ID A0A383WFG8_TETOB Unreviewed; 968 AA.
AC A0A383WFG8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=BQ4739_LOCUS16715 {ECO:0000313|EMBL:SZX76325.1};
OS Tetradesmus obliquus (Green alga) (Acutodesmus obliquus).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Scenedesmaceae; Tetradesmus.
OX NCBI_TaxID=3088 {ECO:0000313|EMBL:SZX76325.1, ECO:0000313|Proteomes:UP000256970};
RN [1] {ECO:0000313|EMBL:SZX76325.1, ECO:0000313|Proteomes:UP000256970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Cai Z.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNXT01001255; SZX76325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A383WFG8; -.
DR STRING; 3088.A0A383WFG8; -.
DR Proteomes; UP000256970; Unassembled WGS sequence.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR14237:SF19; MOLYBDENUM COFACTOR SULFURASE; 1.
DR PANTHER; PTHR14237; MOLYBDOPTERIN COFACTOR SULFURASE MOSC; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000256970}.
FT DOMAIN 111..224
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 64..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 968 AA; 100804 MW; A9AE938B96F79144 CRC64;
MLAELRFRWL RRSAAAADAP QTCSGTLLLR FRRQDNKAQE LSQATAESFE PGVLVADVAD
VADGAAEPQQ QQQQQPQQQT QQQQQQTQQQ QWWQADEGNW LELTSPTELL SFISAVQPPP
AWPALADGPA PKLKLIEFYA RWCGACAAAA PGMAAAASEP QLQASATFAR VNVDRVKPLM
KQLGISRIPT VMLLAPDGRL LDTFRASGDA ARDAILQHSQ ALARARAEGQ PPAAAAPPAV
PLHPAPEQQG EEEVPLDGSN GSSGTSAGSS SSGVTGSEAK EACGLTPEPA CTAPPQPAAG
PAAQPGSSAA EATASAAAAL QQAKQQFLAQ YGAGYGYGGW LDAHYEAEVG ARLGQGHHYL
DYTGAALYPS SLLQSVYADL LAKTYGNPHS AAAASTSPEA LSSGAASGGS SSSGTRVGPA
AASEAVMEQA ALAVLSHLNA DPAEYQVVFT RSATEALKLV GELFPWTAAG SSSSGSGGTT
PSEADMLSNQ QQKEGLAAGP TSSSSNSSSS GSSFIYTRSN HNSVLGVGAY AAAAGAELVP
LTDQQMDDWM AAAAAAAAQP QQQQPQQQLQ GGASQGSRWQ LPWQAKQQDM QPQAPAQSDQ
QQPVNEHQQQ QQQQQGPRYH LIAYPAQDNY AGVVYPLDYI NKAHAASTAT DRYLVLLDAA
AFLPSHPLDL SVHPADFVAA SFYKLFGYPT GLGALVLRSE LVPALRKVYF GGGSVALATP
EGCWHVAKCD PGAALSDGTP NYLGAAALSL AYDSWDSRGG MQAVEEHTQA LRSWLYEQLS
SLQHSNGTPL LQVYGRHAQE QQQQGGQVLQ GAIFNFQVLQ PDGSPLSFSR VERQAAAAGI
DLRSGCVCNP GACYDSLGLS AGEVQGLAGL KEGCGDGMDF ITVLRPAESS NNSTPAAAAA
TLGGVAAGRA DTGSSSSGSG AVSGQQQQQQ QQLVEVQVPL GSVRASLGWA STFEDAYALV
QFLKGYLQ
//