ID R9P0T5_PSEHS Unreviewed; 1519 AA.
AC R9P0T5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 28-JUN-2023, entry version 47.
DE SubName: Full=Sensor histidine kinase/response regulator {ECO:0000313|EMBL:GAC94692.1};
GN ORFNames=PHSY_002265 {ECO:0000313|EMBL:GAC94692.1};
OS Pseudozyma hubeiensis (strain SY62) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC94692.1, ECO:0000313|Proteomes:UP000014071};
RN [1] {ECO:0000313|Proteomes:UP000014071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA Konishi M., Hatada Y., Horiuchi J.;
RT "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT mannosylerythritol lipids.";
RL Genome Announc. 1:E0040913-E0040913(2013).
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DR EMBL; DF238785; GAC94692.1; -; Genomic_DNA.
DR RefSeq; XP_012188279.1; XM_012332889.1.
DR STRING; 1305764.R9P0T5; -.
DR GeneID; 24107558; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_50_4_1; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000014071; 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; 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; SM00065; GAF; 1.
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, ECO:0000313|EMBL:GAC94692.1};
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:UP000014071};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 430..592
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 804..1053
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1340..1475
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 28..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1391
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1519 AA; 166344 MW; 858F7FADE1A0C4AA CRC64;
MQATPSSVRS PTVSQPFIYP MRSAVSIKQP KAEVPSSSQP PDPAIPTARI ASRPASADST
KSPPSNPDII HEGRNRPEDV DKDADRAMAQ MKVPGNEDVD LRDHLEQLTT TRFEYVKTDE
GHMILTGRGG KLARCEDEPI HIPGAVQSFG CMVVVRISPD GEMIVRQASE NSIDILGVSP
SYLFSLPTFL DILDEDQADL LWDNIDSLDQ SSQDLAESGP TVFQLRGYNM AGYDERIAQG
SQRSRWNAWC GAHIPDRRND GEGELTVVLE FELVDDLDNP ISTFSPPTTP LDDRDRESGN
GPGLGLAAGW NRPAAAASSG AESPSISIGT LYSSSSSSTS ATARDAGPRR GLEGLAYTPS
QDELRESTHA VHKPLKALSR MRRNAEIKSQ TRSRRPAVLP SAGGGDGTGG MLDLFGILSQ
VNDQLAAQKD LNEFLKVLVG IIRDITLFSR VMIYQFDEAW NGQVVCELVD WNDSHDLYRG
LHFPATDIPA QARALYKINK VRLLYDRDSP TARMVCRDQA DLDFPVDMTH ALIRAMSPIH
IKYLANMGVR SSMSVSITAF GELWGLISLH NYGAHGKRVS FPIRQLLRLI GESVSSNIER
LSYTRRLSAR KLINTLPTDQ NPSGYIISNA EDLLTLFDAD YGVIAVGNEA KILGPLNASQ
EVLAVTEYLR LKKFEHLVTS QDVRRDFPDM VLSTGLHVIA GLLVVPLSGS GVDFIAFLRK
AQLRHVNWAG KPFKEGKEGD AALEPRKSFK VWSETVEGTC RAWKDEELET ASVLCLVYGK
FISVWRQREQ ALHYNQLNRL LLSNASHEVR TPLNHIINYL ELALDSKLDD DTRENLSKSH
IASKSLLFVI NDLLDLTKQE IGNELLLQEP FDLAATVREA VEMHEWEAKR RKIDFSVSTD
PEVCMVLGDK NRVRQVITNT VTNSVKYTRE GQITVTMRKR SDDEREADLP PGCDMEVELV
VGDTGEGIPQ EKLEVIFREF EQVESVIAQP GRQDALEPEG SESSLVRTEP SDGGLGLGLA
IVARVVKNLG GQLRVDSQVG EGTTFTYYIP FCSAETTTPT EMPAVAGSGA SGTKRSSDTV
SMRRSASIGS GSASSAGKSE IDSLVEAIQQ PVLRDQGVIE DATQQRRNAD GTSPIYNGPR
NVAAGPRPGI ASQRTRSFDS GSHFVEGSGI PVRSVKIDPQ ALDVNDRADR RPPATSAFMS
SATTHARPAR SSHTSDAESF KAEVEQRARE NVPTLDQDTF RLNAGKLRSG QSGAAATTTA
AYDNESSDSP VSPRTVAKDD ASASHTEATT PESDDTQNAN HKEARRGSSS STAARRRMAV
MRGLHKAPGG RSGEKIAPLR VLVVEDDPIN RMILKKRLSI DGHTTLLAVN GEEGVRQFEQ
DAKEIDVILM DLQMPICNGQ EACIRIRELE RKWAEAGERA DRPASQVLNG RVPILAVSAT
LVPQMRQEMV DIGMDGWLLK PIDFARLGAL LKGLLHPEDR AANHWRQGYV WEKGGWLSEP
AQRDVVVAVG GQEVSEPSA
//
