ID E3S1J3_PYRTT Unreviewed; 619 AA.
AC E3S1J3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=PTT_16091 {ECO:0000313|EMBL:EFQ88145.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ88145.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ88145.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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; GL536583; EFQ88145.1; -; Genomic_DNA.
DR RefSeq; XP_003303748.1; XM_003303700.1.
DR AlphaFoldDB; E3S1J3; -.
DR EnsemblFungi; EFQ88145; EFQ88145; PTT_16091.
DR KEGG; pte:PTT_16091; -.
DR eggNOG; ENOG502RV5I; Eukaryota.
DR HOGENOM; CLU_009988_3_0_1; -.
DR OrthoDB; 1831139at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05471; pepsin_like; 1.
DR CDD; cd12087; TM_EGFR-like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR15549:SF26; AXIAL BUDDING PATTERN PROTEIN 2-RELATED; 1.
DR PANTHER; PTHR15549; PAIRED IMMUNOGLOBULIN-LIKE TYPE 2 RECEPTOR; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 433..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..391
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 406..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 619 AA; 66895 MW; EE7A17C34505C0C3 CRC64;
MSLAARRADA PDAPKPYIVP PSKKFDGTDG SWSTFVISVG TPGQQFRVLP STKSGVTFVV
APEGCLPDTD PSDCPTLRGV EVLNSAQGSG FEVSRSATWS AIGQYDVDLE DALNYTARGL
YGLDTVSLGA AADSSSSPTL TDQVVAAVAD PDYFLGMLAL GQAKSSFNSG SKPIDSFLAA
LRESAKIPSF SYAYTAGAKY RLKSVFGSLV LGGYDSTRFR ANTKDFSFTF SQDPSRLLTV
GVDSIMATNT LKGTFSFTSG AHFSVIDSTV PHLWLPKEVC AEFETAFGLT YDPKTDLYLV
NDTIHQQLIS KNPTVTVKLV NSLQDSTTNY TNIELPYAAF DLQASYPYYP NATKYFPIRR
AANESQYVLG RTLLQEAYLI VDYERANFTV VQAVFPDPMP AANVVTITPP SNSSTTPATS
NSSSSSSSPS SGIGTGAIVG LVVGVILALV LAVLAFLFFL RRRRNKQQQQ QQQHHELAGK
NIPEADSRSH LPVVSTPLKA VSPQELNGTP LSELATPINQ EYTNHGYPPD YKAAVNVADE
PQELHGESMT PITPRWKEVH LPRSPTLHDM DRESSASRRV SFMPSDDGCA SSEIEGQSDI
SPLTPRCPDL IHSNRHNLP
//