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Database: UniProt
Entry: S8ALN9_DACHA
LinkDB: S8ALN9_DACHA
Original site: S8ALN9_DACHA 
ID   S8ALN9_DACHA            Unreviewed;       558 AA.
AC   S8ALN9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=H072_4066 {ECO:0000313|EMBL:EPS42046.1};
OS   Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS   (Monacrosporium haptotylum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Dactylellina.
OX   NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS42046.1, ECO:0000313|Proteomes:UP000015100};
RN   [1] {ECO:0000313|EMBL:EPS42046.1, ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS42046.1,
RC   ECO:0000313|Proteomes:UP000015100};
RX   PubMed=24244185;
RA   Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   PLoS Genet. 9:E1003909-E1003909(2013).
RN   [2] {ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA   Ahren D.G.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPS42046.1}.
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DR   EMBL; AQGS01000130; EPS42046.1; -; Genomic_DNA.
DR   RefSeq; XP_011110026.1; XM_011111724.1.
DR   AlphaFoldDB; S8ALN9; -.
DR   STRING; 1284197.S8ALN9; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_036919_0_0_1; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000015100; 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:UP000015100};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        455..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          78..410
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   558 AA;  61350 MW;  422DCFCCE4CFA54A CRC64;
     MRTRVGYSGP LSLFLIFGSA YFLTNQAGLA SRQTWGATAG ENSERGANPP KVRATTREYV
     LLSVVYEYEI LGEYFGYVYT EIKFGRDQQT LKLLVDVPHL SWVPQLPASQ TEFCNNQTNY
     ASCRTAGNSG YYSPGDVSHN DTFNFPAPNT NYTGYWVEDI VTAGNISVNL QFVVAETWGN
     MTPRLGLGLW PFDMDARHPS YIQALQQQGR ISEQFCSCYD ITNAESSGSI VIGGVDLNKF
     TGKLKVWRIN QLPGIISTPA TKIISSSGNW TNFTTSSQEF ALFTPLSSFL HLPKDVLDSI
     LTLLPASPFT VGDGRKVYTL PCDIQVDPTW VINFTFDELV ISIPFTYLIS PLKVSEASAI
     DQCLGLFLPN EKIYYDTSPY DFSYIFGAPF WRSAYIVVNA ADKISALGVA NPNVTTQAIV
     DVGGQFGANI DTVVGTPPAS STPPSDSGAK KKHTVGVIVG SCIGGIALIF ACLGGYFLYW
     RRREKPMPVV PDVPKASEEE EIEMQNLQQT PQGPGELNTL VDDLYDDEQG IVQPRQELAG
     HERVLELPVN ERLVELSG
//
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