ID A0A0D1Z737_9PEZI Unreviewed; 1305 AA.
AC A0A0D1Z737;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PV09_00714 {ECO:0000313|EMBL:KIW08777.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW08777.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW08777.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW08777.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN847530; KIW08777.1; -; Genomic_DNA.
DR RefSeq; XP_016218646.1; XM_016353493.1.
DR STRING; 253628.A0A0D1Z737; -.
DR GeneID; 27308687; -.
DR VEuPathDB; FungiDB:PV09_00714; -.
DR InParanoid; A0A0D1Z737; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000053259; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 4.
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; 2.
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:UP000053259};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 208..263
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 303..355
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 395..447
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 487..539
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 579..631
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 671..722
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 744..968
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1114..1233
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1249..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 151..181
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1249..1264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1163
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1305 AA; 143087 MW; A88E1266D86E5F3A CRC64;
MPSSETTAAL AAILSNIAKS HDPRQSASFK AQIAVNGSPL PQPVLPGEPS PEKETLEREL
AALIARVSYL ESRAANSSAF PMTPSEPGLP PVYPTDALHD PPRTTSIPST RRVSAARDSR
TKWMNEWLAE EPTAGAPLSP QLTEEQLSYI KEHLNRQSDQ LRTQREQIDD LSAQISTQKQ
AHDNSFAHSI EDIGALKREL VKHQQANLAF QKALREIGTI ITAVANGDLG KKVLIHAKEL
DPEIATFKKT TNRMIDQLQE FASQVTRLAR EVGTEGQLGG QAYVPDVKGI WAELTDNVNL
MAENLTNQVR EIAQVTTAVA HGDLSKKIER PAKGEILELQ QTINTMVEQL RSFATEVTRV
ARDVGTEGVL GGQAQVAGVQ GMWEDLTISV NAMAMNLTTQ VRDIAEVTTA VARGDLQHKV
QADCKGEILE LKTTINSMVD RLQQFAQEVT KIAREVGTEG KLGGQATVHG VEGTWADLTD
SVNRLSMNLT TQVREIAMVT TAVANGDLTK KVQADVQGEI LTLKNTINTM VDRLNAFAFE
VSKVAREVGT EGILGGQAEV EQVSGKWKDL TDNVNTMAQN LTTQVRSISD VTQAIARGDM
SRRVEVHARG EIALLKDTIN DMVARLDDWS LSVKRVAREV GVEGKMGGQA DVDGIAGRWR
EITVSVNTMA QNLTAQVRAF GEITTMAMEG KFTSIQVEAS GEMGELKGKI NSMISNLRDS
IEKNTQAREA AELANKTKSE FLANMSHEIR TPMNGIIGMS QLALDTELSS YQREMVTIVH
NLSNQLLTII DDILDISKIE ANRMVMEEIP FSLRGTVFNA LKSLTTRAND RNLDLAYAVE
QHVPDFVVGD SFRLRQIILN LVGNAIKFTE HGVVQVRIKS EQTESCRPDE YMIQFAVMDT
GIGIKADKLS LIFDTFQQAD GSTTRRFGGT GLGLSISRRL VNLMNGEMWV ESEYGVGSTF
NFTCKVRLAD PDLSIIAPQL AAYRKRPVLF VDRNKTGFSR EVMEGLQALQ LLPDRIAPDE
ELPGADAPSR QVYDCIIIDC NDTAQQLRES ERYKYTPLVM LTPNISVSFK NALEDGISSY
MSTPCLPIDL GNALIPALEG RAAPPVSKNS KSLKILLAED NAVNQRLAVK ILEKYNHKVT
VANNGLEAFE KVKLDRYDVI LMDVQMPIMG GFEATANIRE WEQENGVPRT PIIALTAHAM
VGDREKCIQA QMDEYLSKPL KQNQLIQTIL KCSTLGGALL EQSNISTTES EDSNALSLSG
SQQAPKRPGL DVRSTTEFGP ASPSIVTVDQ ADPFNAQLLM RSHSG
//
