ID A0A1V6TX93_9EURO Unreviewed; 2348 AA.
AC A0A1V6TX93;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENFLA_c002G07545 {ECO:0000313|EMBL:OQE30968.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE30968.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
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 -!- 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:OQE30968.1}.
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; MLQL01000002; OQE30968.1; -; Genomic_DNA.
DR STRING; 254877.A0A1V6TX93; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000191342; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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 Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR43047:SF46; HISTIDINE KINASE_RESPONSE REGULATOR, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G12550)-RELATED; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000191342};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 62..387
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1914..2137
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2176..2299
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 60..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2305..2348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2324..2338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2230
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2348 AA; 261154 MW; 4480D3CA8C38229E CRC64;
MEESTLFGDD LPLPPARLFE RLSQLPGYTW DQAVEPFHST YNHWHISGYR HALEPDVLTP
LADSSNPASS GPSSLTRFSP RTEIRPSARA LRRLSASETS SEISLSNHHS LETDQTWIPV
IARISTNIIR LEREFHMLRS IVQSSDPDCN HTIRPVDLIR LQPDDGHSKT LLVAIFESPG
HDRLRDLVTF GPASFAAGSR GEDNNATPSE QVSLQAFFDF AIGACDCLEI LHYGLKTVHG
EIRGDAFHFS AETGAVKLAN TGNGARSFDN VLSEGWSSVS RELGAKYKLQ FIAPEQTGRM
PTEPDSRTDI YALGLFFWSM LVGKLPFEGT DPVDVVQNVL GKRLVPVSGK RMDVPDALSA
VIQKMTQKVV HDRYHTISSV KRDLTYIAKL LGDGDSEALS NFQVAQGDVS SFFTLPTQMF
GRQQEYDKIM NIIEKVNKRQ AIALAKAGTQ SPGTMHALTS ASSISESRIE SLEFASVSSD
SGSFNLPPRS SSNATSHHLA QVTTHESAPG SDTSFSTPKH TIVTDAYCQS PGAVSTRVKS
PSHSRSSHNT DRDSHPSIGP LSQPSTNHTV SQSGSLHSLN KPKNSGKSRR SERCEVIAIS
GPAGIGKTDL LNRIQPTVRK LGCIAITRLD RAKRVPFEPF AKLLASLLRQ IFSERDVTTD
YHNNVRMALR PMWPTLHRVL DLPEQLMSPG AKYRPTEAKA NLLMPDKGEP SKHVNIPGLD
QGQTSQDFFL ANAASKNMRL METFLEILRT LCHFKLITIC LDDLEHADDE TLDLVMKIIK
AKLPCVLILS SRKDEIPSDQ VRSLFEEDLP TITRIALEPL EEKHVMEIVA TTMHQKPDQT
LTPLCAVVQE KSRGNPFYVR VMLETCYRTN CIWYSWKDSK WLFDLDRIFT EFVAPVYGEG
LGLGFLTKRL QDIPQAARSI MVWGALLGSP FSFSLVQKLL TSEFLYSSND DDAVDLTTPQ
NVTLIRQSEG DIVVGLQFLV QANLLNTGKT DDEFRFANER LAQAALSLSE SRNVEKMHFI
VSQALMKYYH DHRSRYSMAH HVALASPTIK SRVSRRLEYR RILWDAGQTA FQSGARPSAL
WYFRHAIALL QDDMWNDLQP DVYYDETMRL FITTSEMSWS QGHNDDALQL INEVFVHGKD
AVSKSRAWII KAKIFAQIGD HHRSMESLLT CLDELGVHLR EPTTYEECDA AYLRLKSYLE
TADMRSIIHK PVSKDPTIET IAAVMSEAMT VTYWDDALTF YRMALEKMNI HIFKGGFTPI
AIGCSHLAMI ALSRFKDSEF GIRLSDLSLE LLEHCPDLST QSRGSIVHNL YVSHLRVPMA
STLPALEASL EASFSMGDPY LTLISISSMA MTRLYLGQDM AQLEAFCVET PEEIPKWQQD
TRGGASLIAV QQVARALQGK TDFRSADSIM SDANHNTTEY MLHLDVNSSN ADRPRDIYWG
LAMIPLFMFG HHTRTIQVGT QLLFTRHRLW SARVSYLIYF YLAASLLTLH NDNPSQGYLD
GKMDTVLEYK AEIDFARAAS EANYGMWALI LEALISEVRN DHSAAIQGFE SAIDHCQIHG
WPLEEALALE LQGEFLVRRG AKRAARAVIQ DAIASWSSIG AGGKSSQLAE KHEWLLKTAT
SAKTVDVGCQ TIDSLLEISR DVVQEEVLIP QQMEEDERRQ QWIEQNGVAA GERSLDISSV
GLDIIDLSSI LESSQVMSSE LQIDKLFMKM LEIILESCNG SDFAIIATDF DDNNGFAIAA
AGDSEKGQQS FPEGLPFSEM EDRMALHISD YVMRTKEEVL VHNVLEDERF SNVSETYLAN
FPTGRSVIAL PVVQGDRLLG VIHLEGKPNW FTQRNVVVLH LLCNQIGISL SNALLFREIR
KVSAKNASMI ESQKRALALA REAEQKAKIA EAEAKHNVKL KEDAARAKSI FLANISHDLR
TPMNGVIGLS ELLKGTYLDK EQDEYVESIR VCADTLLTLI NDILDFSKLE AGKMKISTVP
LNLKQTISEV IRALRYTHRD RGLETIENLD KVPPELVVLG DPVRLHQIFM NLLSNSYKFT
PAGSVTVKAR VAREGKGRVR LECSVSDTGI GIPDEQKARL FRPFSQADAS TERSYGGSGL
GLSICKAIIE DVLGGAIWLE SKSGVGTTVT FHLVFNKAPK KTAVKTAWSQ DLSNAETEAR
RSSARDLTQI PRDQIRVCIA EDNPINQKIA VKFVTGLGLQ CNAYSDGKQA VDALRASSQE
GNPFHVVLMD VMMPTLDGYN ATRELRRDPD PNVNEVLVIA MTASAIEGDR EKCLEAGMNN
YLPKPVRSPI LSELLDKYLA PVPPSYPKSR LAIREKRSKA SIDGGGGTPT SYSSSASDEP
KPFPLEKK
//
