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
//