ID A0A150VGS8_9PEZI Unreviewed; 710 AA.
AC A0A150VGS8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=M433DRAFT_131002 {ECO:0000313|EMBL:KYG49739.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG49739.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG49739.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG49739.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:KYG49739.1}.
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DR EMBL; JPDO01000017; KYG49739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150VGS8; -.
DR STRING; 766039.A0A150VGS8; -.
DR Proteomes; UP000075602; 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; 2.
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 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:UP000075602};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..710
FT /note="Thioredoxin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007571639"
FT TRANSMEM 652..669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..175
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 226..457
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 204..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 710 AA; 79610 MW; FFD47C0D494D0DE7 CRC64;
MRLTPSFLPL AALLAPAWAG LFKRTPPFTS GGSEEGGPTT FNGQQVPELS SIDGEHLADT
IRNGYWLVEF FSPYCSHCKS FAPTWQTLYE FYYTQDPLPQ ISSSGEAEND LNSFTRYYDF
HFGRVDCVAN GDVCASNEIK SFPTVVLFKD GQKVKQEVGA HDIKFMSSWV EEVLEGIRPG
SRPKGGPILP KVGAHEVEKT LMPEQPPLPA AADDPTTQST QTPTASASKS TVSATRLPDP
PNPNGKSTPL TAETFQRLVT TTRDPWFVKF YAPWCHHCQA MAPNWQSMAR QMQDRLNIGE
VNCEVEKRLC KDVKVRGYPT ILFFRGGERI EYDGLRGLGD LLSFANKAVS AGDGIRDVTA
ADFEEMEKNE EVIFLYFYDQ ATTSEDFAAL DRLVMPLIGH AKLVKTSDPA LVARFKISTW
PRLLVSRDGK PTYYTALSPR EMRDYRHVLG WMQAHWLPIV PELTASNAEE VMRGKLVVLG
ILSRERPEEF LSAKREIKNA ALEWIDKQTQ AFQLERQELR DAKQLRIEEA EDRNDQRALR
AAKSIRINMD DIERKEVGFA WVDGVFWERW IRSTFGIAVH LDNERVVMYD HDNHRYWDNT
MTGNAIVPSR TSILETLPRV VSNPPKIAPK RTTTALGHVW WVVKGQLIEH PLVSTGVAIG
IVIGVFIFAR RHLRLGVMST PGYFRVGEKG GPMDGLLGGN SGGAAQGKVD
//
