ID A0A0L6V9U4_9BASI Unreviewed; 1751 AA.
AC A0A0L6V9U4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 22-FEB-2023, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=VP01_229g2 {ECO:0000313|EMBL:KNZ56870.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ56870.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ56870.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ56870.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-2015) 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 -!- 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:KNZ56870.1}.
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DR EMBL; LAVV01007169; KNZ56870.1; -; Genomic_DNA.
DR SMR; A0A0L6V9U4; -.
DR STRING; 27349.A0A0L6V9U4; -.
DR VEuPathDB; FungiDB:VP01_229g2; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000037035; 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; -; 4.
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; 2.
DR Pfam; PF18947; HAMP_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 5.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 6.
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:UP000037035};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 392..445
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 821..868
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 921..973
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1013..1049
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1076..1122
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1132..1171
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1193..1415
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1552..1735
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 37..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1602
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1751 AA; 192434 MW; A384CDA2A7EF00AD CRC64;
MFDDGYLLSQ LFAVANDPSN AIASLKLDLI QRHRKLSSSS EIPTPIAKSP SVSAANPLPP
SSTTSTLVNR HLNSSVSSTS SYASSSSSLD YPYYRASHPH PSPQSQVSTI HNNNNSTQDN
PQSSKFTNTT RVPLTIDFEF THQPHIIPSQ LVSNQPSTHK SLHRSHHSST TITARSPTPS
SQSPTGNECE NINSYPYNQD AHNKLDQQQQ PLEPSTSTEN LTKNVPPYNL AHEPDAMTTT
IQLLIKLAQR IIEAESNREP SPLHSPDHHS FKKHALDSPT VPHEREALLN LTDLTRIEDL
SNYRCDTCRR VYTPIDPDSY SKASTPHRER PCYSRASSIS QMFYIDPNPS DDLYVDHSRQ
SSASEPIISR RSCSVSRPSS ISTAADESEQ IRRLKASIKA IAKVCRALRN GDLTQMINED
VATPDLENLK GDVNSLVRRL RKFTSQVFKV CSDVGQKGLL GKQADLEESA GIWRKMLVDV
NRLTCDFHAP VLLSLASNLS AQVRDISEVT TVSLPSPFPE KEIHPHRSIT NTRISLNTNV
SLIEVQAEGE ILQAKVSVVD SHNTVNKYVY ILFGVLSNLP LQLRSFSFLS RMVDQLNSFA
TEVARIAQMV GTDGILDQQI TVDGVEGPNG QREFNGQVTG KMFIIFLSNL TSQVRSVSLS
LCCDYLRGDV GHCQGGSKPT DRSRGQGRNG RLEENGTVTP FTPLSLPLGW NVNSYILLCL
LCSRSTRWLT HSKSSSRKLA EWLARSASKG SSVDRPIYPM LKRHKLTMPS IIPGAWYDLS
HSVNREPFTE ELYIHAFVHS VNGQQLNLAV SIFTSGCPPI PVRQIASVTR AVAEGDLSQE
VTVQARGEVA ALASTVNGMV AFLRVFAAEV TRVALLTGTE GVLGGKAEVA NVSGEWKVCL
MPVLRMPPGF TLVDRVNTMA KNLTDQVREI ARVTTAVADG DLTSYVTVDA RGEVGQLRDT
VNAMVRFLQD FNSEVTRVAL EVGTAGKLGG SANVKHARGE WHNLVTGLNR MVDRVTGQVR
AISRSTAAVA KGDLSQRVEI DAEGEILQLL LLCLMLPYFS ALTKCRVSPQ LNMFSTEVVR
IAREIADGNL NVRAEVEAVE GVFLHIISEV NKMSGTLSSQ VGTFQAIASF PTDAAAAGDF
SKMANIAAKG DIRALQSNIN TMVTKLRTAF ESNVKAKEAA EAHSLAKSQF LANTSHEIRT
PLNAIIGLTF DTLGSNLTRE QRENLNLVRG QADALLRIIN DILDITKIEA GRMALERCTF
SLREVIFEAL TSLAFGAAAK NLDVFLEIHP AVPDLVVGDG SRLGQVVKNL VGNSQKFTTS
GSITLTAHLM DTDPEGRWRV QFHVIDTGIG IEEDKLQRIF DSFMQADGSV TRKYGGTGLG
LTISRNLVQM MGGHLDVESE VGKGSDFAFD VILGPADPEV ELRKQIEKID TDQCVLLIED
EQLDDVEASC LKFGLSVHRV PSIEEVPSGD LFDCAIISTI EEADKLRSNR FLPLVLRAAT
LPKLDMRRAL DFSLASVIET GKNEAELCNA LHIALKKSMR KLGNHDVKAD WKILLAEDNK
INQIVARRLL ASSGLKCLEV VENGQEAFEA VKANQYDIVL MDVCVTHFRL ENPESSTPAP
LQQYKLTLVG GYIFLQVDAC QGWARSDARY PNVGANSLGD SCAHHWRHRP CARRRPREMH
EGWRTSLIPH VPSLYTLRGL FTCFFGFGGL VMQMSGVCTK PLLVPELLAA MSKAISLHRQ
FARLETSKYA R
//
