ID A7F519_SCLS1 Unreviewed; 1309 AA.
AC A7F519;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 91.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SS1G_12694 {ECO:0000313|EMBL:EDN97840.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN97840.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR EMBL; CH476642; EDN97840.1; -; Genomic_DNA.
DR RefSeq; XP_001586119.1; XM_001586069.1.
DR SMR; A7F519; -.
DR STRING; 665079.A7F519; -.
DR GeneID; 5482414; -.
DR KEGG; ssl:SS1G_12694; -.
DR InParanoid; A7F519; -.
DR OMA; CLAAQMD; -.
DR OrthoDB; 1222064at2759; -.
DR BRENDA; 2.7.13.3; 5625.
DR PHI-base; PHI:2910; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0004673; F:protein histidine kinase activity; IBA:GO_Central.
DR GO; GO:0071474; P:cellular hyperosmotic response; IBA:GO_Central.
DR CDD; cd06225; HAMP; 5.
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; 1.20.120.1530; -; 3.
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; IPR003660; HAMP_dom.
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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00672; HAMP; 3.
DR Pfam; PF18947; HAMP_2; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 6.
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; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 2.
DR PROSITE; PS50885; HAMP; 6.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 196..251
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 291..343
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 383..435
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 475..527
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 567..619
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 659..711
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 733..957
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1108..1227
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1239..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 134..204
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1244..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1157
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1309 AA; 143318 MW; 027CCB57B27C34BF CRC64;
MGDTTIAHTT AILQTLAVLS LDSPQANVYG NKGIRLPGAD TAEKLALERE LAALVSRVQR
LEAKATANNH VLPDTPNEIG APSAFADVLT GAPSRASKST TSRQQLVNSL LAAREAPTGG
ERPPKFTKLS DEELEALREH VDDQSKQLDS QKSELAGVHA QLFEQKQRQE QALNVLEVER
VAALERELKK HQQANEAFQK ALREIGEIVT AVARGDLSKK VQIHSVEMDP EITTFKRVIN
TMMDQLQIFS SEVSRVAREV GTEGILGGQA KISGVDGTWK ELTDNVNVMA QNLTDQVREI
ASVTTAVAHG DLTQKIERPA QGEILQLQQT INTMVDQLRT FAAEVTRVAR DVGTEGILGG
QAEIEGVQGM WNTLIVNVNA MANNLTTQVR DIAIVTTAVA KGDLTQKVQA ECKGEIKQLK
ETINSMVDQL QQFAREVTKI AREVGTEGRL GGQATVHDVE GTWRDLTENV NGMAMNLTTQ
VREIAKVTTA VARGDLTKKI EVEVQGEIAS LKDTINTMVD RLGTFAFEVS KVAREVGTDG
TLGGQAQVDN VEGKWKDLTE NVNTMARNLT TQVRGISTVT QAIANGDMSQ KIEVAAAGEI
LILKETINNM VDRLSIFSNE VQRVAKDVGV DGKMGGQADV AGIGGRWKEI TTDVNTMANN
LTTQVRAFGD ITNAATDGDF TKLITVEASG EMDELKRKIN QMVYNLRDSI QRNTLAREAA
EFANRTKSEF LANMSHEIRT PMNGIIGMTQ LTLDTDLTQY QREMLNIVHN LANSLLTIID
DILDLSKIEA NRMIMEEIPY TLRGTVFNAL KTLAVKANEK FLDLTYRVDS SVPDHVVGDS
FRLRQIILNL VGNAIKFTEH GEVSLTIQKA EQDHCAPNEY AVEFCVSDTG IGIQADKLNL
IFDTFQQADG SMTRKFGGTG LGLSISKRLV NLMRGDVWVK SQYGKGSSFY FTCTVRLATS
DISFIQKQLK PYQGHNVLFI DKGQTGHGKE IITMLTQLGL VPVVVDSEQH TILLGNGRTK
EKIASTYDVI VVDSIETARK LRSIDEFKYI PIVLLAPVVH VSLKSALDLG ITSYMTTPCL
TIDLGNGMIP ALENRAAPSL ADNTKSFDIL LAEDNIVNQR LAVKILEKYH HVVTVVGNGQ
EALDAIKEKR YDVILMDVQM PIMGGFEATA KIREYERSLG TQRTPIIALT AHAMLGDREK
CIQAQMDEYL SKPLKQNHLI QTILKCATLG GALLEKGREV RQSANEESPN SQNGTRSNQH
PASSPTPAHL RPTIEPRAYT TTGPINHGSV ESPSLVTADA EDPLARNLY
//
