ID F2SL47_TRIRC Unreviewed; 758 AA.
AC F2SL47;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=TERG_03628 {ECO:0000313|EMBL:EGD87379.1};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD87379.1, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
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; GG700650; EGD87379.1; -; Genomic_DNA.
DR RefSeq; XP_003236584.1; XM_003236536.1.
DR AlphaFoldDB; F2SL47; -.
DR STRING; 559305.F2SL47; -.
DR GeneID; 10376646; -.
DR VEuPathDB; FungiDB:TERG_03628; -.
DR eggNOG; ENOG502SJ0M; Eukaryota.
DR HOGENOM; CLU_010672_2_0_1; -.
DR InParanoid; F2SL47; -.
DR OMA; HVMITEG; -.
DR OrthoDB; 2691421at2759; -.
DR Proteomes; UP000008864; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR37171; SERINE/THREONINE-PROTEIN KINASE YRZF-RELATED; 1.
DR PANTHER; PTHR37171:SF1; SERINE_THREONINE-PROTEIN KINASE YRZF-RELATED; 1.
DR Pfam; PF06293; Kdo; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000008864}.
FT DOMAIN 569..758
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 402..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 21..73
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 412..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 86249 MW; 3B89ABF26B429E04 CRC64;
MSQDADYKAL LLEAEERARQ EKELRLQAEG LRLQAEGLRL KEEELRLQAE ERASKAEARA
SQEREQRQQA TQKTTFDEYL WGCHRLISLT IRVQRIEHST QGSINKPTGK VCPRYLQQWG
DCSDTLQYFY QHVYEFLRQE RLFLPVITLE GLGQILNHPI GSEKDVEFYG RLAVERHVYN
IISELCKIEE AREVFQLGEE ITFENHANSI DDPDNDIEAN YSPIIDRAFA DQFCIHKVKE
GTTTLLTTVE YKPPHKLPPE YLNSGLRPMD LWEEVVLRDI KAIPPGEKIK YNAEKISASV
LVQEYHVMIT EGLEYSYVTN GISYVFLRVP EDDPQTLYYF LCEPNADVHP DDIGPWTAIA
RVLAFCLMCC QSTARDHTWR NHQLRHGLRW ETDLDYVRSQ IPKEELRQTP PGSEYIPSSS
PAGSFSAPDN RGGIRTRSQT RCAPNTETQG SGPTDSDSDP EAPSGSGAHL GGRKRNLSEL
TSSSSQHGEG AGQRGQRGQR GQVQQRRQHV ESFCTQKCLL GLRLGTRLDM DCPNVGRHRQ
GNTTSTHHSI SADQLVSLIN RQLDENIDLD CTPYGKHGSY GQPFKVTCRS YGYTVLGKGT
TAFRWNEVRR EVEVYRFLHS AQGSAVPVFL GPINLDMVYH VHGAGSIRHM LLMGFGGEEV
GKRSRELASH IERSTQELHD LGVIHGDLKP NNMLWNAELQ RVLLIDFHDS KLMLPLERTK
KKQKVMNQQS KKGSFKRLAD KGETNEGVKR TRLHLCET
//
