ID W2RTN2_9EURO Unreviewed; 1219 AA.
AC W2RTN2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETN39069.1};
GN ORFNames=HMPREF1541_05291 {ECO:0000313|EMBL:ETN39069.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN39069.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN39069.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN39069.1,
RC ECO:0000313|Proteomes:UP000030752};
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 Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB822721; ETN39069.1; -; Genomic_DNA.
DR RefSeq; XP_008717854.1; XM_008719632.1.
DR AlphaFoldDB; W2RTN2; -.
DR STRING; 1220924.W2RTN2; -.
DR GeneID; 19972630; -.
DR VEuPathDB; FungiDB:HMPREF1541_05291; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_82_4_1; -.
DR InParanoid; W2RTN2; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000030752; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; 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; 3.40.50.2300; -; 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; 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; 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); 1.
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:UP000030752};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 755..1022
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1083..1211
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1140
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1219 AA; 135348 MW; 269AB6DEBACEB934 CRC64;
MEADISVASS VKHGLGVVTF EEALDEDLRP VFVLDLTRLA PVENGPLYPL FCNRALAENK
QLHDSVLGFS TDKSSEERPE EYQQFREWIS RLRGTQLPGH SSHAGFRYDG VYWTSSMVRG
RYQIVSGNVC EHTPAVTLTG SAAKVVVDLP RDELARDQSK ADNHGSVTTH GLVPNVSFDA
GDAIVPSRIP RSVAASRRYD PKPPPSVEDE KVMIPQRLSA SMSTDWTAPD PLGVLTPHEI
FARNTDWAST PLGPMSSWSP EFREVVNLLM RNPHPATLFW GEELTMVYND AYRIEVAGNK
HPRLMGSGFF GPFAELWESV RPIFQECART GKSIRKENDR LLIERYGYLE ETFFSWSWTP
LYGGTDRILG FYNAPFETTY QTVGSRRMET LRHLGERVAP ARSVKQFWRD VLIALDANPY
DIPFASLYSI TDSDGSDACS VSSGGVVTSK TCALEGTIGV PDNHPAASPE IDLSGSDGLV
PCFEEAIRTR EPVVLRVTDG NLPDFLLEGI SFRGFGIPSK EALVVPIRPT SGQNTTALLM
IGLNPRRQYD SDYRTFITML NRQLASSLAS VVLLEDEARR NRTAAEVAAL QREQLTEQLA
LQTSRLRRMT EFSPFGMMLV SPDGVLLEGN DRYYEMTNHS RDIAFEMSFM DTVADASKSD
AITMWVNAMR DLKPTTGEIQ LSNNYNTEIN ELTGRPIDCW VLASVVPEIG PDGTLRSVLA
CITDISHMRW AQGLQDQRLR EAEETKRQQN AFIDITSHEM RNPLSAVLIC ADDIRDTLTE
HHFSRDDAEV VKSCIEAAST IALCVQHQKS IVDDILTISK LNSNLLVISP MPTEPVRIIQ
EAMSMFRNEA NAKEIDMSLH LDPSLEDLNI QWLMLDPGRL VQMTINLITN AIKFTKQSPK
RSISVFLGAS LSPPVATRNG FQYVPTREAH VDVASGKEWG NHELVYLRVK VADTGCGLTE
EEKQRLFERF AQASPRTHAH YGGSGLGLFI SRQLAELHGG QIGAASEAGQ GSTFGFFIQC
RKTFDPVVIN GTVMPATLDP SQRVGDIKAE IAAHDTRLES TAQDVLMAES QSTVDIIKSR
ELHVLVVEDN LVNQKLLRKG LEKMGCTVNT ADNGVVALRY LETTELYQPG LTRLSVILMD
LEMPEMDGLT CIARIRELEA KGVLRWHVPA IAVTANVRAE QVTIARNSGM DDIVSKPFRI
AELVGRIEAL VSANRHPAR
//