ID X6MX07_RETFI Unreviewed; 294 AA.
AC X6MX07;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 08-NOV-2023, entry version 36.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
DE Flags: Fragment;
GN ORFNames=RFI_19701 {ECO:0000313|EMBL:ETO17620.1};
OS Reticulomyxa filosa.
OC Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC Reticulomyxidae; Reticulomyxa.
OX NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO17620.1, ECO:0000313|Proteomes:UP000023152};
RN [1] {ECO:0000313|EMBL:ETO17620.1, ECO:0000313|Proteomes:UP000023152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24332546;
RA Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL Curr. Biol. 0:0-0(2013).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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:ETO17620.1}.
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DR EMBL; ASPP01016290; ETO17620.1; -; Genomic_DNA.
DR AlphaFoldDB; X6MX07; -.
DR EnsemblProtists; ETO17620; ETO17620; RFI_19701.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000023152; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000023152}.
FT DOMAIN 124..294
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT NON_TER 294
FT /evidence="ECO:0000313|EMBL:ETO17620.1"
SQ SEQUENCE 294 AA; 33628 MW; 3E4803392A91EF79 CRC64;
MLAFSFVSIE KIFFSHFLCQ WDARKQTADS RTVKIKKLTF QTFCRHIAPF ALSCFCLKVV
QKKSENAVYF VFFVVRKGAK GTKANKKEQN NHKKKKKVDG GKQQKRKFLW VIIIMCNVSV
INFYQGPISL GTPAQDFTIL FDTGSSDLWV LNKGSKCYVC DHTYTYHKYD HSASTTYTPN
GTAFVDQYGL GTYFFFFLIH HIESGCFFLF ATSASNVGVS DGIFGLAFRS LSADKILPPF
FVLWQQGLLE ENLFSMYLQS THNTTDGELL LGGVDNSYYT GQIYYAPIVD ERWY
//