ID A0A409VFW8_9AGAR Unreviewed; 2312 AA.
AC A0A409VFW8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=CVT24_003225 {ECO:0000313|EMBL:PPQ65135.1};
OS Panaeolus cyanescens.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Galeropsidaceae; Panaeolus.
OX NCBI_TaxID=181874 {ECO:0000313|EMBL:PPQ65135.1, ECO:0000313|Proteomes:UP000284842};
RN [1] {ECO:0000313|EMBL:PPQ65135.1, ECO:0000313|Proteomes:UP000284842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2629 {ECO:0000313|EMBL:PPQ65135.1,
RC ECO:0000313|Proteomes:UP000284842};
RX PubMed=30283667; DOI=10.1002/evl3.42;
RA Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA Matheny P.B., Slot J.C.;
RT "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT diversity.";
RL Evol. Lett. 2:88-101(2018).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PPQ65135.1}.
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DR EMBL; NHTK01006074; PPQ65135.1; -; Genomic_DNA.
DR STRING; 181874.A0A409VFW8; -.
DR InParanoid; A0A409VFW8; -.
DR OrthoDB; 1630at2759; -.
DR Proteomes; UP000284842; 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; 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 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:UP000284842};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 1863..2174
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 2177..2309
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 13..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1311..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1504..1527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1595..1621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1736..1857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1748..1762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1796..1810
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1842..1857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2312 AA; 251109 MW; 8BF56622E430DF93 CRC64;
MFSSLFSRLP LSLSSASGGK KGNQEADETV SGQSLSLPWP VTEAAGPSSY ATNRPKREGS
IIWSHQGQAA NGVTISNPIP RMTTNPLADF DDYPSSHHSP RTPNMKGPNS ASIASAGSVK
SGRAPFSSGL IQSSLEDKGQ RNRPQRMGSY SQAPMLHTPV LQNIGTQSSA PLQTPQSHQT
PIQYGQAVTS SAPSTPFYSY APPEVVRVES GTDSEDTTRK VAGSPEMLHQ VPPDILRPSS
LLGEYVPLTR KTQPQPFSEQ PSPETSHALY SYPYGIYGDG MNQARESNTD FDNSPVDEEE
DKEIPEVFHF PPKSVSSSSS SSGQTATATK ATFRQGLKLY VPPYAQSTHS SQSDNSILRS
TYAFPLPPSH FPNFVTGQSL GHNQAYPVDV TTAQQIQIQA PLSSAGDLAY CQGVNTDVYA
NAYNYPLATQ LSPIEEQDYV SPASAAASVS MASSRFKFRL PGFVTADGSK ESVLPSAVVG
RQIGVAEGDD KGSMKTQRTG SIGSVANSLK GHQTVMNMSR AGSLSVLQEG LEAAAEGGST
GSAGDREPGP VLGLSQTSSR SDGQNQPTTP HTPGHRLSAP TSVRDFNPPH TPTPTFLSNP
NASMSMILSP TSTIATTGTT NVSMHTPAST FIHSSGTISP VPGQTPVSSA AGLIVTERPM
SAPAGNVSTT SIGANTTAIQ RPAPVITIKP MPQYQTQQTG DAGAQPGGGG LLKLPSLPNI
TPIDLRFSSF LGKDRGTNKA AGTAQGQGSV PGQAYVDGIE EGEEYYEGDY VVDYDGEYDY
DEEHGEYDRE SLHEDSYIKD VEGQKRNGKG RQVDADEDDD FELDTLGKEG HRLSSESMEP
PPAPLSPMPP KSLRSFKSGD HQLKTGESFI HRRWERDVPM GVSASPTLFR TRSPSRWFFK
KTSDHTPAFW AFWFGFLFPV LWLIAGWHFT NAGEMPPKVT MWEWYFLRGS RWWLQGVTGR
IRTVFGCCVP RRPASQRSSG SAEAPHLHHT SPGSVTLRQG IARKKMSAAQ SQARIGKVYP
ALPRWVAEKQ STDDGRMRLN DPKRSLRGIS FGYPFIPRPL GSHGSYTGMN ASEMGSHSVL
GRMMQRLLHI VTFPNRVLDH LYGVKLREVR GRPEIQPDVD SQALVQRNAP PPVPNTVRYI
QDEQAKQDFL KDNQLVDIIL LASVDGKFHA LNRTTGKTLW SMSSISTTTS VSGPSSLAPL
VRSSQLNFEP DLDDIDFDEE NPRETYIIEP QSGSIYVVHR QNGALQRFPL SMSELADLSP
FSSHDGDEVT IFVAKKETSL VLLELETGKI RATLTAECPF IDVPATSRPI DLDELESDTG
PPEDDRAYSE PTGVYISRTD YQISIYKAKG KGLPMTHFQN LSVSIYGPNK KDQHVQTLYR
KSSDGLYVQS APNGDVYAFQ DLRSEPADGR KQKPIPPGGQ LSWALSFQHP IVAVFDIFRP
TASYHSSHAF ALLQPKPKLN ELFPDKADKE LISRGLSSAF VSMVEESNSL YVMSADEFPL
IAIGKSNEGN HPHHPPSSGE PYSGQKDLEI PRCRANPYDP MCLVGVHKLE DSNGPEWRMK
RLLDAPATSS QTPMGTPGVA VAYGEDGVLI PIVGQSRENG DNTSGAPSPP PVIPSASVPS
PVGVERGASG NGLILSGQRM QGTFSTAWEG LAVAIVVGSV SLYFLWIKFK KAIEDKIREE
HQKILLETKQ AERVPSDIII TQNLAVDRIA SPVEPTIPVP LETVPTLNGN AETTSQELVV
PIPQPSDPAL TANETGDQSP PPTAVPSMIP APNTTEEAED SEGEGEPGTS ATPGKKPRAK
RGKRGRRKKG GAAGLAASNS GNGDAEENGA EAPKEDEKKN SSTGIILSSS SPKPPVVQTP
SLVVSDNILG FGSHGTVVFQ GSLQGRAVAV KRLLQDFVTL AAREVSILQE SDDHPNVIRY
YYQEAHANFL YIALELCPAS LADIVETPDR DAWRDIAVSF DPKKALRQIT SGLRHLHALK
LVHRDIKPQN ILISAAKGAA GSAGSFGKGY RMLISDFGLC KKLDVDQTSF LPTAHGSMAA
GTVGWRAPEI LRGEVKLDEM TSGDDSLSSR GSVATIHGSM SGTPAANGKP TRLTKSVDIF
ALGCLFYYTL TSGSHPFGDR FEREINIMKN AKFLEGLDKF GEEGTEAKDL IVKMLDPEAS
ERPDTTTCLL HPFFWDPARR LNFLQDASDR FEIMCRDPKD PHLLTLEKNA AVVVGNDWYA
RLDKIFVENL GKFRKYDGKS VQDLLRALRN KKHHYQDLPD NVKRHVGPMP DGFLGYFTRR
YPQLFLHVHG VIRETGLNAE SMFRSYFELP DS
//
