVE LKGNEINAAR ESMS
//
