ID E4ZY57_LEPMJ Unreviewed; 1566 AA.
AC E4ZY57;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CBX96302.1};
GN ORFNames=LEMA_P112210.1 {ECO:0000313|EMBL:CBX96302.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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DR EMBL; FP929128; CBX96302.1; -; Genomic_DNA.
DR RefSeq; XP_003839781.1; XM_003839733.1.
DR STRING; 985895.E4ZY57; -.
DR EnsemblFungi; CBX96302; CBX96302; LEMA_P112210.1.
DR GeneID; 13289891; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_50_4_1; -.
DR InParanoid; E4ZY57; -.
DR OMA; WVMKPIN; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.270; -; 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; 3.30.450.20; PAS domain; 1.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013654; PAS_2.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043150; Phytochrome_PHY_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08446; PAS_2; 1.
DR Pfam; PF00360; PHY; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
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}; Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00022543};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 482..644
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 858..1097
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1312..1442
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 15..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1102..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1462..1566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1475..1495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1504..1532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1363
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1566 AA; 172587 MW; 39D70EA3C25B174E CRC64;
MALFQCFQAC THHRRTLQQE EDAPRLMSQP SSPSPPQDPV AASAQTDGTP SYSTVSPIQE
EPGTPIDGAT DATDFAPSSP SNPDANPRRG DNFGPLSPSV TDRVFPIRSV VSVDPSPTPR
GNIGPGDYFH PYSRANDARL EGRRPSHGST TSTASQPSQR AWAARHGGSA TSKTDSRTDS
RRSSLKRPER AEAQKTLAPI PAQLFSDLVS TKSSGSGPEE GSRSPSTQAG RPPSTSARST
KSAMSSLDMG GLVTHRFKHI TTEGGHMIIT GREGDTLQRC EDEPIHVPGA VQGFGLLVAL
QDDTEGSGSL LVRIVSENSK RILGRTPREL FALESFTDIL SEEQADNLLD HIDFIKDEDS
DVIANGPEVF TISIKVAGVS RTRKLWCAVH VNEANPGLVI CEFELEDDPL YPLVPSSEMT
PELPEDTLSS NPTEEELLES TEIKSKPLRV LRSARKRKGE AAAMEVFNIM SQVQEQLAAA
PSLDKFLKVL VGVVKELTGF HRVMIYQFDH TFNGRVVTEL VDPRATKDLY KGLHFPASDI
PKQARELYKL NKVRMLYDRD QETARLVCRT TEDLENPLDL THSYLRAMSP IHIKYLTNMA
VRSSMSISIN AFSELWGLIA CHSYGPRGMR VSFPIRKMCR MVGDAASRNI ERLSYASRLQ
ARKLINTVPT QHNPSGYIIA SSDDLLNLFD ADFGLLSIRD ETKILGRLEN SQEALAMLEY
LRMRKIQSVM TSMDIVQDFP DLRYPPGFHV IAGMLIVPLS VDGEDFIVFF RKGQMKEVKW
AGNPYEKFVK EGTEGYLEPR KSFKTWSETV IGRCREWTEE EIETASVLCL VYGKFIEVWR
QKEAALQSSQ LTRLLLANSA HEVRTPLNAI INYLEIALEG ALDTETRENL SRSHSASKSL
IYVINDLLDL TKTEEGGPLI KGESFDLKAT IIEATDMFRK DAKRKNIGYD VVIHDGLPNL
CIGDQRRIRQ VISNITANAI QNTTSGSVRV ESYVAARSDA EHVDVEIAVS DTGIGMGQKK
LDQLFYDLEQ VQSEATSMLE DALVPDAKKI AAQSEKSTLG LGLAVVARII KNMNGQLRLR
SEEGRGTRFV VSFPFSLPDS EAEANLNSEA SSGIMTPQPG SDELGPSEGE RTLIAPSLSR
HTSDKESHQV SDSIIRRSSA DSLTSKTSLR SFKSGSSARS DMDRLIDAIQ EPHMVGRGNT
GDRSPSARSM RPLLTKPNSL SPNSPSRMRS RSLETLQGLT PIQHRSLDTQ IPGEQHITGS
AAPIRAIRVP NDGGSPIDRR RPSGSILGDL TDEPAPLEVA SAPENFSADY MRVLVAEDDP
VNSRIVKKRL ERLEHVVHLT VNGEECASAY CDNPQDFDIV LMDMQMPIVD GLTSTKMIRS
YEKTHTEIYS PRAALCGRVP IIAVSASLIE RDRQQYIDAG FDAWILKPIS FDRLKRLMAA
VVDSDIRKEC LYQPGEWEKG GWFHTGKKSS KEASTKPAGK ASVGNTSTAT EADVVSNNLM
AGHDGVKDDI DEEQARLMQN QEEGKIEAPE ESCEEQPREE SSEEQPPESL GGEKLAEQPS
EEKPPA
//