ID K3UMB9_FUSPC Unreviewed; 575 AA.
AC K3UMB9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FPSE_06541 {ECO:0000313|EMBL:EKJ73276.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ73276.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ73276.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ73276.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
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:EKJ73276.1}.
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DR EMBL; AFNW01000182; EKJ73276.1; -; Genomic_DNA.
DR RefSeq; XP_009257934.1; XM_009259659.1.
DR AlphaFoldDB; K3UMB9; -.
DR EnsemblFungi; EKJ73276; EKJ73276; FPSE_06541.
DR GeneID; 20365159; -.
DR KEGG; fpu:FPSE_06541; -.
DR eggNOG; KOG0324; Eukaryota.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_033441_0_0_1; -.
DR OrthoDB; 151499at2759; -.
DR Proteomes; UP000007978; Chromosome 3.
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; 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; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51858; PPPDE; 1.
DR PROSITE; PS51396; PUL; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000007978}.
FT DOMAIN 1..141
FT /note="PPPDE"
FT /evidence="ECO:0000259|PROSITE:PS51858"
FT DOMAIN 156..278
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 282..570
FT /note="PUL"
FT /evidence="ECO:0000259|PROSITE:PS51396"
SQ SEQUENCE 575 AA; 62925 MW; A85EABD6E9AEBACF CRC64;
MDVQLFVYDL SRGLARQMSM GILGFQLDAI YHTSIELNGK EYVYDGGIIA IRPGSSHLGQ
PLQKIPLGKT NLPIDVIEEF LDSLRPIFTL EAYDLFHHNC NNFSDSFANF LLGKGIPEHI
VKMPQAVLDS PMGRMLLPQL TQGINAGRQG GSILGLQESS QAPVAAPKHV VRNIANASEF
DRLMSETKNS CAVIFFTSAT CPPCKTLYPI YDELAEEVGD KATLLKVDIS QPQQHEIGSR
YSIRATPTIV TFLHGKEENR WSGADPAALR GNIQLLVQMA HPVHPHERLR LPTFSNPNAK
PVLYTKIPPL DKLMVKMGSE VASKPEVKAL KQYLEDRTKN GPSSAVIPDM GHLSSLIKDS
VASLPIDILF TIVDLFRCAL SDPRISGFFA EEKNHETVLA VLESVAQKTD CPYALRLVTL
QMACNFFSTP LFPDEIMRDS SLRAVIILLV SSSFLDESHN NVRVAASSLL FNLSLANRKA
RSSSKPTLSG DDDLELAASV VEAISLEEKS AEALHGMLLA LGHLVYGTSL DGELPDLLQA
VGAQDSILAK KPKFPDEKLV TEVGTELLGK GLRKP
//