ID A0A0D7BA58_9AGAR Unreviewed; 1147 AA.
AC A0A0D7BA58;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Non-specific serine/threonine protein kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CYLTODRAFT_490952 {ECO:0000313|EMBL:KIY67044.1};
OS Cylindrobasidium torrendii FP15055 ss-10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC Cylindrobasidium.
OX NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY67044.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY67044.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY67044.1,
RC ECO:0000313|Proteomes:UP000054007};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
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; KN880536; KIY67044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7BA58; -.
DR STRING; 1314674.A0A0D7BA58; -.
DR OrthoDB; 1630at2759; -.
DR Proteomes; UP000054007; 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: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 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; IPR018391; PQQ_beta_propeller_repeat.
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; SM00564; PQQ; 2.
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 Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054007};
KW Transferase {ECO:0000256|ARBA:ARBA00022777};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 707..1009
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1012..1144
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 490..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1147 AA; 126669 MW; E08A0E2968EFF6B9 CRC64;
MAGAQRNPAH RLSPFYHHHQ HPLVFVRSAV VGAALCLAMT PLYVAALLLP LSLAFGEIIT
AQRRDLARPT HTLLSTHGVP LSSPKQRIRH EQQLDAELLD IVLVASVDGK FHAMNRKTGQ
TLWSMGGTAA STTQSGASIV PSTLGPLVRT VHPEFDPDLA DELHQETYII EPQSGDIYVM
ATPDSPLLRF PFSMPELVDI SPFSFPDRED RRVFVGRKET SLVLLELETG RIKATLNSEC
PWDPFEDFQD DPDYVDLDEL EGSKPKPKPP TEIFIGRTDY HISIYTRPKP GLPPPPAQNL
SFSAYGPNNQ DNIDQSNYHR TPDNAYIQGL PNGNIMSFKA ADAAPLLWMR QFSSPVVAVF
DVLQKPSPHA HGSHTFALLQ PRPGLQDILP SMDMDKALEN LPNSQNAFVG MVEETGSLFA
MSPLRYPLVA FGDSHTAPRR FLDPPPLPDD IDDITRIRKQ MEREKERERL FSNDGCYAGS
SERRCLIGIR PLEGGDGEGP ESRLRRLLNG APSPFPQLPP AEDDNDTKRA PSRHTEPADE
LRRPEPSTHT RKWLIDAFLL TAFGAFTVWF GLSMMKNFAK GSGSVAIPSA SETSKLEPVH
IAETGSSEPV EQLPTPQLTP GSESLPAVLD EPAKPVPTQA PETDNEEGER SEVDPTTTPK
KKVRRGNRGG AGKKKKAAAV VVDEPTVSPS SSLVIESKPI VTTPSLVVSE TILGFGSHGT
VVFQGSLQGR AVAVKRLLQD FVTLAAREVS ILQDSDDHPN VIRYYYQEAH SNFLYIALEL
CPCSLADIIE TPDREAVRPL AIAFEPKKAL GQLTGGLRHL HALKLVHRDI KPQNILVSST
GKMLISDFGL CKRLDVDQTS FLPTANGAMG AGTVGWRAPE ILRGEVKLDE INDEGSIGSS
RGSGGTVTGG STGSVGSGGP VTGKPTRLTK SVDIFALGCL FYYVLSNGGH PFGDRYEREM
NILKNEKNLE ALERFGEEGS EAGHLIEAML DPEARERPDT TSCLVHPFFW NPGRRLNFLQ
DASDRFEVMC RDPKDANLLS LEKGAQKIVG NDWHSRLDKI FIENLGKFRK YDGKSVQDLL
RALRNKKHHY QDLPESVRRH LGSMPEGYLA YFTRRYPHLV MHVHRVIGET SLRTESMFRS
YYELAEA
//
