ID M7X3H4_RHOT1 Unreviewed; 967 AA.
AC M7X3H4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=RHTO_06612 {ECO:0000313|EMBL:EMS18194.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS18194.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS18194.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS18194.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR EMBL; KB722686; EMS18194.1; -; Genomic_DNA.
DR RefSeq; XP_016269313.1; XM_016420273.1.
DR AlphaFoldDB; M7X3H4; -.
DR GeneID; 27370625; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_271166_0_0_1; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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 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; 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:SF66; CHROMOSOME 8, WHOLE GENOME SHOTGUN SEQUENCE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
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; 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; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EMS18194.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:EMS18194.1}.
FT DOMAIN 488..764
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 807..930
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 446..485
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 940..954
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 859
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 967 AA; 106073 MW; 44C5233C278DBEDD CRC64;
MRDPPAASTG SARLDKPDRA ADGTRSVVPP SLADYLDDLP LPACVFAHST FTRDAIAPPA
YQNLAFEALL AQGKVLSDDT TLPHPLNDIE RTLLDVIDEP SFAQLRQWLL EGVATFPSSS
SSPRKRPRQS SQRHIALQLD ENISFPKLRW RASVRDGYTV LTHLPAVELV HGGGVKSAAV
QEERTGRAGV VRLGELEVSA DRVRDATSLE GLAFTLWHSP IGMFRVNKDL QVTQANPAWR
KTIGIGPGES NDSWGNRIHP DDTERVFAHY AEIAATSPLR RDECEWRWLM GDKEQNRVCV
IEPVIIEGVM EGYSGYLENI DEQKAIVSAS QAREAQLQTE LAILSDTCAV GLSRHALDGT
FLNVNPAWHA IVGMDPEEPL ENWMKNLVPE DHDRVMTLET RDSLSIQFKF KNGRVCLTQI
TPNHREKDKA TGWIGSTTDV TAQARAEEAI LNVSKEREAR AKKEAEEAEQ RRRIAVEEKR
QQELLIDVTS HEIRNPISAI LQNSDFTRSS LQKLRDTLVV LQQRNALPSE LAGSALNDLD
EDIEALDAIT ECGMAQERIA NDILGLAQIQ LSKYNIAPIE FDLTTSLRNI CRMFKNECRT
KDIELNLIIG SSLARLGPKA RVFADPARLT QIIVNLLSNA IRFTAKSSSR IVTLSVELSS
TRPADDAPIV PPKGEDDVRR IEAGQPIFLL FSVEDTGPGM TKEETSRLFA KFMQASPFTH
TTWGGSGLGL WIARNLCELQ AGRIEVASTV GKGSIFRCFI TARAVDNPDA FRDQQASFSE
GYGGPVGGLK MTVGQRGGED APLKGMTVLC CEDNQINRTV LRRQLTKEGC EVLLACDGQE
GLDQLQRRAD GTIDCVLMDI EMPVMDGLAA TRAIRHAEST GQRRGHQPII GLTGNARSGQ
RQIALDAGID VVVTKPYKMP ELISQIRSLL AGASPSASPC HPSAPLPPIH APAPETTSAR
PIPTPSA
//