ID K1VSA5_TRIAC Unreviewed; 1670 AA.
AC K1VSA5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=CnHHK4 {ECO:0000313|EMBL:EKD02437.1};
GN ORFNames=A1Q2_03265 {ECO:0000313|EMBL:EKD02437.1};
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:EKD02437.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKD02437.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD02437.1,
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:EKD02437.1}.
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DR EMBL; AMBO01000283; EKD02437.1; -; Genomic_DNA.
DR STRING; 1220162.K1VSA5; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_82_5_1; -.
DR InParanoid; K1VSA5; -.
DR OMA; PCTETTE; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 2.
DR CDD; cd00130; PAS; 1.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
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; 2.
DR Pfam; PF00512; HisKA; 2.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 2.
DR SMART; SM00388; HisKA; 2.
DR SMART; SM00091; PAS; 1.
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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000006757}.
FT DOMAIN 653..880
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 953..1067
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1083..1120
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1230..1502
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1523..1647
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 114..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1200..1227
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1001
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1578
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1670 AA; 184622 MW; A60EAC8CE3FCDBBF CRC64;
MGTGQSVEHH VHRGASQLCA SDSENRQMHA ARAANINLTQ VPFDYLQFYP YPALVLIHEV
DSEDGAPAPP IDDLEPLTAL WTNTAWKRHA GTRSLAETLS AEDLVRLDHW LSRRTPSEPD
ELSTPVDKAR TTGTLDGNPH GIVNGYLDEH LQKLSLERTK RGGDAPDLCR SPEPISDPPP
EDAPLIVQCS LGLPMALAKT MFPVTVCPPH QLRRPVPQYA LYIVTSMPLQ PSCTASSECQ
CSALDTHLRS IDRTEAVEFG RVVRRWALLA LDARDHDRPW AQEELAMGAQ PPHVICDVQP
AVDLNVVGQQ GSDAHLQQAV FRAFGKPGPQ TWAKLWPSLP PLREAIAGEP FIIRDNFELA
DHNGQKREWY CTHTFLPLAL DDGADVLGFH QVEDTTARVI SARRAEIIRS LSGCGAARTM
EEFDSLTLGI LKEFPKDLPF MICYEVNEWG HDSSSTVDDG RRVRMKYRGS IGVPKGHASA
PSLVELTMPP KLPENVASDA FHAPRLKRNR HGSFDTPTPV GRVSVPTTPL GEEETPDLMP
WPFREALESG HPVIVPDCSE VIRGYSVRVW ESLPRSAIVV PLKRDAPERM SKGLMVIGLS
THLRYDKDYE QFIEDFRQQI SAYYASSLAH SAETNRRMEL AAIDRAKNLF FSSVSHELFT
PLSLISGPID DALADPGMPR GRLRDNLEIS KRNVRRLSRL VSMLMDMSNL EAKQTRGLIA
FHQVNLGELV KNVASMFQKA AAQAEITLDL SDIDQTPRVT YVDRDRFERI LFTLIGNALR
FTLEGWVRIS LRYEGGRALL AVEDTGVGIP RKDIEILGLP FWGDIGKKSN AHEGSGPALL
YAKKLVQLHC GTISIDSRTA AESPDGSHGS CFTVTLPLGF QHLPSESVMV ARPSDGTALK
EFHLSVLEDI SVSHWGWVGS TSGGARPSKP SSEGFPIVAG INPDKLFFQP DDVVLIVDDL
LDTRKYIRHI FEPFCTTLEA RDGVEALEKV RERVPDLIIA DTMLPRMDGV QLLHALRTGQ
DHREKLVPVI LLTSQGSALS DGAFGADDYI SKPFNARELI ARAHMQLQLG KKRQMLEVAY
HQRTSELQVL TDNMPVGIFR TNDEGVINYA NQMWYEITGY PAATPITNWG DYIADEHREH
IGKLWGKYVA DVQQETVQGE FQWKTGRWVS CLCMRLKPIS GVRPGIIGCI MDITDRKLSE
ELQQQRVVEA ETRRAEAEEA KRLQEELIDI TSHEIRNPIS SIMGLAAILR ENLCRFRRTV
QVALDAGTTV VPTAEMLATM DEDMEALDNI HACGLTQERI SNDVLSLGKL SLDKLAMFDV
ATDVRAEVSK LVSVFHNEAA MARVELNLGC SPNLSAAGGR LLLDPVRFGQ VVTNLLSNAI
RFTSTSRERR VSVYFDVGLS PPGAGSCVNP CTKPITSPLP AGTTVYLYGS VADTGPGMTA
AEKESLFQRF SQASAKTHTV FGGSGLGLFV CRKITRRMDG DIDVVSETGQ GSKFQFYVAA
RTPPGTPDPP SPPPPPPGAL HARVLVVEDN IINRTVVLRQ MKQAGVRAEA VTNGLEALER
LRETQKPGGD RFDCVLMDLE MPVMDGYTAT KRLRAEEQAG RLERSRVVAL TGNARQAMIQ
EQMRDFDDVA VKPYRLDALL GKIAATTNAN GETKKRANGN EAWRSRKISD
//
