ID A0A194VXX2_9PEZI Unreviewed; 1226 AA.
AC A0A194VXX2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Two-component system protein A {ECO:0000313|EMBL:KUI68655.1};
GN ORFNames=VM1G_04574 {ECO:0000313|EMBL:KUI68655.1};
OS Valsa mali.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI68655.1};
RN [1] {ECO:0000313|EMBL:KUI68655.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-8 {ECO:0000313|EMBL:KUI68655.1};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CM003101; KUI68655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194VXX2; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000078559; Chromosome 4.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 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; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR PANTHER; PTHR43719:SF30; TWO-COMPONENT SYSTEM RESPONSE REGULATOR; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 620..690
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 772..1041
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1102..1226
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 67..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1160
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1226 AA; 136414 MW; 3E9803F55F50E4DF CRC64;
MDADQVEGLE ALAVREVLDA DSRPTFVIDL DPDEPFRAVS TSISPVFCNA ALRTHERLLD
AVLGNAGDDE LADQGDQPEP PQSGPTLPRP NHEAFKQWAT GVTTHDDSKD VFPLSFIYKD
LLWTGSTVRK RWRLISGNRL WHADGPPLNL ASGAPLEVAT GGSLATQGKR NRVVNAGDLG
SAARASEANK EDTSSRMHAS SSPLFYPRIS MGGSYETGNS SNSHSHNRSL NITLLPERAA
IDWTLPHPEG QLSEHLQYVR SIDWSATSLG AMAQWTIEFR QIANLVMMNP HPSALFCGSR
LTVIYNEAYA IEVAGNKHPS LMGSDFADFF PELWDYCGPM FEESGRTGIS VRKDNDYLPI
YRNGMLEETY YSWTYVPIYN AGQELLGFYN GPVQTTSMVL NQRRMRTVNK IGERTGHAKT
IKQFWKLVLE ALDDNPRDVP FALLYSVGED DDGDFSSVAS EASISLKSCH FEGALGVPEG
HVAVPQQLDL RRSLEGFVPS FREAMRTREP TLLRVKDGTL PESLLEGIEW RGFGDPCKEA
IIFPVRPTNA DNVLAFLVLG VNPRRPYDVE YKEFATMFNR QLATSLASTI LFEEETRRIR
DAVEAAVLEK ERLTQQLDLQ ASRLRRMTEL SPLGMFLITP EGVLREVNDR FFEMTGLPRS
SQFEMSWMDW IMPSSTQQME DGWQKLANEH LPWSGELQLK VRGARPRNLH GEAIDYWVLF
TAQPEISPDG SLLSIMGSIT NISHMKWAQG LQELQLREAE ETRRQQNEFI DITSHEMRNP
LSAILQCADD ITSALAECHT KGTDPPRDLV DSCLESAQTI SLCVQHQKSI VDDILTISKL
DSNLLLITPV ASQPQQVLSR AVKMFESELQ AKDIKAKFEI DPPYKQFAVD WVTLDPSRVL
QILINLLTNA IKFTAPSSRR VLTVAVDASL KRPVLEHIPG FQYVPSNTKT SVTATEDWGD
GEVLYILFRV QDTGCGLTAE EKQILFQRFK QASPRTHAQY GGSGLGLFIS KRIAELHGGQ
IGVASEAGSG SIFSFYIQAR RSAPPVDSQM NHPLPIERHM NGDVSLRRQL TPQRQDVATT
GGLGANLLAT KASKALDPKA MNILIVEDNL INQRVLANQL KKIGATVSLA NDGVEALEFL
RTTRFCETRS GVTLDIILMD LEMPRMDGLT CVREIRRMEL EGEVAGHVPV IAVTANVRAQ
QVTTAKDSGM DDVLSKPFRI PDLLKK
//
