ID A0A024U1U1_9STRA Unreviewed; 1699 AA.
AC A0A024U1U1;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Hybrid signal transduction histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=H310_07616 {ECO:0000313|EMBL:ETW00224.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW00224.1};
RN [1] {ECO:0000313|EMBL:ETW00224.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW00224.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KI913965; ETW00224.1; -; Genomic_DNA.
DR RefSeq; XP_008871249.1; XM_008873027.1.
DR STRING; 157072.A0A024U1U1; -.
DR EnsemblFungi; H310_07616-t26_1; H310_07616-t26_1-p1; H310_07616.
DR EnsemblProtists; ETW00224; ETW00224; H310_07616.
DR GeneID; 20084666; -.
DR VEuPathDB; FungiDB:H310_07616; -.
DR eggNOG; KOG0519; Eukaryota.
DR OrthoDB; 90212at2759; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 6.
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; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 7.
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; IPR036641; HPT_dom_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; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 6.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 6.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00086; PAC; 7.
DR SMART; SM00091; PAS; 7.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 7.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 6.
DR PROSITE; PS50112; PAS; 6.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00022519};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 182..253
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 256..309
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 303..374
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 377..429
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 423..494
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 497..549
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 543..614
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 617..669
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 664..735
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 738..790
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 784..851
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 857..909
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 913..1138
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1180..1301
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1570..1671
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 1400..1445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1679..1699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1682..1699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1231
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1609
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1699 AA; 186961 MW; DDABBACE17AE2D47 CRC64;
MPRHTGRRKV SSQASVEEDA AISSEILPVD YEAMLEAMAT MVVQLDLQGV VTYMNRRAQC
LLECDATSGL GTPFVETFVQ PAGRKSAAGG DVETDGNDAS VSFVTLVDFV SMANKHIQNV
VCTAEPAVFQ CSLQTYGSPS SVLDVLISAS PRLNSTRDVV GCIIVGTDVS SLQDKVPSTS
KSEHVYARIL ERANAPIFGV DHIGRINIWN KKTAEITQYA ADEVMGKHLV DTFIAPAYRG
PVGAVLTQAL NGIETANFEF PLDTKHGGRQ LEILLNATSR YDEVGNIVGV VGIGQDITDR
VAQEQEYSRL IDKANAPIFG VDSNCCVNIW NRKVAEITQY TMDEVVGENL VEKFISEEFR
QGVRDVLSMA LRGDETADFE VPLVTKTGRK VNISLNATAR FDQMGHIIGV VGIGQDITDR
IAQEQEYTRL IDTANAPIFG VDQNGLVNIW NKKAAEITQY TQQDVMGKNL VEKFITEDYR
KAVGYVLSRA LQGTETANFE FPLITKTGRR VEILLNATPR YNELGKVMGM VGIGQDITDR
IAQEQEYSRL IDKANAPIFG VDADLRVNIW NKKAAEITQF TIEEAIGENL VDTFISEEYR
SAVSEVFAKA MTGTETANFE FPLITKSERR VEILLNATPR YNELGVVIGV VGIGQDITDR
IAQEQQEYSR LIDTANAPIF GVDSNMCVNI WNKKAAQITH YSISEVMGEN LVETFISPEY
RPGVADVLSK ALNGIQTANF EFPLITRPGT RIEILLNATP RNDLHGNIVG VVGIGQDITD
RISQEHEYFR LIDSANAPIF GVDTNGNINE WNQKIEFITG YQKDAVFGMG LDTFIIPESR
SQVKQLLNQA LIGIDVGEME LPMITKKGCF LLLLVNASSK KDIHGNIRGV IGVGQDYTAR
KQMEAAKVNF LASFSHELRT PLNGVLGMLE LLKEQKLGKV PERYVHMAYV SGSLLLNLIN
DILDLSKIEA GHLEIQSAPF HIGDLLDYTI EIFKFKAHER GLKLSVVLAP SVPEVVIGDV
VRLRQILLNL LSNAMKFTLK GTITIKCSVA PSNPDQPPHH KRLLFQVIDT GVGMDAEEKS
RLFSLFTKLE RTRKNNPTGS GLGLAICKQL VELMDGQIDV DSELGIGSVF FFSVAVRVIP
EELLPKLAPQ LEPKQSSSLG GGFSPSARDV MESAVPKQAR ILVVEDNDFN WEVVKCFLQG
DDHYLQWEIN GRDAVDAYKA HHDSFDMIFM DCEMPVMDGY SATQAIRQFE IENGLPRIPI
LGLTAYAMCG DREKCVDAGM DEFIVKPISK SGLLKAIAHW MRKRYIPNLN LAESSLLLDG
YPDLVTSSPR SSVETVPDLP PPLQQDYFTN SSRKLNTNLV HASNHTQNLD LTRAISDLEL
EDPMMIGRHR VMPAYETTTL GDTTSNSGGK PCNQSMFSLG MSSSTSNLRS SMSSRSPIQD
STSPMSKTYH TFEQQKYASA AAAAGGPDSL AKRRHTSNSL PDVTKLMRPL AQIVADEGVD
WQQPQHSRSD KESHMNVHAM RQQGQGPPSA LSPAVPPVLA NSNTSSVLDI EIPEGDPVDY
STGVSQCGGN EDLFLKLLEM YYDGLDASVH KLEKAYFNQD VPAVRRESHS LKGSSAYVAA
MRVSKAAFRV QVAADMMLGK EAATPDPATY EASYRLLVHE LKALKGYLRR NFQFARPAMP
TTRGASETTP KGTGPCQVM
//
