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Conserved domains on  [gi|390424086|gb|AFL78592|]
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Glutaredoxin [Alistipes finegoldii DSM 17242]

Protein Classification

TlpA family protein disulfide reductase( domain architecture ID 10001660)

TlpA family protein disulfide reductase such as Bradyrhizobium japonicum thiol:disulfide interchange protein TlpA, an unusual thioredoxin which has been implicated in the biogenesis of cytochrome aa3 and also characterized as a reductant for the copper metallochaperone ScoI, and similar to ResA and DsbE, which are essential proteins in cytochrome c maturation

CATH:  3.40.30.10
Gene Ontology:  GO:0016491
PubMed:  11531338|15667290

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 12-86 2.20e-06

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 42.37  E-value: 2.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390424086  12 CPFCRKALRYIEEAKAAHPELQPVAIEMIEESEQ-------------------SDLADTFDYYYVPTFYV---DG--VKV 67
Cdd:COG0526   40 CPPCRAEMPVLKELAEEYGGVVFVGVDVDENPEAvkaflkelglpypvlldpdGELAKAYGVRGIPTTVLidkDGkiVAR 119

                         90
                 ....*....|....*....
gi 390424086  68 HEGGIYAEEVEKILRSALE 86
Cdd:COG0526  120 HVGPLSPEELEEALEKLLA 138
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 12-86 2.20e-06

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 42.37  E-value: 2.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390424086  12 CPFCRKALRYIEEAKAAHPELQPVAIEMIEESEQ-------------------SDLADTFDYYYVPTFYV---DG--VKV 67
Cdd:COG0526   40 CPPCRAEMPVLKELAEEYGGVVFVGVDVDENPEAvkaflkelglpypvlldpdGELAKAYGVRGIPTTVLidkDGkiVAR 119

                         90
                 ....*....|....*....
gi 390424086  68 HEGGIYAEEVEKILRSALE 86
Cdd:COG0526  120 HVGPLSPEELEEALEKLLA 138
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 4-69 1.26e-05

Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 39.22  E-value: 1.26e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 390424086  4 VKLFYLKNCPFCRKALRYIEEAKAAHPELQPVAIEMIEESEQSDLADTFDYYYVPTFYVDGVKVHE 69
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDPALEKELKRYGVGGVPTLVVFGPGIGV 66
Thioredoxin_3 pfam13192
Thioredoxin domain;
11-81 4.46e-03

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 32.57  E-value: 4.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 390424086  11 NCPFCRKALRYIEEAkAAHPElqpVAIEMIEESEQSDLADtFDYYYVPTFYVDGVKVHEGGI-YAEEVEKIL 81
Cdd:pfam13192  4 GCPKCPQLEKAVKEA-AAELG---IDAEVEKVTDFPEIAK-YGVMSTPALVINGKVVSSGKVpSEEEIRKLL 70
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 12-86 2.20e-06

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 42.37  E-value: 2.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390424086  12 CPFCRKALRYIEEAKAAHPELQPVAIEMIEESEQ-------------------SDLADTFDYYYVPTFYV---DG--VKV 67
Cdd:COG0526   40 CPPCRAEMPVLKELAEEYGGVVFVGVDVDENPEAvkaflkelglpypvlldpdGELAKAYGVRGIPTTVLidkDGkiVAR 119

                         90
                 ....*....|....*....
gi 390424086  68 HEGGIYAEEVEKILRSALE 86
Cdd:COG0526  120 HVGPLSPEELEEALEKLLA 138
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 4-69 1.26e-05

Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 39.22  E-value: 1.26e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 390424086  4 VKLFYLKNCPFCRKALRYIEEAKAAHPELQPVAIEMIEESEQSDLADTFDYYYVPTFYVDGVKVHE 69
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDPALEKELKRYGVGGVPTLVVFGPGIGV 66
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 7-81 1.90e-05

TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 39.08  E-value: 1.90e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 390424086  7 FYLKNCPFCRKALRYIEEAKAAHPElqpVAIEMIEESEQSDLADTFDYYYVPTF--YVDGVKVHE--GGIYAEEVEKIL 81
Cdd:cd02947  17 FWAPWCGPCKAIAPVLEELAEEYPK---VKFVKVDVDENPELAEEYGVRSIPTFlfFKNGKEVDRvvGADPKEELEEFL 92
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
3-82 5.76e-05

