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Database: UniProt
Entry: A0A0D2DW80_9EURO
LinkDB: A0A0D2DW80_9EURO
Original site: A0A0D2DW80_9EURO 
ID   A0A0D2DW80_9EURO        Unreviewed;       734 AA.
AC   A0A0D2DW80;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=Z517_05058 {ECO:0000313|EMBL:KIW82031.1};
OS   Fonsecaea pedrosoi CBS 271.37.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW82031.1, ECO:0000313|Proteomes:UP000053029};
RN   [1] {ECO:0000313|EMBL:KIW82031.1, ECO:0000313|Proteomes:UP000053029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW82031.1,
RC   ECO:0000313|Proteomes:UP000053029};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; KN846971; KIW82031.1; -; Genomic_DNA.
DR   RefSeq; XP_013285839.1; XM_013430385.1.
DR   AlphaFoldDB; A0A0D2DW80; -.
DR   STRING; 1442368.A0A0D2DW80; -.
DR   GeneID; 25304548; -.
DR   VEuPathDB; FungiDB:Z517_05058; -.
DR   HOGENOM; CLU_009988_1_0_1; -.
DR   OrthoDB; 1831139at2759; -.
DR   Proteomes; UP000053029; 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   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR034164; Pepsin-like_dom.
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:SF89; SACCHAROPEPSIN; 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:UP000053029};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..734
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002240734"
FT   TRANSMEM        450..472
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          57..411
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          478..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          618..734
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..507
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..706
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   734 AA;  78863 MW;  B24A940BD9B948D2 CRC64;
     MRSSDYNRLR PCPWSCRRDI LIIFSLILSL GSVGASEPIP IVATTSTDFF GYDGLWSAIS
     IRVGSPEQYL SVFPSTLSQE TWVVGPAGCD GTSICENKRG GLFSANESSS FNARGFFELN
     FNPELGGSGY GYYGLDTLSL NDAISVPDQI ISVVNATEYW VGTLGLGVQQ TRFNGSEDIS
     PLLSSLIQKR NDIPSRSYGY TAGAAYRLKS VPASLTLGGI DANRFVPNNM SFTLSQDYSP
     IVAINSISLS SGAESLPSNW DSNPQTLLDI SQADLFTIDS STPFLWLPEP ACDAFANALN
     LTYDDTLQLY LFPDDNSSSP SALSAWNLTF TFTLSNLPGS SDGIELTLPY DAFNLQLTYP
     FPNLDANFTS PPTNYFPLRK AANSTQYTIG RAFLQETYLT VDYERNNFSI SQAVFTLDAV
     SNVNLLAISR PEGSTWPGPP GSGLSTGAKI GIGIGAGIGA LLALGVALWF CFRKRDEPGN
     SGTEKEKRRS FLSRLQKHPD SKTSVSELLG DKRQPTEVPA DPSVSRFELA ASTPIEMPAG
     PVSPSFFESN EAPRGSALMR NDPRRPAELE QQHSANKAAE AAASERSGSP VPPYSPAEVN
     HRFSNSVSPY SVRHSRAFGT VSSGDQGISP VGASHDGHSR QSSNTNSRSM SSPISPELTS
     RSQAQLLPGG STSPATSTSR GSLLVPQLNG RPPSRSPSSG SRFVEEGLTT VTEERPPGPP
     VRSNTPADRF SWEQ
//
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