ID Q0U6W3_PHANO Unreviewed; 1455 AA.
AC Q0U6W3;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 24-JAN-2024, entry version 110.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAT80314.2};
GN ORFNames=SNOG_12501 {ECO:0000313|EMBL:EAT80314.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT80314.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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DR EMBL; CH445346; EAT80314.2; -; Genomic_DNA.
DR RefSeq; XP_001802722.1; XM_001802670.1.
DR STRING; 321614.Q0U6W3; -.
DR EnsemblFungi; SNOT_12501; SNOT_12501; SNOG_12501.
DR GeneID; 5979631; -.
DR KEGG; pno:SNOG_12501; -.
DR VEuPathDB; FungiDB:JI435_125010; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_50_4_1; -.
DR InParanoid; Q0U6W3; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000001055; 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; 2.
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:UP000001055};
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..1053
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1196..1326
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1455
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1247
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1455 AA; 161224 MW; 23D14D1A21603C73 CRC64;
MAEPPPSTDG EPSDQQHGRI EKHVVSPIQE EPGTPSGTAN KGADILSPSL TSGPMSPTTD
RVFPIRSVVS VDPMPTPKSS NQSPGDYFHP WSRINDSRFP DARRQSQGST TSQSSQASQR
NRLHKQSNAA TPVAEQPPAT RTPVRSSTGS DTSKSTKKAP PHLSAQLFND TASNRSTEEN
SRSPSLMPDM PRSPGGASIA SSLGDVGLIT HRFKHVTTEG GHMIITGRDG DILQRCEDEP
IHIPGAIQGF GLIIALAEDL SDNGNLIVRV VSENSKRVIG RTPKELFALE SFTDILSEEQ
ADNLLDHIDF IKDEDSDVMT NGPEVFTIGI KVPGISRTRK LWCAIHVPAA NPGLIICEFE
LEDDPQFPLV PSNEMTPELP EDTLSSNPTE QELLESTEIK SKPLRVLRSA RKRKGEAAAM
EVFNIMSQVQ EQLAAAPSLD RFLKVLVGVV KELTGFHRVM IYQFDQAFNG RVVTELVDPR
ATKDLFKGLN FPASDIPKQA RDLYKLNKVR MLYDRDQETA RLVCRTIEDL ETPLDLTHSY
LRAMSPIHIK YLANMAVRSS MSISINAFNE LWGLIACHTY GPRGMRVSFP IRKMCRMVGD
AASRNIERLS YASRLQARKL INTVPTQHNP SGYIIASSDD LLKLFDADFG LLSIRDETKI
LGQLENSQEA LAMLEYLRMR KIQSVMTSMD ISQDFPDLRY PPGFHVVAGT LIVPLSASGT
DFIVFFRKGQ LKEVKWAGNP YEKFVKEGTE GYLEPRKSFK TWSETVVGKC REWTEEEVET
ASVLCLVYGK FIEVWRQKEA ALQSSQLTRL LLANSAHEVR TPLNAIINYL EIALEGSLDT
ETRENLARSH SASKSLIYVI NDLLDLTKTE EGGSLIKGES FDLSSTIAEA TDMFRNDAKR
KGIGYEVVEH PGLPKVCIGD QRRVRQAISN ITANAIQHTT QGSVKVEVYV AARPSKEHVD
VEVAVSDTGV GMNTKKLDQL FYDLEQVQSE PASMLEEALV PDPKKITEKD DKTALGLGLA
LVARIIKNMD GQLRIRSEEG RGTRFVIQFP FDLPDTENGD EENTESPDES ITPDANTPRL
GPSEGERDRS PNSHSLRPPL TKRNSLDPGE SPRFRSKSLE HLEGRVVPPQ HRSMDTRIAG
EERISFTGQP LRAVRMPDDG GSPLEKTKPG SILGEVQSEP KEMEPAPKKL TAEHMRVLVA
EDDPVNSRIV KKRLEKLGHE VYLTVNGEEC ASAFGDKPRD FDVVLMDMQM PIVDGLTSTK
MIRSYEKTHT DIYSRRAALC GRVPIIAVSA SLIERDRQQY IDAGFDAWIL KPIPFDRLNK
LMGAIVDVKS REECLYKPGQ WERGGWFHTG QKSSEEASTK PSSQAPVSEI SSKAKEAAPS
EDVIANQDGS PDKIDEEHER LLQNQAEGKI EPPKDDDAPP NDESGAPPKD ESEEEPAQEP
AEETSKDEPE EEAPA
//
