ID M2WKA8_DOTSN Unreviewed; 1145 AA.
AC M2WKA8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=DOTSEDRAFT_179926 {ECO:0000313|EMBL:EME39393.1};
OS Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS fungus) (Mycosphaerella pini).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX NCBI_TaxID=675120 {ECO:0000313|EMBL:EME39393.1, ECO:0000313|Proteomes:UP000016933};
RN [1] {ECO:0000313|Proteomes:UP000016933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT but also signatures of common ancestry.";
RL PLoS Genet. 8:E1003088-E1003088(2012).
RN [2] {ECO:0000313|EMBL:EME39393.1, ECO:0000313|Proteomes:UP000016933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; KB446545; EME39393.1; -; Genomic_DNA.
DR AlphaFoldDB; M2WKA8; -.
DR STRING; 675120.M2WKA8; -.
DR EnsemblFungi; EME39393; EME39393; DOTSEDRAFT_179926.
DR eggNOG; KOG1027; Eukaryota.
DR HOGENOM; CLU_004875_2_0_1; -.
DR OMA; QCYEKDY; -.
DR OrthoDB; 1630at2759; -.
DR Proteomes; UP000016933; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:InterPro.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd09769; Luminal_IRE1; 1.
DR Gene3D; 1.20.1440.180; KEN domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR045133; IRE1/2-like.
DR InterPro; IPR010513; KEN_dom.
DR InterPro; IPR038357; KEN_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13954; IRE1-RELATED; 1.
DR PANTHER; PTHR13954:SF6; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF06479; Ribonuc_2-5A; 1.
DR SMART; SM00564; PQQ; 2.
DR SMART; SM00580; PUG; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS51392; KEN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016933};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1145
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004028584"
FT DOMAIN 694..993
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 996..1142
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 33..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1145 AA; 127413 MW; 10310D37E86A19E7 CRC64;
MPPGPTLRVR DLLFLGILAP IAAAALQQQP NVSPEQYQDD VSSNAAAASA SAADRQWQDS
IANSLQTPHS HSGQRGFRDT DADLNENQRV VRASANHGAL ATVSSPAELN AASGQPPAQW
TSASTAGLTS RQQARSLQDW QVEDLILLAT VDGKLHARDR TTGAPRWTLE TDSEVVETIR
HQQEDPLFVV EPSQDGSIYV LAPGLGLSRL GLTVKQLVEM SPYANDEYPA VAYTAEKKNT
LYTVDAATGN ILKTFSSAGS IVNDDRSCRR ASPLDLEATE CEPMGTLTLG RVDYTIGVQD
RNTGEPITTL RYFEWGPNNR DNDLRRDYEE AMDRKYVVSR YDGSILSVDL RPNGHYESAA
ALPKPRYKQK FPTPVVRVFD IVRPVDDLSG NAALVILPQP DTRKKIETDE EIENVWVGCT
KSGNWYALSE GKYPTVTDKA PEARYYNPDV YDSRKKSALP ISKALYQGVH YMSLSSDSNV
AGKHIGGHER LTIDAPDQGQ ANTSLKPLNV FNQPQSFTWL QVIIALLCVS ILSGSGGYAY
KMKSSIPWAN FKQFKVPENL LPDGPKANIA PNTESTMVRE AEPAQETIFP HDNASSPAPH
VRFAEQPAKD AVNPPKSQPE GEDEDMKEGA EPKKKKATRG KRAGKKHKEK ENALLEAKNA
RNDALIPRPA EVITVAASES AEVSGPLQIN SLVIHTDKMI GQGSCGTVVY EGSFEGRGVA
VKRMLSQYYE LASQEVSFLQ QSDDHPNVVR YFCQQKDNHF LYIAVELCQA SLFEVWEAEK
AKTEERQRQL RTLKVSMQQD MSRTLQQLAA GLCHLHKLRI IHRDIKPQNI LVAYPKKTQP
DTNRLVISDF GLGKNLPENV STLVDPTGNA GTSGWKAPEL ISQPRETSNN THSTSNNGSD
SGVGGVSGVK RAADIFSLGC LFFWVLTDGV HPFEDENGWQ QLRELNIKQD KKKMDALARW
SDAYEPMQLI SSMLEHQPEN RPTAQAVLNH PYFWPAEKRL AFLCDVSDHF EREPRGTYED
WYYGDSAHLR ILEDRSIEVI GASLGDAPPN FLAKLDRSFV DTLGKQRKYS GERLLDLLRA
LRNKKNHYED MPEHVKKLVG PLAGGYLSYW CDRFTRLLMT CYEVVHEARL QGNDRFRGYF
ELGNH
//
