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Conserved domains on  [gi|544903974|ref|WP_021314637|]
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MULTISPECIES: thioredoxin family protein [Enterobacterales]

Protein Classification

thioredoxin family protein( domain architecture ID 10590097)

thioredoxin family protein may function as a thiol disulfide reductase that catalyzes the reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

CATH:  3.40.30.10
EC:  1.8.-.-
Gene Ontology:  GO:0015036
PubMed:  11441809|12074972|9099998|10049365|15558583|30367780
SCOP:  4000237

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_3 pfam13192
Thioredoxin domain;
7-76 5.79e-21

Thioredoxin domain;


:

Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 77.64  E-value: 5.79e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544903974   7 LGTGCSGCKTTIRLIQQVADERGVAIQLEKVESLSEIMKHKVMATPAVVVDNIVVHTGGIPSRDIIESWL 76
Cdd:pfam13192  1 LGPGCPKCPQLEKAVKEAAAELGIDAEVEKVTDFPEIAKYGVMSTPALVINGKVVSSGKVPSEEEIRKLL 70
 
Name Accession Description Interval E-value
Thioredoxin_3 pfam13192
Thioredoxin domain;
7-76 5.79e-21

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 77.64  E-value: 5.79e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544903974   7 LGTGCSGCKTTIRLIQQVADERGVAIQLEKVESLSEIMKHKVMATPAVVVDNIVVHTGGIPSRDIIESWL 76
Cdd:pfam13192  1 LGPGCPKCPQLEKAVKEAAAELGIDAEVEKVTDFPEIAKYGVMSTPALVINGKVVSSGKVPSEEEIRKLL 70
redox_disulf_2 TIGR00412
small redox-active disulfide protein 2; This small protein is found in three archaeal species ...
 4-72 2.01e-11

small redox-active disulfide protein 2; This small protein is found in three archaeal species so far (Methanococcus jannaschii, Archeoglobus fulgidus, and Methanobacterium thermoautotrophicum) as well as in Anabaena PCC7120. It is homologous to thioredoxins, glutaredoxins, and protein disulfide isomerases, and shares with them a redox-active disulfide. The redox active disulfide region CXXC motif resembles neither thioredoxin nor glutaredoxin. A closely related protein found in the same three Archaea, described by redox_disulf_1, has a glutaredoxin-like CP[YH]C sequence; it has been characterized in functional assays as redox-active but unlikely to be a thioredoxin or glutaredoxin. [Unknown function, General]


Pssm-ID: 129506  Cd Length: 76  Bit Score: 53.76  E-value: 2.01e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544903974   4 VKVLGTGCSGCKTTIRLIQQVADERGVAIQLEKVESLSEIMKHKVMATPAVVVDNIVVHTGGIPSRDII 72
Cdd:TIGR00412  3 IQIYGTGCANCQMTEKNVKKAVEELGIDAEFEKVTDMNEILEAGVTATPGVAVDGELVIMGKIPSKEEI 71
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 8-68 9.61e-04

TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c.


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 34.97  E-value: 9.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544903974   8 GTGCSGCKTTIRLIQQVADER---GVAIQLEKVESLSEIMKHK-------------------VMATPAVVV---DNIVVH 62
Cdd:cd03011   29 ATWCPVCRFTSPTVNQLAADYpvvSVALRSGDDGAVARFMQKKgygfpvindpdgvisarwgVSVTPAIVIvdpGGIVFV 108


                 ....*.
gi 544903974  63 TGGIPS 68
Cdd:cd03011  109 TTGVTS 114
 
Name Accession Description Interval E-value
Thioredoxin_3 pfam13192
Thioredoxin domain;
7-76 5.79e-21

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 77.64  E-value: 5.79e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544903974   7 LGTGCSGCKTTIRLIQQVADERGVAIQLEKVESLSEIMKHKVMATPAVVVDNIVVHTGGIPSRDIIESWL 76
Cdd:pfam13192  1 LGPGCPKCPQLEKAVKEAAAELGIDAEVEKVTDFPEIAKYGVMSTPALVINGKVVSSGKVPSEEEIRKLL 70
redox_disulf_2 TIGR00412
small redox-active disulfide protein 2; This small protein is found in three archaeal species ...
 4-72 2.01e-11

small redox-active disulfide protein 2; This small protein is found in three archaeal species so far (Methanococcus jannaschii, Archeoglobus fulgidus, and Methanobacterium thermoautotrophicum) as well as in Anabaena PCC7120. It is homologous to thioredoxins, glutaredoxins, and protein disulfide isomerases, and shares with them a redox-active disulfide. The redox active disulfide region CXXC motif resembles neither thioredoxin nor glutaredoxin. A closely related protein found in the same three Archaea, described by redox_disulf_1, has a glutaredoxin-like CP[YH]C sequence; it has been characterized in functional assays as redox-active but unlikely to be a thioredoxin or glutaredoxin. [Unknown function, General]


Pssm-ID: 129506  Cd Length: 76  Bit Score: 53.76  E-value: 2.01e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544903974   4 VKVLGTGCSGCKTTIRLIQQVADERGVAIQLEKVESLSEIMKHKVMATPAVVVDNIVVHTGGIPSRDII 72
Cdd:TIGR00412  3 IQIYGTGCANCQMTEKNVKKAVEELGIDAEFEKVTDMNEILEAGVTATPGVAVDGELVIMGKIPSKEEI 71
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 8-68 9.61e-04

TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c.


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 34.97  E-value: 9.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544903974   8 GTGCSGCKTTIRLIQQVADER---GVAIQLEKVESLSEIMKHK-------------------VMATPAVVV---DNIVVH 62
Cdd:cd03011   29 ATWCPVCRFTSPTVNQLAADYpvvSVALRSGDDGAVARFMQKKgygfpvindpdgvisarwgVSVTPAIVIvdpGGIVFV 108


                 ....*.
gi 544903974  63 TGGIPS 68
Cdd:cd03011  109 TTGVTS 114
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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