ID A0A3M2S5M6_9HYPO Unreviewed; 574 AA.
AC A0A3M2S5M6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CDV36_007480 {ECO:0000313|EMBL:RMJ12873.1};
OS Fusarium kuroshium.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=2010991 {ECO:0000313|EMBL:RMJ12873.1, ECO:0000313|Proteomes:UP000277212};
RN [1] {ECO:0000313|EMBL:RMJ12873.1, ECO:0000313|Proteomes:UP000277212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR3666 {ECO:0000313|EMBL:RMJ12873.1};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-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:RMJ12873.1}.
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DR EMBL; NKUJ01000123; RMJ12873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2S5M6; -.
DR STRING; 2010991.A0A3M2S5M6; -.
DR Proteomes; UP000277212; 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; 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:UP000277212}.
FT DOMAIN 1..141
FT /note="PPPDE"
FT /evidence="ECO:0000259|PROSITE:PS51858"
FT DOMAIN 154..321
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 278..569
FT /note="PUL"
FT /evidence="ECO:0000259|PROSITE:PS51396"
SQ SEQUENCE 574 AA; 62707 MW; 24B7741274152AAE CRC64;
MDVHLLVYDL SRGLARQMSA GLLGFQLDAI YHTSIELNGR EYVYDGGIIA ITPGSSHLGQ
PMEKIHLGTT NLPMDVIEEF LDSLRPIFTL EAYDLFHHNC NNFSDSFSNF LIGKGIPEHI
VKMPQAVMDS PMGRMLLPQL TQGVNAGRQN GSILGLQQSA QTPTAPKHGV KNVTNLAEFN
RLMEAARSSC AVVFFTSATC PPCKLLYPTY DELAQEVGDK ATLIKIDISN PQAHQIASQY
SISATPTIIT FLRGEQENRW SGADQAALRG NVNLLVQMAF PLHPHEKLRL PTFANPDARP
VLYAKVPPLD KLLAKMGNEV ASKPEVKALK KYLEDRANDG PSSAVVPEMS HLSSLVKDSV
SSLPINILFT IVDLFRCSLS DPRVSGFFAE EKGHETVRAV LDLVNKQTEC PYALRLVTVQ
MACNFFSTPL FPEEIMKDSN LRSAIILLVS SSFLDEGHNN VRVAASSLLF NLSLANRRAR
KNSKPTLSGD DELELAASVV EAITLEEQSA DALHGMLLAL GHLVYGTALD GELPDLLQAV
GAEDSILAKK SKFPDEKLIT EVGAELLGKG LRKP
//
