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Database: UniProt
Entry: M2ZQF1_PSEFD
LinkDB: M2ZQF1_PSEFD
Original site: M2ZQF1_PSEFD 
ID   M2ZQF1_PSEFD            Unreviewed;       423 AA.
AC   M2ZQF1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
DE   Flags: Fragment;
GN   ORFNames=MYCFIDRAFT_117555 {ECO:0000313|EMBL:EME81284.1};
OS   Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS   fungus) (Mycosphaerella fijiensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=383855 {ECO:0000313|EMBL:EME81284.1, ECO:0000313|Proteomes:UP000016932};
RN   [1] {ECO:0000313|EMBL:EME81284.1, ECO:0000313|Proteomes:UP000016932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIRAD86 {ECO:0000313|EMBL:EME81284.1,
RC   ECO:0000313|Proteomes:UP000016932};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; KB446560; EME81284.1; -; Genomic_DNA.
DR   RefSeq; XP_007928513.1; XM_007930322.1.
DR   AlphaFoldDB; M2ZQF1; -.
DR   STRING; 383855.M2ZQF1; -.
DR   GeneID; 19330334; -.
DR   KEGG; pfj:MYCFIDRAFT_117555; -.
DR   eggNOG; ENOG502RV5I; Eukaryota.
DR   HOGENOM; CLU_009988_3_1_1; -.
DR   OrthoDB; 1831139at2759; -.
DR   Proteomes; UP000016932; 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   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR   Pfam; PF00026; Asp; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016932};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          19..366
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          372..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EME81284.1"
FT   NON_TER         423
FT                   /evidence="ECO:0000313|EMBL:EME81284.1"
SQ   SEQUENCE   423 AA;  46451 MW;  B6728638F7E5560D CRC64;
     HAIVLQATGR WQGMEPKWST FSLNIGSNPS QTFDFLPSIS SSQIWLPDPN LICPKSNESV
     KHRCLESRGI PLGTSSLDRS STWLSQGTYH FLQHPLLFSY MTGDFGQDTV ALTTTSTSAQ
     AVAENQLVAQ YGLEDYWIGL AGLTYRSTPL GNGSTSSLLT SLKENGTIPS LSFGYTAGSV
     YGKVYDNFGA LTLGGYDASR RSPQPTENLE VSMDRTKNEL KVELLDISVS NGSTGGQRTL
     LPIGKTYSMF LDTSVSEFWF PSEVCDLFQG SFNLTEDLET GLFGIDHTSR QAMFDNNTSL
     SLVLGGSSDA TTKLKIDLGC EAFGNFSYFP IRRAVDESKF VLGRVFFQET YITVDWTWKN
     FTLSKAQPRV RGIAPNPQDI STPEIAPPAP PRLSSGDKAG IAIGCLMIVS LTLGLLWWVR
     RRR
//
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