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Database: UniProt
Entry: A0A2J5HR29_9EURO
LinkDB: A0A2J5HR29_9EURO
Original site: A0A2J5HR29_9EURO 
ID   A0A2J5HR29_9EURO        Unreviewed;       640 AA.
AC   A0A2J5HR29;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   08-NOV-2023, entry version 19.
DE   SubName: Full=Pkinase-domain-containing protein {ECO:0000313|EMBL:PLN79729.1};
GN   ORFNames=BDW42DRAFT_201575 {ECO:0000313|EMBL:PLN79729.1};
OS   Aspergillus taichungensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=482145 {ECO:0000313|EMBL:PLN79729.1, ECO:0000313|Proteomes:UP000235023};
RN   [1] {ECO:0000313|Proteomes:UP000235023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 19404 {ECO:0000313|Proteomes:UP000235023};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L.,
RA   Theobald S., Kuo A., Bowyer P., Matsuda Y., Lyhne E.K., Kogle M.E.,
RA   Clum A., Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA   LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA   Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R., Nordberg H.P.,
RA   Cantor M.N., Hua S.X.;
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ559556; PLN79729.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J5HR29; -.
DR   OrthoDB; 10768at2759; -.
DR   Proteomes; UP000235023; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd11651; YPK1_N_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF234; SERINE/THREONINE-PROTEIN KINASE YPK2/YKR2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PLN79729.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          297..554
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          555..626
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          23..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          106..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          232..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..250
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..266
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         330
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   640 AA;  71262 MW;  91F1A6956290A705 CRC64;
     MSWKLTKKLK ETHLAPLTQT FARSSSTSTI KGDAAEEAPT PVATQSPSSV SPNNGISASE
     SLVSPPVAPV KPGILIVTLH EGRNFALSPH FQQIFASHFQ NNNAYPVRPS SSSSHSTHGQ
     AASFVQSARP QSTSSGINNA PTIHGRYSTK YLPYALLDFE KNQVFVDAVS GTPENPLWAG
     DNTAFKFDVS RKTELNVQLY LRNPAARPGA GRSEDIFLGA VKVHPRFEEA APPYVEDPKL
     SKKDNQKAAA AHASQERNTG QGQHGNDWLD LQFGTGSIKI GVSFVENKQH SLKLEDFELL
     KVVGKGSFGK VMQVMKKDTG RIYALKTIRK AHIISRSEVT HTLAERSVLA QINNPFIVPL
     KFSFQSPEKL YFVLAFVNGG ELFHHLQREQ RFDINRARFY TAELLCALEC LHGFKVIYRD
     LKPENILLDY TGHIALCDFG LCKLDMKDED RTNTFCGTPE YLAPELLLGN GYTKAVDWWT
     LGVLLYEMLT GLPPFYDENT NDMYRKILQE PLTFPSSDVV PPAARDLLSR LLDRDPQRRL
     GANGAAEIKS HHFFANIDWR KLLQRKYEPS FRPNVVDARD TANFDREFTQ EAPQDSYVDG
     PVLSQTMQQQ FEGWSYNRPV AGLGDAGGSV KDPSFGSIPE
//
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