ID G1XLY9_ARTOA Unreviewed; 1814 AA.
AC G1XLY9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGX45831.1};
GN ORFNames=AOL_s00117g36 {ECO:0000313|EMBL:EGX45831.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX45831.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX45831.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:EGX45831.1}.
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DR EMBL; ADOT01000204; EGX45831.1; -; Genomic_DNA.
DR RefSeq; XP_011125501.1; XM_011127199.1.
DR STRING; 756982.G1XLY9; -.
DR GeneID; 22896480; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000263_0_0_1; -.
DR InParanoid; G1XLY9; -.
DR OMA; WGQKATF; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000008784; 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; 2.
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; IPR000700; PAS-assoc_C.
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; PTHR43719:SF76; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK1; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 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 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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 910..980
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 983..1035
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1042..1098
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1154..1205
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1223..1439
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1741..1814
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 21..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1814 AA; 199659 MW; D5343E266B9C1017 CRC64;
MGRFNISSPI TSVAAVASPS PSLHDRAIPS GTNTPASVAF FPPETNPPTP SAYENPDYPS
PNLYELALLL HSEPGIDGFW DTVVRIMKEF YKVERLSLTI PTDLTDLSNS PWGQRATYND
VDDEEEEETS LLLTYPEEEE AEAGFREAGR RRRESNTTNL TATNGNSYSN GNLEGLDLPS
GPHRGLSQES VETVVIPSDT GGPVFSPVTV NLTQQSLSQW DTNDAGHQSD LHPNYPLDPL
LHIEDDDSKG KVFLNLQPLT YESEPLIDGA GVSRVLERGK TVVLSREYKD MQTKWERLAA
RKEEKARLQD QKKATEPVSE AQPPLKSKRK RFPFPCVEDF QLRYKDTMRP RSPTGTGGGG
ERGAPAFEEF EQAVSSPWSQ SPAPSPAIRA DPTENPFFAP AKVDEECFNP SAESPQYSSA
EPIHAIGLEN ASTVIHIPLV HPSTSIIKFG RRKSAGTALS DVITEKRTPI AILSILSSVI
PYPKNLVHSL THLSPLMATA FALSQAHSNA ALQLSHLQFQ GSEVAAQRKR GDVGSSIMSV
TSPSDYTKSS SNTNSLAGTP NQDLIASFGD PSGKSPMGSP SPRAFNGEEY FSASQRPPNP
KRRTSTGVYH VPMSPGEQPI PTVTKPHQYR IGHLIEEATG RPTRPPMPRT ISEVMEPSPK
KKRDKQANTS GSDKTSDSER EGSVDMPSSE DMQTPKAILT PRTEAGKQTT GFFGTPKTAE
LSMDAILNTP SGKPHYISIP TADMLPLTSV PETPSSVPLP ETPLHGPPMD SREFKIRPGT
LSSPVPDRGG ASTPVMPSAT HDLQAIESAL ESAIYPLPSP STEGLKVESS ESKNDSKKRI
PLRRHSSLAS SYKHHTRLHS RGADFGASFP TIASSSNVPM SPGFGDKNPL KTPLPNQQFE
GSQKNMPPPS NKLLRTIIDA IPVHVFTAAP QTGETTWVNS RMLSYRGATA EEFMADPYEP
FHPDDRTNYV RLWLAAVRKG EPFSYQIRIR RFDGHYRWFM IRAVPLRDNR GMIVHWFGTN
MDIHDQRIAE VNAARQAEMA ESEAKYRSLA NSSPQIVFAA TLSAGITFAN NQWLEYSGQT
LDQALQLGFM EFVHPADRFK CALPGFRVEQ MTAKEKALGA WFKAVSGDVG RDKIPEMMGV
KKKAEEEASS SPPFSTELRL RRKDGEYRWH LVRCVSVEAS NVEGLWFGTC TDINDHKLLE
QRLKDANDAA KKAMESKTRF LSNMSHEIRT PLIGISGMVN FLLDTPLNGE QLDYCHTISS
SSDGLLMVIN DILDLSKVEA GMMRLGEEWF GVRALVEDAQ ELLSTMAISK ELELNYLVEN
GVPDVVRGDR IRLRQVLLNI VGNAIKFTSK GEVFTRCFVI TDQEVPADRV VLGFECYDTG
PGFDKKDEEL MFKPFSQIDG SSTRAHGGSG LGLVISRQLV ELHGGKMMAT SKKGEGSKFW
FSAVCKVHKR GDELTALTTP TTVQTPVTTP PSLVVSSTSS LETEASVGTS CAGDGLGIVG
IGVQPLSTIS QRALAHPVPS AQDPSSMRFS LPAEVQEKVE KAEKAAREKE TEVVVAKEDK
GKKGCYVEKF GILIISFMPF SRLAIESHIR TVLPKRIPAE IKVVKDVEEA RKMLLDRKNG
VQGIFFSHIV INVPDYAQIA RITSIICERE RFSSTTMVIL TTPIHRTGII EENPKLYDNM
GARVQFIYKP IKPSRLSVIF DPEKQCDASM DRYRHTAQQV VESQKAVFRR MEEEVGNKGH
KVLLVEDNPV NQKVLLRFLG RVGVDVETAT DGEECVAKVL EKGVGWYSLI LVSISPPLLP
EYFKGVCIHN LIGD
//
