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
//