ID A0A0L0VDW6_9BASI Unreviewed; 1552 AA.
AC A0A0L0VDW6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KNE97453.1};
GN ORFNames=PSTG_09286 {ECO:0000313|EMBL:KNE97453.1};
OS Puccinia striiformis f. sp. tritici PST-78.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=1165861 {ECO:0000313|EMBL:KNE97453.1, ECO:0000313|Proteomes:UP000054564};
RN [1] {ECO:0000313|Proteomes:UP000054564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race PST-78 {ECO:0000313|Proteomes:UP000054564};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Hulbert S., Chen X., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Puccinia striiformis f. sp. tritici PST-78.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:KNE97453.1}.
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DR EMBL; AJIL01000068; KNE97453.1; -; Genomic_DNA.
DR STRING; 1165861.A0A0L0VDW6; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000054564; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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); 2.
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}; Membrane {ECO:0000256|SAM:Phobius};
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:UP000054564};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1522..1544
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 433..595
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 812..1051
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1331..1495
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 23..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1408..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1250..1265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1408..1442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1382
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1552 AA; 171701 MW; 8D6AD21FA580AA17 CRC64;
MGAPTTPSRR NAGLPTIVER LSSLGSQQDQ CQENVGLGRT GVGSVTGTSH SPTDTDLGPI
GQLFPNSRPE PGRLQNPVTN LNETNRLGVH PHRTPSNTRS DTQADPSAIE EPISVAAKSQ
PTSSLAGQAT VSDLSQSSSP PNLSDPDAYI TTRFEYQQVE DGILIFTGRK GEFTACEDEP
IRTPGAIQGF GVLMAVIVHG ESRPTTRPHS RCDPYDPCNG ISPSPSTPHS ATQETDQAET
EDSGRLEIVQ VSENSRQILG LSPKLLLNLH SFTEVLTPDQ SQQLHGNIEV CFDSESTSAT
GPHTFRLSGR GEIGTGTDGP SSYTEWSCWC AAHRPDPILR PRLMIVEFEL ENDELNPPLI
ISVDPVDADE RGGLDGKPYE PTEQDLIEST TSINQPLRAL ARIRKKGKDF SGDSVEVLSI
MSQLNNQFDK AEDMPTFLKT LVGLVRELTG FDRVMIYKFD ESWNGQVVAE LVDWKRTRDL
YRGLRFPASD IPPQARELYK INKVRMLYDR DQPTARLMCK TQEELAQPLN MTHCHLRAMS
PIHIKYLANV GVRSSFSISI IMNDELWGLI SCHSYGRFGQ RVTFPTRQFC TILGDSVCRN
ILRLNLSQRL QSRKLINTTS TPKNPSGYII AKAEDFLWLF DAQSGVLSIG DEAKILGAVP
NSEEILAILE YFRVKIFDTL QVSTDINQTF PDIDYPGGIE SISGVLVIPL SRGGQDFICF
FRPAESKEIH WAGNPYQKTH SKDDSSHSHN LEPRKSFKIW SETVKGRSKA WTDEQLETGA
VVNLVYGKFI DVWRQKEAVI LDTQLQALLL GNASHEVRTP LHQILSTLEL ALDGHLDKET
RDNLSKSYSA SKSLVHVIND LLDLAKTEHG RDLFSRNPFN LPLALEEAIP IYRREAKRKG
LAFKMVESPL GSPRILEGDR ARLRQVVSNL VGNAVKHTTE GHVRVQWGLV PEDEVVQHCA
EDRPLGPDDI IRISIAVTDT GKGIAKAQLQ NIFRAFKQGG PREPLYDRTS GSIGLGLAVV
GRVVHNMGGQ LKVDSTVNQG STFTIILPFV VPKNHTSGAN NSEDSAHINP IGWRSWRGNR
IGAVSSSRGS QGSSCGSIGA FGSGVDRMME ALSFGSSVGS SSDDHYPLSS TSSFHRKSFS
TRRRMSISSG STASTKGNGS IYSLRSNTGA QMSHRRISSA PNHTLYNEQP SRSRHHPEAQ
RKLVQLAPPP SDGPSKPEGM ITPKEDVLSE EMTRPEAVEP LQQTPTDRSI NRKNSKKDEK
TVSSKLERPT IPATNEAGQP GQSTLTLDNL LSHGVQEANK SSPFGPSNHL QHISDYQKPT
HNRLVAQQPM RVMVVEDDPI NRMILKKRLT SSGHSVSLTV HGQDAFELFE RDPSQHDIIL
MDLQMPICDG MQATRMIRAF EKASSNRLAK TDYQKDDDGE NKKKEHYSQA TEEEDKTATR
HSPKSHLINL GVPIIAVSAS LHERQLHEIL EAGMDGWIPK PVDFTRLATM MIASLDLSTR
AELIYQLSFA FDFQFPLVSR LLSIRLCTLT FLLSFPSLWS ILCYSSNIVN YL
//
