ID A0A0D2FJM2_9EURO Unreviewed; 637 AA.
AC A0A0D2FJM2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Serine/threonine-protein kinase gad8 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV04_06221 {ECO:0000313|EMBL:KIW66940.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW66940.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW66940.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW66940.1,
RC ECO:0000313|Proteomes:UP000054266};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN846959; KIW66939.1; -; Genomic_DNA.
DR EMBL; KN846959; KIW66940.1; -; Genomic_DNA.
DR STRING; 5601.A0A0D2FJM2; -.
DR HOGENOM; CLU_000288_120_0_1; -.
DR OrthoDB; 10768at2759; -.
DR Proteomes; UP000054266; 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:SF243; RIBOSOMAL PROTEIN S6 KINASE; 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
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 295..552
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 553..624
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 14..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 637 AA; 70509 MW; 77CFF0B70FC62408 CRC64;
MSWKLTKKLK ETHLAPLISG SSRSTSTSTV KAEDSSPAHE SPELSTIHSN TSTSSANGIA
ASEQLTSPPV QTTKPGILIV TLHEGKGFSL PQQYQSVFNS HYGSGQTGSV RPSSSYAAGS
MAGSYAPSNR PVSTHAGINA APTIHGRYSS KYLPYALLDF DKLQVFVDAV SGTPENPLWA
GDNTSFKFDV SRVCELSVQL YLRNPAARPG VGRSEDIFLG GARVTPRFEE ARQFVADPKK
SKKDNEKAET AFNAQEKQAG QLGADWVDIQ FGTGSIKVGV NYVENRQGSL KIDDFELLKV
VGRGSFGKVM QVMKKDTGRI YALKTIRKAH IISRSEVAHT LAERSVLAQI NNPFITPLKF
SFQSPDKLYF VLAFVNGGEL FHHLQKEQRF DINRSRFYTA ELLCALECLH GFKVIYRDLK
PENILLDYTG HIALCDFGLC KLDMKDEDRT NTFCGTPEYL APELLLGHGY TKTVDWWTLG
VLLYEMLTGL PPFYDENTNE MYRKILQEPL HFPGPEIVPA AAKDLLQKLL DRNPERRLGA
GGAAEIKAHH FFAGIDWRKL LQRKYEPSFK PNVVDARDTA NFDKEFTSEV PKDSYVEGPV
LSQTMQQQFA GWSYNRPVAG LGDAGGSVRD PSFGSIQ
//