ID A0A0G2E5X1_9EURO Unreviewed; 2219 AA.
AC A0A0G2E5X1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Putative sensor histidine kinase response {ECO:0000313|EMBL:KKY17751.1};
GN ORFNames=UCRPC4_g05384 {ECO:0000313|EMBL:KKY17751.1};
OS Phaeomoniella chlamydospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY17751.1, ECO:0000313|Proteomes:UP000053317};
RN [1] {ECO:0000313|EMBL:KKY17751.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY17751.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY17751.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY17751.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) 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:KKY17751.1}.
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DR EMBL; LCWF01000137; KKY17751.1; -; Genomic_DNA.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000053317; Unassembled WGS sequence.
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; 1.10.510.10; 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 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 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, ECO:0000313|EMBL:KKY17751.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..173
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1673..1894
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1946..2069
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 306..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2087..2219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1632..1666
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 310..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2168..2188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2000
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2219 AA; 244919 MW; E03B8E1C6F80F5DF CRC64;
MQVVLDFAIG AAETLELLHH GARAVHGEIR ADSFHFSRET GCVRLVNCGN GPKAFENMLS
SEGWVMLNQD VGGKNKLQYM APEQTGRLAV EPDARSDIYS LGILLYHMFT GKPAVEGSTA
LEIVQKVLNG RIPWVSNHRE DAPKVVSRII AKMTARAMDE RYNSITGVKH DFVNVSRMLG
EGDIKGLEEY QIATKDVSSF FTLPYKTFGR HDERKKITNL VERAHRRLQS SIAKASASTL
YSISSNSSMS DSRVDTFDVP DAASSDSGSL ALTRSNSITA NQYGMQSFDS PSTMGRATLV
DRFRVHGNNP ESTDHSSAHS SGMSSGQQDT LGYHLNRRRG SQQFRRKVGR CEVLVISGAQ
GSGKTHLIQS VQPIIRKHSY FTMTKFDRAR PSPFEPLMRA ISSLLRQIFS EKDVATPYHE
SIRNSLGPVW GILRVMLGLP ENLLARSTED YSSATKQLPS KLLKHDVLTM ESFSSRSGTS
SAALGLGRQD FLKGSNPGKG GIRFMNTYLD VIRILSSGKL LCICLDDFHA ADEESLELVS
NIVRAKLPIV LMLAGRREED ASPKAMQIMD SDHTCKIDLS NLKEEDVFAY VGETLHRDPS
STLPLAAVVL EKSAGNPFLI KEILQTCYQK NCLWYDWRTS GWEYDLDRVF SEFSSEHLGC
LTNEFITKKL SDLPVASRAI LAWGSLLGQS FSFNLVKILM SGEFSFSTGD EKANDVTCPK
MAVMYRQDEA AIIEGLQCLL TFYILVPGES DDEFKFAYDR YARAVTFMSE AWNRDKMHYI
IAQALMRYGD MEKRDFYSLA QHIRQAQQLI KKTVPERARY REVLSQSARQ AVENGARPTA
LQYFKTAFDL LQEDPWDEKR SDCFYAETLQ LYIQVAELSF ILGNSTVALS LLSEIFAHAR
TPECKTRPWI LQSRILAARG DSQASVKALT TSLSELGIDV KEWTWDDCDA KYKQLQQKVV
KADKQELVAA PPSKDPLVVA AGTVMAEAIG AAYWTDSLLF YRFVLSFWDF HLNRGTPLQI
GLAYCHIAAI ALSRFSDIPF GLVAADMAQT MLELYSDAWT KGRGGTIFGL FVGHVSGPLR
NVLGVLDDAL EYSYASGDRI ISLINLGAMA LIRLLVGQDL AEIEAFCSYG PDEIEGWESD
LRGGTILVAV RQVARALQGK TWSTFMETAL SDDSHDSGRY LTDMSLRASN PERPRDVYLS
ICLQAWYLFG HHQKVLEVGN ALMTTLSDMY STPLVVSVRF YLGLSTLALC YDEPSKEVFA
KAIETVHEYK CSIELWAKAS DVNYLMWAML LDAEMNNVQG RYGTAAGLYE DAIDHSQVHG
FALEEALANE LQAEFFIRKG AKRAGRVMMQ EAIAGWNRIS AGGKAKQLSD KHEWLLKTAT
TARAMDVGVQ TDSSLGDVPL SKAIAADSKK DYTTAWLEPA GQLDPGKLDP SKATDLPGMG
LDILDLSTIL DFSQVISSEL QIDKLLSRMT SIILESVGGQ ADFIAIVIES EDNGWCVAAS
GDNERGVRTY ADGIPFGDVD DLVAQQITHY ILRFKETVFV HNVLDDERFS SVSDAYIARN
PSGRSIIGLP IIQADHLMGV IHVEGAPNSF TQRNLLVLKL LTNQVSISLG NALLYRKVRN
VSAANASMVE SQKRALAAAR DAEAKAKKAE AEAKENVRLK EEAMKARSIF LANVSHELRT
PLNGVIGMSE LLKGTPLDRE QEGYADSIRL CADSLLVVIN DILDYSKLEA RRMRLFEVPL
NLKETIAEVV RAIAYTNRDR GLEFIEDLNL DSKLVLGDPV RLHQVLMNLL SNSAKFTAKG
SITTAAKVLS QSKDKIKVRV SVQDTGIGIT KEQLSRLFQP FSQADNSTQR SYGGSGLGLS
ICKAMIEDLM GGKISMESEP GVGTTVSFVL TLKFASVDAA TGKKEVTAQN PDPMANWSQD
TGFDGNVAPA KASFRDLSQI RRSDVRVCIA EDNPINQKIA ISFVKKMGLY CEAFNDGKQA
LEALQKASKA GSPFHLVLMD CQMPVMDGYD ATKAIRADQD ENVRDVLIIA MTASAIRGDR
EKCLEAGMNN YLAKPVRATV LNSMLDEYLT KSPSNTTNLQ NPFDELAKST RQSDGRATLD
QNRPVDGEIK PQLAKPKRQI KRIKRKSELS DIDTNRSSIN SDTKDGSGNA EDPETTPKPK
PAGSENENLH TRGLSSADKD QSAESAGPLV SQAADGKEYP MQQMKPPSVD GGPSKHDAP
//
