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Database: UniProt
Entry: M7X3H4_RHOT1
LinkDB: M7X3H4_RHOT1
Original site: M7X3H4_RHOT1 
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
//
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