ID E4V3T1_ARTGP Unreviewed; 581 AA.
AC E4V3T1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Thioredoxin {ECO:0008006|Google:ProtNLM};
GN ORFNames=MGYG_07660 {ECO:0000313|EMBL:EFR04655.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SIMILARITY: Belongs to the DeSI family.
CC {ECO:0000256|ARBA:ARBA00008140}.
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DR EMBL; DS989828; EFR04655.1; -; Genomic_DNA.
DR RefSeq; XP_003170418.1; XM_003170370.1.
DR AlphaFoldDB; E4V3T1; -.
DR STRING; 535722.E4V3T1; -.
DR GeneID; 10025659; -.
DR VEuPathDB; FungiDB:MGYG_07660; -.
DR eggNOG; KOG0324; Eukaryota.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_033441_0_0_1; -.
DR InParanoid; E4V3T1; -.
DR OMA; VTLQMAC; -.
DR OrthoDB; 151499at2759; -.
DR Proteomes; UP000002669; 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:UP000002669}.
FT DOMAIN 1..136
FT /note="PPPDE"
FT /evidence="ECO:0000259|PROSITE:PS51858"
FT DOMAIN 149..305
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 281..576
FT /note="PUL"
FT /evidence="ECO:0000259|PROSITE:PS51396"
SQ SEQUENCE 581 AA; 64207 MW; 37DA8BBF084DA23E CRC64;
MDVLLYVYDL SKLSRPLTGV QIDAIYHTSI VLEGTEYFFG RGIQQAAPGS THHGQPMETI
SLGRTDLPMD VISEYMESLA ETYHESSYDL FLRNCNNFTH DLSMFLVGKG IPDHIRNLPE
TFLNTPFGQM MKPYIDGMLR GATQGPAIQP EPVSAPTRAA VPEINSAQQP PKGEVRNAST
LKDIQSLLAS AKSSCAVIFF TSSTCPPCKI VYPTYDQLAE EAGSKAVLIK VDIAQAYDIS
SHYQVRVTPT FITYLKGERE NQWSGANPTE LRGNVQLLLQ MAWPPHPHSS LKLPSLERHI
DQYISYKKVP PLDKLLSKVG PAASDPSIVA LVNFIKASNS TDQTKPPLPD LNQLSFFVKT
KFLSLPAETH FAILDLFRVI FGDPRVSGYY AEEHDHGTIL TLLSRANDLS NTPYSQQLVM
THLACNFFTS HLYLTQLAHH DGLRHACIKL ATNALLDYRS SLRATGASLI FNLAASNHNK
RLLDPPEAES LPEADQFELL ASVVEAIRAE QESPDTLHGL LLSLGLLVHY APVDGEVVEL
CRALEAESVV LKKAGIDAFK KEKALLQEIG RELMGRCLSL N
//
