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
//