ID W6Z1R3_COCMI Unreviewed; 2010 AA.
AC W6Z1R3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Histidine kinase HHK2p {ECO:0008006|Google:ProtNLM};
GN ORFNames=COCMIDRAFT_8705 {ECO:0000313|EMBL:EUC41589.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC41589.1};
RN [1] {ECO:0000313|EMBL:EUC41589.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC41589.1};
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; KI964095; EUC41589.1; -; Genomic_DNA.
DR RefSeq; XP_007691873.1; XM_007693683.1.
DR STRING; 930090.W6Z1R3; -.
DR GeneID; 19126974; -.
DR KEGG; bor:COCMIDRAFT_8705; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000263_0_0_1; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000054032; 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};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 965..1035
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1038..1090
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1097..1152
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 1873..1995
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..285
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 405..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1533..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1569..1696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1539..1554
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1569..1662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1663..1677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1678..1693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1925
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2010 AA; 219852 MW; 72175282BD6881B3 CRC64;
MTKAPTPSPD SKRAPSTTAT PPTPRPPLQR LAASDAKSYP AQTSQTSPRT QQPPNHRDDE
AADIDMSDTD SRHCDDQPAA DSQADETPTE STPHPPQGNV SPDELEVERL RRLQLKVLQQ
QQQQQRARLR ASANSPNANT PGPRRISPIK EEPMPGISPT LEGAFSSPTP SPNPLPTAVT
ASTASTESTE SARTIRGSMP PTPAAHPLRT PSYPFPTVPN TPRWASAFHM PFTNLSPTVS
AGQSREYTVA RERIASESST PAACNTPFAP GGRQHSSPAI EDPRFPSPNL YDVVLRLGVE
PGLAAWWTTV TSIMRDHYGA ERVALAVPAD ASDIENVPWG QKATFTASAN DASAYAATYQ
ESAGQGSNLQ PENTSNPQEG ESGDVPPTTV IPERRPKLFS HHSFAGHERQ KPTMSPDTPM
PAQPIRPRGP LRSASHAPHM GSRPDHPLRQ VSQASFDGMS SAFAESTPTG GPTFSDPEFS
SIGEPSPPSA VYHVLRALDH EPDALIDNSG VNRVLERGRL VTLTRDYSTS FSTSKENLDK
DRTDPVKPSA VQGSAAAQEA LKLAAARGRV GLGSSDPRLP PRYEEYEQYP ASPWAQSPAP
SPAIQNDADA NPFFATGNVD EETFNPSRSP PDYTQYGMVE AIGVDKASTV THIPLIHPTL
SQTMAPTDTN TPSQTPAMSR RQSEQSVGTS FHQGDFVRKA PIAILSLLSP IVPYPRNLTN
SLKHLGPHLA TSFSNAWHFT NAQTQVASIR QRRAATVGAG GMTMSSDSDS LEDLLHLDLG
DITNSAAGSV TSPSDYSSRS RHSPGGSIAG TPGWDTSLGF SSRHSHSGTP GHLAGSEAVE
SYFDARRQAN KTNNNTTSNS QEQSSRKTDK RPGKRVTVNP VAESVKEDPS KPREDKKDEA
SSPRRAQAQD TTKRGHSFLH SYGADFSSSF QSLPAATTPG GRPQMTQGTV RTMSTTETSE
MPPPSESLLR TIIDSLPVQI FTAAPNTGAI SWVNSKFLIY RGQTSRQVLQ NPWDSIHPED
RDAYLEEWGR SLRTGQQLQM KVRLQRFDEC YRWFYVRVAP LRNKRQQIVH WIGTNMDFHE
QHIAEQNSAR QQETAASEAK YRALANSSPQ IVFVVSDRRG LTFCNSQWIS FSGQSESQAL
GNGFLEHVHP DDVIKCKLPE LDEHGVANVP TSLPPEHGHD 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 PPANLQQLQP
SALQKFVQSQ NPGHVPLKRV SSVSSEKSET AKSPVPSVTT SERSRDSPAL SSGSSEHSLT
SSALTGQSSL RSERSSASSY MHETSTASSA NMNLALPPKR SNSDQETRPD ESSTSVDSDE
TVRQGSPHRS LSPLGSALQP PMYSILVVCP LEHSREATIR HIKNTLPQGI PHQVTGQASI
IGAQKMMGGE NPVLFTHVVL VLHDTAEVHA IVDQIFSSTA YSNTSVVIVS DPSQKKELMK
EAPVYDYEQL HNDRRLEFVY RPLKPSKFAI IFDPQKQRES STDRNQDSAQ QVVVSQKLVF
EELKRRVGGK NHKVLLVEDN KINQTVILKF LARIDIATET VLDGVQATEA IFSKPPGYYS
IVLCDLHMPN KDGYQACKEI RRWEKKHGYR RHPIIALSAN VLGDVYAKCA EAGFNSYVTK
PVEFKELSIA MTKFLDPADP SKPPALMKKK
//
