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Database: UniProt
Entry: A0A4Q4U313_9PEZI
LinkDB: A0A4Q4U313_9PEZI
Original site: A0A4Q4U313_9PEZI 
ID   A0A4Q4U313_9PEZI        Unreviewed;      1217 AA.
AC   A0A4Q4U313;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=DL766_009681 {ECO:0000313|EMBL:RYP14441.1};
OS   Monosporascus sp. MC13-8B.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Xylariales incertae sedis; Monosporascus.
OX   NCBI_TaxID=2211646 {ECO:0000313|EMBL:RYP14441.1, ECO:0000313|Proteomes:UP000292509};
RN   [1] {ECO:0000313|EMBL:RYP14441.1, ECO:0000313|Proteomes:UP000292509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC13-8B {ECO:0000313|EMBL:RYP14441.1,
RC   ECO:0000313|Proteomes:UP000292509};
RA   Robinson A.J., Natvig D.O.;
RT   "Complete Genomes of Monosporascus.";
RL   Submitted (JUN-2018) 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:RYP14441.1}.
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DR   EMBL; QJNW01000655; RYP14441.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q4U313; -.
DR   STRING; 2211646.A0A4Q4U313; -.
DR   Proteomes; UP000292509; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 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   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; IPR002372; PQQ_repeat.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
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:SF6; ENDORIBONUCLEASE; 1.
DR   PANTHER; PTHR13954; IRE1-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF01011; PQQ; 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; PS00107; PROTEIN_KINASE_ATP; 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, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000292509};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..1217
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5020218524"
FT   DOMAIN          785..1078
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1081..1213
FT                   /note="KEN"
FT                   /evidence="ECO:0000259|PROSITE:PS51392"
FT   REGION          63..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          647..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..566
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        684..708
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..725
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..740
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         813
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1217 AA;  134431 MW;  0FCF84ED9274AD44 CRC64;
     MLRQPPGEGR LVAQQRKVLL ALAFILLPWI QIVDAQQQQR QQQPSPQQAP IAAHVLHNNV
     ALGQNDDDLN QGRHAGHPRQ ESSPFEGRHA ADDLVATSLK AAINARPTPN SDRDNTVTSH
     KKESFGSLHI PYDASALATL APAQPVRAPS SPRQLPSLLA GAGLSSPQSA RSLENWEVED
     FVLLATVDGH LYAVNRTSGE ERWHLQVEQS VVETIHHKLN NSGAGGGGSE EDNHHPLDDY
     IWAVEPTRNG ALYVWTPSGL TSGLMSTGFT MKQLVDDLGP YAVQNPPVVY TGHKRTTMIT
     LDAATGRVFK WFGQSGSQVD QTATCYRPDG RLVDTGSDEC SNSGTITLSR TEYTVTIHRL
     DDGRAIATLK YSEWGPNNSD YDLHQQYRVA HRNRYITSKT DGKLFALDPS GLSPLVLQSS
     NPVAHVFDIA RPEDTPAGGS PELVVLPQPA PPSQDDEAAH ARSHRVFLNQ TESGSWYAMS
     GVWYPLILEA PTARINRRNW WDVQNTWDAL DEAEVNDALV GTHTLGNVKN MVHRPPSLPP
     GLPAESYSGS HEVETTENSS TPPSPTPHDG ADALTIVDKV IALPQKARDS VIELMVNPIS
     ITIILGLATF KLRDMIHKWK RKRNSKGYPD ASDKVQPRGE SFATVLDTAP AAPGGDKIEG
     VHVGPQTEGR VDAKRADAVV PVVTHEPARD DVEPEQPLQD AESPEKKPKK AHRGRRGGVK
     HRKGLKKQQD RSESRGDSAS PDIDDTIPGI KNVGVPPKLE PNVITLKSNP EDVSGPIIEI
     GGIEVNQDEQ LGMGSNGTVV FAGKFHGRDV AVKRMLTQFW DIATQETQLL LESDHHPNVI
     RYFAMSRNES FLYIALELCQ ASLSDIIDKP HMFRELAQAG EMDLPHVLLQ IANGLSFLHD
     LRIVHRDLKP QNILVTMGRD AKPRLLVSDF GLCKKLEGGQ SSFGATTAHA AGTSGWRAPE
     LLLDDDAREG SMSMASTHSD SSQLVSSDVM PNRRATRSID IFSLGLVFFY VLTKGSHPFD
     CGDRYMREVN IRKGQFNLAP LDVLGDVAYE AKALVEAMLQ SDPRARPTAR DVMAHPFFWS
     AKERLAFLCD VSDHFELEQR DPPSEALSEL EHWAPKVCRG DFLKLLPKEF VDSLGKQRKY
     TGSKLLDLLR ALRNKRFHYG DMSDSLKKVV GPLPDGYLGF WTRRFPNLLI VCCRVVYRVK
     LQDTDTFREY FKPRTPL
//
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