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Database: UniProt
Entry: A0A0W0FF95_9AGAR
LinkDB: A0A0W0FF95_9AGAR
Original site: A0A0W0FF95_9AGAR 
ID   A0A0W0FF95_9AGAR        Unreviewed;      1456 AA.
AC   A0A0W0FF95;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=WG66_12495 {ECO:0000313|EMBL:KTB34954.1};
OS   Moniliophthora roreri.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB34954.1, ECO:0000313|Proteomes:UP000054988};
RN   [1] {ECO:0000313|EMBL:KTB34954.1, ECO:0000313|Proteomes:UP000054988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB34954.1,
RC   ECO:0000313|Proteomes:UP000054988};
RA   Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT   "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT   pod rot of cacao.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KTB34954.1}.
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DR   EMBL; LATX01002022; KTB34954.1; -; Genomic_DNA.
DR   eggNOG; KOG1027; Eukaryota.
DR   Proteomes; UP000054988; Unassembled WGS sequence.
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; 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; 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:ARBA00022527};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054988};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1456
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006901740"
FT   DOMAIN          968..1318
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1321..1453
FT                   /note="KEN"
FT                   /evidence="ECO:0000259|PROSITE:PS51392"
FT   REGION          500..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          627..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          793..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          869..949
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1188..1228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..530
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..547
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..656
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        793..850
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        869..887
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1195..1228
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1456 AA;  158772 MW;  0E945D9385CF1EF3 CRC64;
     MAPIFLLSSL FLSFLIACYA DRVSRELAPF SSGAGSSRFA QRQILTEEHA SSSSTGDADP
     LGDSDLVDIV LVASVDGKFH ALNRTSGHLL WSMAAKDGFS AGTGNSSTLA PLVRTQHPLL
     SNDPNGESNK VTSAYPSPTT EFYIVEPQSG DIYVASTASP LGPLQRFRYS MPELVDMSPF
     SFKDEDYQRM FVGRKESRLI LVELETGKIK EVVGTDECRW DPLEFGFGGE EREEDEGTSY
     VVDLDELEEG AAEIEYVDDD EYSNSSSTYG DDAKKKKPTE VYIGRTDYHI SIYTKPTSVA
     SAKRPVPPVQ NLSFSVYGPN NQDSRLQTTY TRTKDDKYLA SLPSGEVIAF KAHGKGDEKR
     ERIPWLWIKP FQNPIVATFD VFRRRGNNDN SPVGAVDNDS ESHTFVLLQP QPSLTDIHPS
     LDLSLYQSAP ASEDGGEGSG SQTPLTNILP NADSAYVGIL EETGSLFAMS PETYPLVAFG
     GHWAASGTTS RSRLIDGAAN HKYDDDGEED NFISVDELTR RRKEREAETS SSESQSTSSA
     SPITTNGAQS TLRANMCNVE DGGVFDARCL VGVRKLADGA GGVDVGKNTD FGGATGTRRA
     GVVTFETDAD PEGRWRRLLD PPKRGYGEVY REDYEHPSTS VSRPSQPSQR PTHSSDPTVP
     VVEKHVFLGA SSGIIATAFA VALVLVGMWW RGAVGQTALH RLHAPLEPSQ TAKLEPGHEH
     SGVIDPNVLA NGITNGDATV DPHIVKPDTI LLQPDTTVIA DAQLAASQST STQDKIPVRH
     RANSDVFALS EVQSIPSRSP VQKPSRLPSS PKTSTVKLPQ TSSTPTPPTP KVQSRTRKQS
     TSTANRNLID SPRLEESDFE MFEHDGADLE GEGEVDEDGE GENEPEAEGV EAGTPKKSKV
     RRGKRGRKKR KGAAAEGNGN GGTPVPAKGK DKENVPVPSP SPAPAATPLT PSMIVVPPTP
     AVTQPSLIVS DSILGFGSHG TVVFRGDLQG RQVAVKRLLR SFVTLASREV SILQESDDHP
     NVIRYYYQEA HADFLYIALE LCPATLADII EYAAGGGIDW GGSVESRTLG GTGKEGMKPE
     EWDDLIRCFD PKKALKQIAS GLRHLHALKL VHRDIKPQNI LVSAGPGRGA RGTTRGSMGG
     YRMLISDFGL CKKLDMDQTS FLPTAQGAMG AGTVGWRAPE ILRGEVKLDE SASGDDQSSR
     GSSTGTLTNA SIGSTSTTTG STGVSSGAKS TRLTKSVDIF SLGCLFYYTL TNGQHPFGDR
     FEREVNILKG AMNLDGLDRV DGGMWSEEGV EARDLIQRIH THHEHRPDTT TCLLHPFFWD
     SGRRLNFLQD ASDRFEIMCR EPKEAHLISL EEGAADVVGN DWYSRMDKIF IENLGKFRKY
     NGSSVQDLLR ALRNKKHHYQ DLPENVKRHL GAMPEGYLAY FTRRYPKLFM HVHRVIDECD
     LKDESMFRTY FELADQ
//
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