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Database: UniProt
Entry: A0A1Z5KQM2_FISSO
LinkDB: A0A1Z5KQM2_FISSO
Original site: A0A1Z5KQM2_FISSO 
ID   A0A1Z5KQM2_FISSO        Unreviewed;       770 AA.
AC   A0A1Z5KQM2;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   13-SEP-2023, entry version 22.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FisN_1Hh596 {ECO:0000313|EMBL:GAX28613.1};
OS   Fistulifera solaris (Oleaginous diatom).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Bacillariophyceae; Bacillariophycidae; Naviculales; Naviculaceae;
OC   Fistulifera.
OX   NCBI_TaxID=1519565 {ECO:0000313|EMBL:GAX28613.1, ECO:0000313|Proteomes:UP000198406};
RN   [1] {ECO:0000313|EMBL:GAX28613.1, ECO:0000313|Proteomes:UP000198406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCC DA0580 {ECO:0000313|EMBL:GAX28613.1,
RC   ECO:0000313|Proteomes:UP000198406};
RX   PubMed=25634988; DOI=10.1105/tpc.114.135194;
RA   Tanaka T., Maeda Y., Veluchamy A., Tanaka M., Abida H., Marechal E.,
RA   Bowler C., Muto M., Sunaga Y., Tanaka M., Yoshino T., Taniguchi T.,
RA   Fukuda Y., Nemoto M., Matsumoto M., Wong P.S., Aburatani S., Fujibuchi W.;
RT   "Oil accumulation by the oleaginous diatom Fistulifera solaris as revealed
RT   by the genome and transcriptome.";
RL   Plant Cell 27:162-176(2015).
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:GAX28613.1}.
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DR   EMBL; BDSP01000277; GAX28613.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5KQM2; -.
DR   InParanoid; A0A1Z5KQM2; -.
DR   OrthoDB; 37308at2759; -.
DR   Proteomes; UP000198406; Unassembled WGS sequence.
DR   CDD; cd09212; PUB; 1.
DR   CDD; cd02947; TRX_family; 1.
DR   Gene3D; 1.20.58.2190; -; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR036339; PUB-like_dom_sf.
DR   InterPro; IPR018997; PUB_domain.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR   Pfam; PF09409; PUB; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SMART; SM00580; PUG; 1.
DR   SUPFAM; SSF143503; PUG domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198406};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..770
FT                   /note="Thioredoxin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012441921"
FT   DOMAIN          204..246
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          287..403
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          273..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          727..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          557..595
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        737..770
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   770 AA;  84088 MW;  1EBE4EEB2583895C CRC64;
     MGRVISLVTL SVAALAGTEG YSDNSRPAAF FHRMVTEEER SATIELALRK LGVTKSHRSY
     ERQQFTRNIL SKLPRGGYQD SETTDNVDTE QGGLSLEQKV HRAMQKLGIS PPVPPPPSEI
     ATEDDNCVDG VCSIPDAKTD APSTEPPPDP RELAESISKE LNVDVSLVWA ALAATSTGSS
     DEQRVYNVQE AREMIQQELD IISQVSEDAD AVKQLTAEGF SPFLSRRALA FAEMDLDNAR
     AILLADQEDE ETNQEATQPV SAFKTVAVNT DFDPTKMDAQ GSQKPREPTP AKKSDVIFEA
     TASQIQELVL ESPVPVLLDV YADWCGPCKA LTPVLEEMAI KSGGAFRLVK VNSDNERSIA
     SGALQVSALP TVFGISGGKI RHRFQGMPRS QEVFQNFMMG LLVPGQAFDP PVTPAEQKEY
     NELSAKLLQA AGGASFSFGS RERLQDRVVA RLGDLIQQAD GDILEAEGSA QTVRSLLSKV
     IQNPMETKYR TVKLTNKVIA AKVSKYKAAL SILKSAGFQD NGDVMVLGAG KNIINVAPLI
     CARDCIDKWI SEKRYEVAKA TRKRQDEEAR QKLLAEKLER NQDEEEDVED EEETVVDPNA
     CTLKVRMEGK KKVHSLDFHG DDPLSSILEK VFLSTDSHLG QDVQITCVAK KLIVKSSDAV
     SMSKSLRSLG LMPSASIVLS VVSDKKETST SNLAERAAAK KKKRRGSHTM QSVGIYAKDD
     HLKGELVDGG GGVLYEQDVT DDEEEIDEKQ DTDIDEAPKE EDGASEEDTE
//
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