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
//