ID A0A0B1P8X5_UNCNE Unreviewed; 1286 AA.
AC A0A0B1P8X5;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Putative cyanobacterial phytochrome b {ECO:0000313|EMBL:KHJ33386.1};
GN ORFNames=EV44_g3073 {ECO:0000313|EMBL:KHJ33386.1};
OS Uncinula necator (Grape powdery mildew).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=52586 {ECO:0000313|EMBL:KHJ33386.1, ECO:0000313|Proteomes:UP000030854};
RN [1] {ECO:0000313|EMBL:KHJ33386.1, ECO:0000313|Proteomes:UP000030854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=c {ECO:0000313|Proteomes:UP000030854};
RX PubMed=25487071;
RA Jones L., Riaz S., Morales-Cruz A., Amrine K.C., McGuire B., Gubler W.D.,
RA Walker M.A., Cantu D.;
RT "Adaptive genomic structural variation in the grape powdery mildew
RT pathogen, Erysiphe necator.";
RL BMC Genomics 15:1081-1081(2014).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHJ33386.1}.
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DR EMBL; JNVN01001472; KHJ33386.1; -; Genomic_DNA.
DR STRING; 52586.A0A0B1P8X5; -.
DR HOGENOM; CLU_000445_50_4_1; -.
DR OMA; WVMKPIN; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000030854; 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:UP000030854};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 337..499
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 713..950
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1128..1259
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 954..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1179
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1286 AA; 146106 MW; 4DEEB1FEE23B2A6A CRC64;
MQNETDPSNE KNTLSKSASK LLESLEISRP FTDDSFPARP KLDFPQRLSD TQEELSLEKI
NPTKFIGHQA SFGPCLDGTE SQISAKLYKN LGIQYEQLES KPSEANSEAF GFRASRFEHV
ITEDGHAVIT RGELLRCEDE PIHAPEAIQS FGALIALKES QSRKLMILIV SENSNEIIGY
SPQELFQLDC FTDILAEQNV DILMDRIKLT RNADITDYGP EVFTLSIKQP SIKRDESQVL
WCALHVNPTQ PDLIICEFEL EHDFQNPLIP ENNVLLEVPE DMFNNNISES EYAESTIPIN
RPLRINNISH KRQGEPSTTD MFNTVSQVLE QLAAAPDSDT FCRILAGIVK ELTGFHRVMI
YQFDASYNGR VVSEVLDPHV SRQCNLYFLL RTSDIPPQAR RLYQVNKVVV LYDRENVTSR
LIYRSRADFK NSLDLSYSYL RAISPIHIKY LNNMAVRSSM SMSINSLNHL WGLIACHAYG
SKGTRVSFPM RQMFRIVGNA ASRNVERLFC VSHLHTRKLF NTNATKKDTS EFVFASTDDL
LKIFSAEFGL LSIQGVNKII GSCKKQQEAF TVQKYFETRK VTSIISSQDI RSDFPDLKCP
TGFEVITGLL VLPLSASGND FLLFFRKEQV LEVKWAGNPY DKITQHFDID QISPRRSFKV
WKEKVIGKSR EWNDEQIEAA VTLCSMYWKF IEVWRQNEEI LPKNQLTKLL LANSAHELRT
PLNAIINYLE IAMEAPLDQE TRHNLGQSCY ASKSLIYVIN DLLDLTKAEQ GHELVRDEIF
DLHATVEEAM LCFKGDALRK GLNYQVDFKS EVPQFVIGDQ RRLRQAIFNL IANSMQFTTH
GFVWIQVLLK SDIIGGARIE IMIEDSGCGI SDQEIEEMFR DLDNVIIELN VPDENRKLFG
NFLPSRSENQ KLGLGLATVL RIVRIMNGKL RIKSEKGKGS RFIIEVDFNL PGFTNTQKSH
REQSSGSHSA SILKPTEMKK IVPHDYKNSP LAQSYILTSN SENINRNQSD SSQEKDYNNL
LEKKNEKNLA LKNIKVPDKD VPEFMRLNNN KKTTRGLDEN PFDMSNNINS QSPDLGIIKN
PLPDKAAHSS ITRIIDSHSN ESSNTSLEKL GFAIRKEVSP REGIGNLQVL LAEDDFVNCK
IIHKRLGKSG HKVHQTVNGG ECAKVYAEKK DLFDVILMDI QMPIVDGMKS TKMIRSFENN
DPKNVLSKHA RSNGRVPILA VSASLCEDKR QIYIDTGFDG WIMKPIDFKR LNTLLRGISE
TSIRDSCLYS PGKWEKGGWF GSRQTN
//
