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Database: UniProt
Entry: A0A1L9SYR2_9EURO
LinkDB: A0A1L9SYR2_9EURO
Original site: A0A1L9SYR2_9EURO 
ID   A0A1L9SYR2_9EURO        Unreviewed;      1237 AA.
AC   A0A1L9SYR2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ASPSYDRAFT_37391 {ECO:0000313|EMBL:OJJ52362.1};
OS   Aspergillus sydowii CBS 593.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=1036612 {ECO:0000313|EMBL:OJJ52362.1, ECO:0000313|Proteomes:UP000184356};
RN   [1] {ECO:0000313|Proteomes:UP000184356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 593.65 {ECO:0000313|Proteomes:UP000184356};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV878602; OJJ52362.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9SYR2; -.
DR   STRING; 1036612.A0A1L9SYR2; -.
DR   VEuPathDB; FungiDB:ASPSYDRAFT_37391; -.
DR   OrthoDB; 12386at2759; -.
DR   Proteomes; UP000184356; Unassembled WGS sequence.
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; 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:SF5; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000184356}.
FT   DOMAIN          575..867
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1095..1234
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          698..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1024..1093
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1076..1090
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1152
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1237 AA;  136539 MW;  845A95191FE24FD4 CRC64;
     MTMREPVQTG SGERIPQACS NPQYIPPYHS QSHYVPSDPG SQSIFAPEAS QDAALTSFAQ
     LGAIRLATER ALISLFDRTH QHVVAEATPT LDLVGGGYRD EKDRLRLGCC VLPKEKGICH
     HVEGLPSRET ANHDELRSED AFVVMDTSKH ERFNAGNLIE AVSDIRFYAA VPIVSPRGFT
     IGAYSVLDSK PRTTPPNQNE LEFMKNMAAS VMKHLEMEYL ALRNAQAERK MVGLGSFVEG
     RSTLRDSWQE ADAQYAASQA SGSPREGQPN IKQQDLQHFG DEEGGQDLPV RQRPAKQTNG
     TTPRIGTTNK TVRSVAAGES LQDHTLSDNT KKTFSRAANL IRESIGAEGV LFLSADSERF
     GNLVPRNTRK VSGRAPKVPK HSDDDESTDS SGASVDSIAD RELERTPVSE CLGFSTTRES
     SIDPDADAGQ AIVVPEPLFS SLIRRYPRGK IFTYNSSGSV SEDSDGSPAS RAGPDHRRRE
     KRASSRRRKP TFQQDAHSLS SIFAGARSIL MLPIWDSDKN RWFAGTLVWT NDPGQVFTFA
     DEVTYISAFT NSIMTEIRRL DVEIAEKAKT NLVSSITHEL RNPLHGILGT SDILSDTAMN
     ALQHGMVHTI ESCGRTLLDT INNLLDLTFI DKYDRKSQGR HQSRKKKPIP GAPKSPDGLQ
     SKDRGENLNF TNVKLNSVLE EVTECVFAGY SFYTHPQSPP PAMTISSSRW GGPTSKSDPV
     GPRANQVTII FDIQPDTEWN FYTHAGAWRR ILMNIFGNAL KYTRSGFIYL GLSSKQVRPD
     PSSKDSDDQE PEFEVTLTVR DTGKGIGSKY LQNGLFTAFS QEDPLASGSG LGLSIVRQAV
     GFLGGSIEIE STQNVGTTLS IRTPLAPSSD TLDNSSSSAV FQSLQRYTQD KTIGFLGFGS
     DLQSSRDTAL YSSLERLCRE WFGLEVANTS VRGVDKKFDF YLAVQTELNC EDTKGRDLFG
     LSQHLVNREG RFSPVVVICQ SPEEAHRMFV AAKSRNERFY FEFISQPCGP RKLARALDIC
     VKRQTEQRSS GLSPDEPTHW VEMPDSSHLP VDVGPSEPPS NRMKISKRPT ADTMGDGSPK
     GSSEAKSQQE MPEPSVLLVD DNDLNLQLLC AYTERDNHPY MTAKDGAEAV EVYKADPGKY
     QFVIIGSLFT DDLDISMPVM DGFEASRQIR RIEKEHRAKM SESEQKTSPR TVIAALTGLD
     STSAQKEAYS SGIDTFLIKP VKRPELQAIL RRQIHSS
//
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