ID A0A0G0J9E5_9BACT Unreviewed; 537 AA.
AC A0A0G0J9E5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 32.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=US40_C0014G0021 {ECO:0000313|EMBL:KKQ24736.1};
OS Candidatus Roizmanbacteria bacterium GW2011_GWC2_37_13.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1618486 {ECO:0000313|EMBL:KKQ24736.1, ECO:0000313|Proteomes:UP000034917};
RN [1] {ECO:0000313|EMBL:KKQ24736.1, ECO:0000313|Proteomes:UP000034917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKQ24736.1}.
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DR EMBL; LBSV01000014; KKQ24736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0J9E5; -.
DR PATRIC; fig|1618486.3.peg.924; -.
DR Proteomes; UP000034917; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR CDD; cd03012; TlpA_like_DipZ_like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
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; PF00578; AhpC-TSA; 1.
DR Pfam; PF02683; DsbD; 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..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 218..405
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 537 AA; 60363 MW; F2C1D6BCC21B53FC CRC64;
MILLIFFSFL GGIVTILSPC ILPILPVVLS GAVGEGKRKP FGIILGFVFS FTFFTLFLSL
IIKITGISAD ILRNISVFVL FGFGLSLLIP KLQDLVEKIF SRLSGKAAVK VKGGGFFGGI
LIGLSLGLVW TPCVGPILAS IITLAAANTI TSSTILITLA YSIGTAIPML AIMIGGRGLI
NKMPWLLSNT SRIQKLFGLL MVITAFAIYF NFDRKFQAYI LDKFPNYGVG LTKFEDNQEV
KNDLKKLSEK KEDSINDLRT TFYPASPELI QGGEWFNSKP LKLSQLRGKV VLIDFWTYTC
INCIRTLPYL KSWHEKYKDK DLVIIGVHTP EFEFEKNPDN VAKAIKDFDL KYPIIQDNDY
ATWNAYNNRY WPAKYFIDKN GRIRSTHFGE GDYDESEAII QDLLKEAGTI KSDMPIDNLD
YSIDARTPET YLGALRRTEN SDLKYFGDWT VEAERALPKK GSALEYSYSA KNVFLVMGSN
NGKTGIIKIY LDGKLINQIE VDNYRLYDII KLKSSGNHLL RLEFLDSNLE LYAFTFG
//
