ID A0A2S4PVT7_9PEZI Unreviewed; 1324 AA.
AC A0A2S4PVT7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:POS86135.1};
GN ORFNames=EPUL_002320 {ECO:0000313|EMBL:POS86135.1};
OS Erysiphe pulchra.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=225359 {ECO:0000313|EMBL:POS86135.1, ECO:0000313|Proteomes:UP000237438};
RN [1] {ECO:0000313|EMBL:POS86135.1, ECO:0000313|Proteomes:UP000237438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cflorida {ECO:0000313|EMBL:POS86135.1};
RA Wadl P.A., Mack B.M., Moore G., Beltz S.B.;
RT "Development of genomic resources for the powdery mildew, Erysiphe
RT pulchra.";
RL Submitted (OCT-2017) 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:POS86135.1}.
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DR EMBL; PEDP01000403; POS86135.1; -; Genomic_DNA.
DR STRING; 225359.A0A2S4PVT7; -.
DR OrthoDB; 12386at2759; -.
DR Proteomes; UP000237438; 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 CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43719:SF11; HISTIDINE KINASE G7-RELATED; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE 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; SM00065; GAF; 1.
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; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000237438};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 621..913
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1172..1313
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 322..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1224
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1324 AA; 148540 MW; 7A0C1DE7AEBD68D4 CRC64;
MATSKIPPKL SHIEGISDYA RAQELYKYYQ PSAQTHITTS EEDEVNHDLN ISSNVSSSKV
SSPDTALTVF CQLTAWRMDF QRAMISLIDA EIQYFVAEST RSLDLSNNNV HAPGDGLWLG
CSSVTKAGRL CESTIAVAAT KGDRYPHFIV DDLSKDERFN KLPFVSGAPF LKRYIGVPLI
TKRGIPIGSL FVVDDRLGNG LSEENLTFLG TMAKTIMRHF ELIRVVEEHR RAMKMNLGLS
SLIEGRDEPF ETNNEKCDTM DSDLTKKPEP EYACCSKKTN ESIISEKSGV PKNIIQSANG
LEKNENNRQE VKLTLNQKEP DKVVPNEEKM RNTRSRPIKE SYSDKIINPP ENDLEDQSIR
ALFSRAAHLI QMTFELDGGT VFYDARTGSS ETITERKTNS TPCESRINSQ FGSDYSTSED
ESESSRNPKS KTIHSPFSQD VLPSGRSSHP KDSFYPLSNK TLNKRVEMLG YATCEYSSLH
GDTFPGYQVF RPLRLKTLQS LLRQYPRGEI WAFNKNGQIS RSASRKSKLC KKGIQARTPL
DANFLSWYFP GVHQLLFIPL WDAGRSRWFG GCFTWSKDPT RILSKQMELT FLTVFGNSIM
AEWARIDTEI ADQKKSDFIG SISHELRSPL HGILASVEFL EEVLTGWEKQ LVETIESCGR
TLLDTINHIL DFSKINHFES HWRRSKRAKS RTGIPITIEQ ANFSMLSLFQ DIDISVICEE
VVDSVYAGHV FQNITAQSFN QISDTQGKMS NARHPLTYTE QVRKSQKLQN DVVVVLDIDP
KNYHITSQPG ALRRLIMNLL GNSLKYTSHG YIVIRLDCHD IEDYVTDGPN GVEETIPRSM
LVFTVTDTGR GIAPEFLRNK LYIPFAQENI LSSGTGLGLS IVRAIVSLLE GEISIDSEIG
CGTHVKVSIP VLHRMPQIPV SPEGVFDSIN KEPQCVHDAV INLRNRTVGH KVSLYGFDES
TEDSILTEQR SVMKESIKKY LINWYHMQAV PYGEKVDFII ANAANHSTIL SIALNAVKTH
GNHPCIIVLC CHSSILDRIY TVEETQCKVG YTAMPIGPTK LAKAIIQTMD ALPTLLTHKI
RSQELETNCL DSLIKKSPAD SQGTNKKIAK LESPQKVIVS PMTKVDTKNE YKNSPLLKNN
TKLVPRNDSS IISKKMNIPK PTILGAQHKV PSILLVDDNQ INLRLLSTYL SRRAYPCVDT
AQNGLEAVKK FEAFSSGYDI IFMDITMPVL DGFGATRQIR GIEKKMASST WKSALKNSID
SSVEQKRKPA LIIAFTGRSS IEDQSEAIRS GIDLFMTKPV PFREVDRICD NWIANHMQST
TTSS
//
