ID F2Q464_TRIEC Unreviewed; 499 AA.
AC F2Q464;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Aspartic-type endopeptidase {ECO:0000313|EMBL:EGE08932.1};
GN ORFNames=TEQG_07887 {ECO:0000313|EMBL:EGE08932.1};
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).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS995790; EGE08932.1; -; Genomic_DNA.
DR AlphaFoldDB; F2Q464; -.
DR VEuPathDB; FungiDB:TEQG_07887; -.
DR eggNOG; ENOG502SA90; Eukaryota.
DR HOGENOM; CLU_028892_1_0_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd12087; TM_EGFR-like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR049328; TM_ErbB1.
DR Pfam; PF00026; Asp; 1.
DR Pfam; PF21314; TM_ErbB1; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..499
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003288391"
FT TRANSMEM 410..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..381
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 98..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 499 AA; 53634 MW; EC955857BB8B3EDC CRC64;
MGCSLLLTCA YLLVSFSGLV RSACNAPPLF LSIGNGTISD REVVRWGLAV EFGTPSQTIV
AALDADWNST SFWNTSFPCG NLSRPACSWV HGGSFNDKGS TSWREPEDPQ QTDKSPTGGT
INIRGTDTLK VGSGISLDQF PVYFPKPGVI PQNGIGFGPN STFLNRLYDQ GKIASRSWSL
FWGLQGAEQE NQMNGSLVLG GYDQAKIAGG IPLKAQFSDG IGCPSSLLVY LSNIVVNHIN
GNKTSLLTTP GSALRACIKP DNPQVVLPED VFGNLKKAFP GKAVEHSTGI YPTSLAYEPE
DVFMGNITFI LSSGLQVTIP NHQLVLPNVE IDDNGQQKLI DGNKTINFGQ SRHEAMPYLG
QPFLTSAYIH VNNDLKEFSV WQANPTTDTN LITIQSGSNC DDNSSLSGGA IAGIVVGAVA
FLAIAALGLF FFLKRRNQNR DRDSKAGLPL VNTSQRAEED KKDTPLEMDA GVSQQAPSEL
PSRDYEPQEL PADVPTSNK
//
