ID M2V6K9_COCH5 Unreviewed; 2013 AA.
AC M2V6K9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Histidine kinase HHK2p {ECO:0008006|Google:ProtNLM};
GN ORFNames=COCHEDRAFT_1211307 {ECO:0000313|EMBL:EMD95358.1};
OS Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS corn leaf blight fungus) (Bipolaris maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=701091 {ECO:0000313|EMBL:EMD95358.1, ECO:0000313|Proteomes:UP000016936};
RN [1] {ECO:0000313|EMBL:EMD95358.1, ECO:0000313|Proteomes:UP000016936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
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).
RN [2] {ECO:0000313|Proteomes:UP000016936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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DR EMBL; KB445571; EMD95358.1; -; Genomic_DNA.
DR STRING; 701091.M2V6K9; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000263_0_0_1; -.
DR OMA; WGQKATF; -.
DR Proteomes; UP000016936; 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 NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43719:SF76; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK1; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13188; PAS_8; 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; 2.
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:UP000016936};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 964..1034
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1037..1089
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1096..1151
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1233..1287
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1298..1525
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1876..1998
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1533..1557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1585..1699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1539..1557
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1585..1684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1928
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2013 AA; 219999 MW; E4B99CFCC9D57065 CRC64;
MTKAPTPSPD SKRATSTTAT PPTPRPPLQR LAASDAKSYP SQVSQTSPRT QQPPDHRDNE
AADIDMSDTD SRHCNDQPAA DPQADQTPTE STAHPPHGNV SPDELEVERL RRLQLKVLQQ
QQQQRARLRA STSSPNANTP GPRRISPIKE EPMPGISPTL EGAFSSPTPS PSPLPTAVTA
STASTESTES AKTIRGSMPP TPATHPLRTP SYPFPTVPNT PRWASAFHMP FTNLSPTVSA
GQSREYTVAR ERIASESSTP AACNTPFAPG GRQHSSPAIE DPRFPSPNLY DVVLRLGAEP
GLAAWWTTVT SIMRDHYGAE RVALAVPADA SDIENVPWGQ KATFTASAND TSAYAATYQE
SAGQSSNLQP ENTSNPQQGE SVDTPPTTVI PERRPKLFSH HSFAGHERQK PTMSPDTPMP
AQPIRPRGPL RSVSHAPHMG SRPDHPLRQV SQASFDGMSS AFAESTPTGG PTFSDPEFSS
IGEPSPPSAV YHVLRALDHE PDALIDNSGV NRVLERGRLV TLTRDYSTSF STSKENLEKD
RTDPVKPSAV QGSAAAQEAF KLAAARGRVG LGTSDPRLPP RYEEYEQYPA SPWAQSPAPS
PAIQNDADAN PFFATGNVDE ETFNPSRSPP DYTQYGMVEA IGVDKASTVT HIPLIHPTLS
QTMAPTDTST PSQTPAMSRR QSEQSVGTSF HQGDFVRKAP IAILSLLSPI VPYPRNLTNS
LKHLGPHLAT SFSNAWHFTN AQTQVASIRQ RRAATGGAGG MAMSSDSDSL EDLLHLDLGD
IANSAAGSVT SPSDYSSRSR HSPGGSIAGT PGWDTSLGFS SRHSHSGTPG HLAGSEAVES
YFDARRQANK TNHNAASNSQ EQSSRKTDKR SGKRVTVNPV AENVKEDPSK PREDKKDEVS
SPRYAQAQDT TKRGHSFLHS YGADFSSSFQ SLPAATTPGG RPQVPQGSLR TMSVTESSEM
PPPSESLLRT IIDSLPVQIF TAAPNTGAIS WVNSKFLIYR GQTSRQVLQN PWDSIHPEDR
DAYLDEWSRS LRTGQQLQMK VRLQRFDECY RWFYVRVAPL RNKRQQIVHW IGTNMDFHEQ
HIAEQNSARQ QETAASEAKY RALANSSPQI VFVVSDRRGL TFCNSQWISF SGQSESQALG
NGFLEHVHPD DVIKCKLPEL DEHGVANVPT TLPAEQGQQD SNASDASSET ERTITSPSGS
SPDRMDLPQA KLSKLASTGI LRVVKDAHGR ASYSTEVRLR NKDGDYRWHL VRILLEKSLA
ETSDEETWYG TATDINDHKL LEQTLKETMD AKSKFLSNMS HEIRTPLNGI SGMVNFLLDS
VLNTEQLEHV NIIKASTDSL LNLINDILDL SKVEAGMIKL SMEWLHLPSL LEEVNDLNMG
LAIQKGLELN YLVDEGVPAE VKGDKFRIRQ VLLNVVGNAI KFTEHGEIFI RCKLQPSDRS
RPLKENETMI RFEVVDTGQG FTDAEAKYLF KRFSQIDASS TRQHGGTGLG LAISMQFVEL
HGGRMDARSA PGKGSTFFFT IKFGLPTADD YPKPLVSTPG TPAFEPPIAP PPANLPQLQP
SALQKFVQSQ NPGYVPLKRV SSVSSEKSES AKSAKSPVLS VTASERSRDS PALSSGSSDH
SLTSSALTGQ SSLRSERSSA SSYMHETNPA SNANMNLALP PKRTNSDQET QPGESSTSVD
SDETVRPGSP HRSLSPLGSS LQPPMYSILV VCPLEHSREA TIRHIKNTLP QGIPHQVTGQ
PSIIGAQKMM GGENPVLFTH VVLVLHDTAE VHAIVDQIFS STAYSNTSVV IVSDPSQKKE
LMKEAPVYDY EQLHNDRRLE FVYRPLKPSK FAIIFDPQKQ RESSTDRNQD SAQQVVVSQK
LVFEELKRRV GGKNHKVLLV EDNKINQTVI LKFLARIDIA TETVLDGVQA TEAIFSKPAG
YYSIVLCDLH MPNKDGYQAC KEIRRWEKKH GYRRHPIIAL SANVLGDVYA KCAEAGFNSY
VTKPVEFKEL SIAMTTFLDP ADPSKPPALM KKK
//
