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Database: UniProt
Entry: S7ZCK4_PENO1
LinkDB: S7ZCK4_PENO1
Original site: S7ZCK4_PENO1 
ID   S7ZCK4_PENO1            Unreviewed;       712 AA.
AC   S7ZCK4;
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_03286 {ECO:0000313|EMBL:EPS28340.1};
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:EPS28340.1, ECO:0000313|Proteomes:UP000019376};
RN   [1] {ECO:0000313|EMBL:EPS28340.1, 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; KB644410; EPS28340.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7ZCK4; -.
DR   STRING; 933388.S7ZCK4; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_000445_114_15_1; -.
DR   OrthoDB; 1222064at2759; -.
DR   PhylomeDB; S7ZCK4; -.
DR   Proteomes; UP000019376; 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; 1.
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; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43719:SF77; TWO-COMPONENT SYSTEM PROTEIN A; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 1.
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); 1.
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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000019376};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          189..262
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          264..315
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          330..553
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          588..705
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          24..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         640
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   712 AA;  79022 MW;  97DE29B0AED583CF CRC64;
     MALEQQMVQF NLQDCRPLDF DMVITPPSEN EHESHDKMVN PPRYDRGTVQ TPPSPSGPGP
     ADPMSRIYRF TPTPTMVLNE SLQIVELSES YLALVHRRRE NLLTRSLYDL SPHLVSAPDV
     ASLSGVLATA ISTRAPQVLQ VAPAAKYQPD RQLRVTPIFE GNSLIYVLLE MHPIQTELPP
     SQSAEQEISE ETYKVLIDAV KDCGIFMLDT RGHVATWNKG ASMLSGYSTD EILGQHFSIF
     YGADDRVAQK PARELEMCVQ NGKVEDEGWR YRKDGSRFWA NVLLSPVYQQ GRLAGFAKVT
     RDLTERRSAE ARLIEAYEES SKMKMEFLAN MSHELRTPMN GMLLALTTLM KTPLTGDQQE
     YASILEDSTT ILLQVINDVL DYSKLSSGSF SLTTDVLNVP SIVNAVVRNC QPSLKAGVVL
     ESTIAPGFPE NTKGDPLRFR QVLQNLVGNA VKFTEKGYVR VKASYAVHPS DSQAYVISIQ
     VEDSGIGVPE TAANTLFTPF TRFADSATRR YQGTGLGLSI CKSLAELMDG VVGFHNNPQQ
     PGSVFWLTVK MSRVERPVAR LFRSLQSSGE SPVVDTSVML QRVAAQKQIL LVEDNKVNQT
     IMLKLLGTLG FQKVEAAWDG AEAVRLVKQK PLAYHVILMD ISMPVMDGLT ATEQIREMKV
     NVPIIALTGH ALKGDAETYL SRGMDDYIAK PLHRQQIIDV LWKWCGSDSH GS
//
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