ID A6RBT8_AJECN Unreviewed; 337 AA.
AC A6RBT8;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Thioredoxin {ECO:0008006|Google:ProtNLM};
GN ORFNames=HCAG_07096 {ECO:0000313|EMBL:EDN10635.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN10635.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987}.
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DR EMBL; CH476662; EDN10635.1; -; Genomic_DNA.
DR AlphaFoldDB; A6RBT8; -.
DR STRING; 339724.A6RBT8; -.
DR VEuPathDB; FungiDB:HCAG_07096; -.
DR HOGENOM; CLU_072377_0_0_1; -.
DR OMA; PIFEMFP; -.
DR OrthoDB; 45858at2759; -.
DR Proteomes; UP000009297; Unassembled WGS sequence.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 2.60.120.470; PITH domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR010400; PITH_dom.
DR InterPro; IPR037047; PITH_dom_sf.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01068; thioredoxin; 1.
DR PANTHER; PTHR46115:SF5; THIOREDOXIN DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46115; THIOREDOXIN-LIKE PROTEIN 1; 1.
DR Pfam; PF06201; PITH; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51532; PITH; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000009297}.
FT DOMAIN 1..109
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 133..335
FT /note="PITH"
FT /evidence="ECO:0000259|PROSITE:PS51532"
FT REGION 175..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 337 AA; 36652 MW; 03CE1BCB5DDF8838 CRC64;
MPKIVHISSQ TQLAELLSSS SIVVVDFYAD WCGPCKVIAP IFESLSNKFS SPTKISFAKV
DVDSNQELAA SYGVSAMPTF LIFNNGAVAH SIRGANPQLL TSKIEEFARS VGSNGDGAAG
TAGEASGNGS RWLGGSVPKG YSDVSGEVEI KDIDLLNYDN QVGSARSLFA AEKPSGFSSA
ESSGNGKDKA SATPDWVESD TDEQLMLFLP FQSSIKLHSL QITSLAPRES DDDVPMRPKT
LKLYANRAHI IGFEDADEDS PTQEIELLPQ DWDEETKTAT VELRFVKFQR IMSLVVYFVD
GDGDRERIRV DRLRLFGEAG EKRELGKLEK IGDEPGE
//
