ID S7ZNC1_PENO1 Unreviewed; 991 AA.
AC S7ZNC1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PDE_07140 {ECO:0000313|EMBL:EPS32180.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS32180.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS32180.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB644414; EPS32180.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZNC1; -.
DR STRING; 933388.S7ZNC1; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_012737_0_0_1; -.
DR OrthoDB; 12386at2759; -.
DR PhylomeDB; S7ZNC1; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
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:SF72; 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:UP000019376}.
FT DOMAIN 408..652
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 856..985
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 776..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 915
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 991 AA; 110484 MW; 6A44B30F52714338 CRC64;
MAFFPKADGT ILRPAGSVVP PRPSRQTTVG PIYDLVNYEN PIKPWSSDVE KTFYTKESTN
LVTPIPEKPP TFSHRYLRAF LAENERLRLS VLWYYTRGIL EEDELLAGLQ EKAQLAQEST
EWEFAVVGIL DINVYSRLAT VGLELGNLPR GETICAHTVT QPPGNVFLLP SLMEDWRFQK
CPYLEDGKLH AYAGVPLRFK TESGPTVSLG SLCVASGQSR EPLTKAEHQI LVRLGDWIVA
DLVQCTRARR QRDRLRMSEL LAQAQRQMDM NKTVSTAPII DILRQVYPGA EIRVHPSRVT
HVEFGGLDPI SVEELEKGVW ENTKYLDDFI ANLNHLPTPT NQPARIISAP CDGVSGPCLL
LVAINDFHHV FDDADAWFVQ ACAGVLSQMW RKSLLAEAMI AKEKFLRAFS HQLRTPIHGI
LGSVELLTEE LKSRSLLGDS ISTSAVEPVT ASERNHGEPS TYLDIIKMAG RDLTAIIDNL
IMLNKWSDIA MAERIYKMHT FDELETEVAN EIARFTSGDS RYTCSVFLDR KSQDEHLVKF
FTDIAVLRDT LLPLVINALQ HSPSGVVSIT TSLSTDTKQL VVDIEDNGSG IPASDHERIF
EAYEKVDSHS AGAGLGLTLA SKFASLIDGS IELVSSEVGR GSHFRATFDQ IHCGSVDSVP
QPLAKSLGDM PLRFYQLLSD SDLCLADRFT SFLLHNGFSR SESPQNCLIV FEAEVDMDRH
LKKLGQIDHD QVAICLVPEK RSPQRTERNV VYIRGPFRVS AYRAALQTAL KYHQSRATHP
RPPTLSQSKQ LHNIPLTSRE ETKNTTETGS SLVTLNQPSH SVLDTAQPHL NEAYLENPIT
LSSLTLSSPR STSHPMTLIV DDNFVNLRIM ESYCSKRKLP YLSAVNGRQA VEIYTKHQTQ
QSSGLGPQIE MIFMDLQMPV CGGIEATRQI RQLESSNNWI KSAVFVMTGQ DSPSDREATE
LAGVDEYFVK PVIVKQLDLI VKKHFPAFAG S
//