ID A0A364N3J4_9PLEO Unreviewed; 1711 AA.
AC A0A364N3J4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Two component histidine kinase 1 {ECO:0000313|EMBL:RAR11033.1};
DE EC=2.7.13.3 {ECO:0000313|EMBL:RAR11033.1};
GN ORFNames=DDE83_004791 {ECO:0000313|EMBL:RAR11033.1};
OS Stemphylium lycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Stemphylium.
OX NCBI_TaxID=183478 {ECO:0000313|EMBL:RAR11033.1, ECO:0000313|Proteomes:UP000249619};
RN [1] {ECO:0000313|Proteomes:UP000249619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIDEFI 213 {ECO:0000313|Proteomes:UP000249619};
RA Medina R., Franco M.E.E., Lucentini C.G., Saparrat M.C.N., Balatti P.A.;
RT "Draft genome sequence of Stemphylium lycopersici strain CIDEFI 213.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:RAR11033.1}.
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DR EMBL; QGDH01000061; RAR11033.1; -; Genomic_DNA.
DR STRING; 183478.A0A364N3J4; -.
DR Proteomes; UP000249619; Unassembled WGS sequence.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR CDD; cd12360; RRM_cwf2; 1.
DR CDD; cd05233; SDR_c; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR034181; Cwc2_RRM.
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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR032297; Torus.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR43719:SF60; HISTIDINE KINASE G2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13561; adh_short_C2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF16131; Torus; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00360; RRM; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:RAR11033.1};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022728};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00022728};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000249619};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728};
KW Transferase {ECO:0000313|EMBL:RAR11033.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT DOMAIN 436..707
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 862..993
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1428..1455
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 1491..1565
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT ZN_FING 1428..1455
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 259..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1687..1711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1056
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 923
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1711 AA; 189145 MW; 323866AA385D8610 CRC64;
MTTNGDATVD SLYEWGVPLC KLAPEGKYPN YKAGEMTSSK YRSKAGLYFK KVEENRARTY
KPRDVKRRLS NDVSTYEEAK KVQAERIART ARTACTGAME NLDKLSATGL PVFDLNKENL
VRKDWSQTAI GPRESWPTAL TILVNTCVLP MPHCSAIFWG KDLTVVHNLA WEKGRGKLDG
QASLARETYG HEALGTLRTV LRGRTVKVAA RYFLECLPED KNSQLLLSTI LDEHGTRQGV
LAQLLENQNV DRYMPIEGLD ELSRQHPGRR LKDENHKPKS RHASTEHADS MQTNMFQRFA
ELLPNGLAIL DKDAEAIFVN DGFFKLTTNK GNNEFRAWPE SIHPDDYEDV MSAYRKAFES
RTELQIEFRC DVTAPTEKRG EQWRLFLLKP LSEEADAGFI SAVIDITDIK QAQLTQEQAA
NEAKERKEQQ ERFIDMVSHE IRNPLSAVLH LAEEVKEVTK EIGDQHDDTR DQVADILDAA
DTILLCVSHQ NTLVDDILSF SKLDSMMLSL VPRETRPKWE FSQALRVFHS EFKAKNIKFH
YAMDVSYEEQ KVDTVVADLN RMKQVLVNLI TNAVKFTSRK NGERNITVSM GASVQRPTSY
PPNVIYFSEE KEAFHLDSTM TSEWGAGDAM YLMVAVKDTG IGISKEGQAK LFERFRQATP
KTQENYGGSG LGLFISRKLC TLHGGDIGVS SKEGEGSTFG FFFKVRRAVA GDGQVRPSQS
RSNSETSNAS TRQSDNAGSK PSRPGFSRAN SRTNSNLQSI KERTSERPEA KTLTSHHGVD
TEEMEPSLKN PPVEQRPESH PASSGDSRYQ ETASAAKGVM SEKPHIERKL PDLRRGETSR
QEEGAQEISR SQSDPRTEEN HTLLLVEDNL INQKVLRRQL QSRGFQVFTA NNGQEAIDAV
AERGRQAENG PDDRNYFDVI LMDQEMPIKD GNAATQEIRQ LQEEGKAGYS HILGVSANVR
QAQTNSMRDA GMDDVISKPF KVDDLVRKVR ALVLDNGGSV RHDNRPNGQP DAQKNGKSND
GEARDSLSPW DAERSNSNGN DQREREDSKR GGSRTRSRAE APNTMAKEFQ GKTVLITGAA
SGIGRATALK LSSLGATVSL CDVNATNLEA VASESSTPSY TQKVDVGNKA DVESFVANTV
KQLGGVDYVF NCAGVNPTSM KLEDTKEEYW DKLVNTNLKG VFLVTQACLP HLQRGSAIVN
VSSISGIRGS ALQSVYCTTK FGLIGMTKSH ALEFGPRGIR VNCVAPGYID TPSNAGIVKG
GEAVERMRNG NALERLGTPE EVADVVAFLF GDGARYVNGA VLEIDGAVKM SSTTKTQPVQ
TSIAPDASLE AAASSTDLVP TTEQTIITTN AEGKKVKKII RRKRRPARPQ VDPATIKPQE
VAQTGNIYNV WYNKWSGGDR EDKYLSKTAA QGRCNVAKDS GYTKADKTPG AYFCLFFARG
ICPKGVDCEY LHRLPTVTDI FPSNVDCFGR DKHADYRDDM GGVGTFQRQN RTLYIGRIHP
TDDIEEIVAR HMQEWGEIER TRVLTARGVA FVTYLNEANS QFAKEAMAHQ SFDHNEILNV
RWATVDPNPQ AAKREAKRIE EQAAEAIRKA LPAAYVAELE GRDPEGKKRR KVEGSFGLQG
YEAPDDVWYA KEKGEWEAAK QIEAGGMGER MMIEGAGGGG GDAANQQQLQ QSNGILSGST
LAALKGYKAT PSNKRPAPSA GPLVDYGSDS D
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