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Database: UniProt
Entry: K1VMH1_TRIAC
LinkDB: K1VMH1_TRIAC
Original site: K1VMH1_TRIAC 
ID   K1VMH1_TRIAC            Unreviewed;       855 AA.
AC   K1VMH1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Multi-sensor hybrid histidine kinase {ECO:0000313|EMBL:EKD05385.1};
GN   ORFNames=A1Q2_00315 {ECO:0000313|EMBL:EKD05385.1};
OS   Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Trichosporon.
OX   NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD05385.1, ECO:0000313|Proteomes:UP000006757};
RN   [1] {ECO:0000313|EMBL:EKD05385.1, ECO:0000313|Proteomes:UP000006757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD05385.1,
RC   ECO:0000313|Proteomes:UP000006757};
RX   PubMed=23193141; DOI=10.1128/EC.00264-12;
RA   Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT   "Genome sequence of the Trichosporon asahii environmental strain CBS
RT   8904.";
RL   Eukaryot. Cell 11:1586-1587(2012).
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:EKD05385.1}.
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DR   EMBL; AMBO01000103; EKD05385.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1VMH1; -.
DR   STRING; 1220162.K1VMH1; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_334058_0_0_1; -.
DR   InParanoid; K1VMH1; -.
DR   OrthoDB; 2734979at2759; -.
DR   Proteomes; UP000006757; 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   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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 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   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EKD05385.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000006757};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          248..478
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          641..758
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          761..855
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        763..833
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        841..855
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         691
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   855 AA;  92945 MW;  DE8A828C3F3230F1 CRC64;
     MPDHIPVARR PSMSTLSVTG ETMTTSSQAP NGGGETLSSS QDTQTLSERD QLDTLALMRS
     SLALAQEKDS LVLLCTLLKI LCQFMRCDYA AIGLTDEGDR SVLRLKAAGP FQRILPYDLD
     VAEVSAQTVC PTSIMLHVSR TGIPITQPAK AFRLRNDPFF DDRQPRMLMC LPVINQGIQS
     GVILLMSMSN AATALQSESA REVISTLATF AYIIHMHHVF TSRLKTEVTM RTRELTAALQ
     AKTLFLSQCS HELRSPLAAI MGLAAVLENS AGLTPVQREH LGTILTSGND LLALISNILD
     HSKLESNSVL LEHIPFSVRD VVESALDTVA PVAQSKNVEL TVLSIFRNDP PGLLGDPFRV
     KQVVLNLLSN AVKFTPPGER GKRTARVTVE RMWEDLGDGQ IKIILAVEDT GVGIPASKLN
     KLFKSFSQVD ESITRSYGGS GLGLVISRDL ACLLGGDCTV ESEFGKGSKF TFSFVGTRDP
     NWKPTVIRRF PQPKRIFVLC SRDMVWGRLL EEDSKEFNCI PTRFVDDAKL ALDPGRVNGL
     NSGIEYAFIL IDAPAVDLET LTRMRELQPR AKFLFVTRIT EIAAEMDRLQ LSRESILARP
     LKFKSVHDAI IPEDTPKGGN LPAPKAKRPI NKQLGKDKPL TVLVVDDAPV NIQVCRRILE
     LYGYKDVDSA TDGLQATELA EKRRYDLILL DLQMPVLDGF GALERIKASP LAGEPCCVSL
     SANVDKATRD RCSDVGFFAV LDKPVDIPRL GEILIKVHNH RNGLPTDQPT SPKVSALLSP
     KTSPTLSPKV SHSDSATPKP SVNCTASSPT LSPKASRGDQ ITSTAQSNDA EPPSPSATPK
     PTPAVNANAS ANGTV
//
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