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Database: UniProt
Entry: S7ZNC1_PENO1
LinkDB: S7ZNC1_PENO1
Original site: S7ZNC1_PENO1 
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).
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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
//
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