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Database: UniProt
Entry: A0A0V0ZPM4_9BILA
LinkDB: A0A0V0ZPM4_9BILA
Original site: A0A0V0ZPM4_9BILA 
ID   A0A0V0ZPM4_9BILA        Unreviewed;       413 AA.
AC   A0A0V0ZPM4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   08-NOV-2023, entry version 21.
DE   SubName: Full=Pepsin A {ECO:0000313|EMBL:KRY14236.1};
DE   Flags: Fragment;
GN   Name=PGA {ECO:0000313|EMBL:KRY14236.1};
GN   ORFNames=T12_7989 {ECO:0000313|EMBL:KRY14236.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY14236.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY14236.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY14236.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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:KRY14236.1}.
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DR   EMBL; JYDQ01000121; KRY14236.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0ZPM4; -.
DR   Proteomes; UP000054783; 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:SF8; ASPARTIC PROTEASE 1-RELATED; 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; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..413
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006873939"
FT   DOMAIN          65..407
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRY14236.1"
FT   NON_TER         413
FT                   /evidence="ECO:0000313|EMBL:KRY14236.1"
SQ   SEQUENCE   413 AA;  47558 MW;  C071D97629A18F49 CRC64;
     LKMRRFLIAT LFLITTGFSA KVPIKEIALR IPREWILSIG KLYDNDNSSL FSESLFDSLK
     HLSFYYVDVE IGTPAQKFRL LIDTASSSLI VAGTEYDSDI AIACRKQCHD EDHSCVRVCY
     ENFNASDWNV WRKNRFNADK SETFVKKSTF KEYAFNDFAM GITGTDSICL GEKCAKHQHF
     GIANTLGLIF FLLPCDGSLG LGFQTLNKDY SVPLMQRILR QDKTSLPTFT IWIDQSNDDG
     NFDGQLTIGE YDEEHCQMLT CQWMKLARRR YWEFEFENIV VTNDLEIRNA DRTPMKGMFN
     SRIPWIAMAP VHVKAICNEL ELEFVSYMPV IKIPCNRQHS LKPMKLVLEN IIIPIPTSAY
     FAQKNDTCYL MIIAAETAQG IDVEFGNYFM RQNCHVYNPH ANKMAICNRK QSE
//
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