ID A0A2T2PBQ4_CORCC Unreviewed; 1525 AA.
AC A0A2T2PBQ4;
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=Phytochrome-like histidine kinase PHY1p {ECO:0008006|Google:ProtNLM};
GN ORFNames=BS50DRAFT_32393 {ECO:0000313|EMBL:PSN75080.1};
OS Corynespora cassiicola Philippines.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Corynesporascaceae; Corynespora.
OX NCBI_TaxID=1448308 {ECO:0000313|EMBL:PSN75080.1, ECO:0000313|Proteomes:UP000240883};
RN [1] {ECO:0000313|EMBL:PSN75080.1, ECO:0000313|Proteomes:UP000240883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philippines {ECO:0000313|EMBL:PSN75080.1,
RC ECO:0000313|Proteomes:UP000240883};
RX PubMed=29551995; DOI=10.3389/fmicb.2018.00276;
RA Lopez D., Ribeiro S., Label P., Fumanal B., Venisse J.S., Kohler A.,
RA de Oliveira R.R., Labutti K., Lipzen A., Lail K., Bauer D., Ohm R.A.,
RA Barry K.W., Spatafora J., Grigoriev I.V., Martin F.M., Pujade-Renaud V.;
RT "Genome-Wide Analysis of Corynespora cassiicola Leaf Fall Disease Putative
RT Effectors.";
RL Front. Microbiol. 9:276-276(2018).
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DR EMBL; KZ678128; PSN75080.1; -; Genomic_DNA.
DR STRING; 1448308.A0A2T2PBQ4; -.
DR Proteomes; UP000240883; 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:UP000240883};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 460..622
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 836..1075
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1296..1426
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1448..1476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1347
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1525 AA; 168004 MW; 19E5CAC2698368D4 CRC64;
MSQPPRSPDL DPSADRPHDV PSAPLSPSSP IPVHQPWSSP ADSATKQPGS SPPQASSAAM
SPGGDGIGTL SPSANDRVFP IRSVVSVDPT PTPTQRGTAD YFHPYGRPID SRIPTETRRP
SQGSSASQSS QTSQRGLTHR HSMSATPKAE QASEARRGSI WLPQRSETSR AMAPPQLPSH
IFNDINSTKS AESGDPNPSP SISQPHDAAA SLSGGASIRS GVSSMGDAGL LVTHRFKHVV
TEGGHAVITG RDGDTLQRCE DEPIHIPGAV QGFGLLIALH EDPGGSGSLP VHIVSENSRR
IIGRSPRELF ALESFTDILS EEQADNLLDH IDFIKDEDAD VATNGPEVFT MSIKVPNARS
RKLWCAVHIN DRNPGMIICE FELEDDQLYP LVPPNDLTPD LPADTLDSNP TAEEFLESTE
IKSRPLRVLR SARKRKGEAA AMEVFNIMSQ VQEQLADAPN LEKFLKVLVG VVKELTGFHR
VMVYQFDQAF NGRVVTEVVD PRATKDLYKG LNFPASDIPK QARDLYKLNR VRMLYDRDQE
TARLVCRTSE DLEAPLDLTH SYLRAMSPIH LKYLANMAVR SSMSISINAF GELWGLIACH
SYGPRGMRVS FPIRKMCRLV GDSASRNIER LSYASRLQAR KLINTVPTEH NPSGYIIASS
DDLLKLFDAD FGLLSIRDET KILGQLEQSQ EALAMLEYFR MRKIQSVMTS QDVTQDFPDL
RYPPGFQVIA GMLIVPLSVG GSDFIVFFRR GQLKEVKWAG NPYEKFVKEG TEGYLEPRKS
FKVWSETVVG RCREWTEEEI ETAAVLCLVY GKFIEVWRQK EAALQSSQLT RLLLANSAHE
VRTPLNAIIN YLEIALEGSL DTETRENLAK SHSASKSLIY VINDLLDLTK TEEGVPLIKG
ETFDLKSTLK EATDLFLGDA KRKNISYEVV EHSGIPQKCI GDQRRVRQAV SNITANAIQN
TTQGGVKVEM YVASRSEPDH IDIEVAVTDT GVGMSTKKMD QLFNDLEQVQ TESATMLEDA
IVPNPQQSLD KDEKTTLGLG LAVVARIIRN MNGQMRLKSE EGKGSRFVIQ LPFELPDTEI
QESSEASPSE ESSTPQADTP SPGQAEGERT LVAPSLSRGD SGGNIITNKV MRRESAESLR
SKRSLSSFKS GNSSIKSQRS DVDRLIEAIQ EPHLVERPSS ERSTSARSMR PTLTKRNSLD
QSLPTSPPRA RSKSLELIDA QQGSLPSHQR SLDSKMQVPG EEHILASGTP LRALKIPEGP
GSPSELPQHR TGSILGEVYS EPEQIPQEPL TADNMRVLVA EDDPVNSRII KKRLEKIGHK
VHLTVNGEEC ASAFGDQPRD FDVVLMDMQM PIVDGLTSAK MIRSFEKTHT DIYSPRAALC
GRVPIIAVSA SLLERSRKEY INAGFDAWIL KPISFDRLSQ LMKAIVDRNV RESCVYKPGE
WERGGWFHSG QKTSNDASNT PFDQSPQLTP SSAVEEAAQS DEPVAGDEAG DIPDEQERLL
QEQDKGKGKR VHYQGDEPPD EPSET
//
