ID G4TZ02_SERID Unreviewed; 544 AA.
AC G4TZ02;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Related to aspartic peptidase A1-Laccaria bicolor {ECO:0000313|EMBL:CCA76545.1};
GN ORFNames=PIIN_10538 {ECO:0000313|EMBL:CCA76545.1};
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:CCA76545.1, ECO:0000313|Proteomes:UP000007148};
RN [1] {ECO:0000313|EMBL:CCA76545.1, ECO:0000313|Proteomes:UP000007148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA76545.1,
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:CCA76545.1}.
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DR EMBL; CAFZ01000821; CCA76545.1; -; Genomic_DNA.
DR AlphaFoldDB; G4TZ02; -.
DR STRING; 1109443.G4TZ02; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_1_2_1; -.
DR InParanoid; G4TZ02; -.
DR OMA; TIQMANH; -.
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:InterPro.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 3.
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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..544
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003469026"
FT TRANSMEM 520..543
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..437
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 19..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 57090 MW; 8031CB6573249B71 CRC64;
MQNVSLLLAI CAVLASATPS PTAAPDAGRA ASPLHKRSQL DARNNQIISI PLVRRSRPRP
FRKGKLSSKE LADIDYVTDV AALQASRDAL IEKYAETRGA DVVKRLQEKR EAEESALNGK
RDIKTIQMAN HQFDTTYSAV VSLGTPPKPF NLLLDTGSSG SVSGRTGSDV VELGGYTIND
QVIGIVDQAQ RAMPGSVEGL MGFAFGTISK AGGTPWWLRV IAGDANDTGG TPDGRVMSFW
FSRYIDSADS AEIHPGGQFT IGGTNSSLYT GDINYIDVIQ PAKWWLIPIQ SAGIENGPSV
SVTEGRQNAI IDTGTTLVGG EDIVLDAIYA NITGAIKGGE LTIRLTGFWT LPCDTTAVVT
LTFGGVTYTY SAVDLLYQRI DDIKPNYCLS SLFVFSSADP HSLYYTPNGS PYWIVGDAFL
KNVYSVYSLG SGGSGDAGVQ GMGNNGATAQ VGFAKLSNVS GEIGSTGNTT TTTLTGTTTT
RGPRPASTDL PVGVIPDVDT TIVVVVTATP DATQPAPSSA FATAGIATSF ALVSTLGAMV
LLFL
//
