ID A0A0L1IWG7_ASPNO Unreviewed; 1225 AA.
AC A0A0L1IWG7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Sensor histidine kinase/response regulator {ECO:0000313|EMBL:KNG83844.1};
GN ORFNames=ANOM_007364 {ECO:0000313|EMBL:KNG83844.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG83844.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG83844.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG83844.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) 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:KNG83844.1}.
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DR EMBL; JNOM01000243; KNG83844.1; -; Genomic_DNA.
DR RefSeq; XP_015404767.1; XM_015552620.1.
DR AlphaFoldDB; A0A0L1IWG7; -.
DR STRING; 1509407.A0A0L1IWG7; -.
DR GeneID; 26809168; -.
DR OrthoDB; 12386at2759; -.
DR Proteomes; UP000037505; 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, ECO:0000313|EMBL:KNG83844.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 604..869
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1095..1214
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 270..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1082
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1144
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1225 AA; 136800 MW; 90BD152B5F461EBB CRC64;
MHSRESSGEG WEGGPRKYAY NREGAREREM HLYLPYWGFS DSEKHAQQSI GTHPNVSRDN
VLTVFAQLAA LRMGAQRALI SLFDKSMQHV VAEATPGLSL RGTETCERTE ALWLGVCRLP
RQKIAMCYHA VRSFVEDGED IFVATDLAED ERFKHHPSVT AYPHNRFYVS VPIQSPDAYV
IGSVAVLDDR PRDGVRDEQV RFLKELSATV MDHLLSQRAM REEYREEKMV RALGLFVRGK
SDLNEWFYSR NSPDKKYGSK MAHINRRLEQ LQVSVSSPDE DEEQQEWMDK DGEATTGKAK
ENKKYKYRSP VRKFGNQQDS KKEDEDEVDN KKSKRQRPRL SPTTSQLQET LAPSNVRSVV
NRAASLIYQA LDVEGAMFID ASVYARRQTM GSTETTHDTP EAYSIGNQVD EDQVPSASCP
ESGFQGSTDN EKEARSLVLG HFTSSTSDQA ENLKNSHYIS LSGAFVSHLI DQYPKGKIFH
IEEDGSIALS YEGLADEMDY SENGGRGAQT TEAQKKDVQQ ETMDIKQLMK VLPDARCIAI
FPVWDFQRSR WFAVNLVWTD DPGRVLSEPK DLTYMAAFSN TVMAEVSRLD LEAADRAKGD
FISSISHELR SPLHGLLGTV ELLQDMVNSY AQRSLIETIY SCGRTLLDTL NHLLDYAKIN
TLTRPRLSDM AGRQGGTDVS KPQSAAPGFL QDEDLGVLAQ EVIEGLLAGA EYQRRGPNGN
NGVAMKNNVN TPESRLMTIV DIEWQDSWQF SVYAGAWRRV VMNLFGNALK YTRTGYIRLL
MKKDTLITDG KGPSAAVHIT ISDSGRGMSE DFLKNHLYSA FLQEDTTSPG LGVGLHLVHQ
IVKSLNGQIK FTSEVGRGTS VDVVLPVTPP ERSTSVQSSD YTGLRDRLNG MTVSLFTRSS
QMGDLGFDQQ TFEDVLSSLG RMVSGWFGLR VLSHDELTYE QPDFAIITEH EYYKYYRQGS
NEPAPDSSEI KPSLPLIVLG TRTSSWKALG ETVDDSVIFL TQPVSPKTLS TAFEHCLGLS
GHSEESMPKS DHCPHRPARK ISQGSNRGPE VQANNSKPEH LQQTDVDGDD AATSDDKQES
SNSEGEAQVN YMPGNILLVE DNQVNLKIIE MCVKSAGFKY QTASNGRDAL EKFKADRYDA
VVMDISMPVM DGLTATREMR HFERTKKLPP ATIIILTAVL SASMQHETMI SGANMFLTKP
TSLKQLKEIL QKLSEGKDVS DEMSS
//
