ID W9VP39_9EURO Unreviewed; 1401 AA.
AC W9VP39;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 28-JUN-2023, entry version 43.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EXJ53866.1};
GN ORFNames=A1O7_09202 {ECO:0000313|EMBL:EXJ53866.1};
OS Cladophialophora yegresii CBS 114405.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182544 {ECO:0000313|EMBL:EXJ53866.1, ECO:0000313|Proteomes:UP000019473};
RN [1] {ECO:0000313|EMBL:EXJ53866.1, ECO:0000313|Proteomes:UP000019473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114405 {ECO:0000313|EMBL:EXJ53866.1,
RC ECO:0000313|Proteomes:UP000019473};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora yegresii CBS 114405.";
RL Submitted (MAR-2013) 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:EXJ53866.1}.
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DR EMBL; AMGW01000007; EXJ53866.1; -; Genomic_DNA.
DR RefSeq; XP_007761381.1; XM_007763191.1.
DR STRING; 1182544.W9VP39; -.
DR GeneID; 19183766; -.
DR VEuPathDB; FungiDB:A1O7_09202; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_50_4_1; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000019473; 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; 2.
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:UP000019473};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 382..544
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 759..1000
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1201..1332
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1359..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1026
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1252
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1401 AA; 154409 MW; 67DD5A36D19D8190 CRC64;
MFTGRSSGDP IVATPLSPKS DDGKAILSPG SIDRVFPARS AISIDPVATP MPRMDSSGGY
PGMRAAARQR APSITLSGQP PVPTTRTTSV SDASEIGSVS DAAQRPFDSA PQASGNLDHK
ILANMVTEDT ASRKSEASSV SGGMPIPAQQ GTGLVTARFK HVVTEEGHAV VTGRDGETLQ
RCEDEPIHIP GAIQSFGLLI ALREENEKLV VRIASENSAQ IIGYTPQQLF KVESFLDIFS
EEQADNLLDH VDFIREEGAG DATSTGPDVF MLSIKPPHSR TRRLWCAMHL SETDAGLLIC
EFELEDDTIN PLVPSEDRIT PEAPEDTLGS QPTQEELMDS TVNISKPLRV LRSARKKRTE
AAAMEVFNIM SQVQEQLSTA PTLQTFLKVL IGIVKELTGF HRVMIYQFDH SWNGRVVAEL
VDPRATKDLY KGLNFPASDI PKQARDLYKI NKVRLLYDRD QETSRLVCRT LEDLERPLDM
THANLRAMSP IHIKYLANMG VRSSMSISIS AFNELWGLIS CHSYGSRGMR VSFPIRKMCR
LVGETASRNV ERLSYASRLQ ARKLINTSST ATNPSGYIVA SSDDLLKLFE ADLGALSIRD
ETKILGNPRG HLQEVLAMVE YLRMRRMSAV FCSQDFTNDF PDLRYEPGWK FLAGVLFVPL
STGGNDFIAF FRRGVLQEVK WAGNPYEKFV KEGTEGYLEP RTSFKQWTET IVGRCRDWTD
EEIETASVLC LVYGKFIEVW RQKEAALQNS QLTRLLLANS AHEVRTPLNA IINYLEIAME
GALDQDTREN LARSHSASKS LVYVINDLLD LTKTEGGQTL VKDEPFNLLQ TIKDATNPFI
GDAKRKNLEY EVEISPSLPR SVLGDHRRVR QVVSNLIANA VQHTREGKVV VEAYPCPTSQ
PQPGKTEIEI VVEDSGAGMS QAKVDALFKE LEEVSYEEDL PDSKAIITDP LPEQPQSENA
TLGLGLALVA RTIRNMKGQL RVKTEEGKGS RFVIVLGFDT DGPEPVQLAI QPTSPDLSSR
PATSPGHQEG EVTLIYRNPQ KGPDSMSTRP APPPRRASAE SMNSLASLKS AMSLKSDTSR
KSGADRLIDA IQQPLQFADQ KTSSPGPTHD EAFRRRSLES PTKSKSLPSP RDLKSAMRTS
GWEKVKDSGT PLRPVRVPDD QEDGASGSKI GPRILFREPV SECSQSDTTE VSKANPTENF
SVLVAEDDPI NSKIMKKRLE KLGHSAQMTV NGEECSSAYA EQPAWFDAIL MDLQMPIVDG
FSSTKMIRSF EKTQGKSCLS SRAGQNGRLP IFAVSASLVE KERNKYVDTG FDGWILKPVD
FKRVDLLLKG IVDGEARNEC LYEPGKWERG GWFSTREEQH NPFDVDTHPN QEKQATSVPG
PASTGDGAQV SSLSDGPGTE R
//
