ID A0A395MDF3_9HYPO Unreviewed; 743 AA.
AC A0A395MDF3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Protein disulfide-isomerase {ECO:0000313|EMBL:RFN45952.1};
GN ORFNames=FIE12Z_9799 {ECO:0000313|EMBL:RFN45952.1};
OS Fusarium flagelliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN45952.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN45952.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN45952.1,
RC ECO:0000313|Proteomes:UP000265631};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RFN45952.1}.
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DR EMBL; PXXK01000330; RFN45952.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395MDF3; -.
DR STRING; 2594813.A0A395MDF3; -.
DR OrthoDB; 52245at2759; -.
DR Proteomes; UP000265631; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd02961; PDI_a_family; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR45672; PROTEIN DISULFIDE-ISOMERASE C17H9.14C-RELATED; 1.
DR PANTHER; PTHR45672:SF3; THIOREDOXIN DOMAIN-CONTAINING PROTEIN 5; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 3.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:RFN45952.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000265631};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..743
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017221149"
FT TRANSMEM 693..710
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..158
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 274..416
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 160..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 84309 MW; F33BB683CE340502 CRC64;
MRFSPLATLA GLSAFVLADE VKNPVSEPSV FNGKTVPSLV ELTPANWEEQ AKKNKFMMVK
HFSPYCKHCT RFAPTFQTLY EFYYTSKPQV DDPEATFTKY YDFIFGTVNC VAYYDFCMEH
EIQSYPTTIL YENGKVFEAL RGIKNMTVLT TTIEKALAKE HPGRPELVEL PNPGDKVYPP
PKVEEKPTEA AVEKKETQAP AVKPAVEAEK PIEAVVEPAG KTEGKSLDDV TEMPKAEVKS
DKAESAEKPA EDASKSSFGA DWKVPSTGQM LKKPKPQDPT PKYNLEGIST PLTPDNFDTL
VTNSKDPWFI KFYAPWCSHC KAMAPTWQQL AKKMQGKLNI GEVNCEADHK LCTQMGVKAF
PTIYFVTGAE KAEYKGLRGV GDFVTYAEGA IEVAGGVLDV DAESFKELEK TEEVLFVYFY
DHATTTEDFK AIDALPLNLI GRGKIVKTSD PELYKRFKIT TWPRLLVSRE GRATYYTPIT
PDEMRDVDSL VSWMKSTWLP LVPEMTALNA KQIMSHKLVV LAILNRDDED RLQSSISELK
NAANEWVDRQ VQEFQLERKK LRDAKQMRIE EAQSRDDQRG LRNAKAIKID MDSTRRKEVG
FAWVDGVFWQ RWIAATYNID VRDGERVIIN EEDRHKFWDT TPTGNQIMIS HTSIMDTLDK
IVYGPNPIPP KYTISSFSKF FFDIKMNFID HPFLSMGFVI AVGFGVYSWL RNRTRRPRGT
FFRDDNMGLK DGLLGQNGNA KSD
//