ID A0A3N4JQJ1_9PEZI Unreviewed; 1232 AA.
AC A0A3N4JQJ1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 13-SEP-2023, entry version 20.
DE RecName: Full=Cyanobacterial phytochrome B {ECO:0008006|Google:ProtNLM};
GN ORFNames=L873DRAFT_1679861 {ECO:0000313|EMBL:RPB00553.1};
OS Choiromyces venosus 120613-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Choiromyces.
OX NCBI_TaxID=1336337 {ECO:0000313|EMBL:RPB00553.1, ECO:0000313|Proteomes:UP000276215};
RN [1] {ECO:0000313|EMBL:RPB00553.1, ECO:0000313|Proteomes:UP000276215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=120613-1 {ECO:0000313|EMBL:RPB00553.1,
RC ECO:0000313|Proteomes:UP000276215};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(2018).
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DR EMBL; ML120379; RPB00553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4JQJ1; -.
DR STRING; 1336337.A0A3N4JQJ1; -.
DR Proteomes; UP000276215; 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; 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; 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; 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|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:UP000276215};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 255..417
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 631..875
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1048..1179
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1099
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1232 AA; 136962 MW; 63D819A74DD5E3A0 CRC64;
MFRSASESPD KGSGDGISPG GSDEGYVTAR FKHMVTDEGH MVVTGVSGSE RIQRCEDEPI
HIPGAVQGFG VLIALKEDVE GRLEVKIASE NSKQIIGYSP AALFALESFC NILSEEQAEN
LYEHLDFVRE YVSDPVQSGP DVFPLAITSP NSTEIKLWCA IHIAEKNPDL LICEFELKDD
HIYPLFSPTE EETPLPPEDT LNSNPSEQDL LESTLSASRP LRVLRHARKR KGQAAAMEAF
NLMSQIQEQL SSAPTLGVFF KVVVGIVKEL TGFHRVMIYQ FDEVWNGRVV TELVDPRATK
DLYKGLHFPA SDIPKQARDL YLLNKVRLLY DRDQMTARLI CKSKEYLDDP LDMTHSYLRA
ISPIHIKYLK NMAVRASMSI SLTAFDELWG LISCHSYGQK GMRVSFPIRK MCRLIGETAS
RNIERLSYAS RLQARKLINT VPIEQNPSSY IIASSDDLLK LFDADFGLLS IREETKVLGK
LEHSQESLAM LEYLRVRKFT SVLTSQNLSV DFPDFNYEPG LTIIAGLLLV PLSVGGQDFI
VFFRKGQLWK VNWGGNPYEK NLKEGTERYL EPRKSFKTWS ETVVGKCRDW TEEQIETAAV
LCLVYGKFIE VWRKKEAALQ TSQLTRLLLA NASHEVRTPL NAIINYLEIA LESPLDNETR
DNLMRSHSAS KSLIYVINDL LDLTRTEEGK NLIMQEAFDL PETVREATER YKSDAERKNI
TFEVEYEGLP RFVKGDQARL RQAVSNIAGN AVKHTSEGGV KVEIWMPHGP DGQCQIEIAV
QDTGVGMSSE KLEALFREFE QVQTEEDAMD RQEAIGNESP PRSSFNAVSR IPGQKILGLG
LAVVARIVRN MNGQLRLKSE QGKGSRFTIS LPLSLAPEAE LDSERKKKVA ERQKSPSPQP
SSVTPTPSEV SLIDSQGRGS RDMARRNSGA SMNNLGLFSS AKSGGSEIDR LVHAISSPHL
STASSNPPAR PNAGTRTKSF SNAMGLVAPQ QQPGQEIIEG SIAPLKTVRV PGGNSDPISP
PAVDTAPPMQ LPPIVDSNSP TEPSGKFEVL VAEDDPINSK IIKKRLEKMG HGVVLTVNGE
ECADLFFKQG QNYDIVLMDM QMPIMDGGTS TTRIRQFEGA DSDRRIPKRH RINGRVPIFA
VSATLVEERR TEYIDFGFDG WILKPVDFKR LKLLLDGIRD PAIRAKNAYE PGHWEQGGWF
SQTPGGAKPS PPKHEDISSA ALKTEGKDPD GI
//
