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
//