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Database: UniProt
Entry: C5FJ66_ARTOC
LinkDB: C5FJ66_ARTOC
Original site: C5FJ66_ARTOC 
ID   C5FJ66_ARTOC            Unreviewed;       638 AA.
AC   C5FJ66;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Serine/threonine-protein kinase gad8 {ECO:0000313|EMBL:EEQ29396.1};
GN   ORFNames=MCYG_02215 {ECO:0000313|EMBL:EEQ29396.1};
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ29396.1, ECO:0000313|Proteomes:UP000002035};
RN   [1] {ECO:0000313|Proteomes:UP000002035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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DR   EMBL; DS995702; EEQ29396.1; -; Genomic_DNA.
DR   RefSeq; XP_002849281.1; XM_002849235.1.
DR   AlphaFoldDB; C5FJ66; -.
DR   STRING; 554155.C5FJ66; -.
DR   GeneID; 9223218; -.
DR   VEuPathDB; FungiDB:MCYG_02215; -.
DR   eggNOG; KOG0598; Eukaryota.
DR   HOGENOM; CLU_000288_120_0_1; -.
DR   OMA; YLVMEFE; -.
DR   OrthoDB; 10768at2759; -.
DR   Proteomes; UP000002035; 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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEQ29396.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002035};
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..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..70
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   638 AA;  70940 MW;  0D0829E2F9B0750B CRC64;
     MSWNLTKKLK ETHLAPLANT FSRSSTGSSP KGDASTEDGA PLSKTPTASS STSSNGIAAS
     DATTNSPTQS LKPGILIVTL HEGKGFSLSP HYEHVFNSHY QGSSGSYSAS MRPSSSHASH
     IPNSFTHAMR PQSTSGGINA APTNHGRYSA KHLPYALLDF DKLQVFVDSV SGTPENPLWA
     GDNTSFKFDV SRVTDLNVQV YIRNPAARPG SGRSDDIFLG ACKINPRFEE PRRFVEDPKA
     SKKEREKAAA AFAQKEKQLG QLGSEWIDLQ FGTGSIKIGV SFVENRQRSL TMADFELLKV
     VGRGSFGKVM QVMKRDTKRI YAMKTIRKAH IISRSEVEHT LAERSVLSQI SNPFIVPLKF
     SFQSPEKLYL VLAFVNGGEL FHHLQREQRF DINRARFYTA ELLCALECLH GFKVIYRDLK
     PENILLDYSG HIALCDFGLC KLGMKDEDRT NTFCGTPEYL APELLLGHGY TKTVDWWTLG
     VLLYEMLTGL PPFYDEDTNE MYRKILHDPL TFPNQEVVPA AARDLLSRLL DRDPHRRLGA
     GGAGEIKGHH FFANIDWRKL LQRKYEPSFR PNVADARDTA NFDIEFTSEV PVDSYEEGSG
     LSRTMQKPFE GWSYNRPVAG LNDGGGSVRD PAFGSIPE
//
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