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Database: UniProt
Entry: D8LN57_ECTSI
LinkDB: D8LN57_ECTSI
Original site: D8LN57_ECTSI 
ID   D8LN57_ECTSI            Unreviewed;      1154 AA.
AC   D8LN57;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Esi_0043_0092 {ECO:0000313|EMBL:CBN74820.1};
OS   Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC   Ectocarpales; Ectocarpaceae; Ectocarpus.
OX   NCBI_TaxID=2880 {ECO:0000313|EMBL:CBN74820.1, ECO:0000313|Proteomes:UP000002630};
RN   [1] {ECO:0000313|EMBL:CBN74820.1, ECO:0000313|Proteomes:UP000002630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX   PubMed=20520714; DOI=10.1038/nature09016;
RA   Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA   Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA   Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA   Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA   Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA   Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA   Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA   Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA   Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA   Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA   Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA   Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA   Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA   Yamagishi T., Van de Peer Y., Wincker P.;
RT   "The Ectocarpus genome and the independent evolution of multicellularity in
RT   brown algae.";
RL   Nature 465:617-621(2010).
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DR   EMBL; FN648630; CBN74820.1; -; Genomic_DNA.
DR   AlphaFoldDB; D8LN57; -.
DR   STRING; 2880.D8LN57; -.
DR   EnsemblProtists; CBN74820; CBN74820; Esi_0043_0092.
DR   eggNOG; KOG0910; Eukaryota.
DR   InParanoid; D8LN57; -.
DR   OrthoDB; 37308at2759; -.
DR   Proteomes; UP000002630; Chromosome LG03.
DR   CDD; cd09212; PUB; 1.
DR   CDD; cd02947; TRX_family; 1.
DR   CDD; cd14291; UBA1_NUB1_like; 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; 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   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   Pfam; PF00627; UBA; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF143503; PUG domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
DR   PROSITE; PS50030; UBA; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1154
FT                   /note="Thioredoxin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003117315"
FT   DOMAIN          353..392
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          398..438
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          506..629
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          25..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          795..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          986..1113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          383..410
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        27..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..208
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..508
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..816
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        986..1006
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1007..1039
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1061..1076
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1154 AA;  120787 MW;  7074596FCEA76C24 CRC64;
     MLMILRTAMA AAALLAAVDQ ASGFVSTRRR HHGSSSSPGT RHSYNGGDGL ASGGAPLTST
     TVDHLTLSRE SPYPFESSAA RTVRGLVATQ RSKRSNRGGG NGATVQPRPG METQLGGWSY
     ARTVLTNLSK GAGREGESGT DESGDAAAAA GGSAQSSSGG SSGGKGADGA PAKGNKGAGG
     GGAGLGIGGG GGDGDDDDDD EEEEEKKGKE AGDEDGLDSW DLSEFGDSQD GLGIEFSEAG
     VGEDEEQQEG ENGGLSGAKA AVDGGDDAQA GQEQGGALPQ EYEVVCDGDV CERRPVGPNP
     AQTVPAVDGA AAEAGAATGA ASAGAAASSG ADNALVPDAG GDSDGGGGVP PSAVDPGVAQ
     LVSMGWEAEE STAALEASGG DVVAAAEALA AQEEEDLERY EEGLADLQQR GWDSDVAMSA
     MREAGGNSTA ALHALEEEDR VLSMQFEQSI EEMVEHGWDE EVARKALLMQ WQKDIEGKGG
     SRKDQKQFEK TVQGVHQKGV KEGKASTTKK SEPPAPTPAK REDVVFEVTD KTLQKVVLES
     PVPVILDVYA EWCGPCKQLT PALEEAAMRS GGMFRVAKVD AEKQRSIAEV LGIHAFPSVF
     GMKDGIILDN FVGGLAQDEM QSFMMGVVMG MPPPKDQALR EHQKSQAELR GISRKLAHVA
     GLAVLGSRKK ESLCLKVDKA LGETLEGELP EGGGPAAENA PAVAAAKKAA RTVITVLMSA
     YKFPEDPKYR TLSTTSKAYE EVLAPHPPML EALRLAGFRH KDGDESHLTL LHRNMAVLAS
     VQDRVEVWNK GIKMPQIEED SEDEYDDSED EEDEEELERI KQARERLATV AKLEITDSSG
     GHEAVVKLTM EADSTLGELF RTLQEEEGFG ADLVLKTAFP KRELAASDES CHSSTLLSLG
     LAPSARLVAT TAAALAAEQE AEGGDAEAAA VRKEELRAKM MEKARDGKRK GIKKAGTLFG
     ADDGIIEVKK GKHQEYFGGD STVTLAAEDS DDEDGDEGDG SDNQEAASQE DDFGQSGGEP
     SLSDDQENDN GSSYSSSENE EGEGGEEQMT DASRNDDNGE EDYSPESEEE SDLSDERFSE
     GDTGTSATES EGTRTDFDAD EASYASGVGG EEHRWGELAK LLVQSHGRRE CFGALLRDSS
     PPFFGSSTGW LSVR
//
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