ID   T1J1H2_STRMM            Unreviewed;      1590 AA.
AC   T1J1H2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
OS   Strigamia maritima (European centipede) (Geophilus maritimus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX   NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR007391-PA, ECO:0000313|Proteomes:UP000014500};
RN   [1] {ECO:0000313|Proteomes:UP000014500}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA   Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA   Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA   Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA   Muzny D.M., Gibbs R.;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:SMAR007391-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (FEB-2015) to UniProtKB.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JH431785; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 126957.T1J1H2; -.
DR   EnsemblMetazoa; SMAR007391-RA; SMAR007391-PA; SMAR007391.
DR   eggNOG; KOG0191; Eukaryota.
DR   HOGENOM; CLU_001030_1_0_1; -.
DR   OMA; CTDHENC; -.
DR   OrthoDB; 3043426at2759; -.
DR   PhylomeDB; T1J1H2; -.
DR   Proteomes; UP000014500; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd02961; PDI_a_family; 7.
DR   CDD; cd02947; TRX_family; 2.
DR   Gene3D; 3.40.50.11390; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 13.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR19991; L 2 01289; 1.
DR   PANTHER; PTHR19991:SF3; LETHAL (2) 01289, ISOFORM F; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 13.
DR   PROSITE; PS51352; THIOREDOXIN_2; 3.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1590
FT                   /note="Thioredoxin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004579121"
FT   TRANSMEM        1560..1583
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          575..686
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          1111..1242
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          1425..1553
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   1590 AA;  184867 MW;  EBC45EDB7F1731C5 CRC64;
     MARVVTLLPL ILIAFLLPFR SVGRRSADDE AVIEEVDGKG LKALVEEESY LAVFFCKYTI
     SLHSTDHDGR LCGEECEQIM HELEKIDDDT DKFGVAFVKC QDRKLAKSYG VNRFPALVYF
     RNKEPAIYDG ELKDEDKVLA WLTDLDSMDN PDAIEEVNSI ILHKVIDDSD FVAVFFYKEN
     CKKCEKVLKE LENIDDDADK LGIAFVKIRD QAINEEYGFD DLPTLVYYRK EIPLVYDGDL
     TDEEEVLAWL VANKNLGDDD DIIEDVTARS LTQLIESVDH LAVLFYDNDE DETEAILKEL
     ENIDDDSDKH GIHMVKIDDD QVAHEYGIDE LPTLVYFEKQ IPSVYDGDLT DERQVLNWEE
     EVLQWLIHQV ESDEIEDVSD KMLQLLVEKE KHLAVLFYDK DDKKSEKVLM ELENIDDDCD
     KHGITFVKVD DDSVAKAYGI EDIPILIYFE DEIPNIYDGD LMNEEKVLTW LIHQVHTDEI
     EDVNDDMLRM LIKKTPHLVA LFYDKDDKTS AIVLEELEEI DDDADKYDIS IVKIDHDEMA
     KDFGFETIPA LVYFEHGIPN VYEGDLTVEE DVLEWLIHQK SEDTIEEVTD EMVEDLIREH
     EYVVVFFTGQ SCRDCDIVLE ELEKIDDDTD DHGIHFLTTE ETDLAKKFGI KTFPSLVLFR
     NGEPVLYKGD LKDEEKVLAW LTHEETLEIP DQIEEVNAKM LDKILDNSDH VAVFFYNENC
     KKCDKMLVEL EHIDDEADEY DIDFVKISDP GIAKEYGLKS LPALLFFRKK FPQIYEGSLE
     DEDKVLDWLI AAKNMPHDVI EVVDRNTMEV LMDDVDHLAV FFFKDNCKKC EATLQELENI
     DDETDEQGIH FVKTNDVQLA QELGINEFPS LVYFEEKVPS IYEGDLSKEE SVLEWLIHQK
     MEDTIENINR DMLNTLIEER DYVSVYFYKE KDADCEYVLK ILELIDDDCS DYGVELLKMN
     DPLMAKKYGI RNLPGLVLFR HGKPIIYKGD LEDEDDILEW LTNPDNLELE DQIERVNRKM
     FEKIRKRTDY LAAYFYSDEN CKQCSKVLAE IENIDDEAHA EGIHFVKVDD EQLAKDYGVF
     ALPAVVFFKN RASEPVIYAG DLKNEERILD WLLANKDPST DYIEEVDGKA VKDIVKKSEH
     VIVFFYNKED CENCGKVLEE LENIDDDTDR HGILFVKTQD LSLANAYGVH DFPALIYFEK
     HVPNIYEGDL LAEEDVLQWL ITQKTEDTIE TVNRDLLERM IEDTQYLAVF FYKPNCKACD
     QTLEELENID DDLDLFGINM VKIQDTILAK RYGIKTVPAV VYFRNGNPLV YEGDLKNEEL
     LLEWLIDDDN RELADEIEAV NNRMLEKLLE DSSFLAVFFY DEGECPECSA VLAELENIDD
     EADTFGIDFV KINDPMAAER FNILTTPALV YFRKKIPIIY EGDLLDEERI LTWLTSQDVF
     EIKDEIEEVN RKMLDKLLDE NDFVAVFFYD YDCPKCEEVL EELEHIDDEA DNLDITFVKI
     KDPRFAKKYG INQLPALVYF RRKFPSIYRV MYVFSGDLLA EDEVLEWLQK NRYRHPELNL
     FMYALAAITL AFVLYTIFLM FCFKGHQKTA
//