ID A0A0F4GXS0_9PEZI Unreviewed; 1585 AA.
AC A0A0F4GXS0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 28-JUN-2023, entry version 34.
DE SubName: Full=Putative phytochrome-like histidine kinase phy1p protein {ECO:0000313|EMBL:KJY00986.1};
GN ORFNames=TI39_contig306g00008 {ECO:0000313|EMBL:KJY00986.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJY00986.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJY00986.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJY00986.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-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:KJY00986.1}.
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DR EMBL; LAFY01000298; KJY00986.1; -; Genomic_DNA.
DR STRING; 1047168.A0A0F4GXS0; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000033647; 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, ECO:0000313|EMBL:KJY00986.1};
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:UP000033647};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 448..610
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 824..1066
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1353..1488
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1512..1532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1555..1585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1404
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1585 AA; 174482 MW; E0EAB13B2B355924 CRC64;
MSEQERSDHK DIDPSSDVVA PKDQSPTRVR PNLVQEPFQR FNQDNRSRPA PISTDEQLSP
EAADRVYPIR SVVSMDPNPT PGARGERHEY FGSASNARRT STNAGIEHVT TPGRARQGSA
DRIASPRTSG DHPPSQRTDR QASTSTTSST PRTPQPPTPA GTRQQPHVFS DMMTGDGGSD
TQSQKSGQSQ AQSDGPSDRP APIRSTSIKS GTTSLDEVGP HVTARFKHVV SEGGHAIITG
RDGDTLQRCE DEPIHIPGAV QGFGLLIALE EQQEGKLIVR VVSENCKRLI GYSPMQLFAL
ESFTDILSEE QADNLLDHVD FIRDEDADVV VNGPEVFTLS IRSPQKKNQK FWCAMHINEA
NPDLVICEFE LEDDQLNPLQ APNDSTPEPP EDTLNSQPTE EELVESTHNT SKPLRVLRSA
RKRKGEAAAM EVFNIMSQVQ EQLAAAPTLE SFLKILVGVI KELTGFHRVM IYQFDHSWNG
RVVTELIDPR ATKDLYKGLN FPASDIPKQA RELYKVNKVR MLYDRDQETA RLVCRTVEDL
ETPLDLTYSY LRAMSPIHLK YLANMAVRSS MSISINAFDE LWGLIACHTY GPRGMRVSFP
IRKMCRLVGD SASRNIERLS YASRLQARKL INTVPTQANP SGYIIASSED LLKLFDADFG
LLSIHGETKI MGNVEHTQEA LAMLEYLRMR CITNVMTSQD IAGDFPDLRY TPGFTEIAGL
LLVPLSAGGQ DFIVFFRRGQ LREVKWAGNP YEKFIKEGTE GYLEPRKSFK TWSETVVGKC
REWSEEEIET AAVLCLVYGK FIEVWRQKEA ALQNSQLTKL LLANSAHEVR TPLNAIINYL
EIAMEGSLDQ ETRENLTKSH SASKSLIYVI NDLLDLTKTE EGGELVKDEV FDLGATLFEA
TDVFKGDARR KNITYNVQDL SGLTSPVIGD QRRVRQAISN VTANAIQNTV EGGVTIEMHV
ASRESPEHVD VEISVADTGC GMNSKKLDAL FRDLEQVQME SDQLLTSADP DSKSLRSENS
KSGEGRTLGL GLAVVARIIR NMNGQLRLKS EEGKGSRFVI QFPFDLPEPE EGQKRIDEGT
SSVGSATPMN EQTSSLNTSG QGSGSGSGSS ATATVTTPPT GDTEGMMTLI ERSSSGTLPA
RRNSAEVQGG GASIRLSRKS SSDSFQSKKS LNSMLSARSA MSKSSNRSAM SEADRLIEAI
QEPHRVEGWQ DGSVNRSTSR GNTMSARPML SKRHSTAGSG GNLITSPLKH RPRSIEVAPV
PDHMRSQKLA TTDRPSTPSR KPGQSTVTDQ GTPVRSIRIP DYAGLDSPKD DGFRSPASHE
RALLSTTLLE EPPSAIASPK DGESPRLDTH HMRVLVAEDD PVNSRIIKKR LEKLGHEVVL
TVNGEECSSM YCDDPGQFDI VLMDMQMPIV DGLTSAKMIR SFETTHPTPS PTPLLSPRAA
LNGRLPVIAV SASLEERNLQ TYIRTGFDGW ILKPISFPRL SEIMEGIVDP QVRRENLYRA
GGWERGGWFE EGKKAEERRE DVVGDKVDLK PSEKPPVSTP SEGVKIAAVS DGPAGKEEHA
SEQSREQERL LAVQKEGREE GGKEG
//
