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Database: UniProt
Entry: A0A3N2PRF5_9PEZI
LinkDB: A0A3N2PRF5_9PEZI
Original site: A0A3N2PRF5_9PEZI 
ID   A0A3N2PRF5_9PEZI        Unreviewed;      1549 AA.
AC   A0A3N2PRF5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=SODALDRAFT_360750 {ECO:0000313|EMBL:ROT37075.1};
OS   Sodiomyces alkalinus F11.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX   NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT37075.1, ECO:0000313|Proteomes:UP000272025};
RN   [1] {ECO:0000313|EMBL:ROT37075.1, ECO:0000313|Proteomes:UP000272025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F11 {ECO:0000313|EMBL:ROT37075.1,
RC   ECO:0000313|Proteomes:UP000272025};
RX   PubMed=30368956; DOI=10.1111/mec.14912;
RA   Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA   Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA   Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA   Grigoriev I.V., Debets A.J.M.;
RT   "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT   shifted to a protein diet.";
RL   Mol. Ecol. 27:4808-4819(2018).
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; ML119057; ROT37075.1; -; Genomic_DNA.
DR   STRING; 1314773.A0A3N2PRF5; -.
DR   OrthoDB; 1630at2759; -.
DR   Proteomes; UP000272025; 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; IPR018391; PQQ_beta_propeller_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; 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; 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   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000272025};
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          1074..1366
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1369..1500
FT                   /note="KEN"
FT                   /evidence="ECO:0000259|PROSITE:PS51392"
FT   REGION          298..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          891..1030
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..932
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        942..959
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        960..974
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        996..1016
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1549 AA;  172938 MW;  4AECF8BCDE9B6CA8 CRC64;
     MHLFGPRNRL FACVEVRTII SREWCERLVG GGKAFCRGSS LRRSIGTPTQ IAAFSKCEYY
     SFQIIYSYGV RDSIVTPTRA FHSLALALGP SFPDPFGPSL GPGTRNLFHI ILNNQFFRII
     FDSSPLLLQF LQSLQFLLLL HPLNPVACLV WTQVLRDSRA RHLANKTLGP QRSAIIIVPT
     PFALQSHAPF SRLLESFLVL TSFGSDFLFL LRSQPNGAAL IPSSVLLPHP NMPPRRPPGD
     GGLGSPKCLL TLAVLLFTYL PLAEAQQQQR RADAQPLAQV QPDDLARHIL PAADRQWLHP
     SDASKGDDHT GHPIILSGEE RAVIEKKTTE RSQDRNRDGD RIINRNDKRN HNIHLEIPNR
     HDINYIKNNN TPNQNDARAV ATLAPAQSVR APPSSHRLIT RPDTGSGSGI STQPGARSLG
     EWEVEDFVLL ATVDGDLYAS DRQTGTVRWH LEVDQPMVET VHHRLNTSEL DDDHHPVDHY
     VWAVEPTRDG SLYIWMPGAP DPAILPTGLT MKSLVEELSP LANDNPPVIY TGTKKTTMIT
     IDASTGRVLK WFGSSGSHVN EEESCLRPSG IYDFDREECS STGTITLGRT EYEVAISRKD
     GRAIANLRYA EWTPNNFDRD LMSTYRRTLD NRYHSSRHDG GVYAFDLDAS DERLIFADKF
     DSPVARVFDV CRPWGVTPDQ NPDLLVLPQP IPPPQNDDVA RLRSSHVFLN QTGAGSWYAL
     SGLSYPLIVD APPALTSLRQ WLELDRPWGL LTQNQKSAAM IGRHSFDSVR EKGPQYYPPT
     LPGGSVSQPV DDHENDSTLP TLVPDDLDGP TIVAKVRSIP QQAANSFVDL FKNPVLISIL
     VLSFFFYHKD LIRWSKAKSR KFLLQREQWS KPGDLVSADL ALGSSVHAEV PALDPRTDDT
     PEEKAQQQQV QQQQQQQQQQ QQQQQQLVEP SAVDEHTTAV PERTENSGLS EKSNSGQAPS
     PSSTPPPPPD LAASPAKPAA KIDAENSAAG PPEKKKGKAH RGRRGGVKHR KNGPKKRDIS
     TSRDDEPAAT TVEDAVKNAK RLGNSPKLEP DVVTITNDMQ SVTGPVFKLG SIEVDMEHQL
     GTGSNGTLVF AGRFDGREVA VKRMLIQFYD IASQETRLLR ESDDHPNVIR YYAQEARDGF
     LYIALERCAA SLADVVERPS RFPQLAQAGR ADLPAVLYQI ANGINHLHSL RIVHRDLKPQ
     NILVNMDKGG RARLLVSDFG LCKKLEGGQS SFGATTGRAA GTTGWRAPEL LLDDDKDPLT
     DASINSGSGT PLVNSDLLPN RRATRSIDIF SLGLVFFYVL SNGQHPFDCG DRYMREVNIR
     KGNHNLSPLS VLGDYASEAK DLIRTMLDSN PKARPTTHDV MSHPFFWSAK KRLAFLCDVS
     DHFEKEPRDP PSEPLLKLEE YAPIATKGDF LRHLPREFVD SLGKQRKYTG TRLLDLLRAL
     RNKRNHYEDM SDSLKRTVGP LPEGYLSFWT VRFPELLLAC WNVVWELRFR SKFYQSPLSI
     WRETKRPRIY LDSTLPGFVI QGISPDDTLN NALQSRWHSF RDHRSTQFS
//
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