ID W9WES2_9EURO Unreviewed; 1285 AA.
AC W9WES2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EXJ66418.1};
GN ORFNames=A1O5_10570 {ECO:0000313|EMBL:EXJ66418.1};
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:EXJ66418.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ66418.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ66418.1,
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 -!- SIMILARITY: Belongs to the ERT1/acuK family.
CC {ECO:0000256|ARBA:ARBA00010855}.
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:EXJ66418.1}.
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DR EMBL; AMGX01000020; EXJ66418.1; -; Genomic_DNA.
DR RefSeq; XP_007749336.1; XM_007751146.1.
DR STRING; 1182543.W9WES2; -.
DR GeneID; 19195263; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_82_4_1; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000019471; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR PANTHER; PTHR43719:SF30; TWO-COMPONENT SYSTEM RESPONSE REGULATOR; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 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); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000019471};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 660..730
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 733..791
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 809..1082
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1144..1275
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1204
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1285 AA; 141987 MW; 3165E17A38604C2B CRC64;
MAATSIPVRI SPQASRAGSR HKRASSDTRR PNETQLLHAI PLIEYLQLDE RPTFVVDIVD
TVNLNPSGLN LIFANTALKS RNSLFDHVQG RSEDSTQLLD LGTPFSDFKA WALSPLTEPD
IVPTFPFAGW LWQGALIRKR LKVIHGRQHP FSTPLVADGG GGRLGMQQYQ GLGSASASTS
GGARGDTELQ SYFDIPPRTS GEVPRTLNRL VTEAIPDVSP NGLDPTSPVP SGDLTYSELL
SGSFQASSDQ RVISAGAHIN LDTDMVTVDE KGYFDWTRLP MSPSLPAHIR FARGVDWSAT
SLGPIQDWSV ELRGMCNLIM ASPHPSAMYW GPDHIAIYNE AYVLLAGQKH PALMGARYRD
AWFEIWDALK GVFDNAFKNA QATMKDDDCL FIMRNGFLEE TYFSWSIIPL IGADGGVVGL
YNPAFEKTRR KIAERRMLTL REIGERTAAA REVSQFWGLL LQGLEYNEYD APMVLVYSLN
EDLAESEVAS SGSSGAASNK VCYLEGSLGI PAGHRSAPPV IDMKTGTRGF AASFRQALTT
DRPIVLRVDD GSLDPDMLEN IEWRGFGDPS KIVVISPIHP TTGESTLGFL VMATNPRRPY
DEDYDLFVQL LGRQLATSIA SVVLFEDEIK KGERAAQLAA QDRIELSNQL LARTQQAAEA
ENKFARMAEL APVGIFIGNL DGKINFANDA WYNISSYPRD VPVDNEWIEY VLEEDQAKVR
ELWTTMLEKR CAISLEFRFK SPWGDKLGNT GQTWVLTSAS PERDEDGRIR QIFGSMTDIS
AQKFAESLQT RRMEEAVELK RKQERYIDTT SHEMRNPLSA ILQCADSITG SLSEMRDANG
LTKPQQEILD LTIDSAQTIT LCAQHQKRIV DDVLTLSKLD SAMMAVTPVD TRPIAVVHKV
LKMFDAELKT ADIRLELKID TSFTAQEIDW VRIDPHRLSQ VLINLMTNAI KFTTTQENRV
IRMHIAASEE KPSQEDKWRL TYIPSRSPKE KDVTAAAEWG LGEPVYLHFA VQDTGRGLDE
LEKKQLFQRF SQASPRTHVT YGGSGLGLFI SRELVELQGG EIGVASESGK GSIFAFYIKA
RRSKGDIATL EEIPGSSAPH SRKASKTTPL TGLAMQVLQP PSGASLASAK TASASLTTQA
DAVHVLIVED NLINQKVLAA QLRKIGCVVH VANHGGEAIE QIRKSKFHSD HVTDGVKVDV
VLMDLEMPVM DGQTCARKLR EMQETGELVA HVPVIAVTAN ARAEQIEMTL QSGIDDVVSK
PFRLPELVPK MKDVLAKFKR DGERV
//
