ID A0A1J9PAC1_9EURO Unreviewed; 592 AA.
AC A0A1J9PAC1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 28.
DE RecName: Full=Thioredoxin {ECO:0008006|Google:ProtNLM};
GN ORFNames=AJ78_06090 {ECO:0000313|EMBL:OJD13456.1};
OS Emergomyces pasteurianus Ep9510.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD13456.1, ECO:0000313|Proteomes:UP000182235};
RN [1] {ECO:0000313|EMBL:OJD13456.1, ECO:0000313|Proteomes:UP000182235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD13456.1,
RC ECO:0000313|Proteomes:UP000182235};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA McEwen J.G.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-2015) 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:OJD13456.1}.
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DR EMBL; LGRN01000298; OJD13456.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9PAC1; -.
DR STRING; 1447872.A0A1J9PAC1; -.
DR VEuPathDB; FungiDB:AJ78_06090; -.
DR OrthoDB; 151499at2759; -.
DR Proteomes; UP000182235; 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:UP000182235}.
FT DOMAIN 1..141
FT /note="PPPDE"
FT /evidence="ECO:0000259|PROSITE:PS51858"
FT DOMAIN 171..319
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 310..587
FT /note="PUL"
FT /evidence="ECO:0000259|PROSITE:PS51396"
FT REGION 148..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 592 AA; 64799 MW; 7CD3765A4539F7BA CRC64;
MDVVLYVYDI SKGLARQLSL AITGTQIDAI YHTSLVFGGV EYFFGRGIQQ APPGLTHHGE
PIETIHMGTS ELPIDVIIEY MESLAEVYTQ DSYDLFLRNC NNFTHDLATF LVGKGIPDHI
RNLPETFLST PFGQMMKPYI DGMLRGATQG PEGPHPVAAN QPPLSGANGA ARSITGYPKP
SLSSQKGYVR NVTTNREVDE LLSSASSSCA VIFFTSATCP PCKLMYPVYD ELAEEAGDKA
ILIKVDLSRA FDVSAKYGVR ATPTFMTFLK GKKENEWSGA NESKLRGNVR LVIDMAWPPH
PHRRLKLPSL ERPIGTYILY KKVPPLEKLI QKLGPAGDEP ALQSLIKFVK STDSSGPAGA
ALPNLSLLQD FIKSKFPSLT QGIHFAVIDL VRVAFSDPRV SGFFAEEHAH QSLLTLLGGT
GDLSNCPYNQ QLVMTQLACN LFTSPLYLDQ IVSHDTLRET CIKIATSSLH APHVSLRAAG
ASFMYNLASF NHNERLDEAP DRLSEADQVE LVASLLEAIR LETASVESLH GHLLSLGLFV
YLAPYDGEVM DLCRVMDAQE IVKEKLKVKA LADEPLLQEV GQELLGKGLI SA
//
