ID A0A2X0PCL8_9BASI Unreviewed; 1459 AA.
AC A0A2X0PCL8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=BQ5605_C005g03357 protein {ECO:0000313|EMBL:SGY74350.1};
GN Name=BQ5605_C005g03357 {ECO:0000313|EMBL:SGY74350.1};
GN ORFNames=BQ5605_C005G03357 {ECO:0000313|EMBL:SGY74350.1};
OS Microbotryum silenes-dioicae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=796604 {ECO:0000313|EMBL:SGY74350.1, ECO:0000313|Proteomes:UP000249464};
RN [1] {ECO:0000313|EMBL:SGY74350.1, ECO:0000313|Proteomes:UP000249464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FQNC01000047; SGY74350.1; -; Genomic_DNA.
DR STRING; 796604.A0A2X0PCL8; -.
DR Proteomes; UP000249464; 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:UP000249464};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 409..571
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 786..1025
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1284..1416
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1334
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1459 AA; 159799 MW; EB8A5BBF3F607C34 CRC64;
MSNESIQTIQ GIKSGQRQRP DSIALPARDD FALTSPLSPP ASTTSSGGAS SVDRPGGALP
SSRLFPMRNV MHYHSSKGKE RAAPMSPGSP PSSGYPIMSP AFSRASGTSA LTSSIEPFTF
HASAMPTTRK LASRPETPGT ASSAPTVPSE GAQSDIPLLM TARFEHSVAP DGSHHVLTGR
DGVMERCEDE PIWLPGAIQA FGVLIAFEEQ PDGKLRVQQV SENSNFILGM RPNDFFCTQC
LTSLLDPEEA DALRDALEAL DDRDADSANL YEGPINFQLS GTGRPGSAAA DAQDSSRLEW
SCHAALHRPD RVNRPKMAVL ELELMDDTVN PLTTESTEPA LHEEKGGMET DQPFEPTEED
LQESTVSLVK PLRSLARMKR QRRAKRSQAD VDVVTLLSNI NNQLSKAEDL NVFLRITAGV
FKELTEFDRA MVYQFDEKWN GRVVAEQVDW SRTKDLFRGL NFPASDIPAQ ARELYRVNKV
RLLYDRDQPT ARLCCRDVSE VDNPLDMTHC HLRAMSPIHI KYLGNMGVRS SMSISITAFG
DLWGLVALHT YGRYGHRVSF PVRQLCKLLG SSISRNIERL SYAKRLHARK LINTAPSEAN
PSGYILAKSE DLLLLFDADF GVLSIGDEAK ILGSVVNSQE LLAVLEYLRV KQFTTMQHSQ
DIRADYNDID YPGPFEMIAG LLAVPLSSEG RDFIVFFRRG QLQEVKWAGN PYANKTEDGD
VGQRLEPRKS FKTWSEVVLG KCRAWTDEQM ETAGVLCLVY GKFITVWREK ESALKTSQLN
SLLLANASHE VRTPLNAIIN YLELALDSEV TGEVRENLTR SHAASRSLIH VINDLLDLTR
TERGQDLYLQ DPFNLSTTLE DALSVHRAEA KRRGITLDVV ETPQGTPTNL LGDRGKIRTI
VSNIVGNAVK HTKSSGSVTV EWGEMTDVDL EDAMDKKTDS IRIGLSMIDT GVGISESRLE
SLFREFEQVS TVGDDQGGEV ASSGGTVGLG LAVVARIIRN LGGQLRVESK EGEGSKFMVI
IPFRLPQQPI SPPSSSTMDD DTSAASSRTM SIANGHRSMT RSNSTGSAGS KNSDIDSIIS
AMSSSHISPG AARHMTSGNQ RMLQAKTSRA SNPSTSNRSN RSEGSMRSNR SYNSTGTVGS
KARSNGSIEI DSSNVALRAI RVPPLMRSAQ ELNSPDGDQE RTIVRRGSLT RTGSRSGVLA
SSEEHRGEIN AAPATTKRIT NNRAAIASPT SSTRMDFADA IAKQDGAVET GDASLQPLIE
SPIHVSQYKA SPPAVQEDNV PSMRVLVVED ELVNRMILQK RLTKDGHDVV VVEHGGDAVR
LFKEDRQFDC ILMDLQMPIM GGLEATRQIR RIEHDEPVSL AQQRPSSILN GQIPILAVSA
SLPERERPLI VEAGMDGWCL KPVDVKRLRK LMRGAIDVAV RSEDVYQAGS FEKGGWNFEA
PSHRPSKPDV ADWVQNLSK
//
