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Database: UniProt
Entry: A0A178BBB6_9PLEO
LinkDB: A0A178BBB6_9PLEO
Original site: A0A178BBB6_9PLEO 
ID   A0A178BBB6_9PLEO        Unreviewed;      1195 AA.
AC   A0A178BBB6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Non-specific serine/threonine protein kinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=IQ06DRAFT_288482 {ECO:0000313|EMBL:OAL06609.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL06609.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAL06609.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL06609.1,
RC   ECO:0000313|Proteomes:UP000077206};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KV441705; OAL06609.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178BBB6; -.
DR   STRING; 765868.A0A178BBB6; -.
DR   InParanoid; A0A178BBB6; -.
DR   OrthoDB; 1630at2759; -.
DR   Proteomes; UP000077206; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
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   CDD; cd09769; Luminal_IRE1; 1.
DR   CDD; cd10422; RNase_Ire1; 1.
DR   CDD; cd13982; STKc_IRE1; 1.
DR   Gene3D; 1.20.1440.180; KEN domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
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; SM00580; PUG; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..1195
FT                   /note="Non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008082793"
FT   DOMAIN          756..1055
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1058..1192
FT                   /note="KEN"
FT                   /evidence="ECO:0000259|PROSITE:PS51392"
FT   REGION          54..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..686
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..702
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1195 AA;  133734 MW;  10A641E2FF0B6FB6 CRC64;
     MPRPRRPPGA GPALTILALL LLPSILVAAQ QQQPVEHHAR NRSPSAGGRV EHARIVPPQN
     HQPNSRRGSV SDAERRQQYT PILAQNERAV ATKVSSAPAI SAVGARHGAG AASGVLAPSA
     RSLQDWEVED FVLLATVDGH IHARDRYNGE EIWEIAGKPM LETIYNVSEG RVSLQDQPFV
     WIVEPREDGA LYVLLPGPYP VLQSLGLTVK QLTDIAPYSS DDPELPVVYN VEKKTFMLNV
     DAATGLVKQS FSPSGTYGNT DDSCASSVKN VFNERDCRGT FEIGQTEYTI IIHNKKTNQH
     VCTIKYAEWV SNNRDIDLKS QYTRTMDDQY IYGRFNGEVF SYDHKRPRPA QRPLFHQHLS
     YPVARVFDVA RPANDDNAQA PLVLLPQPAG PTVIEEKANH VWLNTTEEGA WYALSEISYP
     AVTDGAPAAS CYDETELLSW DATHSLPADE KTLVGVHVLD NRVQPPTRFR AIAAPTQYQI
     EDGQVVSIPP TTSPREVPTI DPPQKPFLER QQYTLGPTEF IAICILVVIS ISFGKWRGPG
     KLAPYWDYMA NITSNLTSHG KQPSKNKAEP VPVAAAMEGE PAKQNQVMPQ VAELLASEQP
     KEQPIEVLAE KPHLDAPFQL EPKEKKVTFD VPEEDDDMAP LSRTTTAEPG SPGQDETLTT
     MDSSTEALPS ANGPDSVPQD QSSTPGTPKK KKTHRGKRGG RKLNKNQQKE EDELGRIVDA
     AKQLDPSPGL HPDEMTLNGD DMQDVTNIKR IGKLTIDQDR LLGNGSGGTF VFEGKWNERE
     VAIKRMLPQY FGLAEQEVKL LQESDLHPNV IRYFDDEKDE NFLYIAVELC QASLFDLYRD
     GRPGEELTES QQKLALDISR NIPRVLYQLA YGLNHLHSLR IIHRDIKPQN ILIAYPSRNQ
     TNCPRLVISD FGLCKTLPDN VSTLIGTTGN AGTVGWKAPE LISQPKELMN GSSTGMSRDS
     SSSTDPVAQG VKRAVDIFSL GCVFFYVLTN GCHPFDDDEG WMQIREYNIK KEKANLKQLR
     LGADSEEPYH LIQWMLKTRP EDRPTAVQVM NHPFFWSAEK RLNFLCDCSD HWEREPRDPP
     SEHLAILEEY SYEVLDQKRN FLGKLDAAFI NSLGKQRKYT GDRMLDLLRA LRNKKNHYED
     MDETVKAKVG PLPDGYLSYW TIKFPQLLMG CYQCVLECGL EGEPRFRPYF EGQTM
//
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