ID W9WSR6_9EURO Unreviewed; 1888 AA.
AC W9WSR6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EXJ67706.1};
GN ORFNames=A1O5_09052 {ECO:0000313|EMBL:EXJ67706.1};
OS Cladophialophora psammophila CBS 110553.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ67706.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ67706.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ67706.1,
RC ECO:0000313|Proteomes:UP000019471};
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 psammophila CBS 110553.";
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:EXJ67706.1}.
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DR EMBL; AMGX01000015; EXJ67706.1; -; Genomic_DNA.
DR RefSeq; XP_007747822.1; XM_007749632.1.
DR STRING; 1182543.W9WSR6; -.
DR GeneID; 19193749; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000263_0_0_1; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000019471; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF74; HISTIDINE KINASE D5; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; 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; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000019471}.
FT DOMAIN 1189..1417
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1750..1872
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1422..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1487..1546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..535
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1802
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1888 AA; 205294 MW; CA023654E028E8BE CRC64;
MKSSKSQRLG MPPRGRSSRS TDGHGSATRS EEEIVGDRRS GTDASSHTPT SAHHQVTTIL
TRENSAGMEA MRRRMSAALA QKQQMRAAAA AASASSGSSD TAKQDDSSEP STSLQQTESS
SDESVNTGAL STDSARTIRA SFDMTPGTVR TPSYPFPRMA LRLNRQISHR SGPSHRPFTL
LSPTNEPPLS ADPAQPPHPQ RQASSSDLST PIGQTPMSPG YPEDPTFPAP DLYDIILMLN
AEPGLEMWWV NVTEILSEVY GAERASLAVP GDITDLENVP WGQKATYNVN GSEGVPSSQL
ESLATSDADA TSVGRRPDPG NRIPSDASSA PPRRPPLLSR HSIAGPTPDP SARGARQRPA
GPVRAYSTVP KEPAEEVMAI LPLLPRLTRQ AATPRSTSVA DSDPLAFRGQ YNLSGSASST
LRCHVHRSIQ PLEAESDPLL VRTGVASLFG KRKPVVLTRA YTDTAPRQSP KVKGREDDRS
APPTPSPGGF EDRKLARPGD NSTLQSAFRA FDEYEQPEPS PWSQSPSPSP AARPDPAESP
FFTQPTASID ETAFEQNPPA YDYASTANQS LSAIGADMSK TLIHVPLIQP VLARGTMASN
LRFPIAILSF LSPLNPYPRS LRHSLEALLP HLASSYSLAQ QYSALQDRLR GTPGSRHGAA
FGLGGTFSDE GSELELVAEL SGQIAQDKEN AKSWTHQEDL SPGVLRESPG SSVASTPLLE
QFGLSSGQPP TPGGKTGSEM VDSYFSARRQ RAGQQPLTPG PRPTKDETEQ AKHSTEKTSA
SSKAAGKKTT TGSATKTQPD PPSPMALRTA SIASEGEAGD HSFALYDRID APRRNTARRI
SEHKDDGERP LPELISSLML NAVPLQLFLA KPNTGDLVWT NRKFDAFRSQ GEGRVRDPWK
NVHPADRNGL VKLWNEALRT GSQFTHYIRV KRFNSDSDFR WFVFRASTLL SNSGRLLYWI
GSFLDVHEQY MKNLEASEKE AIMARDTKIR ALADAIPQIL FEAIEGDGIV AVNQQWHSYS
GQTLEDARGL GFAKHVHRDD LHKCGILAPS DVAAIARSSA ASASSSSESN RTVAAVAPPL
PAQKNLFSPD LSSLDRMIKS GSVVVEKDEN GRLSYLTEIR LKSRGGGYRW FLVRLVRVDT
GLWQSQSGKA SWYGTCTDIE TRKALERELN QANEKVHSEM ESKTKFFANM SHEIRTPLNG
ILGSMPWLVE SELDHDQRRT VDTIQNSANN LRELVDNILD VTKVEAGKMT LLPKWFHVRT
LCEEVVDTVS SRAIERGLEL NYSLEANVPS MVKGDAFRVR QVLLNLLGNS VKFTEQGEVY
MRCSYRKADP ANSTAQADNS GLLSFTVVDT GRGFNKDDFK RLFKQFGQIG GGSSHEAGSG
LGLFLSKQLV EMHGGELSVK SKAGEGSTFS FYIRVEVAPP GSEVTSPQVA ARAGQQQRQS
PSLGGSARSR SDNKTTTMAS ARGLSYSEGV IQTPGLSRYV SSPLQQAPAS PVVSSPTLVS
PPVLPSDSSG LSMRSNSGNI ASTSSATSTV QTPEFAPPPE SAVSTNERQI LTEKAIAAHP
IFKRSKSDND GSGLVSEQAH PQMYSIIIIC PAEHARTAIK QHIEHVVPYS IAANVTTIPD
ISSFLGLLNG PSPATFTHIV LDIPATSDIM LFMRQMVNYG GPVTPALVVI TDHYQKRDIL
DDFTALTASG RKAYMIHKPV KPSVFAMIFD PAQLRNLSKD RAREVAQSSS DDFRHIANLV
KDKIGGREHR VLLVEDSDVN RMVIQRYLKK VALVNDCAKD GQQCVDMVLG KPHGYYSLII
CDIQMPVKNG YEACTEIREW ERSHRYRPSP IMALTAHAMP EERAAAANAG FTDYLTKPVD
FNVLGTMMMT LLDPSVPHVF LRDRPLES
//
