ID T0LUH8_COLGC Unreviewed; 1497 AA.
AC T0LUH8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Hsp90-like protein {ECO:0000313|EMBL:EQB55416.1};
GN ORFNames=CGLO_04655 {ECO:0000313|EMBL:EQB55416.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB55416.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:EQB55416.1}.
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DR EMBL; AMYD01000939; EQB55416.1; -; Genomic_DNA.
DR STRING; 1237896.T0LUH8; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_50_4_1; -.
DR OMA; WVMKPIN; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000015530; 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; IPR000014; PAS.
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; PS50112; PAS; 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:UP000015530};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 287..341
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 463..625
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 839..1072
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1306..1437
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1468..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1357
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1497 AA; 164629 MW; 0A7344AF307FEE05 CRC64;
MDARSDTRRP SVTFADQSTT DDSSEATPIA SSHSNPAAPH VDDSSTPDAF AASAASSAPV
SANTATPSCS SSWSASSDRQ LGHGASPDPS DRVFPIRSVV SVQRTGRSSS EHDYFPRLPD
HGQYPAPRPG NPRIDTAALG AASRRDSASA TTSHSHPSTV TSPSDRQPVL TRRKNTGSGP
LSSVQADAVR HANSKPLELF QDVISDGEDE SVPGDDSSQR PASLTTSQLS ELGTDGLFTT
RFKYVMTDEG HHVITGTDNV LQRCEDEPIH TPGAVQGFGA LVAIREEADG RFSVRYASEN
TERLTGYSPQ LLFRLNSFLD ILTEEQQDNL LDHIDFIRDE DADPAINGPE VFSLSIRPPR
RKSVKLWCAI HINPAHPDLI ICEFEIDDDH QFPLRPPEEA TPNTPEDTLQ SNPTMEELAE
STEILSKPLR VLRSARKRRG DAGAMQVFDI MSQVQEQLAA ASNLEGFLKI LVGIVKELTG
FHRVMIYQFD SSYNGKVVTE LVDTTHTKDL YKGLHFPASD IPRQARDLYK LNKVRLLYDR
DLETARLVCK AKEDLDLPLD LSHSYLRAMS PIHLKYLANM AVRSSMSVSI NAFNELWGLI
ACHSYGRKGM RVSFPIRKMC RLVGDTASRN IERLSYATRL QARKLINTAP TDKNPSGYII
ASSDDLLKLF DADFGMLSIK GETKILGEIE QSQEALAMLE YLRLRELTSV VTSQDIREDF
PDLHYPLGFT VIAGLLYVPL SVGGNDFIVF FRKGQVKEVK WAGNPYEKTL REGTAAYLEP
RKSFKTWHET VLGKCREWSE EQVETSAVLC LVYGKFIEVW RQKEAALQSS RLTRLLLANS
AHEVRTPLNA IINYLEIALE GSLDQETRDN LAKSHSASKS LIYVINDLLD LTQTEEGQNL
VKDEVFDFGM CIREATEPFV NDAKRKGIEY QVIEHPGLPR HVCGDSRRLR QAISNVAANA
VQNTANGYVK VELYVSEVLD RRVRIEILVE DTGKGMTARQ LDTLFRDLEQ VSVELGETTL
PSKDDEAGKE DRILGLGLAV VARIVRNMDG QLRLKSEQGT GSRFIIQLPF DIPDDAPAPA
GGLRHSESAA ASSVASVTTA VMPDSDGELM LIDRGSKQTQ QNDGFEEMMP GDSGPKAETR
SLESQKSAAT GTSRASDNSS RSDADRLIDA IQTPLSIGEV DMSRPFAQRQ FSRETLYRPK
SSDGNSSSVM GSPNSLRTSR KNGPAIDSSS RHEVGFSSVK DTKTPIRAVK IPDEYLESPS
SMPQESASSR VLFEVSEKHT HGAASESGTI GTTTSVVSGP DTTKLQVLIA EDDPINSRIL
RKRLEKSGHQ VSHAVNGEDC ATVYREKSSA FDVVLMDMQM PIVDGLTSTK MIRAFEKSSE
HGGHSSIASH NGRIPIFAVS ASLIERERDK YVSAGFDGWI LKPIDFRRLN TLLLGIVEDD
TRAMCLYAPG QWERGGWFNV RDCSGGDEKI LGKETSDDES ATPTGQDGVT READGTA
//
