ID A0A091AZ02_9GAMM Unreviewed; 710 AA.
AC A0A091AZ02;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=N787_12685 {ECO:0000313|EMBL:KFN45543.1};
OS Arenimonas metalli CF5-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Arenimonas.
OX NCBI_TaxID=1384056 {ECO:0000313|EMBL:KFN45543.1, ECO:0000313|Proteomes:UP000029393};
RN [1] {ECO:0000313|EMBL:KFN45543.1, ECO:0000313|Proteomes:UP000029393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF5-1 {ECO:0000313|EMBL:KFN45543.1,
RC ECO:0000313|Proteomes:UP000029393};
RA Chen F., Wang G.;
RT "Genome sequencing of Arenimonas metalli.";
RL Submitted (SEP-2013) 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:KFN45543.1}.
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DR EMBL; AVCK01000027; KFN45543.1; -; Genomic_DNA.
DR RefSeq; WP_034213135.1; NZ_AVCK01000027.1.
DR AlphaFoldDB; A0A091AZ02; -.
DR STRING; 1384056.N787_12685; -.
DR PATRIC; fig|1384056.3.peg.1865; -.
DR eggNOG; COG4232; Bacteria.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000029393; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR CDD; cd02953; DsbDgamma; 1.
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; IPR035671; DsbD_gamma.
DR InterPro; IPR028250; DsbDN.
DR InterPro; IPR036929; DsbDN_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR32234:SF3; SUPPRESSION OF COPPER SENSITIVITY PROTEIN; 1.
DR PANTHER; PTHR32234; THIOL:DISULFIDE INTERCHANGE PROTEIN 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; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000029393};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..710
FT /note="Thioredoxin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001871060"
FT TRANSMEM 315..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 397..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 439..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 535..555
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 567..586
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 582..710
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 710 AA; 74652 MW; 21E72F66A0516122 CRC64;
MTRWLLAALA ALLLAPTAQA VDEADLLPID QAFALSARAT ERGRIEFHWE IAPGYYLYRH
RTGVELVEGG FKSNPLELPD GEAYTDEFFG DVETYRNQLT AVLTGATADD ATALRFKVKY
QGCADVGVCY PPHTKTVTVA LPAGAGGDPL AALGGARGPD LFGDTDPARA AGGLPLPEEQ
AFRFEAIAGG PDKLLLRFDP APGYYLYRDR STVEVEGDGV TAGAINWPPA QSHRDEHFGD
VMVYFDPVDA TLPLQRTNTA ATVLTVRTTF QGCQTDGICY PPMTRTATVT LPAGAGAAAP
ADAPRETPPA RAPTALWLAL LLALGGGVIL NLMPCVLPVL SLKALSLAQG GGQAKRQALW
YTAGVLASFA AVGAIALALR QAGLALGWGF QLQQPGVIAA LALVMIAIGL SLSGVVSFGA
SLAGTGQSLA QKSGPAGDFF TGVLAVVVAS PCTAPFMGTA LAFAFAASPA VAILVFLALG
LGLALPFLLI GFVPALASRL PKPGAWMDTL KQVLAFPMYL TAVWLLWVLA KQRGADAIGL
VLAGAVVLGL GLWWWEKARW GRLLPRVLAA LVVLAALWPV LVVQRMPVPE RAVAAEEGVV
AFSQDKLDQL RRDGRVVFVN MTADWCVTCK ANERTVLARE GFRTALDAAG AVYMKGDWTD
VDPAITAFLE SHGAVGVPLY VVYPRNGEPR VLPTVLTQDL VAGALAEAAN
//
