ID X0CWC4_FUSOX Unreviewed; 1499 AA.
AC X0CWC4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 13-SEP-2023, entry version 41.
DE RecName: Full=Cyanobacterial phytochrome B {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOQG_01375 {ECO:0000313|EMBL:EXK98471.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK98471.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK98471.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK98471.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; JH658363; EXK98471.1; -; Genomic_DNA.
DR HOGENOM; CLU_000445_50_4_1; -.
DR Proteomes; UP000030663; 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};
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:UP000030663};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 466..628
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 842..1074
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1298..1429
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1349
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1499 AA; 165030 MW; FA1773C807E75DC2 CRC64;
MDAPHEKDDQ DVNQAQPEQQ GQLEQEQQEQ EHDPSSASLP TYTSYPPPPQ SSTASSSTFR
PMGQDLPNLR TSPSDATPTR TTRAVSSAAP SEQNSIANSD PPFSPWSVGS DKQLGYHSAA
SDISGDRVFP IRSVISVDPN PNLRRSDTVP ANYHSRAHSE RIDALMRRKN TMSGPMSSIQ
LDANRHGSST TPLQLDISTS DNETETEESG PMGHSAPAAA ASGHEPDVSS AGQSSADVPL
VTSRFTHVVT DDGHAVITGR DGILQRCEDE PIHTPGAIQT FGALVALREE NDGCFVARYI
SENSERMLGY TPKQLFQLKN FLDILTEEQQ DNLLDHIDFI RDEDADPAVN GPEVFSLSIR
SPKRKSTKLW CAIHINPAHP DLIICEFELD DDAEYPLRPV DELTPDTPHD TLQSNPTLEE
IEDSTEVLSK PLRILRSARK RRGEQGAMQV FDIMSQVQEQ LSSAPNLEAF LKILVGIVKE
LTGFHRVMIY QFDSSFNGKV VTELVDTSMT RDLYKGLHFP ASDIPRQARD LYKLNKVRLL
YDRDQDTSRI VCRTKEDLDV PLDMSHSYLR AMSPIHIKYL KNMAVRSSMS ISINAFNELW
GLISCHSYGN HGMRVSFPIR KMCRLVGDTA SRNIERLSYA SRLQARKLIN TAPTDKNPSG
YIIASSEDLL KLFDADFGLL SIKGETKIMG LVEQSQEALA MLEYLRMRQL TSVVASQDVK
EDFPDLRYPP GFQVVAGLLY VPLSVGGNDF IVFFRKGQIK EVKWAGNPYE KFVREGTAGY
LEPRKSFKTW HETVVGKCRE WNEEQVETAA VLCLVYGKFI EVWRQKEMAL QNSKLTRLLL
ANSAHEVRTP LNAIINYLEI ALEGSLDQET RDNLARSHSA SKSLIYVIND LLDLTKTEEG
QNLVKDEVFD LASCIREATG PFLNDAKRKG IHYTVVQHPG LPRFVHGDER RIRQALSNVT
ANAVAHTHSG HVKVEVFVSE VKDRQAVVDF VIEDSGIGMS ASQLDTLFRD LEQVSSEEAP
MSGTKLEEMP REMRTLGLGL AVVARIVRNM DGQLRLKSEV GQGSRFVVQL PFLLSNECPS
SQGNENVPTS GSTNKSTNSA DSANTATSAP LSLTAAPEGE ITLVDRVSSM TSAVEGGDAS
MKQGSRASQR SMSSCGSHGS HQSDADRLID AISTPLSLND KEGGEYPLPG SVNSGGGSMR
PTSRGAISLS GRSVSPPRSP VATKPHSEPG SAGVVDSKTP IRAVKIPDEY SDMPQRPQPS
EHSRVLFEMK GNDRPVTKAA TESVTSGGTQ MTETQHLEVL VAEDDPINMK ILRKRLERVG
HGVHHTVNGE DCAAAYRERS KEFDVVLMDM QMPIVDGLTS TKMIRSMEAS VEHQGHSSLA
NSNYRIPIFA VSASLVEREK QTYVDAGFDG WILKPIDFKR LNTLLAGISD EEVRKSCLYE
PGQWERGGWF VPRASLGGSV TSDETTPKAE HDAKDKDIGN TVAAEAQAEG DAVEPTPST
//
