ID A0A0F7ZTI7_9HYPO Unreviewed; 1463 AA.
AC A0A0F7ZTI7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 36.
DE RecName: Full=Cyanobacterial phytochrome B {ECO:0008006|Google:ProtNLM};
GN ORFNames=HIM_07380 {ECO:0000313|EMBL:KJZ73183.1};
OS Hirsutella minnesotensis 3608.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ73183.1, ECO:0000313|Proteomes:UP000054481};
RN [1] {ECO:0000313|EMBL:KJZ73183.1, ECO:0000313|Proteomes:UP000054481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3608 {ECO:0000313|EMBL:KJZ73183.1,
RC ECO:0000313|Proteomes:UP000054481};
RX PubMed=25359922; DOI=10.1093/gbe/evu241;
RA Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA Bushley K.E., Xiang M., Liu X.;
RT "Comparative genomics and transcriptomics analyses reveal divergent
RT lifestyle features of nematode endoparasitic fungus Hirsutella
RT minnesotensis.";
RL Genome Biol. Evol. 6:3077-3093(2014).
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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DR EMBL; KQ030537; KJZ73183.1; -; Genomic_DNA.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000054481; 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; IPR000014; PAS.
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; PS50112; PAS; 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:UP000054481};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 288..342
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 465..627
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 841..1074
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1287..1418
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1338
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1463 AA; 160969 MW; 15F33F61334E8B0C CRC64;
MNESQDSRPS SAHPSSHSGS DNEGSLGARA TPRAAQSSLP HHMRQASSSP PATDGPHPIT
ASPGHFSSCS LGSDKHTGPH SAASDMSADR VFPIRSVITV DPFHRANVPP TEDYFMSPSD
SESRAIPIHR LSVSRQETLQ SESRRGDTLS PSSNSVSASD YVASARQKRA MSGPFSSIQA
DAARQGTVGP LNLAIATSDE GSDASDHQPG EQRSPPGVPN RRSTSAHAEH QSLPDIAHVT
TRFTHVETSD GHSVITGRDG VLQQCEDEPI HTPGAVQGFG VLLAMREESD GSFGVRYVSE
NSEKILGYSP QQLFRLKNFM DILTEEQQDN LLDHIDFIRD EDADPAVNGP EVLSISIRRP
KKRKSVKLWC ALHTNPAHPD LIICEFELDD DTDYPLRPAD ELTPDIPHDT LHSNPTLEEI
EESTEILSKP LRILRSARKR RGEQGAMQVF DIMSQIQDQL ASAANLETFL KILVGIVKEL
TGFHRVMIYQ FDSSFNGKVV TELVDTSQTL DLYMGLHFPA SDIPRQARDL YRINKVRLLY
DRDLETARIV CRAQEDLDVP LDMTHAYLRA MSPIHLKYLG NMAVRSSMSI SINAFNELWG
LLACHSYGPH GMRVSFPIRK MCRLVGDTAS RNIERLSYAS RLQARKLINT ASTDQNPSGY
IIASSDDLLK LFDADFGLLS IKGETKILGS MEQSQEALAM LEYLRMRSLT SVLTSQDVKE
DFPDLRYPPG FQVIAGLLYV PLSVGGSDFI VFFRKGQVKE VKWAGNPYEK TIRHGTEGYL
EPRSSFKAWR ETVIGKCREW NEEQVETAAV LCLVYGKFIE VWRQKEAALQ SSKLTRLLLA
NSAHEVRTPL NAIINYLEIA LEGSLDQETR ENLARSHSAS KSLICVINDL LDLTKTEEGQ
NLVKDEIFDL TVCIQEATDP FHNDAKRKGI AYEVTQHPGL PQFVHGDGRR VRQVISNITA
NAVAHTDTGS VCVEMFVSEV KERQAVVDIV VADSGIGMSP RQLDALFREL EQVSSEEPEP
NASSNPEDKP QTARTLGLGL AVVGRIVRNM DGQLRLKSEE GQGSRFVVQL PFHLPDESPG
EDSLQAGSLL SKSSNPVAAP ESLSAPPVGE IMLIDRGSSL NLVSDADKPG MEDGSMSSSH
RSVGSLGSHG SHQSDAERLI NAIQTPLSLN EQAGYFTKRP DSKDGSNRAP SRTSASINTL
SVSPQSRKFL LSSPRAPPPE PGTTEVRDSK TPIRAIKVPE DFQEMPPQPQ HDEGSRVLFE
VSSDHGSKTA TAQGAGECQK PDTSSLRTLV AEDDPINMKI LSKRLERAGH EVRHAVNGED
CASLYKENSS SFDVILMDMQ MPIVDGLTST KMIRSAERSS EHHGYSKLAA LNGRVPIFAV
SASLVEKEKQ TYVDAGFDGW ILKPIDFKRL ATLLQGIYDD ETRYKSLYVA GEWERGGWFA
AREGPDGMWS DEITPRAEKS SGT
//
