ID S8BXI6_DACHA Unreviewed; 687 AA.
AC S8BXI6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=H072_6165 {ECO:0000313|EMBL:EPS40042.1};
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:EPS40042.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS40042.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS40042.1,
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 -!- 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:EPS40042.1}.
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DR EMBL; AQGS01000439; EPS40042.1; -; Genomic_DNA.
DR RefSeq; XP_011111964.1; XM_011113662.1.
DR AlphaFoldDB; S8BXI6; -.
DR STRING; 1284197.S8BXI6; -.
DR eggNOG; ENOG502RV5I; Eukaryota.
DR HOGENOM; CLU_009988_3_0_1; -.
DR OMA; MRCRKER; -.
DR OrthoDB; 1831139at2759; -.
DR Proteomes; UP000015100; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 4: Predicted;
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 483..507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 55..413
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 434..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 687 AA; 74485 MW; 3743C21CEEA836D5 CRC64;
MEPFLIFRKA SYSTFATLTA LANLACLVAA YNIPPLYLPP AIGSQAWYGP DGMWSALTFR
VGNSPQQVNL IPTTNTNDLW TVSPTGCDSA TWSKLNNQSV PSSCTVVRGG VFDTSKSSTW
SSVTSALGFS EQRFFDMGLN VTVNYGTDTL RIGNGDALVL EDHLVANYAD PEQFLTGIIG
LSVANVTFDQ QTTYKALLTT LYDQKKIPSQ SWGYTAGAYY REKRVPCSVV LGGYDLDRFV
LHDREFTLSP DLYAIAGLQN INATSSTSAN RTLLSDPIQV YIDSTTPYYY FPESVCNSFA
ELFGLFYDSD SELYFYTSDQ AYETAKKSDY TLSFTLTNNT DAFGQAIVLY IPFAAFDLSH
QFYNGSSASG DDSSRPYFPI KRGSREDTYT LGRAFLQETY LIVDYYRVTF SVHQAWFNGN
TGAYQNVVTI TDPDTDNTST VTTGGAPAAT SLGPNESGSP PPPPGMESGT PQSQGGGGSK
NGAIIGGAVA GGIVVIALIG GLIFLLLRRQ KRHKAQQIAM EPHHFPSGAD INDIVTSPVE
QKPVEMGQTS PRQELPGKEA VSPQELEAEV PGSLIAAKPL PELDGTAINR SRGLDSSGDT
LVLPRETVVE TPQNQVLHPQ TDEVESRTSY ESEISEKQYP ASESGSYMVS PITPTWQHAA
TSHASGGELG PQVIMEEREV PRSPGNM
//
