ID A0A139IAI9_9PEZI Unreviewed; 1208 AA.
AC A0A139IAI9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AC579_7023 {ECO:0000313|EMBL:KXT11659.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT11659.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT11659.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT11659.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXT11659.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFZO01000187; KXT11659.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139IAI9; -.
DR STRING; 113226.A0A139IAI9; -.
DR Proteomes; UP000073492; 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; 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 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF80; HISTIDINE KINASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000073492};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 535..811
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1080..1207
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 241..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1137
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1208 AA; 133293 MW; 09443259693D2457 CRC64;
MPYSLQNRET QRYYQPWLAA HGSSLNVAKH VDSLAQLDLH KQGYSPIASR DRSLTAFAQL
VAIRLDVRRC MVSLIDTTNQ YILAEATRTH SVTRAFAEDG DELWLGSSIL ARADAVCEHS
MYSTCSGLEA DGRTYTTAGM IVNDCRADHR FSKRPYVLSE PGVRFYAGVP LQSRTGYMIG
ALAVSNDAPR DGLSAHELRY MQEVAQSAME HLEWARDRVD RFKGERIVRG MAQFIDDCSS
LRDGAEGEKS RRPTPHEQSV SSQSDPLRAP RPGLAKRVSS RNLHTQCNKP DGMSSMFASA
AEILRDSTIA DGCAIFGSTA DSGRKAVFKH PPNSYDTIYE RKSQPSPASD SDRHETGTSD
SDSSPSARPC KLMAFSVADQ HARKSIEDGT ALTVGTLDKY FALFPQGRSF SFNDEGKGIS
SEEESNSERE AETPTTTIDD SPNARVKPRN RKRHMDHKEL LKKIPGAKTV VFLPLYDHSE
EKLVAGCFLW SSTVGRISLD ADLSHLRAFS NCIIGEVIRM NMQRNEAAKT TFIASMSHEL
RSPLHGILGA AEFLAETTTD AYSAGLVTSI VTCGKTLLDT LNHVLDYSKI NKLGKTQMRR
RARQNKPVNL TSDSTLDSLN MTADVDLGIL VEEVAEAVTA GHTFKKLPGA TALAKPAHQT
SESVDALTNS SANDHARDGV SVLLDISPRR SWIVRIQPGA LRRIIMNLLG NALKYTSSGF
VAVSLRAQES SDSSKIINAL IRVVDSGKGM SESFQRDKIF VPFSQEDPFQ PGTGLGLSIV
KQIVDSLGGS VQVHSELDVG TEIDIHLSLT AAHVPTEVDA NGLPAPDSEM IETERLTKGK
HLVILDPADP NRCRAPTHRV ARFHQTIKEV CTNWFGMRVT RSTDIDVDDA DLYVFGEPPP
LEKLADHHHR EGHPEHLKRI VPIVIICEND QDAITMTRHE QETLRKLGKI VEVMPQPCGP
RKLAKAFVHC LQRAEDVRER LEDSYQTAPG PQGAGPSEES AAATNSMQPN ADAHDSTRVP
PSRTNNLRNS VSSALSYPAT TPIDPLTPSL RSPFTEERDP IPVVIQDNAP PTKSEPDPLH
LLLVDDNKIN RQLLVMFMKK CEFTYLEAEN GQEALDLYRS SISDLPNRKH FDFVLMDISM
PIMDGMEATR RIRDFEKENG IKRVTVIALT GLASEKAREE AETSGIDVFL PKPVKFGELR
KLLIQQAG
//
