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Conserved domains on  [gi|1631943158|ref|YP_009620825|]
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thioredoxin domain [Pseudomonas phage nickie]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 6-74 3.12e-20

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is 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 the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd03418:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 75  Bit Score: 76.47  E-value: 3.12e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631943158  6 TIYTMPNCPHCVAAKELFKRDGLQFTEI----TEFTKEELIGRVGPVRTLPQILIENgegvHHIGGFTDLQAF 74
Cdd:cd03418    3 EIYTKPNCPYCVRAKALLDKKGVDYEEIdvdgDPALREEMINRSGGRRTVPQIFIGD----VHIGGCDDLYAL 71
 
Name Accession Description Interval E-value
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 6-74 3.12e-20

Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of bacterial GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including E. coli GRX1 and GRX3, which are members of this subfamily.


Pssm-ID: 239510 [Multi-domain]  Cd Length: 75  Bit Score: 76.47  E-value: 3.12e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631943158  6 TIYTMPNCPHCVAAKELFKRDGLQFTEI----TEFTKEELIGRVGPVRTLPQILIENgegvHHIGGFTDLQAF 74
Cdd:cd03418    3 EIYTKPNCPYCVRAKALLDKKGVDYEEIdvdgDPALREEMINRSGGRRTVPQIFIGD----VHIGGCDDLYAL 71
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 6-82 1.20e-19

Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This family of glutaredoxins includes the E. coli protein GrxC (Grx3) which appears to have a secondary role in reducing ribonucleotide reductase (in the absence of GrxA) possibly indicating a role in the reduction of other protein disulfides. [Energy metabolism, Electron transport]


Pssm-ID: 274017 [Multi-domain]  Cd Length: 79  Bit Score: 74.99  E-value: 1.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631943158  6 TIYTMPNCPHCVAAKELFKRDGLQFTEI----TEFTKEELIGRVGPvRTLPQILIengeGVHHIGGFTDLQAF-RAGKLD 80
Cdd:TIGR02181  2 TIYTKPYCPYCTRAKALLSSKGVTFTEIrvdgDPALRDEMMQRSGR-RTVPQIFI----GDVHVGGCDDLYALdREGKLD 76


                 ..
gi 1631943158 81 TL 82
Cdd:TIGR02181 77 PL 78
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
6-82 2.10e-16

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 66.76  E-value: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631943158  6 TIYTMPNCPHCVAAKELFKRDGLQFTEIT----EFTKEELIGRVGpVRTLPQILIeNGEgvhHIGGFTDlqafraGKLDT 81
Cdd:COG0695    3 TLYTTPGCPYCARAKRLLDEKGIPYEEIDvdedPEAREELRERSG-RRTVPVIFI-GGE---HLGGFDE------GELDA 71


                 .
gi 1631943158 82 L 82
Cdd:COG0695   72 L 72
grxA PRK11200
glutaredoxin 1; Provisional
 6-74 7.25e-14

glutaredoxin 1; Provisional


Pssm-ID: 183036 [Multi-domain]  Cd Length: 85  Bit Score: 60.43  E-value: 7.25e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1631943158  6 TIYTMPNCPHCVAAKEL-----FKRDGLQF--TEITE--FTKEELIGRVG-PVRTLPQILIENgegvHHIGGFTDLQAF 74
Cdd:PRK11200   4 VIFGRPGCPYCVRAKELaeklsEERDDFDYryVDIHAegISKADLEKTVGkPVETVPQIFVDQ----KHIGGCTDFEAY 78
Glutaredoxin pfam00462
Glutaredoxin;
6-62 5.24e-11

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 52.51  E-value: 5.24e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631943158  6 TIYTMPNCPHCVAAKELFKRDGLQFTEI-----TEFtKEELIGRVGpVRTLPQILIeNGEGV 62
Cdd:pfam00462  2 VLYTKPTCPFCKRAKRLLKSLGVDFEEIdvdedPEI-REELKELSG-WPTVPQVFI-DGEHI 60
Uxx_star NF041212
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ...
 6-60 5.03e-09

Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like folds, a length of about 75 amino acids, and a CxxC, C/UxxT, or CxxS motif near the N-terminus end with a UXX-COOH motif. That final motif typically is missed during coding region feature prediction by genome annotation pipelines. This HMM covers proteins from several distinctive families with this feature. The seed alignment illustrates the final selenocysteine or aligned Cys or Ser residues, but the HMM also hits proteins that lack an equivalent motif at the C-terminus. This C-terminal selenocysteine-containing motif has not yet been described in the literature.


Pssm-ID: 469116 [Multi-domain]  Cd Length: 70  Bit Score: 47.84  E-value: 5.03e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 1631943158  6 TIYTMPNCPHCVAAKELFKRDGLQFTEI----TEFTKEELIGRVGPVRTLPqILIENGE 60
Cdd:NF041212   2 VIYTKPGCPYCAAAKEDLARRGIPFEEIdvskDPEALEEMLRLTGGERIVP-VIVEGGE 59
 
Name Accession Description Interval E-value
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 6-74 3.12e-20

Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of bacterial GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including E. coli GRX1 and GRX3, which are members of this subfamily.


