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Database: UniProt
Entry: A0A2J6Q028_9HELO
LinkDB: A0A2J6Q028_9HELO
Original site: A0A2J6Q028_9HELO 
ID   A0A2J6Q028_9HELO        Unreviewed;      1149 AA.
AC   A0A2J6Q028;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=NA56DRAFT_575061 {ECO:0000313|EMBL:PMD19622.1};
OS   Hyaloscypha hepaticicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX   NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD19622.1, ECO:0000313|Proteomes:UP000235672};
RN   [1] {ECO:0000313|EMBL:PMD19622.1, ECO:0000313|Proteomes:UP000235672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD19622.1,
RC   ECO:0000313|Proteomes:UP000235672};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ613488; PMD19622.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6Q028; -.
DR   STRING; 1745343.A0A2J6Q028; -.
DR   OrthoDB; 1630at2759; -.
DR   Proteomes; UP000235672; 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; 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; 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; 2.
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:UP000235672};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..1149
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014433183"
FT   DOMAIN          715..1011
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1014..1146
FT                   /note="KEN"
FT                   /evidence="ECO:0000259|PROSITE:PS51392"
FT   REGION          575..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..609
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..650
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        658..673
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1149 AA;  128001 MW;  142F6B5B9A68ED80 CRC64;
     MPRRRPPREG PVVNNFFLFA AAIFFLPWLV EAQQQQRPAV QQRHESPHES LDLEASHTLE
     VTKIPHQVET PLTHNRRKNT LSVTNGPAKN DASAIATLAP APSAVAAPFS RLPGTSGLSS
     PHTARSLEDW EVEDFVLLAT VDGKLHARDR KTGKEKWSLE YHKPMVEINQ NRSNPTPIDE
     EYDPVSIDDY LWIVEPSRDG ALYIYKPGGP NPGLVNTNLT MKYLVEEMSG YVSQDPPITY
     IGGKNTNIIT VDANSGKILS FFGQEGAFLN DEKCVASNGP VDSKEECPKT STLTVGRTEY
     WVKIAGNDGH HIATLTFSEW TPNNFDTDLL RQYHSTLDGK YIYTSHDGGV FGFDHNRDSP
     DEPGRLFTHK FTSPVVRVFD VAKPWNGGRE ADLVILPQPS PPHREDVVTA SHRAGSIFLN
     HTESGSWYAL SGKTYPLAVQ GIRPAQCSQH GWLQHRPQWD LTNGQQLHEA LVGLHSIDNG
     RWEPLLSISG PMDDNQTVDP ISNNTPALVE EQGFFPPVRQ WPSLAAKYGR DTVQNPLLIV
     MLVVMIWSYQ KQIKSWVHRT GEKFMKSYSV EAEDKTLPEA DDAPNVAEKD ELKISSVDGA
     DEAPEKAEKT EAVLNPVAPR PDSPDEESPP PPGKEKKKAH RGRRGGVKHK KGRAGSTDGG
     SQDGSTPKTQ PTIDDAVKDA QNMGPQTKLE PDIITVTSDP QEVSGPIIKI ASLEVNTEKL
     IGTGSNGTMV FEGKFDGREV AVKRMLIQFF DIASQETKLL RESDDHPNVI RYFAQQAAAG
     FLYIALELCP ASLADVIDKP MKYQEIAQAG EKDLPNVLYQ ITNGLSHLHS LRIVHRDLKP
     QNILVAMGKD GKPRLLVSDF GLCKKLEGEQ SSFRATTAHA AGTSGWRAPE LLLDDDAKDG
     HHAIVDASTD GGSGPVVLGA ENLPNRRATR AIDIFSLGLV FFYVLTKGSH PFDCGDRFMR
     EVNIRKGSYD LTLLEVLGDY AYEAKDLISS MLARDPKQRP QAHQVMAHPF FWSPKKRLNF
     LCDVSDHFEK EKRDPPTAAL TELESYAPSV CGSDFLKLLG KEFVESMGKQ RKYTGTRLLD
     LLRALRNKRN HYEDMSDKLK KDVGPLPDGY LSFWTRRFPN LLITCWNVVY DVQWDETDRF
     REYYLPAGL
//
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