ID A0A428PJG6_9HYPO Unreviewed; 574 AA.
AC A0A428PJG6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CEP53_007838 {ECO:0000313|EMBL:RSL53198.1};
OS Fusarium sp. AF-6.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325737 {ECO:0000313|EMBL:RSL53198.1, ECO:0000313|Proteomes:UP000287544};
RN [1] {ECO:0000313|EMBL:RSL53198.1, ECO:0000313|Proteomes:UP000287544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62590 {ECO:0000313|EMBL:RSL53198.1,
RC ECO:0000313|Proteomes:UP000287544};
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:RSL53198.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NKCJ01000174; RSL53198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428PJG6; -.
DR STRING; 1325737.A0A428PJG6; -.
DR Proteomes; UP000287544; 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:UP000287544}.
FT DOMAIN 1..141
FT /note="PPPDE"
FT /evidence="ECO:0000259|PROSITE:PS51858"
FT DOMAIN 154..322
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; 62692 MW; 4BC2FFF28C6DA1BD CRC64;
MDVHLLVYDL SRGLARQMSA GLLGFQLDAI YHTSIELNGR EYVYDGGIIA ITPGSSHLGQ
PMEKIHLGTT NLPMDVIEEF LDSLRPIFTL EAYDLFHHNC NNFSDSFSNF LIGKGIPEHI
VKMPQAVMDS PMGRMLLPQL TQGVNAGRQN GSILGLQQSA QTPAAPKHGV KNVTNLAEFN
RLMEAARSSC AVVFFTSATC PPCKLLYPTY DELAQEVGHK ATLIKIDISN LQAHQIASQY
SISATPTIIT FLRGEQENRW SGADQAALRG NVNLLVQMAF PLHPHEKLRL PTFANPDAKP
VLYAKVPPLD KLLVKMGNEV ASKPEVKALK KYLEDRAKDG PSSAVVPEMS NLSSLVKDSV
SSLPINILFT IVDLFRCSLS DPRVSGFFAE EKGHETVRAV IDLVNKQTEC PYALRLVTVQ
MACNFFSTPL FPEEVMKDSN LRSAIILLVS SSFLDEGHNN VRVAASSLLF NLSLANRRAR
KNSKPTLSGD DELELAASVV EAITLEEQSA DALHGMLLAL GHLVYGTALD GELPDLLQAV
GAEDSILAKK SKFPDEKLIT EVGAELLGKG LRKP
//
