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Database: UniProt
Entry: C5FG50_ARTOC
LinkDB: C5FG50_ARTOC
Original site: C5FG50_ARTOC 
ID   C5FG50_ARTOC            Unreviewed;       601 AA.
AC   C5FG50;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=MAP kinase activator {ECO:0000313|EMBL:EEQ29735.1};
GN   ORFNames=MCYG_02554 {ECO:0000313|EMBL:EEQ29735.1};
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:EEQ29735.1, 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; EEQ29735.1; -; Genomic_DNA.
DR   RefSeq; XP_002849620.1; XM_002849574.1.
DR   AlphaFoldDB; C5FG50; -.
DR   STRING; 554155.C5FG50; -.
DR   GeneID; 9222590; -.
DR   VEuPathDB; FungiDB:MCYG_02554; -.
DR   eggNOG; KOG4773; Eukaryota.
DR   HOGENOM; CLU_014957_1_0_1; -.
DR   OMA; FICAHHN; -.
DR   OrthoDB; 1368965at2759; -.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05992; PB1; 1.
DR   CDD; cd06890; PX_Bem1p; 1.
DR   CDD; cd11879; SH3_Bem1p_2; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 2.
DR   InterPro; IPR035550; Bem1/Scd2_PX.
DR   InterPro; IPR035549; Bem1/Scd2_SH3_2.
DR   InterPro; IPR000270; PB1_dom.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR15706:SF2; BUD EMERGENCE PROTEIN 1; 1.
DR   PANTHER; PTHR15706; SH3 MULTIPLE DOMAIN; 1.
DR   Pfam; PF00564; PB1; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF00018; SH3_1; 2.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00666; PB1; 1.
DR   SMART; SM00312; PX; 1.
DR   SMART; SM00326; SH3; 2.
DR   SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 2.
DR   PROSITE; PS51745; PB1; 1.
DR   PROSITE; PS50195; PX; 1.
DR   PROSITE; PS50002; SH3; 2.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EEQ29735.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002035};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transferase {ECO:0000313|EMBL:EEQ29735.1}.
FT   DOMAIN          32..97
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          159..221
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          304..424
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   DOMAIN          525..601
FT                   /note="PB1"
FT                   /evidence="ECO:0000259|PROSITE:PS51745"
FT   REGION          102..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          282..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          425..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..522
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   601 AA;  68050 MW;  49D448B075BC5233 CRC64;
     MKVSRLPRSL KGEKEKSQHV SITPKSALAI LPPKKVIKAL YDYQPSPDNR EELAFSKGDF
     FHVISREDDL SWYEACNPLF PNARGLVPVA FFEVIGKNQR DSGDSVHAPV DLQQQQQQHH
     HHQPRLAHDS GFSDSSNNNK TEEKASHFRM SSLGKAGAAA MVYGIVMYDF NAERPDELDA
     KAGEAIIVIA QSNPEWFVAK PIGRLGGPGL IPVSFIEIRD MSTGKSAADP LEAVRRAGVP
     RVEEWKKMTA EYKNSSISLG KFENGAQQAA AELERMNLNS RSNVHQRNPS KGYPQQQHQQ
     QQHYQVPIPV QASIPRYCFD NDKYWYIVEV QMEDGRWWEL SRYYHDFYDF QIALLSKFEE
     EAGNRGGQRT LPFMPGPVTQ VTNAISNSRR QSLDEYVKQL LAMPPHISRC QLVRQLFAPR
     PGDFEIDPTV MSDDYRLSTG SQQSSGHNPS RTASRQSSQG QMNAASQGYH PSQRPTHQRN
     QGSISHQPQQ LLQQQQQQQQ PPPMSRQGSS FNSNSNQMPS QNPGAIKIKV FFQDDIIVIR
     VPDDISLRQL IDKLRDRLKV DAMVVRYKDE PSNSFVELLN DADLETAIRR NAKLMLYVST
     V
//
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