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
//