ID F2Q378_TRIEC Unreviewed; 781 AA.
AC F2Q378;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Protein kinase subdomain-containing protein {ECO:0000313|EMBL:EGE08596.1};
GN ORFNames=TEQG_07514 {ECO:0000313|EMBL:EGE08596.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
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; DS995783; EGE08596.1; -; Genomic_DNA.
DR AlphaFoldDB; F2Q378; -.
DR VEuPathDB; FungiDB:TEQG_07514; -.
DR eggNOG; ENOG502SHD6; Eukaryota.
DR HOGENOM; CLU_010672_3_1_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EGE08596.1};
KW Transferase {ECO:0000313|EMBL:EGE08596.1}.
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 88618 MW; 90B83C6A42B063FD CRC64;
MADDEIQRLR AQLRDEQRRR QEAERAKQEA ERAKQEAERA KQEAERAKQE AEQLQQTFEE
QLRPLTLFEY LDACHTYLFS GIAAGTLKSS TKGRADNAVG KLRPNYIRKW SSFDDEQTEI
WDQLLNMENE GFIEQLKFDS SHGMITLGKK TRKKISSELD LRHFQRDAIT EPVGSIIEAL
FDNESLRHVF GIQGQVTFEN HANTLVDSEE EEAEGAMGRP SKLRKGASGA ATPTNVESSR
RTLADEFCIY NAGEKAKKPA MVGELKPPHK LSLKVIKKGL RKMELDEVVE RRHDDTDKIR
HRRLMAAVIT QAFSYMIKAG VEYGYISTGE AFIFLHFKAD EPGTLYYRLS VPETDVNQES
EDDHGNRLRK TAVGQVLAFT LRAMRTNPLD QKWKDWAISQ LKVWVITEGD LYLPTSEEDE
KQDEQPPTPY RPSKSAQMVI RNTPVRTRSR SSRSTCKPTS SQQNSSGEDD KDDESDHDSP
SQRPRRSANV MVVIPPPQPP ISDSSYTGPV CRDGVRRYCT QKCLLGLLNG GLLDKTCPNV
KEHGTEVHQI DHSTFISLLL AQILQKIVSP WTQPLGCESL HRHGTRGALF EVILFKYGYT
LIGKGFPSWF GKYLKNEQAL YNQLRPVQGI HVPVCLGTID VSKRPMFYDG IADIPHLLLL
AHAGTGILEC GVAKNKIISA ASESLRAIHA LGVLHRDAEP RNLLWSEEGK NVLVIDFERA
EVLRSERAPL GSMSLNRKRK KGSGNMEEET KVVTKERWID HRLEEELRGM RGYLKWNLSY
I
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