ID A0A0L6WBR5_9AGAR Unreviewed; 1725 AA.
AC A0A0L6WBR5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Cyanobacterial phytochrome B {ECO:0000313|EMBL:KNZ73017.1};
GN ORFNames=J132_01402 {ECO:0000313|EMBL:KNZ73017.1};
OS Termitomyces sp. J132.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC Termitomyces.
OX NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ73017.1, ECO:0000313|Proteomes:UP000053712};
RN [1] {ECO:0000313|Proteomes:UP000053712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA Hu H., Poulsen M.;
RT "The genome of Termitomyces.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ412824; KNZ73017.1; -; Genomic_DNA.
DR STRING; 1306850.A0A0L6WBR5; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000053712; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.40.50.1820; alpha/beta hydrolase; 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; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_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; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043150; Phytochrome_PHY_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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; PF00561; Abhydrolase_1; 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; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00022543};
KW Reference proteome {ECO:0000313|Proteomes:UP000053712};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 852..1022
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 1234..1480
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1572..1701
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 417..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1622
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1725 AA; 192063 MW; 1E20C5C83DE2ECE8 CRC64;
MAERYLLERL RFYFALLGGL YAALVVLLTV PFFQSHALYL NAVRLPFFAQ FHMPEKYGLA
PNKTLNLHIK TPDNETLGAW FVLSDQYYQS LSQIPANPDT HVPLAIKRHP TVLFFHGNAA
TRAFRTRVLH YEAYSSRLGT NVLAIDYRGF ADSTGTPSEQ GLVTDARAAW DWLLQQGARE
DNILIVGHSL GTGVTSQLAA QFMSKTLMDE ETPISPFRVF KIFPYIPDLI TRAVVHNFDS
LEVVPRIKGP VLIAHAEDDW DIPYTHSHVL FDAFMKPLLP LVDIPDSLTL TQESWETFSA
ERKVWITKRA EILRTTELQN FGTVTEFEEE GRKVVFLKTL AGGHDYLGIQ EGVQDLIRTV
FNVHRPYYPA ADDSHMTQAH KSSPSASYVY PVKSLLAGHI QPAGVQLPHD KTSLAKACSR
VSTHQSPLPN DSHSMIRSSK SDRDIHNYPD KSQHPTHHRE SSNQSCSPNY SVGEPDLRHS
FSHYSKNNFV SASYLTQSLP NNESHSHPEA IVPSDSGFAE FSAERSSPLN PTDFVYLPPS
NTPLSPDASS NDDPSAAAGL PLLSSVLSTS REVSAPSSPP SSPSFSGSTN LDGCDIASET
EEHVSFRFEH REDGDGNHVI VGREGVLKKC EDEPICTPGS VQAFGVLIAV QEVEDTLVVR
QASENSTELL GLPPRYLFSL SCFTDTLPGS QANLLWENIP DAGDSKDDDD GGPQVFLLSG
WGAPGTEFSG DRRSWTCWCV IHRPTLTNDS SSPTDDMLIM EFELERDLFN PLYPPLRAEG
SPLLESTTVY SKSISALERL RKMTFVPASS AGRTRRSQHR HGVMGSNHLN FGMMDMFAVL
SQINEQLGAV DSLELFLKVV VGVIKDLTQF HRVMVYQFDE SWNGQVVAEL VDWTQTRDLY
KGLHFPASDI PAQARALYTI NLGFTPRPDK VRILYNRSQN TARLVVKSKE DLEVPLNMSH
CYLRAMSPIH IKYLANMGVR ASMSISILAF GSLWGLITCH SYGPHGMRVS FPVRQMLRLL
SQSISRNIER LSYARRLHTR KLINSMVSTR NSTGYIVCNT DDLLGLFDAD SGILVIGGGA
RIIGASHHGQ EILIMAEYLR LKKFNTIQVS QTVSQDFPDL KLTTGLQVIA GLLLVPLSNQ
GTDFIAFLRR GQPREVRWAG KPYKEGHEHE HSLEPRKSFK TWSEIVAGQS RAWTDEQLET
AGVLALVYGK FIEVWRQKES ALQTTKLTEI LLSNASHEVR TPLNHIIKRA PYLEMALDGP
LDSDARENLS RSHAASKSLL FTINDLLVCF LAFLVWLQFI FHKDLTRLES GRQTSFHEPF
DLRNTIDKAT RLYRKEAERR NIQFRLELEK SPGTVVGDAT KIQTVVQNLT ANALKYTTEG
TITVSCAVFG EPEGTRPPNQ TVVDIAVADT GSGMPAQKLE RIFRDLEKVD TLESKASGNA
GLGLGLAVVA RITEQLDGQL RVDSKVGVGS RFSFLVSLAL SSDPISSPLP LSSVGSSGKS
DDLDSFVEAL VGYGGSPPFP QKRIEAGEML PIKAVKVDTF AAEVQTMTRR SQANLAILPF
TKVTTAEHPY LRILIVEDND VNRLILAKRL TLDHHTVVNT TNGQEALDRI QSDREFDVVL
MDLQMPILNG FEATQKIREL ERTSRLLTRP AHQLNGRIPI FAVSASLAEK QHDELVQIGV
DGWILKPIDF RRLAVIMKGV TDADQRARDI YRIGCNWEEG GWLKK
//