ID A0A0G4L6T3_9PEZI Unreviewed; 718 AA.
AC A0A0G4L6T3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=BN1708_003028 {ECO:0000313|EMBL:CRK17747.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK17747.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK17747.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK17747.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; CVQH01008890; CRK17747.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4L6T3; -.
DR STRING; 100787.A0A0G4L6T3; -.
DR OrthoDB; 52245at2759; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; PTHR46426; PROTEIN DISULFIDE-ISOMERASE TMX3; 1.
DR PANTHER; PTHR46426:SF1; PROTEIN DISULFIDE-ISOMERASE TMX3; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 3.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..718
FT /note="Thioredoxin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002566274"
FT TRANSMEM 659..677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..159
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 235..358
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 163..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 80218 MW; 859BE4DA3AE8399D CRC64;
MKLSTLLVLA TSTLALAVKK TNKLKDEDPN TYFNSVKVPP MLELTPDNFD KEINATKLVV
VKHYSPYCPH CIDYAPTYQT LYEYYYTSKP VTTEDVSFME FYDIRFATIN CIAFFDLCVS
LKVQSYPSTI LYKDGQAAEI VKGVKGLDVL TAAFEPFLEA AKPGTRPKEL NLPNTGDKQT
PDFSPAAAIT SDTKTDAAAG AQTDDLPKAA PEESKDKSSA TPDKTTPEKT VPSPKKTIPE
APPKPTETFN PDGVSVALTA EKYETLVTGS KKPWFIKFYA PWCHHCQALA PTWAQLGKEM
KDKLNIGEVN CDVEAKLCKE VGVRAFPTLL FIKGTERAEY EGLRGLGDLK SYGEGAAAAA
VGVVDVDAAA LEALEQKEEV VFVYFYDHAT TSEDFASLEK MPVNLVGRAR IVKTQDPKLA
ERYKITTFPR LLVSRSGRPT YYNPLTPREM RDVEGILAWM RSVWLPMVPE LVATNSREIM
DGKIVVLAII NRNDAETLSD AKRELNKAAN DWMDKQIVLF QKERQELRDA KQLKIDEAED
RGDERAKDNA KLIRVDMSKS PRKEVAFAWI DGVFWQRWLK TTYGIDVSTG GNRVIINDED
RHRYWDVTDT NTNILLSHTS ILDTLPKVTA SPPEIRAKTT LSFISKIFFD LRMSFVDHPF
LSVGAVLAVM FAGAGWVRNR MRRHRGGHFV RLDDSWSTKE LMKEGLIGGG PSGNGKVD
//