ID A1CTR5_ASPCL Unreviewed; 697 AA.
AC A1CTR5;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE SubName: Full=Sensor histidine kinase/response regulator Fos-1 {ECO:0000313|EMBL:EAW06702.1};
GN ORFNames=ACLA_083970 {ECO:0000313|EMBL:EAW06702.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW06702.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW06702.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS027060; EAW06702.1; -; Genomic_DNA.
DR RefSeq; XP_001268128.1; XM_001268127.1.
DR AlphaFoldDB; A1CTR5; -.
DR STRING; 344612.A1CTR5; -.
DR EnsemblFungi; EAW06702; EAW06702; ACLA_083970.
DR GeneID; 4699941; -.
DR KEGG; act:ACLA_083970; -.
DR VEuPathDB; FungiDB:ACLA_083970; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_114_15_1; -.
DR OMA; QHFSIFY; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EAW06702.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Transferase {ECO:0000313|EMBL:EAW06702.1}.
FT DOMAIN 198..239
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 257..308
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 323..545
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 578..695
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 630
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 697 AA; 77464 MW; 024E23E4BBC42601 CRC64;
MALDKQLLHL HIGDGQPAPI NVSSIATPPD EEQLDMQTNR KDASCGNELD SMQDHQLSMN
RIFRHTPVPT IVLDSSLRVI EVSDSHLTFS QRSRDFMLGA SIYELPLSSI PAPDIATLNG
ALRVAITSRA VQVIDTIHMP RISSYFSLRI TPIFDGASLL NLVLEAHNVT RTHTESLHNA
YINETYKILV DTVRDYAIFM LDARGNIATW NSGAEIIKGY KAHDIIGRHF SVFYSSEDRL
ADKPGKELEV CLRDGRVEDE GWRYRKDGSR FWANVMITSI FQFGRHVGFV KVTRDLTERK
AAEARMVAAF EESSKMKSDF LANMSHEIRT PMNGMHLALT MLTGTELNDP QREYASIIED
SMSILLQVIN DVLDYSKLSS GSFSLNTDVL SVENISAAVM RNCKALNPAV KIISSMPPNF
PKMLRGDPLR YRQVIQNLVG NAMKFTEQGT VNVNHSFAVD DAHSNLYTVT TEVVDTGIGV
PEEAINTLFT PFTRFADSAT KRYQGTGLGL SICKSLAELM DGTVGYKPNP NGKGSVFWLT
AKMCGVDVPP AGKTYVPTTA DDTYEPMDEV KQIAPHLHVL LVEDNMVNQI VMLKLLKSLG
FERVDTAWDG AEAVRLVKQT PFSYNAILMD INMPVMNGLE ATACIRDMNL DVPIIALTGN
ALKGDAETYL AKGMTDYIAK PVHRKHLVQL LWKWLGS
//