ID A0A1V6RGB3_9EURO Unreviewed; 1026 AA.
AC A0A1V6RGB3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PENVUL_c045G03565 {ECO:0000313|EMBL:OQE00855.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE00855.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQE00855.1}.
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DR EMBL; MDYP01000045; OQE00855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6RGB3; -.
DR SMR; A0A1V6RGB3; -.
DR STRING; 29845.A0A1V6RGB3; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000191518; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 3.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1530; -; 2.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00672; HAMP; 2.
DR Pfam; PF18947; HAMP_2; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 5.
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; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 2.
DR PROSITE; PS50885; HAMP; 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000191518};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 79..134
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 174..226
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 266..318
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 358..410
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 450..502
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 524..749
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 894..1013
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 943
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1026 AA; 111980 MW; 759954E02587D4D0 CRC64;
MAAMVDPARP ALVSDADLMQ ARAALQHQQS PELSVPREFI SLIVDELIYR RECHSSIAEI
EHERANLRKE LLKHTHINEA FQKELREIGE IITQVAHGDL SQRARMHPLE MSPDIATFKQ
TINTMMDQLQ VFSQEVSKVA REVGTEGVLG GQAKIEGIQG IWHELTVNVN AMANNLTTQV
RDITTVTTAV AKGDLQRKVQ ADCKGEILLL KNIINSMVDQ LREFAFEVSR VAREVGSDGV
LGGQAVVHGV EGTWKNLTDN VNRMASNLTQ QVREIADVTT AVARGDLTKK VTADVKGEIL
DLKLTINAMV DRLNQFAFEV SRVAREVGTD GTLGGQAQVE NVEGRWRDLT DNVNTMAQNL
TLQVRQISNV TQAIARGDLS TKIEVHAQGE ILTLKETINS MMDGLGEFAG EVKGVARDVG
VRGKLGGQAN VAGSNGIWRS ISEDVNTMAD NLTSQVRAFG EITEAAMSGD FTKLITVSAS
GEMDDLKQKI NKMISSLRDS IQRNTAAREA AELANRSKSE FLANMSHEIR TPMNGIIGLS
SLALDTDDLQ APVRETLTMV HNLAISLLTI IDDILDISKI EANHMIIEKT PFSLGATVLS
VLKALSVETN EKALGLVYTI DGEVPDYLVG DAYRLRQVML NLVGNAIKFT DHGEIRVTIK
RAQDAKCASD ETAFQFSVSD PGIGIDESKL GLIFDKFQQA DGSMTRRFGG TGLGLAISKR
LVSLMGGDIW VTSNVGEGST FSFTCRVKLA QPPTSFADQL VPHRGRRVLF FDHGLTRSFP
VATVLKELGL DPVVVTEEEL ECGQLKTDWG CTFDAILIEN LEIAAKLRAC ADLQPIPLVI
TAHTVSLALR AAGELGVVSY ITVPCRPIDL WNGILPALGN RATRTPSGYT RSLAILLAED
NDVNQKVAVR ILEKFNHNVT VVENGLQAVK EVKQHRYDVV LMDVQMPVMG GFEATGNIRQ
HEKINGLPHT PIIALTAHAM LGDRDKCIQA GMDDYLSKPL DSSRMMQTIL KCSTMNLASS
LPAIEG
//
