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Database: UniProt
Entry: A0A094JX40_9PEZI
LinkDB: A0A094JX40_9PEZI
Original site: A0A094JX40_9PEZI 
ID   A0A094JX40_9PEZI        Unreviewed;       513 AA.
AC   A0A094JX40;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=V502_06476 {ECO:0000313|EMBL:KFZ13678.1};
OS   Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ13678.1, ECO:0000313|Proteomes:UP000029308};
RN   [1] {ECO:0000313|EMBL:KFZ13678.1, ECO:0000313|Proteomes:UP000029308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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:KFZ13678.1}.
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DR   EMBL; JPKE01002395; KFZ13678.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094JX40; -.
DR   STRING; 1420915.A0A094JX40; -.
DR   HOGENOM; CLU_013253_9_3_1; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000029308; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05474; SAP_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; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR033876; SAP-like.
DR   PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-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   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029308};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..513
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001905624"
FT   TRANSMEM        492..512
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          61..416
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          437..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        79
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        322..376
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   513 AA;  53709 MW;  758236C646C18CEA CRC64;
     MPSSAALNLL LPLLLASSSL AGVVPIPIWK NPASPQLARR DIHSRATVLQ VLDNSHLRGS
     YYANITVGTP PQPVSVIIDT GSSDLWVLAK TANVCLDPSI IQQLPGDVGC IGGTYDSSKS
     STYDKLTDNT FKIQYVDQTA SKGDYISETV SFNGQNKSNN AIKELQIGLA YNSTLPVGVM
     GVGYNASVAA ASPYSNIIDL MVEQGLINTR AYSLWLDDLS AATGQVLFGG IDTAKYDGAL
     SILPVLGAEG ERPTSFAVAL RGISVGHKGK MTSITSDEFA IPVILDSGTT HTLLPKTVVN
     AIIRGLGAYD FTNEVGAILV DCGLRTQNPD FVFGYRFGNS TAGPTINVKL SELILDFNGL
     DQSLIKDSFK AWDSVCYLAI ADSSTVTSEA IYLLGDTFLR SAYVVYDIDN DEIGIAQSNF
     NSETNNIVEI MAGEKIPSIT GQPDTPSATP TATTTSTRDS GFQGLVTTST KGAATSSSAA
     IAGARLPAGG SAGLLVMAVS ICFAGLGGLM IVV
//
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