ID A0A1F6XE11_9BACT Unreviewed; 588 AA.
AC A0A1F6XE11;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=A2933_01070 {ECO:0000313|EMBL:OGI92484.1};
OS Candidatus Nomurabacteria bacterium RIFCSPLOWO2_01_FULL_46_18.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801783 {ECO:0000313|EMBL:OGI92484.1, ECO:0000313|Proteomes:UP000179381};
RN [1] {ECO:0000313|EMBL:OGI92484.1, ECO:0000313|Proteomes:UP000179381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OGI92484.1}.
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DR EMBL; MFVH01000009; OGI92484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6XE11; -.
DR Proteomes; UP000179381; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR041017; Thioredoxin_10.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42852:SF13; PROTEIN DIPZ; 1.
DR PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR Pfam; PF02683; DsbD; 1.
DR Pfam; PF08534; Redoxin; 1.
DR Pfam; PF17991; Thioredoxin_10; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 42..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 273..427
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 588 AA; 65926 MW; ECD8AA4CAA7E089F CRC64;
MLLLLISFIA GVLTVLAPCI LPLLPVIIGH SITDTTPSRK RLFVVVASLG ISVILFTLLL
KASSLLINIP QDFWKWISGG IIFLFGLTMV FPNLWEKFSF ANTLSIKSNK VLTTGYQKNS
VWGDVIIGAS LGPIFSACSP TYFVILATVL PVSFFLGIVY LFTYVLGLSL ALIVVALLGE
RIMVKVGKVS DPRGWFKKIF GVIFILVAIA IISGYDKKLQ ISLLDAGFLD VTKIEQKLLE
KNDKKDMITN GASSVDENTE VGDKIEGNEE LFLNIKEKSK KFILAPDIST PDGFINTNNL
PITISEFKGK KVVLLDIWTY SCINCQRTIP YLNEWHKEYE DEGLVIIGLH TPEFSFEKVQ
RNVEKAVKDF GIKYPVVLDN DFSTWNAYKN QYWPRKYLID IDGYIVYDHA GEGQYKETEV
AIQKALRERA DRLGMNIEVS SNISKPENVV SVESGKVKSP EVYFGWARNE FLGNGVASAR
EEQVFYLPES ISPNKLYLEG IWSFSYEYAE NENTASIVFK YEAKNVYITA GSAGGVEIEI
YKDDVFVKKV TIKDETLYTL IQDADYGKHV LRIVVPKAGL QAFTFTFG
//
