ID W2SEZ1_9EURO Unreviewed; 487 AA.
AC W2SEZ1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 08-NOV-2023, entry version 41.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=HMPREF1541_00789 {ECO:0000313|EMBL:ETN46603.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN46603.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN46603.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN46603.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB822711; ETN46603.1; -; Genomic_DNA.
DR RefSeq; XP_008711315.1; XM_008713093.1.
DR AlphaFoldDB; W2SEZ1; -.
DR STRING; 1220924.W2SEZ1; -.
DR MEROPS; A01.077; -.
DR GeneID; 19968128; -.
DR VEuPathDB; FungiDB:HMPREF1541_00789; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_10_1_1; -.
DR InParanoid; W2SEZ1; -.
DR OrthoDB; 3087283at2759; -.
DR Proteomes; UP000030752; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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:SF75; ENDOPEPTIDASE (CTSD), PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07040)-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000030752};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..487
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004825246"
FT DOMAIN 87..392
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 395..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 105
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 287
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 118..123
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 487 AA; 51540 MW; 16104497666246E4 CRC64;
MHQRWLSLPL LTSTVSAFYP YQDESSKSKR FYPTLPQQAN EEDSGVYTLD LKKTPRKRQN
AFMIDESSDP SEPHALAIHQ DGSDYSYFSS LLFGSKGQEM HMLVDTGSTN TWVFGSDCRS
SACSIHNTFG SDDSTTLNTS TKTFSLAYGT GEVEGVMAED KVAFANYTLQ LQFGLAKTAS
NDFNNYPMDG ILGLGPASSN DLGSQTVMQA LDVQTGLKDN ILGIHLQRAT DDTKDGQLTI
GGVDSSKFKG DLSYTQTKSG SSWEIPVDDV FVGGQACKFT GKSAIIDTGT SYTLMPPNDA
KTLHGLIPGS SSSGEAYTVP CDASTTVEVS FSKVKYSISP KDYIGRRGSG NTCASNIIGH
QPFGADQWIL GDIFLKNVYT VFDFDKDRIG FGTMSGTSST SSSSSSSNSG SSTSDASSSQ
TSMATTTSSG GASSTTGDEA QETSGSTDSS PFGNDGESSS NSAGGRLTLN RIGWMLISTV
AVGLATS
//