ID G0WC39_NAUDC Unreviewed; 1259 AA.
AC G0WC39;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=NDAI0F00310 {ECO:0000313|EMBL:CCD25350.1};
GN OrderedLocusNames=NDAI_0F00310 {ECO:0000313|EMBL:CCD25350.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD25350.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD25350.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE580272; CCD25350.1; -; Genomic_DNA.
DR RefSeq; XP_003670593.1; XM_003670545.1.
DR AlphaFoldDB; G0WC39; -.
DR STRING; 1071378.G0WC39; -.
DR GeneID; 11497137; -.
DR KEGG; ndi:NDAI_0F00310; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_003731_0_0_1; -.
DR OMA; WGDSNRI; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000000689; Chromosome 6.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000689};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 529..561
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 594..960
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1130..1251
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 373..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 560..587
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 762..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1185
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1259 AA; 139627 MW; CF6677B29B595822 CRC64;
MKIPDKFVLK PPFRIGIRAQ LTALVSIVAC VSLMILAITT GVYFTANYKN LRSDRLYIAA
QLKSSQIDQT LNYLYYQCYY VSSRDTLQYA LTNYVAGNKS NENWADSASI LQKFLSSSNL
FSVAKVYDAS FTTVLNVTNN GTGDQIPDSI LAKLLPLSTN IPLSSSLETT GILTDPVLNS
STYLMSMSLP IFANPSVILA ESRVYGYLTV VMSAEGLRTV FNDTTALEKS NVAIVSAVYN
NVSALTAYRF VFAPMGAPSY IINSTYRLTN GSFLSSALRE GKGGSLKSTK FFYSKNVAIG
YSPCTFSFVN WVAVVSQAES VFLSPSTKLA KIIAGTVVAI GVFVFIMTFP LAHWAVKPIV
RLQKATELIS EGRGLKSTNP DSRSVSRNNS LKLPSRNTSH YRNRSSASSV QQYTGEKQIY
PTHSYQHNTI RNMSPQRLSP SPLGLSINRH NHNNDINNNN NNNNNISPDN NLNLPLHGNN
FQSDSVSNLS PRQGTPELRR SSSVGVFSDH TEFSTKSGHL TTSANLIEAR VPDYRRLFSD
ELSDLTDTFN TMTDALDQHY ALLEDRVRAR TKQLEAAKIE AERANEAKTV FIANISHELR
TPLNGILGMT AISMEETDIS KIRSSLKLIF RSGELLLHIL TELLTFSKNV LKRTTLEKRD
FCITDVALQI KSIFGKVAKD QRVKLSITLT PNTIRTMVLY GDSNRIIQIV MNLVSNALKF
TPVDGKVNVK VKLIGEYDEA LSAKNNFKEV YVKQGTELLG CSNPIEKTNE SIPSPKSENN
NSSSTTSGKD TTNSETSFED EKSADDLDDE KIATKDAENE NTDDTENLDE QTDSVCDNIS
LVSTSTSSYD DAIFNSQFKK SPGLYDDDEN NDAGVLIEDP KTWVIQISVE DTGPGIDKTL
QESVFQPFVQ GDQTLSRQYG GTGLGLSICR QLANMMHGTM KLKSEVGVGS TFTFTVPLKQ
TREINFDDME HPFEDEFNPE SRKNRKVKFK LARSIRSKKS RASTVTFGTV TDLNHVPENE
EEIKNGSQAS VGSSGSSSSD GEESNNSNNS TTHHSEDRTN TSENTNNNNI HEKEHKHKHE
HTHNHSHNHG DYPVSLDRPF LQSTGTATSS RNVPVLSESN KDEDPAQNIK ILVAEDNHVN
QEVIKRMLNL EGVNKIDLAC DGQEAFDKVK TLSEQNDSYN IIFMDVQMPK VDGLLSTKMI
RKDLHYDHPI VALTAFADDS NIKECLESGM NGFLSKPIKR PKLRTIIKEY CPGWKSPTE
//
