GenomeNet

Database: UniProt
Entry: U1G2J6_ENDPU
LinkDB: U1G2J6_ENDPU
Original site: U1G2J6_ENDPU 
ID   U1G2J6_ENDPU            Unreviewed;       413 AA.
AC   U1G2J6;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=EPUS_00496 {ECO:0000313|EMBL:ERF71507.1};
OS   Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX   NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF71507.1, ECO:0000313|Proteomes:UP000019373};
RN   [1] {ECO:0000313|Proteomes:UP000019373}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX   PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA   Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA   Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT   "Genome characteristics reveal the impact of lichenization on lichen-
RT   forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL   BMC Genomics 15:34-34(2014).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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; KE721204; ERF71507.1; -; Genomic_DNA.
DR   RefSeq; XP_007802716.1; XM_007804525.1.
DR   AlphaFoldDB; U1G2J6; -.
DR   GeneID; 19235557; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_039077_0_0_1; -.
DR   OMA; FVDWTWI; -.
DR   OrthoDB; 2342359at2759; -.
DR   Proteomes; UP000019373; Unassembled WGS sequence.
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:SF51; NAPSIN-A; 1.
DR   Pfam; PF00026; Asp; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..413
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004611582"
FT   DOMAIN          48..409
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DISULFID        335..370
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   413 AA;  46011 MW;  12AAAA90E598ED96 CRC64;
     MHMSLRNTLL ASSSLSSFAF VSGSPARQRA AEAVSYDLPL TWSSFGFLSS HMSLGTPPQQ
     ITTFVDWTWI SQYVFTTTCH GVADKPFDCF AKEQSIFNQS QSSTFLDESY LYPSRTWNPN
     HFFFYEDLTV DYASDIGVVG PSSARLTIQT ADFQFDISDA PYPLTGVYGL SPVFKADNRS
     MQSPFYQAWS AGAWPEPFVA FHYCYNGSVD TTKSTCGGYD GLQTLGGFNM SLIDGEMSWY
     DIVFFTDVNE IDFEYSPPIY NYWTLQLTEL SLGDKVQALN KSRGAGAIFD HASYGRGAPL
     SVNAYEELIS ISGATPIALD SPPNNGNQSF YEVDCDRVEA LPPIKYRFGG SERPWEIVPS
     NYVETINDTC VLNVRTLGDG DMIAGNFGET FAKDKYIVFD FEKLKVGLAD VRW
//
DBGET integrated database retrieval system