ID A0A2S4PY26_9PEZI Unreviewed; 537 AA.
AC A0A2S4PY26;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=EPUL_000436 {ECO:0000313|EMBL:POS86943.1};
OS Erysiphe pulchra.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=225359 {ECO:0000313|EMBL:POS86943.1, ECO:0000313|Proteomes:UP000237438};
RN [1] {ECO:0000313|EMBL:POS86943.1, ECO:0000313|Proteomes:UP000237438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cflorida {ECO:0000313|EMBL:POS86943.1};
RA Wadl P.A., Mack B.M., Moore G., Beltz S.B.;
RT "Development of genomic resources for the powdery mildew, Erysiphe
RT pulchra.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DeSI family.
CC {ECO:0000256|ARBA:ARBA00008140}.
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:POS86943.1}.
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DR EMBL; PEDP01000221; POS86943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4PY26; -.
DR STRING; 225359.A0A2S4PY26; -.
DR OrthoDB; 151499at2759; -.
DR Proteomes; UP000237438; Unassembled WGS sequence.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.90.1720.30; PPPDE domains; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR008580; PPPDE_dom.
DR InterPro; IPR042266; PPPDE_sf.
DR InterPro; IPR013535; PUL_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12378; DESUMOYLATING ISOPEPTIDASE; 1.
DR PANTHER; PTHR12378:SF7; DESUMOYLATING ISOPEPTIDASE 1; 1.
DR Pfam; PF05903; Peptidase_C97; 1.
DR Pfam; PF08324; PUL; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SMART; SM01179; DUF862; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51858; PPPDE; 1.
DR PROSITE; PS51396; PUL; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000237438}.
FT DOMAIN 1..105
FT /note="PPPDE"
FT /evidence="ECO:0000259|PROSITE:PS51858"
FT DOMAIN 246..534
FT /note="PUL"
FT /evidence="ECO:0000259|PROSITE:PS51396"
SQ SEQUENCE 537 AA; 59279 MW; 845094ED0590E8F7 CRC64;
MESLEYVYDG GVKIVPAGKT HLGPPLKTAF LGKTELPMEV ILEFLESLKE IYNEEAYDIW
THNCNNFSND FATFLVGHGI PSYISNLPQT VLRTPFGQMI KPYVDRIARQ AQANKGGLLG
IEETAKIQPS IGHRSKVNFV TSKIEMDNHL QKAGKSCAII FFTSQNCGPC KALYPLYQRM
ADDAQGKAVF VMIDIAKNRE IGMKYSITAT PTFITFLHGT QENRWTGSDP ATLKGNLEML
LLLAHPPHPH DSLSLIEFRS ADSQPVLFTK IPPLAKLKIK LGSFSENNVM LEILKFISSG
ASEGSSKLPC PDLNAFSRFI WSAPSKLPLE VLFVVVDLFR VGLADTSFNA YFAKEKDHKT
VTLIISHVNS LENCPYSLRL VTLQLCCNLF ISDIFQSQIL GCSSLYEPII QLVTSCLLDE
KNQNVRVAAA SLAFNLATVN QKARSNKNQE ILPEAQQVEL AASLLEAIKN EEQSPEAMKG
FLLALANLIF RAPGDGELGD LLKSMASHDI ILSKQNSFPN EPLIEEIGKV LLGEGLS
//
