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Database: UniProt
Entry: M3D3F7_SPHMS
LinkDB: M3D3F7_SPHMS
Original site: M3D3F7_SPHMS 
ID   M3D3F7_SPHMS            Unreviewed;      2502 AA.
AC   M3D3F7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Histidine kinase HHK1p {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SEPMUDRAFT_133173 {ECO:0000313|EMBL:EMF12419.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF12419.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF12419.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF12419.1,
RC   ECO:0000313|Proteomes:UP000016931};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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DR   EMBL; KB456264; EMF12419.1; -; Genomic_DNA.
DR   RefSeq; XP_016760540.1; XM_016902548.1.
DR   STRING; 692275.M3D3F7; -.
DR   GeneID; 27899685; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_001037_0_0_1; -.
DR   OMA; QLPGYTW; -.
DR   OrthoDB; 1222064at2759; -.
DR   Proteomes; UP000016931; 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; 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; 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   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR041664; AAA_16.
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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR43047:SF46; HISTIDINE KINASE_RESPONSE REGULATOR, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G12550)-RELATED; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF13191; AAA_16; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00069; Pkinase; 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   SMART; SM00220; S_TKc; 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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000016931};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          65..386
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1914..2136
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          2187..2310
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          82..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          697..718
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1640..1672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2334..2502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1873..1910
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        83..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..558
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1640..1670
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2340..2370
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2412..2438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2442..2459
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2241
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   2502 AA;  277351 MW;  4D2A80A0DFA64BF4 CRC64;
     MLQSLAGNMD LVVEDEADRV GEDEADRVVE DEAQVASIRR FFERLREDVP GYEFSDEVPP
     FHSSYDNWHF FGRKKNAKAT AAGAASRKSS LSAVTDSRPP SVRTRSDYDA ATPDEEQEQP
     IWVVGRLSKQ ILRLEREFKL CQQLFQTAED HKHFVRPISL LRLPARQPGD VPLCISIVEA
     PGKDYLQDLV NLGSDFYGGV PGSQQIQHRE QVPLLTFLDF AIGASECLEI LHHGSDIVHG
     EIRGDAFHYN KDTGTVRMIN FGSGVRSFEH GLTSANWTTL MSQRGVEHRL QFIAPEQTGR
     LPAEPDARTD IYSLGILFWT MLTGQPPFEG KSPLDVMQNV LGRRIPLASS IRTDVPDVLS
     RLIQKMTARN MDDRYNSTTG VKHDLQKLKK ILTDGDQEAL ASFKLAEKDV SCFFVLPSNL
     VGREEQRAKI IEVIERAAAK AARSTLSRKA LYSLSSTGSS VISSDPQIAN LLDDISDSTS
     STDRERTDNH LTSIPEAIPS EQRMYRTSLD YPDRTARTGS TVSPAASINE DGGLTSQGYK
     DTSYDSHGSG TSGNREGSES LFRTMSSYQL GSMTSEPSSL LRTAQKIKRK GRTEIISICG
     QAGFGKSALV QSVQVRARKY GYFATAKFDP VRKAPFDPVV RVMSSLFRQI FSENDVSTPF
     HENVRTFVKP YWGILHTYLD LPVWLLAPTI NGKMAASQGP SEMRSAHGQL ERPPERKTCN
     AASTQEWLRS GGSSKSSRFM SIFLDVLRLL AVQKFACFCL DDIQFADPES LELLQIIVKS
     HIPLVLMLTY REEKPITPAV AKLLEKATRV DVGPFSDNQL TEYVSQTLHR PAEYVTPLVA
     IIHEKTQGSP FFVREMLDSA YRKKCIYYCW KCGHWEFSLD RLFAEFSTPD AGKFSTDDFI
     LRRMKELAID AQTVLAWAAI IGNSFSFKVV RRLMSCACSE LSPQPLIPPQ SKDAVAGLQT
     ALASFVVMPT DDEDRFKFSH DRYIAAADSL CKDYVREEMH YVVASSMMKH SPYDPVSQPS
     VVLFEQARHI CKGVDAIKLR VPVKTAYREL LYQAAETARE SGARTSSLYY FKVCLDILPE
     NPWADKTGDA SYSETLSLHI RAAEALGYAG DHETASKLLT AVFEHALNAT DKAPAAIILG
     RMHVQKGDSK MAFDVLKRAL ADLGLSIEEK SLEECDEEFQ SLLPRLKENP PDFTGVDPKD
     IDRSLSTLAA LLTEIQLAAF WTDHVLYYNV TLAILKVYLE RGMFSAVALG YVNMAAIIIW
     RFSMIDIAME LGSHACQVLE FFDQEQYTIG RVLTLYAAFL GHMQFDFAGN FKFLNRALDA
     ASSAGDKIAH LLNIGTSAAY RLWASENLAE TEAYIISVGD EFPDWQENLR GGVFLVSTRQ
     MVRALAGKTN YKSASEVLSD CSHSSNDYIK FIKAKASNPE RPLSIYMAHQ LQALYRFGYY
     HEAVVLGERL LPMTDGLMCM RYRYSVMFYH ALAMIACIRE NPVRPDREEL MAKVMHYRAL
     IEIMAAINNA NYVTHLSLLN AEIADIQQDY DHVLTHYEKA VDHALVSNVT LDEALALEQY
     ADWLVRRGSA RPGRGIILDA ISAYRRVGAF GKADHVKDKY EYLLYGTRSL SNVDTGTQTV
     NDASTSAPYA YKLERIASHQ ASQTPADRTE EWLEPTSGQS RLTSSIRDSM NREPPAALSS
     AVGLDMIDLA GILESSQLLS SELNVDRLLS KLTDIIVDSA GAELVGLVVE NDQGEWCVAS
     VGTPDDIEAP AMGIPLAEIQ DPVAKQVTMY VLRFKEEVFL RQVLDDERFS NVPDSWLEQN
     PDGASMVSIP ILHGENVLLG SLYCQAPPNT FTERTVTLLK LLVNQIAISI ANALLFKRAE
     RVQASNASML IVQKQALAQA QEQEKKAKAA EAEAKEMVRL KDEAAKAKSM FLANVSHELR
     TPLNGVIGMS EMLKATPLNR EQEEHADSIR VCADTLLSVI NDILDFSKLE AGKMQVFSVP
     LSLTETITEV VRALSYTNIE RNLVTKTELH LDKELVVMGD PVRLHQILMN LMSNAYKFTA
     RGTVTVHAKV DREDAESITV TTSVQDTGIG ITEEQQKKLF LPFSQADSST ARSYGGTGLG
     LSICKAILEN VMKGQIWLES TPNVGTKVSF RLSFKKVNAS DLHEQSGTAP HGREADPMAI
     FTPPAADDGP GARAVVSLQG IPRDQLKVCI AEDNPINQKI AINFVKKLGF SCEAYGDGQQ
     AVDALTRASE DNRPFHLVLM DVQMPVLDGY NATREIRKHP DPRVRDILVI AMTASAIRGD
     REKCLEAGMN NYLAKPVRAD TLKQMLESYL HQPRKDMPNL QDEANRLVEN VENEEARQQH
     HLQQQQQQQQ NASRNGKENA KSNNATAGTG GIGSRLPELT KSGDLRRQAP QRPRSAQRAT
     AIHLSPEEMI PKPKASSSSS SSGSSSSSTS STRAGQDPSM KEQLKLVDRQ IKELRDRPSR
     AGSVSPAPPL KDRSGSGGEN AKRGSTDGRK DGVEGGGEDG GQ
//
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