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Database: UniProt
Entry: A0A067CRG3_SAPPC
LinkDB: A0A067CRG3_SAPPC
Original site: A0A067CRG3_SAPPC 
ID   A0A067CRG3_SAPPC        Unreviewed;       692 AA.
AC   A0A067CRG3;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SPRG_02085 {ECO:0000313|EMBL:KDO33274.1};
OS   Saprolegnia parasitica (strain CBS 223.65).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Saprolegnia.
OX   NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO33274.1, ECO:0000313|Proteomes:UP000030745};
RN   [1] {ECO:0000313|EMBL:KDO33274.1, ECO:0000313|Proteomes:UP000030745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO33274.1,
RC   ECO:0000313|Proteomes:UP000030745};
RX   PubMed=23785293;
RA   Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA   van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA   Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA   Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA   Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA   Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA   Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA   Russ C., Tyler B.M., van West P.;
RT   "Distinctive expansion of potential virulence genes in the genome of the
RT   oomycete fish pathogen Saprolegnia parasitica.";
RL   PLoS Genet. 9:E1003272-E1003272(2013).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; KK583193; KDO33274.1; -; Genomic_DNA.
DR   RefSeq; XP_012196028.1; XM_012340638.1.
DR   AlphaFoldDB; A0A067CRG3; -.
DR   STRING; 695850.A0A067CRG3; -.
DR   EnsemblProtists; KDO33274; KDO33274; SPRG_02085.
DR   GeneID; 24124650; -.
DR   KEGG; spar:SPRG_02085; -.
DR   VEuPathDB; FungiDB:SPRG_02085; -.
DR   OMA; RAHQTHV; -.
DR   OrthoDB; 68776at2759; -.
DR   Proteomes; UP000030745; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; 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   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
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   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030745};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..692
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001638028"
FT   TRANSMEM        420..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        455..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        489..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        530..552
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        572..594
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        615..641
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          68..385
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DOMAIN          418..672
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   ACT_SITE        86
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        273
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        264..268
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   692 AA;  74558 MW;  24C825D3A096AF61 CRC64;
     MVTLSRVVLL AGLLAVAAAD GLLRIPLQRK PKAPSAAPVG LNPSDLLSAS AVAAAGYVPL
     TNYVEFQFYG EISIGTPPQK LQVCFDTGSS DLWVPAHECD HCAGTHRFAR NASSTFALAA
     DPNFTVAYGS GGARGIAGTE TISIGGFSAS EVPFGVVQHE QASLANMKAD GLLGLAFDGL
     ATISHPPAFM LLVLQNANLA PQFAFYLTPE PNQEGSMLLL GGGDPAWLDG ASYMTFDVVP
     QYGYWTFWRV QVHSLLIGNR LNACDAGCIA FIDTGTSLLG VPAPLYAGVL DAIAQYATRA
     GCYCMLTAYG YQCYMCSASN FPPLRIGFGG SGYFVLTGED YALCMGATCL ILLQPSGQDM
     WTIGDVFLKK FKSLYDVRKR TVAFLCPDDA PEMCGPERGD VTPRAFLDNM SLSAMDAHTI
     LILFVTGCSI LGSLFIVLTY FMYPMLQSKR VLVLLYYLSL CHLVYNGTLW ISALFQYSSG
     SAGCGLQLVL QQFAGVGTLL LSAVISIELL RAVRGWQSHT KDYSAVYHTV IWGICTLCGC
     VTIWTGVLGY VPNAYGPSRA CWAEHTPAWG RVTFFYVPVV GTLLLSLYAV FAALHRLQST
     NLIQTESGRR SSRLLVSYVS VLAISLVVPT VVGVLSLYAT IPESLSFVSE LCFYSQGLLH
     GFVWACSPSF QQAYAQRYYM MGDEEVACLV AE
//
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