ID K0K6P2_WICCF Unreviewed; 1165 AA.
AC K0K6P2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=NIK1 {ECO:0000313|EMBL:CCH40585.1};
GN ORFNames=BN7_118 {ECO:0000313|EMBL:CCH40585.1};
OS Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS 3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH40585.1, ECO:0000313|Proteomes:UP000009328};
RN [1] {ECO:0000313|EMBL:CCH40585.1, ECO:0000313|Proteomes:UP000009328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX PubMed=23193139; DOI=10.1128/EC.00258-12;
RA Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA Tauch A., Kohler T., Brinkrolf K.;
RT "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL Eukaryot. Cell 11:1582-1583(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};
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:CCH40585.1}.
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DR EMBL; CAIF01000001; CCH40585.1; -; Genomic_DNA.
DR AlphaFoldDB; K0K6P2; -.
DR STRING; 1206466.K0K6P2; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_3_1_1; -.
DR InParanoid; K0K6P2; -.
DR Proteomes; UP000009328; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 3.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1530; -; 3.
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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00672; HAMP; 3.
DR Pfam; PF18947; HAMP_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 5.
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; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 2.
DR PROSITE; PS50885; HAMP; 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCH40585.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000009328};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCH40585.1}.
FT DOMAIN 51..105
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 144..196
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 236..288
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 328..380
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 420..472
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 494..746
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 891..1015
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1058..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 29..59
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1128..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 940
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1165 AA; 128089 MW; 112EB91541D28B88 CRC64;
MSVDIISTLQ DPEAFHNAVS TNEGIESIRL NLIQHLDNKE QEIKQLESAK KSFQKASMEI
GNVLIAVAMG DLTKQVEIND EPDPEILKVK MTINTMVDQL HTFASEVTKI ATDVAHGEFG
GQVKNQGTVG IWRTLSDNLN VMALNLTNQV REIAEVVRAV AGGDLSRKIN VHAQGEILEL
QNIINTMVDQ LKTFAFEVTR VSRETGVEGR LGGQAVVIGA EGIWKELTDN VNAMATNLTN
QVRNIANVTT AVAKGDLSKK VTADCKGEIL DLKSTINQMV DSLQTFALEV TSLATDVGIK
GILGGQAVVN GVEGAWKDLT DNVNAMATNL TNQVRSIAAV TTAVAHGDLS QKIDVKAQGE
ILELKSTINK MVDSLQVFVS EVTRVAKDVG IDGKLGVQAQ VSDVDGLWKE IITNVNVMAA
NLTSQVRAFA QITAAATDGD FTKFITVEAS GEMDTLKTKI NQMVFNLRES IKRNTAAREA
AELANRAKSE FLGIFSHELR TPFNGILNYT QLTLDTELSQ YQREMLSTVH NLANSLLTII
DDILDISKIE ANRMTIEQVE FTLRGTVFGA LKTLAVKSIE KPIDLIYQVD ASFPDSLIGD
SFRLRQVILN LVGNAIKFTS KGHVSLSVKK ATTSLEQQIT STVQNNNFVI GHDSSTIVES
NKAPEDDVLV LEFCVSDTGI GIRKEKLDLI FENFTQADGS TTRKFGGTGL GLSISKRLIH
LMGGEIWVTS AYGKGSRFYF TIAVRPVKQV FSKQSDALLT FNLHQILFIS TEHTVEEAEK
IEQELRELNL RPTTVRKIED ANLQEPCKYD VIIIDSLETG NKLRLLPDIK YIPFVLIHKS
IPSLNMRICL DLGIQSYGNT PCSIMDLAGY LKPALESRIV PSDDDAPQSY NILLAEDNLV
NQKLAVRILE KYGHEVTVAK NGLEAFEEVK KSRYDVVLMD VQMPIMGGFE ATEEIRKWEK
NMNPIDPLSV RVPIIALTAH AMLGDREKCM QAQMDEYISK PLKPNLLIQT IAKTIHHVNK
LKEIASMNPT NNQLANEGLL NLPSNGNSTQ NITELIAQHQ QSSQQQPQAK RSSSNEELGK
VHYSINDPTT LNNFATALSP ALRTSIERPT LSTNNRSITD SAVRTLSSIT NSPIEGEFST
SPSKLLPNQD DSSNKDKDGD EQVEI
//
