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}.
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; 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
//