ID   F2UMH3_SALR5            Unreviewed;       286 AA.
AC   F2UMH3;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=GST N-terminal domain-containing protein {ECO:0000259|PROSITE:PS50404};
GN   ORFNames=PTSG_09388 {ECO:0000313|EMBL:EGD78322.1};
OS   Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX   NCBI_TaxID=946362 {ECO:0000313|EMBL:EGD78322.1, ECO:0000313|Proteomes:UP000007799};
RN   [1] {ECO:0000313|Proteomes:UP000007799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Salpingoeca rosetta.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FAX family. {ECO:0000256|ARBA:ARBA00006475}.
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DR   EMBL; GL832982; EGD78322.1; -; Genomic_DNA.
DR   RefSeq; XP_004989645.1; XM_004989588.1.
DR   AlphaFoldDB; F2UMH3; -.
DR   STRING; 946362.F2UMH3; -.
DR   EnsemblProtists; EGD78322; EGD78322; PTSG_09388.
DR   GeneID; 16070196; -.
DR   KEGG; sre:PTSG_09388; -.
DR   eggNOG; KOG4244; Eukaryota.
DR   InParanoid; F2UMH3; -.
DR   OMA; YPLQDCG; -.
DR   OrthoDB; 3684737at2759; -.
DR   Proteomes; UP000007799; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd03193; GST_C_Metaxin; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR026928; FAX/IsoI-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR033468; Metaxin_GST.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12289; METAXIN RELATED; 1.
DR   PANTHER; PTHR12289:SF41; METAXIN-1 HOMOLOG; 1.
DR   Pfam; PF17171; GST_C_6; 1.
DR   Pfam; PF17172; GST_N_4; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01200; SUF1.1; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007799};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          53..123
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
SQ   SEQUENCE   286 AA;  32326 MW;  1AC8B5666C73E594 CRC64;
     MWLEVVLAGG SALAAVLLVY LYRSKFMLPR HPEAPDTPRS GNPADEVVLY SFPPVPGTLF
     STSPFGAKLE IFLRLANIPF TTKPADLARA PKGKVPYIQH GNNLIGDSTF IIRYLLATYG
     KPHQSYFGKL RLSLTPYEVS IGHMVQVLCE TNIYNALLWS RWLCGESDFV KNNFFGMIPR
     PIRGLIFAMV QRSMFDWLWG QGFIRHSPHD VVTLSKLDID AIDTLLGNKS FLFGDEPTVY
     DCTAFSFLEP FVNSDLELQG LRTYVCSKGR IVNFVNRMRH LIPQDK
//