ID G4TZ52_SERID Unreviewed; 449 AA.
AC G4TZ52;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Related to aspartic protease {ECO:0000313|EMBL:CCA76595.1};
GN ORFNames=PIIN_10586 {ECO:0000313|EMBL:CCA76595.1};
OS Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS (Piriformospora indica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Sebacinales; Serendipitaceae; Serendipita.
OX NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA76595.1, ECO:0000313|Proteomes:UP000007148};
RN [1] {ECO:0000313|EMBL:CCA76595.1, ECO:0000313|Proteomes:UP000007148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA76595.1,
RC ECO:0000313|Proteomes:UP000007148};
RX PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA Kogel K.H.;
RT "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT the Mutualistic Root Symbiont Piriformospora indica.";
RL PLoS Pathog. 7:e1002290-e1002290(2011).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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:CCA76595.1}.
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DR EMBL; CAFZ01000855; CCA76595.1; -; Genomic_DNA.
DR AlphaFoldDB; G4TZ52; -.
DR STRING; 1109443.G4TZ52; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_1_2_1; -.
DR InParanoid; G4TZ52; -.
DR OrthoDB; 1203010at2759; -.
DR Proteomes; UP000007148; 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: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; 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:SF6; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00026; Asp; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CCA76595.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:CCA76595.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007148};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..449
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003469270"
FT TRANSMEM 425..447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..389
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 51..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 449 AA; 47920 MW; 33763DB76502D5E7 CRC64;
MRLSFLLATT LLFASSATFA LPNNPTVARR DAGMAPVTVP LIRRRLEFEK RDHTHEESTK
ISVNPRGTYG KHSKRSAELG RRALSTVDLW IRSSSCVYCA SHATGALFNQ TESSTFSYVQ
GGLDGLFFGE FISGILGSDV VQMGQFQVAS QVFGLATSVR NTILAGNSSG IMGLGFRPSV
ITGAHPWWQQ ASNGWDAPQM SFYFTRSRSG PYASIEEPGG QFTLGGTNSS LFQGSINFNN
LVHEQDWVIL MDEIGIANNA SIQISSPSQS AAIDMGIEGI GGPSSVLDQF YSLIPGATRS
QISSSLYVIP CNTTVQATLM FGGRTYTMQA SDLIGSKLSG GQQCIGTFFV LTPRNDLPSS
DMPAWRIGSA FLKNVYTVLQ SEPAAIGFAT LRDNVQEFGT LGFAGLSIDE NGHANAAASP
RHRTITLGSG GVFATSVLWA VVGLAAVMS
//