ID A0A1X7RVZ5_ZYMTR Unreviewed; 2434 AA.
AC A0A1X7RVZ5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ZT3D7_G6692 {ECO:0000313|EMBL:SMQ51539.1};
OS Zymoseptoria tritici ST99CH_3D7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ51539.1, ECO:0000313|Proteomes:UP000215127};
RN [1] {ECO:0000313|EMBL:SMQ51539.1, ECO:0000313|Proteomes:UP000215127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LT853697; SMQ51539.1; -; Genomic_DNA.
DR STRING; 1276538.A0A1X7RVZ5; -.
DR Proteomes; UP000215127; Chromosome 6.
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; 1.25.40.10; Tetratricopeptide repeat 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 SMART; SM00220; S_TKc; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000215127};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 58..368
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1884..2106
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2158..2281
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 62..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2106..2128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2305..2434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1840..1870
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 62..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2305..2338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2339..2383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2384..2400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2413..2434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2212
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2434 AA; 269289 MW; DECF301B73F02A73 CRC64;
MDDATSVETP RAVEESRNAP FRRFFERIRD DVKGYVFDDT ISPFHSSYDN WHFFGRRVRS
SKSTPSGTAS SAPSNTSASR PSSVRTRSDY DGVTVDEERE KDQWVVARVS KQVLRLEREF
KLCQTLHEKA SQRRHFVEPL DFFRLPARQP GEVTLCASIV RAPSKNYLSE VLEFGPNFYL
STSDSSHVQR REQIELLTFL DFAIGTTECL EILHHGNDMV HGEIRGDAFH FNRDTRAVRM
INFGSGVRSF EHGLSSANWS TLMSERGIQQ RLMSVAPEQT GRLPAEPDAR TDIYSLGILL
WTILTGRVPF EGITPLDIMQ NVLSRRIAPC SSIRQDVPDA VSKVLQKMTS RSMEDRYNST
TGVKHDFQVL KQILTDGDQS ALSDFKVATA DVSCFFVLPS TLVGREIQRD TILNIIEKAA
KKSARAAPVT RAGLKSLSSS SSLIQGERSE LFDETMSDST SSTGGRDHRR DDSRLSSIPE
FSPYENNIRQ EKFEAVMSNR SGSVASSVAT EENDIKPLEK QDSTDSRGSI SNNLHSNGGS
LHQTLSSYQI NGERSTADSG SMLRTAQKLK RKGKAEIIGI YGATGCGKSA LVQSLQSTAR
RHCYFASAKF DQVRNSPFEA MVRVMSSVFR QIFSENDVNT PFHENIRIFV KPFWGVFHSF
LDLPIWLLDV KASDAGATSP KTSLGVAPDR KSCNLANAQD WLRMGGSNKS SRFLHIFLDV
LRLLAVQKLV TWVLEDLESA DPESLELIQI IVKNRLPIVL LLSYSREDML NEPIKRILEH
AVKVEVGPWS EAETAKFISE TLHRPEEDIT PLIGVVQEKT QGNPFAVREM LDSAHRGKAI
TFCWQHSLWE FSMDKLFEQF ASPDAYSSND FVLRRMRTLS IDARTMLAWA SLMGSSFQFH
LIRGVMSCSC GSLIEQPLIP PISKDAVAGL QIALASFVVM PTEHEDRFKF SHDRYIAAAE
ILADQYDKSA MHYVAAASII KHDPYDPVTQ PSKALFELAR HICEGIETIK RRVQNKFLYR
DLLYQAAETA RESGARTSGL YYFKHCLQLL PDDPWDDYSG DTTYTECLTL KTRAAEAYWY
SGQHAEAAKL LEEVNSHARE VSDRAPVAIL RSRMFAQRGD SAAAFKLLKT ALAELGLDIP
DRTWDEADDE FQRLVPLIRS DLPQIDGFDP ASVDKDLTTL AALLTELQSA AFWNSDILFF
NASLTILSCF LERGLFPQVA LGYVNLAAIA ASRFSMITTA VEFGNTAVRI LELFESESYT
LGRGLTLHVL WLGHIQLPIR DNFTVLNRGL EAASAAGDKI LHLLSIGITA AMRLWSSDNL
AEIELFIASV GEEFPEWPQN TRGGAFLMGV RQYVCALAGK TYYGSPAQVL CDASHSTTDY
VDYLKSTVSN PDRPLSIYYS YEMEALYRFG HYKEAMDFGV QLLPLIDGLL CMRYRYGTMF
YTAMAILACI REDPGRSDRA DLLARVGAYT AQIEVVASVN SINFAVFLNL LSAELADVEE
RYGEVLGFYE EAVNHANLTS NLLEEALCNE LYGDWLVRRG AARPARGILL DCVSAYRRVG
AFGKAEHVSQ QYDYLLSGTM SLSAVHAGTQ TATNEDSGTD DPAYADKLES ITRDHVPQSS
ADRTHEWLDP QPVPASHMDA GGKEASTVLS SAVGLDMIDL AGILQSSQLL SSELQVDRLL
ARLTSIIVDS TGAELVGLVV EAEGGEYCLA SLGTPDGITA HEQPIPLDQV DVVLQQVTLF
CLRFKENVFL SNILKDERFS NVPESWLKEN PEGASMISIP ILHGNNVLLG SLYCQAPPNS
FTERTVTLLK LLVNQIAISI ANALLFKRSE KIQASNTSML EVQKQALAQA REAEKKAKAA
EVKAMEMVRL KEEAAKAKSM FLANVSHELR TPLNGVIGMS EMLKSTQLSK EQEEHADSIR
VCADTLLSVI NDILDFSKLE AGKMQVFSVP LSLGETINEV VRALSYTNLE RNLETITALE
LPPELVVMGD PVRLHQILMN LMSNAYKFTS KGSVTIRATV DSEDDEVIKV TISVADTGIG
ISEEQQKKLF LPFSQADSST ARSYGGTGLG LSICKAILEN VMHGQIWLTS APGVGTTVSF
SLPFKKVHPG GDSTQSNGPT PHSRETDPMA IFTPPAVDDG PGARAIRSLQ GIPRDQLRVC
IAEDNPINQK IAISFVRKLS FRCEAYGDGQ QAVDALTRAS EEGDPFHLVL MDVQMPVLDG
YNATREIRKH SDPAVRDILV IAMTASAIRG DREKCLEAGM NNYLAKPVRA DTLKQMLESY
LHQPAKAMPN LQEEANQLVN RVVSGSEAKS GTTGNDGRVE AKRNVSTTMP TTNRLGDNTE
ETASRDEPSV SPRSDTTEIH VGASKKTEVP ERPARDSRTA SLSSKRKSQE NNNAPVARST
GSPRPSARRG GPGIERALDE RRKKTEDESS GSST
//
