ID A0A0D9P8C2_METAN Unreviewed; 2087 AA.
AC A0A0D9P8C2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Peroxide stress-activated histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=H634G_03573 {ECO:0000313|EMBL:KJK81040.1};
OS Metarhizium anisopliae BRIP 53293.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1291518 {ECO:0000313|EMBL:KJK81040.1, ECO:0000313|Proteomes:UP000054544};
RN [1] {ECO:0000313|Proteomes:UP000054544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRIP 53293 {ECO:0000313|Proteomes:UP000054544};
RX PubMed=25102932; DOI=10.1186/1471-2164-15-660;
RA Pattemore J.A., Hane J.K., Williams A.H., Wilson B.A., Stodart B.J.,
RA Ash G.J.;
RT "The genome sequence of the biocontrol fungus Metarhizium anisopliae and
RT comparative genomics of Metarhizium species.";
RL BMC Genomics 15:660-660(2014).
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DR EMBL; KE384727; KJK81040.1; -; Genomic_DNA.
DR STRING; 1291518.A0A0D9P8C2; -.
DR Proteomes; UP000054544; Unassembled WGS sequence.
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; cd00130; PAS; 2.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF74; HISTIDINE KINASE D5; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 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:UP000054544}.
FT DOMAIN 1138..1190
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1197..1252
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1354..1408
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1419..1646
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1965..2087
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 20..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1258..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1644..1743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1767..1789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1655..1691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2017
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2087 AA; 227773 MW; CA945E805FC1F69D CRC64;
MHSLDSPPLD INYYISPSTC VDSTTPDSTR ATAEASTVAA VNPASPPSPS HRSPTTRKLA
AGSGITRDGV IVGKFVLVEE AEAEAEDAAR ISTGHARTRM AQRRSSYPFS SASELSGRGL
REWQSSKERR VHGDEAIAPH TAAEDNWSPA GTDLGNHPPA AVLATSQQQL NEYRARLARD
QEIRELSLKG LLMTQSEKTR VSPILEEAAG MSSPPMLTAA LTTTSTESGN TVRGTMTPAA
VAQTPSYPFP RMARFPSHQT SSKWVPYQPT ASPLSRQQFQ SPLEYRGLLD KVSSESSTPA
SNVAFEPPGA ASENPHGFDF PSPNLYDLSL MLSAEPGLDA WWNTVVQIMR DIYKAERVTL
AIPADTTDIE NVPWGQKATY NEHQEDELSL GYLAKASSAS DGAAAFDDRT ADSPSTSASR
PGLRSRHSYT AFEENKHKSL DQNSIMPPPK RPTNLSRSKT QYPSPRVAAE LHDDYTKLNK
DALDEHDATA ETQQAIPSWE APFMARYEGQ GQVLPVLQAL DYEADPLIDH TGVMRVLERG
RPVALTRTYP YLPRTKPDPK QTVEQKSASK GSSADSKRIK RPRTESVSKL STIFAGTTQS
KGIGNNHVGD KLKTTTISSS LDDEDPRPPT PKYEEYEQTP PSPWSQSPAP SPAVRADPKE
NPFFTDAMVD EDSFNPGSPP TSYTGMRPPE AIGVDNSWTV LHIPLTHVLL SKPTRSFKLD
TAALEQKSHL RSRDERHVSA EADQVSPEQV KRNRSSPIAV LSILSPIIPY SSNLRHSLEN
LAPHMATSFS LCRHYSNLET ELAGLRRRRP STTGFGAVAP FGSHVDGGAF LASAQALVHQ
NSLGGSITSP SDYSAISKST TASPLVTPGW EHGSLNHLVD RRQPLGSPSG SQALESYFAT
KQRLVVKEAS NSATQRPRTL SKDSSPTEKR HSSLAGVRFG NEAASSPQQS VAERGYFESE
DSMTKPQKEE EEDEEDAGAL SSSGGGASEL VSDKAEDGGK ADLNTNNDAS HYGHSVLHSY
GADFSSTFQS LPPSSSLSAR LPPPPAVPPR SGSLTSMAGD MPPPSDRLKG LILDSLPAHV
FVSLPQTGET VWVNSRFLSY RGQTVADLSA DPWGSIHPDD RAGYLKAWGH SLRTGEQFSR
SVRIKRFDGA YRWFYARAVA SKDKRGVIMQ FLGSYMDIHD QHIAELKAAR QEEIEASEAK
HRLLANLIPQ IIFTATEDDA ITFANDQWLS YTGQSFEDSL GLGFMDHVHP DDLARCRIPI
EHGGQPSNDA QSPPEEKGHG GASSSGTQTT PTARNAQQQP AVGKSGMRNV QPALSRASSS
GSESIYSLPS AELTELARKG IIKVTTDTSG RLSYTTEVRL RSKTGEYRWH LIRCVEIDTF
DFGRGASSYF GSATDINDHK LLEAKLKEAM ESKGRFLSNM SHEIRTPLIG ISGMVSFLQD
TTLNEEQRDY TNTIQTSANS LIMIINDILD LSKVDAGMMK LKYEWFHTRS LIEDVNELVS
TMAIAKRLEL NYLVEADVPA WVKGDKVRIR QVLLNVIGNA IKFTAEGEVF SRCRVYTEED
PAVCNENEIM LQFAITDTGR GFTKEEAELI FKPFSQIDGS STRQHGGSGL GLVISRQLVE
LHGGKMEGTA IPGKGSTFTF TARFTLPSPE DHPNIPISPG STASTGSRQG SSENVNHQTT
GLSAVEELRG SSSSSREGEE EGANPKGIDP ASPVSACASG GLEPLSRPPR YLTGPPSSAS
GHSGLARFSE AAKASGQDLS QMKLEMAVDR GSPSRPSTSE VGSPRPKSDL RPPLYSILII
CAQHHSREAT TQHIEMTLPK DVPHRITAIA SIEDAEPFLG GEDAMRFTHI VLNLASAEAI
IDVMDRITKS QKIEGTTIVI LCDSVQRQAV QKLAADTKHE RFLSENLVTF IYKPVKPSRF
AVIFDPEKVR DLSTDRNRST AQQMVENQKA SYQEIEKRMG NKGYRVLLVE DNPVNQKVLN
KYLKKIGVEV EVAVDGVECT EIVLSKPHSY YSLILCDLHM PRKDGYQACR EIREWEKLSS
LPKLPIIALS ANVMSDVQEK CVAAGFSDYV TKPVDFIDLS RAMAKFF
//
