ID A0A2X0LC53_9BASI Unreviewed; 782 AA.
AC A0A2X0LC53;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=BZ3500_MvSof-1268-A1-R1_Chr7-3g09623 protein {ECO:0000313|EMBL:SDA02298.1};
GN ORFNames=BZ3500_MVSOF-1268-A1-R1_CHR7-3G09623
GN {ECO:0000313|EMBL:SDA02298.1};
OS Microbotryum saponariae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=289078 {ECO:0000313|EMBL:SDA02298.1, ECO:0000313|Proteomes:UP000249723};
RN [1] {ECO:0000313|Proteomes:UP000249723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jeantristanb JTB J.-T., Ricardo R.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FMWP01000125; SDA02298.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X0LC53; -.
DR STRING; 289078.A0A2X0LC53; -.
DR Proteomes; UP000249723; 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; IPR017937; Thioredoxin_CS.
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 SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000249723};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..782
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015846439"
FT TRANSMEM 732..750
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..145
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 327..443
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 156..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..190
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 86408 MW; 8DA29A762E3804A8 CRC64;
MTRIGLPLSQ LVMTALVLLA LPLGRTSGAA PITPMEMAGE SLTAETWNTV NNGTWLVEHY
SPYCHHCRSF APKWKELYDL KRVPTTSQNF YFAQVDCAAN GDLCHLNNVK YYPSIFLYHH
GVFIEEYSGK RAVFDLDQYI DRHMLKIKQA KALEAKKAAA PPEVKVETAP KKQENEEEED
EEDAEENDTD PLDNGPQGQV KTDRLAAAIK GKTGEKDTSA AKPKGPTREA KLHLNDEDAQ
EEKASPSALE VILEGAKKAA PVVVSPPLLK AGKISKELLD AAVGSKFDKT ADGRAPKGGV
ARLDKGSADS DSPSSFVAQP HQPIDEKRNN HPLPDGQVHI LEPTQIDALN ADDAPPSFVK
FYAPWCGHCK ALQPRWVDLA EQLKGRVDVY EMDCDQKSTS KTCAAEKVQS YPTLMLYHQG
QKVEYNGPRD VETMRRFVTR VVDSSQVKPL ANEYELKRVV AAEPVVMLFL YSPSLSKDDL
KVAMTAARSL QGEPSFYTST SPDLFSLYSV QQDAVFLVLK GQHLQPSSRH AFPSASTSGL
ATREARIENI SNWMRWAKLP ALVELNSATI HDVLPATGDD VPLVVLGLFS KSQMGKDYED
QKTAFEALAK GWAERRSKGD KLAREVVWAW VDADRWMGWL KGMYSVNWGK RPGIVVSDPK
ELAYWNRDLS SEPITSDSVY ETVEQGILTN RLKPLSSRSF FDRLAHVSLN SVESRLALLT
DSSFKSYFSS HPFALVFFVI SSWLAGWWFL RQCLGRRGGA SLMGGSSGAA GASGKGGSAK
YE
//
