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Conserved domains on  [gi|502935761|ref|WP_013170737|]
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MULTISPECIES: thioredoxin family protein [Arcanobacterium]

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;
6-76 3.75e-32

Thioredoxin domain;


:

Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 106.14  E-value: 3.75e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502935761   6 LGPGCRNCVNLEKQTRKAIADLNLDADIEHVTDYADIMSYGIMSTPGLVINGEVVVSGRVPKANEIAQLLT 76
Cdd:pfam13192  1 LGPGCPKCPQLEKAVKEAAAELGIDAEVEKVTDFPEIAKYGVMSTPALVINGKVVSSGKVPSEEEIRKLLE 71
 
Name Accession Description Interval E-value
Thioredoxin_3 pfam13192
Thioredoxin domain;
6-76 3.75e-32

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 106.14  E-value: 3.75e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502935761   6 LGPGCRNCVNLEKQTRKAIADLNLDADIEHVTDYADIMSYGIMSTPGLVINGEVVVSGRVPKANEIAQLLT 76
Cdd:pfam13192  1 LGPGCPKCPQLEKAVKEAAAELGIDAEVEKVTDFPEIAKYGVMSTPALVINGKVVSSGKVPSEEEIRKLLE 71
redox_disulf_2 TIGR00412
small redox-active disulfide protein 2; This small protein is found in three archaeal species ...
 1-75 1.75e-20

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: 76.87  E-value: 1.75e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502935761   1 MNIKILGPGCRNCVNLEKQTRKAIADLNLDADIEHVTDYADIMSYGIMSTPGLVINGEVVVSGRVPKANEIAQLL 75
Cdd:TIGR00412  1 MKIQIYGTGCANCQMTEKNVKKAVEELGIDAEFEKVTDMNEILEAGVTATPGVAVDGELVIMGKIPSKEEIKEIL 75
AhpF COG3634
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
42-76 1.70e-04

Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];


Pssm-ID: 442851 [Multi-domain]  Cd Length: 200  Bit Score: 37.42  E-value: 1.70e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 502935761  42 IMSYGIMSTPGLVINGEVVVSGRVPKANEIAQLLT 76
Cdd:COG3634  166 AEKYGVMSVPTVVLNGEVFFVGRMPEEEILEKLDT 200
AhpF_NTD_C cd03026
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) ...
 10-64 6.15e-04

TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) subfamily, C-terminal TRX-fold subdomain; AhpF is a homodimeric flavoenzyme which catalyzes the NADH-dependent reduction of the peroxiredoxin AhpC, which then reduces hydrogen peroxide and organic hydroperoxides. AhpF contains an NTD containing two contiguous TRX-fold subdomains similar to Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). It also contains a catalytic core similar to TRX reductase containing FAD and NADH binding domains with an active site disulfide. The proposed mechanism of action of AhpF is similar to a TRX/TRX reductase system. The flow of reducing equivalents goes from NADH -> catalytic core of AhpF -> NTD of AhpF -> AhpC -> peroxide substrates. The catalytic CXXC motif of the NTD of AhpF is contained in its C-terminal TRX subdomain.


Pssm-ID: 239324 [Multi-domain]  Cd Length: 89  Bit Score: 34.96  E-value: 6.15e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502935761 10 CRNCVNLeKQTRKAIADLNLDA-----DIEHVTDYADimSYGIMSTPGLVINGEVVVSGR 64
Cdd:cd03026  24 CHNCPDV-VQALNLMAVLNPNIehemiDGALFQDEVE--ERGIMSVPAIFLNGELFGFGR 80
 
Name Accession Description Interval E-value
Thioredoxin_3 pfam13192
Thioredoxin domain;
6-76 3.75e-32

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 106.14  E-value: 3.75e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502935761   6 LGPGCRNCVNLEKQTRKAIADLNLDADIEHVTDYADIMSYGIMSTPGLVINGEVVVSGRVPKANEIAQLLT 76
Cdd:pfam13192  1 LGPGCPKCPQLEKAVKEAAAELGIDAEVEKVTDFPEIAKYGVMSTPALVINGKVVSSGKVPSEEEIRKLLE 71
redox_disulf_2 TIGR00412
small redox-active disulfide protein 2; This small protein is found in three archaeal species ...
 1-75 1.75e-20

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: 76.87  E-value: 1.75e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502935761   1 MNIKILGPGCRNCVNLEKQTRKAIADLNLDADIEHVTDYADIMSYGIMSTPGLVINGEVVVSGRVPKANEIAQLL 75
Cdd:TIGR00412  1 MKIQIYGTGCANCQMTEKNVKKAVEELGIDAEFEKVTDMNEILEAGVTATPGVAVDGELVIMGKIPSKEEIKEIL 75
AhpF COG3634
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
42-76 1.70e-04

Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];


Pssm-ID: 442851 [Multi-domain]  Cd Length: 200  Bit Score: 37.42  E-value: 1.70e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 502935761  42 IMSYGIMSTPGLVINGEVVVSGRVPKANEIAQLLT 76
Cdd:COG3634  166 AEKYGVMSVPTVVLNGEVFFVGRMPEEEILEKLDT 200
AhpF_NTD_C cd03026
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) ...
 10-64 6.15e-04

TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) subfamily, C-terminal TRX-fold subdomain; AhpF is a homodimeric flavoenzyme which catalyzes the NADH-dependent reduction of the peroxiredoxin AhpC, which then reduces hydrogen peroxide and organic hydroperoxides. AhpF contains an NTD containing two contiguous TRX-fold subdomains similar to Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). It also contains a catalytic core similar to TRX reductase containing FAD and NADH binding domains with an active site disulfide. The proposed mechanism of action of AhpF is similar to a TRX/TRX reductase system. The flow of reducing equivalents goes from NADH -> catalytic core of AhpF -> NTD of AhpF -> AhpC -> peroxide substrates. The catalytic CXXC motif of the NTD of AhpF is contained in its C-terminal TRX subdomain.


Pssm-ID: 239324 [Multi-domain]  Cd Length: 89  Bit Score: 34.96  E-value: 6.15e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502935761 10 CRNCVNLeKQTRKAIADLNLDA-----DIEHVTDYADimSYGIMSTPGLVINGEVVVSGR 64
Cdd:cd03026  24 CHNCPDV-VQALNLMAVLNPNIehemiDGALFQDEVE--ERGIMSVPAIFLNGELFGFGR 80
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 17-75 7.46e-04

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 35.74  E-value: 7.46e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502935761  17 EKQTRKAIADLNLDADIEhvTDYADIMSYGIMSTPGLVINGEvVVSGRVPkANEIAQLL 75
Cdd:COG1651   94 AAKFDACLNSGAVAAKVE--ADTALAQALGVTGTPTFVVNGK-LVSGAVP-YEELEAAL 148
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 22-75 1.54e-03

Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442047 [Multi-domain]  Cd Length: 205  Bit Score: 34.86  E-value: 1.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 502935761  22 KAIADLNLDADIEHV-TDYADIMSYGIMSTPGLVINGEVVVSGRVPKAnEIAQLL 75
Cdd:COG2761  147 EFRADLESDEAAAAVrADEAEARELGVTGVPTFVFDGKYAVSGAQPYE-VFEQAL 200
TRX_GRX_like cd02973
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ...
 42-64 1.76e-03

Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins that show similarity to both TRX and GRX, including the C-terminal TRX-fold subdomain of Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). All members contain a redox-active CXXC motif and may function as PDOs. The archaeal proteins Mj0307 and Mt807 show structures more similar to GRX, but activities more similar to TRX. Some members of the family are similar to PfPDO in that they contain a second CXXC motif located in a second TRX-fold subdomain at the N-terminus; the superimposable N- and C-terminal TRX subdomains form a compact structure. PfPDO is postulated to be the archaeal counterpart of bacterial DsbA and eukaryotic protein disulfide isomerase (PDI). The C-terminal CXXC motif of PfPDO is required for its oxidase, reductase and isomerase activities. Also included in the family is the C-terminal TRX-fold subdomain of the N-terminal domain (NTD) of bacterial AhpF, which has a similar fold as PfPDO with two TRX-fold subdomains but without the second CXXC motif.


Pssm-ID: 239271 [Multi-domain]  Cd Length: 67  Bit Score: 33.31  E-value: 1.76e-03
                        10        20
                ....*....|....*....|...
gi 502935761 42 IMSYGIMSTPGLVINGEVVVSGR 64
Cdd:cd02973  45 ADEYGVMSVPAIVINGKVEFVGR 67
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 7-75 3.76e-03

NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein.


Pssm-ID: 239274 [Multi-domain]  Cd Length: 73  Bit Score: 32.58  E-value: 3.76e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502935761  7 GPGCRNCvnleKQTRKAIADLNLD---ADIEHVTDYADIMS--YGIMSTPGLVINGEVVVSgrvPKANEIAQLL 75
Cdd:cd02976   7 KPDCPYC----KATKRFLDERGIPfeeVDVDEDPEALEELKklNGYRSVPVVVIGDEHLSG---FRPDKLRALL 73
 
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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