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Database: UniProt
Entry: E9ELV9_METRA
LinkDB: E9ELV9_METRA
Original site: E9ELV9_METRA 
ID   E9ELV9_METRA            Unreviewed;      1373 AA.
AC   E9ELV9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 2.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Autoinducer 2 sensor kinase/phosphatase luxQ {ECO:0000313|EMBL:EFZ03544.2};
GN   ORFNames=MAA_00618 {ECO:0000313|EMBL:EFZ03544.2};
OS   Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS   anisopliae (strain ARSEF 23)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655844 {ECO:0000313|EMBL:EFZ03544.2, ECO:0000313|Proteomes:UP000002498};
RN   [1] {ECO:0000313|EMBL:EFZ03544.2, ECO:0000313|Proteomes:UP000002498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
RN   [2] {ECO:0000313|EMBL:EFZ03544.2, ECO:0000313|Proteomes:UP000002498}
RP   GENOME REANNOTATION.
RC   STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:EFZ03544.2}.
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DR   EMBL; ADNJ02000007; EFZ03544.2; -; Genomic_DNA.
DR   RefSeq; XP_007816807.2; XM_007818616.2.
DR   GeneID; 19254904; -.
DR   KEGG; maj:MAA_00618; -.
DR   HOGENOM; CLU_000445_114_5_1; -.
DR   OrthoDB; 1222064at2759; -.
DR   Proteomes; UP000002498; Unassembled WGS sequence.
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; 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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
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   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EFZ03544.2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:EFZ03544.2}.
FT   DOMAIN          509..579
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          806..1029
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1106..1232
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          194..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1267..1373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          770..797
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        196..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1358..1373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1161
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1373 AA;  153038 MW;  D95805CE6AC2D49A CRC64;
     MASENLVEGN AASPDIAASV APIAAPDQVS QQHEHVIPLV DGDPKRPALE ALYATPTHHD
     ETPRLSDGRR FLRDPLSLAH QGGRSQSQSP LRLPIPSITP GQLAFSAMQY LPVPVIVLNN
     LKTVVLANEA MGRMMGLTSE TTSQDDATAA LEHLRGQTLS QIGIDMLQDG RPVWITWESF
     LDSLVQEVGI RPPASHAQQP QVSQANPGDA TPTLDSSPIP ATEPRCPPMA LPSQDAVIEV
     VVSRKDMNKT TYDSRYKARA SEYQAFAKMI ITVWEIENKQ TFFTLTFTNT TSAASSPPNT
     KKLVAKPSVL EAADRRTIAI SAPSSVASSR DSNSPSFYSP GIVTMSSSPF PPMGPPSLAS
     HSSTPSLLQK ITLMKDALLD NTQMPILAIW KDGSVIFPNK AARQLQSLDA DLDNCADGLD
     LLRKWELWDE SFTRKLDVSE YPISILLRTE FPFASMRVGL VDRDGKKLIH DVLGEAIRDD
     VTGEFLAAVV TGRDVTVITE QITQIKERDD ERFKLICDTM PQLVWTASPD GLHDFFNTRW
     YSYTGLTPEE CLGMEWQMPF HPDDRHEALT RWKRSLETGE PFVTEYRCRS KEGEWRWFLG
     RALAVRNKDS GNIEKWFGTC TDVHESIETK FDAKRTRQQL LSVIAHSQVT IFTVDTSRRV
     NMLEGALIWN HTYEDVHDPS RWYIGENMHT VFNRLVDQLP EGEQLDFLQP IEDILEGRTT
     EDVKQHGLDD RWYRTRFLPM YGKKTHDGKT TSDSTIEGVI GVIMDVTELR DREEALLKQS
     REKRKAVANE AAAKEANRLK SQFLANMSHE IRTPITGVLG MAELLSHMDL DEEQRDYIDN
     IQSSATSLLT VINDILDFSK VESGRLDVEE VQFSLSLVVK EVVRMLRFAV ERKNLDFQSD
     IGSDIENDMV VIGDPGRVRQ IITNLLTNSI KFTNQGYVRF SVTTESETSD SINIKFVVED
     TGIGIQEDVR KRLFQPFSQG DASTARRFGG TGLGLTICKN LLDLMHGRII LESTVDSGTK
     ASFWIPFNKP HGPRKSHPVQ SGAIPDRLQS DLSISCNSSE YEQVGGTSTG SDGIGISSSI
     PRRRLSVRTP PCVDQDMPRT ERAKTHILVV EDNPVNQMIA IKTIQKLGFQ VTAAWNGKEA
     LEYLMATSRG QNMKPDMILM DVQMPIIDGY KCTHLLRHHS PYKTLLQDVP IVAMTASAIH
     GDREKCNKAG MDDYLAKPVT MNILERMLIR WCLSRRKVSV TVEESSDCSQ ISEHCDNAGI
     PHVGVEEQAT ESEQRVQDEP HGSPMTPRPF NTANGQPEPS PFDSPAAPGL NVQVRHQEGE
     KELSSMLQEN KLIDAAGGPS FYRTPSFQGP SSGEALTEEN MKKLKSETSH LDR
//
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