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).
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; 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
//