ID A0A2A5X304_9GAMM Unreviewed; 748 AA.
AC A0A2A5X304;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=CNF00_00385 {ECO:0000313|EMBL:PDH43185.1};
OS Candidatus Thioglobus sp. MED-G25.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Thioglobus.
OX NCBI_TaxID=1986229 {ECO:0000313|EMBL:PDH43185.1, ECO:0000313|Proteomes:UP000219647};
RN [1] {ECO:0000313|EMBL:PDH43185.1, ECO:0000313|Proteomes:UP000219647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED-G25 {ECO:0000313|EMBL:PDH43185.1};
RA Haro-Moreno J.M., Lopez-Perez M., De La Torre J., Picazo A., Camacho A.,
RA Rodriguez-Valera F.;
RT "Fine stratification of microbial communities through a metagenomic profile
RT of the photic zone.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:PDH43185.1}.
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DR EMBL; NTKC01000001; PDH43185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5X304; -.
DR Proteomes; UP000219647; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IEA:UniProtKB-EC.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 2.60.40.1250; Thiol:disulfide interchange protein DsbD, N-terminal domain; 2.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR028250; DsbDN.
DR InterPro; IPR036929; DsbDN_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR32234; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 1.
DR PANTHER; PTHR32234:SF0; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 1.
DR Pfam; PF02683; DsbD; 1.
DR Pfam; PF11412; DsbD_N; 2.
DR Pfam; PF13899; Thioredoxin_7; 1.
DR SUPFAM; SSF74863; Thiol:disulfide interchange protein DsbD, N-terminal domain (DsbD-alpha); 2.
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 Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..748
FT /note="Thioredoxin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013128453"
FT TRANSMEM 328..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 407..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 449..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 488..516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 528..545
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 551..566
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 621..748
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 152..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 80850 MW; 83242C846027535A CRC64;
MKPITALLLL LSVMLSPLNG VAQQDSNLLP AEEAFKFHAS VVNPNTIEAV WTIAEGYYMY
RSKFGFTAEP VQAVLGDARY PAGTIKHDEY FGEVETYTDS VRITLPLDRD HFVGGPLVLF
AAGQGCNKPV GVCYPPITQR VQIVVPVTTS SLSNDQRSGS VKTSSESSST GGSVTELQTL
LGTTAGDVQK FLDPEDAFQV EIEIVGENAL AAHFKIAPGY YLYRDKIAFQ VVQGKAQVRA
FDLPPGTVKQ DPYFGAVDVY LISRSIIVPI ERNNPMADTL SVSVNFQGCA EKGICYAPMN
TIRKIEFPSF VNTKTKGQAD EALSARNLIA FFGAAFVTGL LLTFTPCVLP LIPILSSIIV
GQGGTSSRLR GGAISLAYVL GTAATYAAIG AVAGATGEQL QAYFQNIWAI GLISIILTLM
ALSMFGLYEI QMPAFVQSIL TARTTSLSAG SFGMIFLLGA VSALVVGACV SPLLISVLSI
AIFHGDPYLG AGLMFSMALG MGVVLIAIGF GAGILLPRTG AWMDRVKHLF GVMLIGVAIY
LLGTIPAVPV LLLWAVLLIM FGIYLVKSQA PMLKWRYAWN ALGTLCIIWG MLAMFGGLNG
GRNILQPVSL ALFSEDVLND AMSVKGQPQF YKVTSVAEFE QLLSDARSDE QSVILDFYAD
WCTDCLRMEK TTFNDPQVRT DLTQFRLLKL DVTDPSDPVG KTIKQRYGVY GPPALLFFDA
QGQELLAKRL YGYLGPNRFL SLLKSLRE
//
