ID   D0RQU4_9PROT            Unreviewed;       172 AA.
AC   D0RQU4;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Thiol-disulfide isomerase-like thioredoxin {ECO:0000313|EMBL:EMH80785.1};
GN   ORFNames=HIMB114_00011840 {ECO:0000313|EMBL:EMH80785.1};
OS   alpha proteobacterium HIMB114.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC   Candidatus Pelagibacteraceae.
OX   NCBI_TaxID=684719 {ECO:0000313|EMBL:EMH80785.1, ECO:0000313|Proteomes:UP000033990};
RN   [1] {ECO:0000313|EMBL:EMH80785.1, ECO:0000313|Proteomes:UP000033990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HIMB114 {ECO:0000313|EMBL:EMH80785.1,
RC   ECO:0000313|Proteomes:UP000033990};
RA   Rappe M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EMH80785.1, ECO:0000313|Proteomes:UP000033990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HIMB114 {ECO:0000313|EMBL:EMH80785.1,
RC   ECO:0000313|Proteomes:UP000033990};
RA   Grote J., Thrash C., Huggett M.J., Landry Z., Carini P., Giovannoni S.J.,
RA   Rappe M.S., Brinkac L., Kim M., Beeson K., Ferriera S., Sutton G.,
RA   Friedman R., Venter J.C.;
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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:EMH80785.1}.
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DR   EMBL; ADAC02000001; EMH80785.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0RQU4; -.
DR   STRING; 684719.HIMB114_00011840; -.
DR   eggNOG; COG0526; Bacteria.
DR   OrthoDB; 9799347at2; -.
DR   Proteomes; UP000033990; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   PANTHER; PTHR42852:SF6; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Cytochrome c-type biogenesis {ECO:0000256|ARBA:ARBA00022748};
KW   Isomerase {ECO:0000313|EMBL:EMH80785.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033990};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          37..172
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   172 AA;  19711 MW;  3C06B875E923C601 CRC64;
     MYLKKGFKIL SLILASIIIF YFFYYSLFQE KKLNPKVMIG SQMPNLQSKT LYKNKVLSLS
     NIVSNEKFVV NIFASWCVPC KIEHPILIQL KNSKIKIIGI NYKDNQKNAK AFIEKYQNPF
     EKVLIDSDGA LSIQLGAFGV PETFLVDKNF TIIAKHIGPI DNNFVKKVIN LK
//