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Database: UniProt
Entry: S3D805_GLAL2
LinkDB: S3D805_GLAL2
Original site: S3D805_GLAL2 
ID   S3D805_GLAL2            Unreviewed;       574 AA.
AC   S3D805;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Thioredoxin-like protein {ECO:0000313|EMBL:EPE34637.1};
GN   ORFNames=GLAREA_10331 {ECO:0000313|EMBL:EPE34637.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE34637.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE34637.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(2013).
CC   -!- SIMILARITY: Belongs to the DeSI family.
CC       {ECO:0000256|ARBA:ARBA00008140}.
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DR   EMBL; KE145356; EPE34637.1; -; Genomic_DNA.
DR   RefSeq; XP_008078572.1; XM_008080381.1.
DR   AlphaFoldDB; S3D805; -.
DR   STRING; 1116229.S3D805; -.
DR   GeneID; 19469378; -.
DR   KEGG; glz:GLAREA_10331; -.
DR   eggNOG; KOG0324; Eukaryota.
DR   eggNOG; KOG0907; Eukaryota.
DR   HOGENOM; CLU_033441_0_0_1; -.
DR   OMA; VTLQMAC; -.
DR   OrthoDB; 151499at2759; -.
DR   Proteomes; UP000016922; 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:UP000016922}.
FT   DOMAIN          1..141
FT                   /note="PPPDE"
FT                   /evidence="ECO:0000259|PROSITE:PS51858"
FT   DOMAIN          157..279
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          280..571
FT                   /note="PUL"
FT                   /evidence="ECO:0000259|PROSITE:PS51396"
FT   REGION          154..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   574 AA;  63499 MW;  07BECD36A1FBD670 CRC64;
     MDVQLYVYDL SNGLARQISA PLLGTFIDMI YHTSIVIEGV EYTYDGGIKA LESGKTHLGP
     PLQVVNLGRT ELPMEVILEY LDSMKDTYTK EAYNLWTNNC NNFSNDFSMF LLGKGIPEHI
     TNLPSTFLNS PYGRALMPEI NKMVDRRNRK QGALLGLGTD DDAPPKPGQV DSSVRHISSM
     PKLESALEEA KRSSAMIFFT SENCPPCKTL YPLYDRLAEE SVHKCILIMV DVSRAYNIGT
     KYNIRSTPTF MSFLHGVEQE RWSGADPAKL QGNIQMLAQM AFPQHAHENL DLPALRASNT
     HPVLFSKVPP LGKLKVKMGA IAEDAAVSGI LHFVSIRAEK NPSEATLPDM EAFSRFLRSA
     PSKLPIETMF TIVDLLRLAL VDSRVTGYFA EEKNHFTISP LITYVNDLEN CPYPLRLVTL
     QMCCNLFSSP LYPPHILKCP SLSSPIVELI TTSLLDSTHH NVRVAAAGLA FNMTTANFKT
     RKQEGREGLP ESDQIELAAC LLEAISVEEQ SPEALKGYLL AFGYLVYCVP AGGDLVDLLK
     SMDAQGTVLS KKKLFADEKL ILDIGNTLLG QGLK
//
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