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Database: UniProt
Entry: M5GEH2_DACPD
LinkDB: M5GEH2_DACPD
Original site: M5GEH2_DACPD 
ID   M5GEH2_DACPD            Unreviewed;       611 AA.
AC   M5GEH2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   13-SEP-2023, entry version 42.
DE   SubName: Full=DUF862-domain-containing protein {ECO:0000313|EMBL:EJU03248.1};
GN   ORFNames=DACRYDRAFT_78156 {ECO:0000313|EMBL:EJU03248.1};
OS   Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX   NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU03248.1, ECO:0000313|Proteomes:UP000030653};
RN   [1] {ECO:0000313|EMBL:EJU03248.1, ECO:0000313|Proteomes:UP000030653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU03248.1,
RC   ECO:0000313|Proteomes:UP000030653};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- SIMILARITY: Belongs to the DeSI family.
CC       {ECO:0000256|ARBA:ARBA00008140}.
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DR   EMBL; JH795860; EJU03248.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5GEH2; -.
DR   STRING; 1858805.M5GEH2; -.
DR   HOGENOM; CLU_033441_0_0_1; -.
DR   OMA; VTLQMAC; -.
DR   OrthoDB; 151499at2759; -.
DR   Proteomes; UP000030653; 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; 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; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030653}.
FT   DOMAIN          2..142
FT                   /note="PPPDE"
FT                   /evidence="ECO:0000259|PROSITE:PS51858"
FT   DOMAIN          174..299
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          316..609
FT                   /note="PUL"
FT                   /evidence="ECO:0000259|PROSITE:PS51396"
FT   REGION          140..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..164
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   611 AA;  66048 MW;  37E1328D35FE05A2 CRC64;
     MSKVELYVYD LSSGMARSLS LQLTGRQIDG IWHTSVVVFG KEVFYGQGIS VVSPGTSHHG
     RPLQILDMGL THLDEGTFQE YIDELSSHYT ADKYHLLEFN CNSFTNDVVG FLTGGSIPGF
     IKDLPADFLN TPLGAALRPT IDSMFRGPPT APPTPGPSLP SGTSPSPSSS PLASLVSRPP
     PVPETATLTA PLQLATNPSS LRSLLNSHKA ATVLFTAPAT CAPCRVIDPF FSELAQLRTA
     EGLAYVKVDL DVGLGRAAAQ EWGVSATPTV MCFLKGKKRG EVRGANVREI RTQVDLLICE
     LYPPHPHTRQ DLPAIQGISL SPILFSQIPK LDSALSKFLS FVNAASASEG DKKRYQFLFR
     QVLLLLEPQA KLPPAQLRST LQAWSAATVD LAALLPEGEL FPLADFWRLA VLSSPVAHAL
     SGNIEGIKSL LSLAYYSGAS TPRPYLLTTL RLCANLFAYP DLARLVFPSE GEKQDLVSFL
     VCTLLSDDAG IRTATASVTF NLGALHQQAV RQALEKHTRP PSEDWIIEVV SALIEALSRE
     TSSEEVVHRL VASLALFVFR APGWEELREL LQVLQAQEVL LDKLLPGGCG EIGVRQKSVQ
     VLVKELAGLC A
//
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