ID A0A067PR48_9AGAM Unreviewed; 2402 AA.
AC A0A067PR48;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=dolichol kinase {ECO:0000256|ARBA:ARBA00012132};
DE EC=2.7.1.108 {ECO:0000256|ARBA:ARBA00012132};
GN ORFNames=JAAARDRAFT_47842 {ECO:0000313|EMBL:KDQ57239.1};
OS Jaapia argillacea MUCL 33604.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Jaapiales; Jaapiaceae; Jaapia.
OX NCBI_TaxID=933084 {ECO:0000313|EMBL:KDQ57239.1, ECO:0000313|Proteomes:UP000027265};
RN [1] {ECO:0000313|Proteomes:UP000027265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL 33604 {ECO:0000313|Proteomes:UP000027265};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC -!- SIMILARITY: Belongs to the polyprenol kinase family.
CC {ECO:0000256|ARBA:ARBA00010794}.
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DR EMBL; KL197720; KDQ57239.1; -; Genomic_DNA.
DR STRING; 933084.A0A067PR48; -.
DR HOGENOM; CLU_000445_114_44_1; -.
DR InParanoid; A0A067PR48; -.
DR OrthoDB; 12386at2759; -.
DR Proteomes; UP000027265; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; IPR032974; Polypren_kinase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR13205:SF15; DOLICHOL KINASE; 1.
DR PANTHER; PTHR13205; TRANSMEMBRANE PROTEIN 15-RELATED; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00387; HATPase_c; 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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000027265};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 306..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 465..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 513..537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 557..578
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 672..696
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 708..725
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 737..754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1914..2031
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2296..2402
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2181..2232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2246..2270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2181..2209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2346
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2402 AA; 263961 MW; 55E3671C898B4F48 CRC64;
MRPESQPTAT LTRSRSSPSP PPSPKPPSGR GDSSRNHPLK NRGRRRPESL LIPDGNVQPS
PSLDWSTSYQ AGSSSRLVGG HILKQDPVGS ETAIMADILM DTLQTQLTRI PTTCTFSIDS
RKAGESFLLV ACLIFVANKL SICTRELYTA ELWIPRVSHL SELLFLVLAS ILYVAWTQVS
LSKPSSGSPA SETISLNRSP SPWTREGREH RRVLTPKLVK KDDFGFVWMT VPKNYRESSD
DGILTALLLG PLVASAMLYS SVTSVAVSHT KISLPSTWLI EEPYSFQNVA YPRTAPEALL
VSRLNLVNLA TFCSTILLIH VCASWWIEYI HRQGNASTGP EGERKSVPRS ESKRSWLYVL
FTFGVTLALL VVRALFADAG SGIWQPHASP VDLNYFEVAV GGLFYQFALY TSIRLAHRSF
TLGELGLVCF GATSLFMEMV NITIARLWPV TTPFIKTYRL PTPLLVFQIA LIPGSFLTGF
LLCPLLVLSR HIGKQYVRRL RVRQERLAHR RGLAGGFYLG TVLIVGGLIG MWTRWCLRNR
DPWLWVLFWL LEGKKKWSRI ALVLYWALLG SLSVAGWNRQ LARSRRYRVR NPAATTNESF
PGRDSSESHP SPDTTIPATP TSATGSLGLS FSNLPNLPNL PNTANMSNVA TDLLDAADKH
VPTLGLNARR KFFHALAVAM FLPGVALDPA FTHLAFSAAF ALFTFAEYVR YFALYPFGAA
VHVFMNEFLD QKDGGTVILS HFYLLTGCAG SLWLEGSSKF LLFTGILTLG VGDAIASIVG
KRIGIHVWSP TTPKTLEGSV AFTVSVLGCV WLLRLCGFAE SFSVVKITNP VEPHDIEFQN
ECLEDDIIGV SGVRKLTPMD PGTQPNLAPP LDPTLVPWNP SVPAQIAVSQ HTPMSPIPSV
VIAPSRGPRR PPRPSTASSV EKSFTLLPSV QTGRRSRREF SPLSTQGSFA LQPNGTAATD
AVASSVQQPL EHLEGIGFFG EGTSQLGWDS SPFQGTEEES DGTYSDIVSS QDKNATVQAD
YDWATFIEAY SSGRWDPHRT PKPPRTRMAT RFPSPNAHLD LHLPPTEPSC SQVIPDPVGT
TAPQDINGCE TIPPGPAKSP VAASSPDKST QKDSRKNRPD IPLNIPPPPR IRSSFADFRS
SLPARPFGTP SDSSNPPLPT SPDIATHTAA MRLAAARVSL APLALPSPER ELTDPFRGVT
AVIPGAHSRE PPSDTNRSPE VRKSRLGSFW RGTQDVEDTG LATIPGSVSP SPSPGEMTAD
VHLPSFTLNS IPPATAPAGS STEIAGDYFG PVENMKIDPS PTGSEIVDIE RPQKLPVYRR
HPSAPPFESE VVTVPAVPRR VCLTRQMSAP LPTSHERPFH PGRLSSEGSV SQAGRAAREE
QMYEELGYLA PPNPQDELER RRALYKFNIW NTGHDPNFDR IVHLAKLVFN TKIVVITLID
GTEHWHWTAI LLSKTQHSLC TRHPATVGDG VYGDEPMIVL NTMEDWRFAQ NFAADQVLRR
GPVAYIRWFQ RRHASPSFIW LEIGPDLTGE IRLAVIDDVP RQDFSPRQRH TLKEFAAIAM
REMELWRDKM EQFTRECLEI DGPADQGSQT MFTPSSMEKI YERAAKLVKR TLDVECATVM
DVSHCEVLET PSAEAAILVT SHHTDPQAGT THHRLSPQDY TSLAEFFAKN PDGKIFDGIV
PTCLRAFLPT RIQYALTVPI FNIDKRPFAL LCAYTTSEQK KRFLEGHELS YLRAIGVIIL
SAVLKRRMIL ADQAKGLFIS KLVQQLNPIG MNITNFCQIL AAAELLAESP LNHSQVSFLQ
TVQACGTSLV ETVNHVLDFT KLSGNSKAGG VEQVILRSKV DLMQLVEEAV EGSWIGYKAR
MASLRDSEIG SVYSPPDPQR PGVVNALATN HVETVVDIDP KDADWVLMCE KGGIRRILMN
IFGNSLKFTT SGFVHVVLRQ LPPSSDTPPA QVKVELFVSD TGKTSQGISQ NFLKNQLFHP
FSQENPLQTG TGLGLAIVNS IVHSPSVDGN VDVWSVEGVG TEIKITFNAE RVMDEDHLGA
DNNHMGLDGL SHRPTVSLLG FDHRHRGIEL LRESIENYLV SWWGFAVRNE TDPDLGDVII
VNEDISPVAD AVVRKDASRA FLILSSARGE PQLMAMINNF EQIGGFARLL YKPVGPSRLR
GALKLCMHSL HMGERARVSS LDNPSSFTSA ITRDRSTHST MGQSALSRRN SEETHVRSVP
PARPHLGPRA LTMHPLGTWR DLEATQEEQT PSPALDTRTR AASLSQDSPK HTISIGAGGT
LLKSSVGHVN VIGRLRVLVV EDNSILRNLL IKWLKNKGHE YRDAVDGREG VRVFEEEGPF
DVVLIDLSMP VLDGVGATTE IRALESARRS SQSSNNSTRI LALTGMSSLE DKRRAFEAGV
DG
//
