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
//