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 37.48  E-value: 5.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390424086  3 PVKLFYLKNCPFCRKALRYIEEAKaahpelqpVAIEMIEESEQSDLADTF----DYYYVPTFYVDGVKVheGGIYAEEVE 78
Cdd:COG0695   1 KVTLYTTPGCPYCARAKRLLDEKG--------IPYEEIDVDEDPEAREELrersGRRTVPVIFIGGEHL--GGFDEGELD 70


                ....
gi 390424086 79 KILR 82
Cdd:COG0695  71 ALLA 74
AhpF COG3634
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
12-82 2.72e-04

Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];


Pssm-ID: 442851 [Multi-domain]  Cd Length: 200  Bit Score: 37.42  E-value: 2.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 390424086  12 CPFCRKALRyieeakAAHPelqpVAI-------EMIEESEQSDLADTFDYYYVPTFYVDGVKVHEGGIYAEE-VEKILR 82
Cdd:COG3634  132 CPNCPDVVQ------ALNL----MAVlnpnithEMIDGAEFPDEAEKYGVMSVPTVVLNGEVFFVGRMPEEEiLEKLDT 200
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 4-69 3.55e-04

Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK subfamily, a member of the DsbA family). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxin 2 and stringent starvation protein A.


Pssm-ID: 238319 [Multi-domain]  Cd Length: 71  Bit Score: 35.24  E-value: 3.55e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 390424086  4 VKLFYLKNCPFCRKALRYIEEAKAAHpELQPVAiemIEESEQSDLADTFDYYYVPTFYVDGVKVHE 69
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPY-ELVPVD---LGEGEQEEFLALNPLGKVPVLEDGGLVLTE 62
TRX_GRX_like cd02973
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ...
 4-70 3.73e-04

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: 35.24  E-value: 3.73e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 390424086  4 VKLFYLKNCPFCRKALRYIEEAKAAHPElqpVAIEMIEESEQSDLADTFDYYYVPTFYVDGVKVHEG 70
Cdd:cd02973   3 IEVFVSPTCPYCPDAVQAANRIAALNPN---ISAEMIDAAEFPDLADEYGVMSVPAIVINGKVEFVG 66
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
2-86 8.37e-04

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 35.61  E-value: 8.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390424086   2 KPVKL-FYLKNCPFCRKALRYIEEAKAAHPEL--QPVAI---------EMIEE---------SEQSDLADTFDYYYVPTF 60
Cdd:COG1225   22 KPVVLyFYATWCPGCTAELPELRDLYEEFKDKgvEVLGVssdsdeahkKFAEKyglpfpllsDPDGEVAKAYGVRGTPTT 101

                         90       100       110
                 ....*....|....*....|....*....|..
gi 390424086  61 YV---DG--VKVHEGGI-YAEEVEKILRSALE 86
Cdd:COG1225  102 FLidpDGkiRYVWVGPVdPRPHLEEVLEALLA 133
Thioredoxin_3 pfam13192
Thioredoxin domain;
11-81 4.46e-03

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 32.57  E-value: 4.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 390424086  11 NCPFCRKALRYIEEAkAAHPElqpVAIEMIEESEQSDLADtFDYYYVPTFYVDGVKVHEGGI-YAEEVEKIL 81
Cdd:pfam13192  4 GCPKCPQLEKAVKEA-AAELG---IDAEVEKVTDFPEIAK-YGVMSTPALVINGKVVSSGKVpSEEEIRKLL 70
Glutaredoxin pfam00462
Glutaredoxin;
4-67 5.15e-03

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 32.09  E-value: 5.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 390424086   4 VKLFYLKNCPFCRKALRYIEEAKAAHPElqpVAIEMIEEsEQSDLADTFDYYYVPTFYVDGVKV 67
Cdd:pfam00462  1 VVLYTKPTCPFCKRAKRLLKSLGVDFEE---IDVDEDPE-IREELKELSGWPTVPQVFIDGEHI 60
 
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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