ID A0A427XLE8_9TREE Unreviewed; 1101 AA.
AC A0A427XLE8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=HisKA {ECO:0000313|EMBL:RSH79721.1};
GN Name=CNHHK7_3 {ECO:0000313|EMBL:RSH79721.1};
GN ORFNames=EHS24_009373 {ECO:0000313|EMBL:RSH79721.1};
OS Apiotrichum porosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Apiotrichum.
OX NCBI_TaxID=105984 {ECO:0000313|EMBL:RSH79721.1, ECO:0000313|Proteomes:UP000279236};
RN [1] {ECO:0000313|EMBL:RSH79721.1, ECO:0000313|Proteomes:UP000279236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27194 {ECO:0000313|EMBL:RSH79721.1,
RC ECO:0000313|Proteomes:UP000279236};
RA Aliyu H., Gorte O., Ochsenreither K.;
RT "Genome sequence of Apiotrichum porosum DSM 27194.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:RSH79721.1}.
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DR EMBL; RSCE01000009; RSH79721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427XLE8; -.
DR STRING; 105984.A0A427XLE8; -.
DR OrthoDB; 1938358at2759; -.
DR Proteomes; UP000279236; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 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 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; 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; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; 2.
DR SUPFAM; SSF52172; CheY-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 Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000279236};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 363..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 402..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 426..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 514..834
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 969..1091
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1026
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1101 AA; 120976 MW; 740D910556740820 CRC64;
MVKTKASPAT PSGSGSSSTA TITRHRHRRP GLGTWDMASA NPTLRRAKAG LSVADELKVG
DDSTTGSGTS NTAVPVERRL PSKSPRARFA APKSRLMTFA ANIARQMSMT PVPSTESGTG
DSHMSDIETG ASSSSVHGAT MGPPFPNADA GNRHGEYLTY GPERGEREPW SRSSASMRSA
EPEKDAAGTT PMCPRRRRQA RQTRRQSNAS EEPAGPVNWL VVDNDFAAFT QPAFDPEEER
QRVQKERQRD ADIERAMINA AEVESAYNAT PSHFSDGGSS RLRRRGGWGR RLWDAWLWLY
HCAWYASKPS AFIGSLFLLT QWVLSMSLAT NMNTYGYTVY FGAAGLFTVP LPLLVLFDGQ
RRFKWIFQAW VGAATWVWGF IYTRQMTKCH FFGNNPTCTS NYLHLFAVLF GLPTMGIVAL
SQNRVIHIAV SLSWTITAGI LFGKEPKTPN IMWRSVAIFQ LYHLFLALNS YYRERSDRAF
FTLRSQLKSQ YKAVQTAQAM ERRADQSKKR FVSYIFHEVR VPLNTARLAV TNLDSEGAFA
QMHADQQDLI LGLDGSLRMM EKVLNDMLSF NRMESGNLIL ARKPFDLHKS IHYVALSHRA
IAELTGLDFE LELDWRIDAM GSTVIGDEMR FKQVCSNLVS NAFKFTSEGG VRIVTKLVYP
EVPEVAEAGP HPVVVEKIVS DGEVVHPELT LPETVDAETP VVEESLEEQH QDDDEKGYVP
IHEPPSPRSG TPVQESPNPS TPHVTYRPRP EYSKAVIRVE IHDTGAGISP SDVRHNRLFS
PYVQTEIGRR QGGKGSGLGL ALVMQIVKLS HGRLGVDSEQ GKGSVFWFEL PYSIPPPERA
MCQRRASPVS FNLPFAGSIL PLDTETGLPH TDSPFSGAAS APMSPMSSIS ISGPPGGQHP
AHRLPGFEQQ HQSLAAATAA STMTPLSETP QGLALPASAV LPSSSAYYKH RRLSHASHTS
SQHSASPLTV LVVDDDPLTR KLMARMLTRM GHDVAMAENG AIALQKIVAS WKGEGEGAPV
DVVFLDNQMP LMSGVEVARE VRRLGITVYI VGCTGNALRE DQDEYLVAGA DDIIPKPVAQ
TEIVAKLAEA RRRKHGTPSS N
//
