ID A0A319C5Z2_9EURO Unreviewed; 1347 AA.
AC A0A319C5Z2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 28-JUN-2023, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BO82DRAFT_403235 {ECO:0000313|EMBL:PYH80685.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH80685.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH80685.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH80685.1,
RC ECO:0000313|Proteomes:UP000248340};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
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; KZ821708; PYH80685.1; -; Genomic_DNA.
DR STRING; 1448315.A0A319C5Z2; -.
DR VEuPathDB; FungiDB:BO82DRAFT_403235; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000248340; 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; 5.
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; -; 3.
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; 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; 3.
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; 6.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50885; HAMP; 6.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PYH80685.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000248340};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 237..292
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 332..384
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 424..476
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 516..568
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 608..660
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 700..752
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 774..999
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1152..1271
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 25..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 189..245
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 146..161
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1201
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1347 AA; 147748 MW; 8E9403B6FD5D739B CRC64;
MAGADETLAA ATAILRELAR ESPGAPPFDF EFSHTSSTNG CDSKVAKLPG EKSAAKVAFE
QELEALVRRV HHLEFQSVSH RSPPGITLKA FQPTLVPSEN DPETPWAFGL PRLASSDGSD
SSCLIQQHNP HRSHGSRRSA PGPEDGEAEE DIDDEDSDED EDLGSRTRLV REEDISYLRN
HVQKQAEEIS FQKDIIAQVR DELQQQEEQT RRALTKVENE DVVLLERELR KHQQANEAFQ
KALREIGGII TQVANGDLSM KVQIHPLEMD PEIATFKRTI NTMMDQLQVF GSEVSRVARE
VGTEGILGGQ AQITGVHGIW KELTENVNIM AKNLTDQVRE IAAVTTAVAH GDLSQKIESR
AQGEILELQQ TINTMVDQLR TFATEVTRVA RDVGTEGVLG GQAQIEGVQG MWNELTVNVN
AMANNLTTQV RDIATVTKAV AKGDLTQKVQ ANCKGEIAEL KNIINSMVDQ LRQFAQEVTK
IAKEVGTDGV LGGQATVNDV EGTWKDLTEN VNRMANNLTT QVREIADVTT AVAKGDLTKK
VTANVQGEIL DLKSTINGMV DRLNTFAFEV SKVAREVGTD GTLGGQAKVD NVEGKWKDLT
DNVNTMAQNL TSQVRSISDV TQAIAKGDLS KKIEVHAQGE ILTLKVTINH MVDRLAKFAT
ELKKVARDVG VDGKMGGQAN VEGIAGTWKE ITEDVNTMAE NLTSQVRAFG EITDAATDGD
FTKLITVNAS GEMDELKRKI NKMVSNLRDS IQRNTAAREA AELANRTKSE FLANMSHEIR
TPMNGIIGMT QLTLDTDDLK PYTREMLNVV HNLANSLLTI IDDILDISKI EANRMVIESI
PFTVRGTVFN ALKTLAVKAN EKFLSLTYQV DNTVPDYVIG DPFRLRQIIL NLVGNAIKFT
EHGEVKLTIC KSDREQCAAD EYAFEFSVSD TGIGIEEDKL DLIFDTFQQA DGSTTRRFGG
TGLGLSISKR LVNLMGGDVW VTSEYGHGST FHFTCVVKLA DQSLSVIASQ LLPYKHHRVL
FIDKGENGGQ AENVMKMLKQ IDLEPIVVRN EDHVPPPEIQ DPSGKESGHA YDVIIVDSVA
TARLLRTFDD FKYVPIVLVC PLVCVSLKSA LDLGISSYMT TPCQPIDLGN GMLPALEGRS
TPITTDHSRS FDILLAEDND VNQKLAVKIL EKHNHNVSVV SNGLEAVEAV KQRRYDVILM
DVQMPVMGGF EATGKIREYE RESGLSRTPI IALTAHAMLG DREKCIQAQM DEYLSKPLKQ
NQMMQTILKC ATLGGSLLEK SKESRISSSG EMHPVHHSPA DGKHQRPGME ARALTASGAM
NGGSLASPTL EKEDLTMERA LLRSNSS
//
