ID A0A421D495_9EURO Unreviewed; 1227 AA.
AC A0A421D495;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Sensor histidine kinase/response regulator {ECO:0008006|Google:ProtNLM};
GN ORFNames=CFD26_102129 {ECO:0000313|EMBL:RLL96927.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RLL96927.1, ECO:0000313|Proteomes:UP000215289};
RN [1] {ECO:0000313|EMBL:RLL96927.1, ECO:0000313|Proteomes:UP000215289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL96927.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) 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:RLL96927.1}.
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DR EMBL; NIDN02000094; RLL96927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421D495; -.
DR STRING; 1245748.A0A421D495; -.
DR Proteomes; UP000215289; 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; PTHR43719:SF11; HISTIDINE KINASE G7-RELATED; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE 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:UP000215289};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 622..885
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1100..1219
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1149
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1227 AA; 136323 MW; FB34A3EAAEFBD502 CRC64;
MDSPASSTQG RDAGPRKYAF NREGAREREM HLYLPYWGFS ESEKFAQQSI GKHPNVSRDN
VLTVFAQLAA LRMHAQRALI SLFDKTMQHV VAEATPDLSL RAADGRDKAD ALWLGVRRLP
RQKVTMCYYA VKSFIEEGRD IFVANDLTSD DRFKNHPSVT GHPHNRFYVS VPITSPDDYV
IGSLAVLDDR PRDGVTEDQE HLLKELSATI MDHLLCQRAM REEYREEKMV RALGLFVKGK
SDLNEWIDSG DARDKKYGGQ FAQLNKRLEK LQVSQSSGQD AEDGKGDAGN AVNAVNASNA
SNDQVKKMTK AGNHGRHGSP VQRFKQDGEE EADEEVQRRK PDEKSHKKHR PMLSPTTSQL
RDSLAPSNVR SVVNRAASMI YQALDVEGAM FIDASVYARR QTVGFTDSKL DDPEAYNGQR
QVDNNSGEEQ APSPSNPESR SDTDASDDDS QSRSLVLGHY TSSTSEGGVN LKDSHYVSLS
GGFVSHLIDQ YPRGKIFHVE DDGSISLSYE GLADEMGYSQ TGSRGAMSTE PEKKDIQQET
TDIKEMMKVL PEARCIAVYP VWDFQRGRWF TVCVVWTNDP GRVLSEPKDL TYLAAFSNTV
MAEVSRLDLE AADRAKSDFI SSISHELRSP LHGLLGTVEL LQEMVNSYAQ RSLIETVYSC
GRTLLDTLNH LLDYAKINTL TRPRPSDRAG GHATDVSKPQ TAVPGSLQDE NLSVLVQEVV
EGLLAGAEYQ RRGANGDSDA LAKKEDLGPK DRLITIVDIE WQDSWQFSVY AGAWRRVVMN
LFGNALKYTQ TGYIRLRMRR DSLLVDGKRT PAIRMTFSDS GRGMSKDFLT NHLYSAFLQE
DTTSPGLGVG LHLVHQIVKS LKGQIKFSSE VGKGTDVDVV LPIEPPEQSS PSSPRSFAPL
KEQLSGKTVS LFTRSSKLGD LGFDSRVFDR IRTSLGRMVT GWFGLRVLSP DELDTTKPDF
AIVTEYEYRN YYIEGSNEPK PDGGEIQPAL PLIVLSARTS SWKTLGDSVE DSVIFLTQPV
SPKTLATAFE HCLGRPERSS TSTPRNLPSP VQEDKIPDVD KMFENRRNGE KDQVLDSVLG
RAVNGEAGQQ QPSNRKGAKN ILLVEDNQVN LKIIEMCVKT AGFAYDTAKN GLEALEKFKA
DTYDAVVMDI SMPVMDGLTA TRQIRSFERK TKRPPTTIII LTAVLSASMQ HEAMMSGVNL
FLTKPTPLKQ LKEILRNLSD GKDVSQN
//
