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Database: UniProt
Entry: C5KRI3_PERM5
LinkDB: C5KRI3_PERM5
Original site: C5KRI3_PERM5 
ID   C5KRI3_PERM5            Unreviewed;       420 AA.
AC   C5KRI3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-NOV-2023, entry version 59.
DE   SubName: Full=Aspartyl proteinase, putative {ECO:0000313|EMBL:EER12910.1};
GN   ORFNames=Pmar_PMAR007833 {ECO:0000313|EMBL:EER12910.1};
OS   Perkinsus marinus (strain ATCC 50983 / TXsc).
OC   Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC   Perkinsus.
OX   NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN   [1] {ECO:0000313|EMBL:EER12910.1, ECO:0000313|Proteomes:UP000007800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA   El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL   Submitted (JUL-2008) 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; GG675803; EER12910.1; -; Genomic_DNA.
DR   RefSeq; XP_002781115.1; XM_002781069.1.
DR   AlphaFoldDB; C5KRI3; -.
DR   EnsemblProtists; EER12910; EER12910; Pmar_PMAR007833.
DR   GeneID; 9055869; -.
DR   InParanoid; C5KRI3; -.
DR   OMA; YWQIAIQ; -.
DR   OrthoDB; 1120702at2759; -.
DR   Proteomes; UP000007800; 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:SF51; NAPSIN-A; 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   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007800};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..345
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        38
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        231
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        273..308
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   420 AA;  45823 MW;  2DDE6F0F9C810887 CRC64;
     MVGNFSYYVE PILNLANLQY YGPITVGTPE QALTVQFDTG SSDLWVPQTM YDYHTSQTSS
     SSTTQRVLEY GKGAVFGNLT NDRVCLGLSG ELCIPGQNFI LASAQRDMNM RFFDGIMGLA
     WPGLSRTGTT VLEHLSEIMD YPLISFSFTD DPIFTMSLGS TVTFGAIEEE NYRKGTFTWA
     PVVGDLWWSI EVSIGVLSPP SKASPKSIGS ASNSTLDSGS VMISNQQAAL DTGTSYITVP
     RNIFLPLLTA LLPHEVLMTC SVLLPGGFLT CPCGAQNSAG SMVIIIQGMR YTVTPTDYFT
     LPTPQNECMI ELQMSPDGLP IILGDTFLKK HYTVFDAKER RVGVAVSAYG GVFGDLDGSR
     SSMPIKEKEN SVDSSYRLFG VVLVTVLLVL SAAYLVPRFV NRFTHRSALK RPLLETTDAR
//
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