ID A0A165NHK4_EXIGL Unreviewed; 1491 AA.
AC A0A165NHK4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=EXIGLDRAFT_720395 {ECO:0000313|EMBL:KZW00758.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW00758.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZW00758.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZW00758.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV425898; KZW00758.1; -; Genomic_DNA.
DR STRING; 1314781.A0A165NHK4; -.
DR InParanoid; A0A165NHK4; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 2.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 2.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 2.
DR SMART; SM00388; HisKA; 2.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 2.
DR PROSITE; PS50109; HIS_KIN; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 572..784
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 857..973
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1020..1275
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1360..1485
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 429..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 906
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1413
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1491 AA; 164455 MW; BEAF7D0296E9555D CRC64;
MPASSLCNAM TALNLPDGVV ALLNAYVHPA FLLLRDQFAL DAENPAESAP LKPYWNNHAF
LDLERLPAHE HEEWHRGCTQ LVSRALNSST DPDACTAICG PYTAVVTILG GEYVVVTTSR
TALPSASDAD GLQVAPARGE ELGVALPTVV PSRRTIFCRD RTNVDAVFRR DLARTTAGQR
IIAYPWHTTS LGPLDDWLPE FKCCVLGILD MPECVSVWVG EGPIAVYNDS YPKLLGNKHP
QALGKPMRDV HSEIWQDLED DVRQAFAGHS IHRKNHLLFV NRNTPGVAAP EEFYYNRTYI
PWRTNGRILG IVSHSTETTA EVLACRRLST LRDMQLRTVS TSTVSEFYAA TLEALEVNAL
DLPFVLVYGA KPEYNKKKPA QGQDEKEGDR EPTRYRLSLV GSLGVPEGHP SAQAEVLVKL
GSADDCLSSA ESTSTAGDET SSSWASSRSF RNAPHHDAWP FTDVLAARGN LVTVFPLGSR
VDGFAQRGWD YPCTHAVAFA IGAGGKDGPA GGVVVIGLNP CRPYDADYAN FVRMLSCQMT
TGLTTVIDCE NQMQRMEELA SIDRAKTTFF SNVSHELRTP LTLILGPVED ILGEPIPVEV
RTRLEVVLRN ASRLHRLVNS VLDFSRLKAG RVNKFVPVDL GALTANFASL FRSAIERGRV
QYSVECDEGP LVYLDPDSWE KIVTNIISNA FKYCLKGTIE VRVQFTRKEA IFSCSDTGCG
IPEKELDNIF TRFHRVACTA RSHEGTGIGL SLTHETVKAL GGRLEVASVY GQGSTFTVTL
PLGTSHIPPE RLNAEAEPVR GVTRGLQRYG ARMVEEAAEW ATNDSAPRTP SASSDGISTA
TSETAFEVGY TAEKREPVIV VADDNADLRQ YCTMLLSSKY KILTFADGRS ALDYVRKHEV
DLILSDIEMP RMDGYAFLSA VREDANLNLL PFILLSAHAG SEARVVGLNA GADDYLVKPF
SSKELLARVK THVELGQGRR ELEARVQDRT KLLIEIESQL RLKVAEEQHM RKQQEIVVDL
TSHELRNPLN ATWQNAELVE DALERLRPLI PEEGATALNE AQGAIESIAL SVAHQTRIAD
DILNFSKISM ALLTIHTTPF PIFDTIQDVC RLWEIETRER DIELELVAEP GVCGVWIVSD
PQRISQVTIN FLLNALRYTF DCPLRHITVT VRFLTHVGPA RKNAYRVAGE KVHYRDGCWL
QIAVRDTGPG LSVDDLKKLF ERFAQAHPSK DQFSGGHGLG LFVSRHLVSL LDGFIEVESV
RGEGATFSFC IPVEQTEPQI GGAQGWRNRI LGRSARRASI SARPSLKVRE VIQSEPILPS
SARVQQPPEV TAAPKADVVS RLQEAAFAEG PTKSRSADLH VLVVEDNIIN RKVLVRQLQG
KGFRTSSAAH GQEALDLLLH PTIQHSVDIV LMDIEMPVKD GKAACIELRA SEEAQGPARR
RLPVIAVTGN AREEQVRECL AIGFDEVAIK PYRIEDIVRL ISVVRERFQS L
//