Pssm-ID: 239510 [Multi-domain]  Cd Length: 75  Bit Score: 76.47  E-value: 3.12e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631943158  6 TIYTMPNCPHCVAAKELFKRDGLQFTEI----TEFTKEELIGRVGPVRTLPQILIENgegvHHIGGFTDLQAF 74
Cdd:cd03418    3 EIYTKPNCPYCVRAKALLDKKGVDYEEIdvdgDPALREEMINRSGGRRTVPQIFIGD----VHIGGCDDLYAL 71
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 6-82 1.20e-19

Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This family of glutaredoxins includes the E. coli protein GrxC (Grx3) which appears to have a secondary role in reducing ribonucleotide reductase (in the absence of GrxA) possibly indicating a role in the reduction of other protein disulfides. [Energy metabolism, Electron transport]


Pssm-ID: 274017 [Multi-domain]  Cd Length: 79  Bit Score: 74.99  E-value: 1.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631943158  6 TIYTMPNCPHCVAAKELFKRDGLQFTEI----TEFTKEELIGRVGPvRTLPQILIengeGVHHIGGFTDLQAF-RAGKLD 80
Cdd:TIGR02181  2 TIYTKPYCPYCTRAKALLSSKGVTFTEIrvdgDPALRDEMMQRSGR-RTVPQIFI----GDVHVGGCDDLYALdREGKLD 76


                 ..
gi 1631943158 81 TL 82
Cdd:TIGR02181 77 PL 78
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
6-82 2.10e-16

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 66.76  E-value: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631943158  6 TIYTMPNCPHCVAAKELFKRDGLQFTEIT----EFTKEELIGRVGpVRTLPQILIeNGEgvhHIGGFTDlqafraGKLDT 81
Cdd:COG0695    3 TLYTTPGCPYCARAKRLLDEKGIPYEEIDvdedPEAREELRERSG-RRTVPVIFI-GGE---HLGGFDE------GELDA 71


                 .
gi 1631943158 82 L 82
Cdd:COG0695   72 L 72
grxA PRK11200
glutaredoxin 1; Provisional
 6-74 7.25e-14

glutaredoxin 1; Provisional


Pssm-ID: 183036 [Multi-domain]  Cd Length: 85  Bit Score: 60.43  E-value: 7.25e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1631943158  6 TIYTMPNCPHCVAAKEL-----FKRDGLQF--TEITE--FTKEELIGRVG-PVRTLPQILIENgegvHHIGGFTDLQAF 74
Cdd:PRK11200   4 VIFGRPGCPYCVRAKELaeklsEERDDFDYryVDIHAegISKADLEKTVGkPVETVPQIFVDQ----KHIGGCTDFEAY 78
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 6-73 1.98e-13

Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.


Pssm-ID: 239017 [Multi-domain]  Cd Length: 72  Bit Score: 59.02  E-value: 1.98e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631943158  6 TIYTMPNCPHCVAAKELFKRDGLQFTEIT----EFTKEELIGRVGPvRTLPQILIeNGEgvhHIGGFTDLQA 73
Cdd:cd02066    3 VVFSKSTCPYCKRAKRLLESLGIEFEEIDiledGELREELKELSGW-PTVPQIFI-NGE---FIGGYDDLKA 69
PRK10638 PRK10638
glutaredoxin 3; Provisional
 2-84 3.76e-12

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 56.37  E-value: 3.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631943158  2 MNHYTIYTMPNCPHCVAAKELFKRDGLQFTEIT----EFTKEELIGRVGPVrTLPQILIENgegvHHIGGFTDLQAFRA- 76
Cdd:PRK10638   1 MANVEIYTKATCPFCHRAKALLNSKGVSFQEIPidgdAAKREEMIKRSGRT-TVPQIFIDA----QHIGGCDDLYALDAr 75


                 ....*...
gi 1631943158 77 GKLDTLRK 84
Cdd:PRK10638  76 GGLDPLLK 83
Glutaredoxin pfam00462
Glutaredoxin;
6-62 5.24e-11

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 52.51  E-value: 5.24e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631943158  6 TIYTMPNCPHCVAAKELFKRDGLQFTEI-----TEFtKEELIGRVGpVRTLPQILIeNGEGV 62
Cdd:pfam00462  2 VLYTKPTCPFCKRAKRLLKSLGVDFEEIdvdedPEI-REELKELSG-WPTVPQVFI-DGEHI 60
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 6-76 7.09e-11

Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing peroxiredoxin (PRX) and GRX domains, which is found in some pathogenic bacteria and cyanobacteria. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins. PRX-GRX hybrid proteins from Haemophilus influenza and Neisseria meningitis exhibit GSH-dependent peroxidase activity. The flow of reducing equivalents in the catalytic cycle of the hybrid protein goes from NADPH -> GSH reductase -> GSH -> GRX domain of hybrid -> PRX domain of hybrid -> peroxide substrate.


Pssm-ID: 239327 [Multi-domain]  Cd Length: 72  Bit Score: 52.52  E-value: 7.09e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631943158  6 TIYTMPNCPHCVAAKELFKRDGLQFTEITeFTKEELIGRVGPVR---TLPQILIeNGEgvhHIGGFTDLQAFRA 76
Cdd:cd03029    4 SLFTKPGCPFCARAKAALQENGISYEEIP-LGKDITGRSLRAVTgamTVPQVFI-DGE---LIGGSDDLEKYFA 72
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 6-82 1.09e-09

Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.


Pssm-ID: 239511 [Multi-domain]  Cd Length: 82  Bit Score: 49.85  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631943158  6 TIYTMPNCPHCVAAKELFKRDGLQFT--EITEFTK----EELIGRVGPVRTLPQILIeNGEgvhHIGGFTDLQA-FRAGK 78
Cdd:cd03419    3 VVFSKSYCPYCKRAKSLLKELGVKPAvvELDQHEDgseiQDYLQELTGQRTVPNVFI-GGK---FIGGCDDLMAlHKSGK 78


                 ....
gi 1631943158 79 LDTL 82
Cdd:cd03419   79 LVKL 82
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 6-70 2.17e-09

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: 48.76  E-value: 2.17e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1631943158  6 TIYTMPNCPHCVAAKELFKRDGLQFTEITEFTKEELIGRVG---PVRTLPQILIENgegvHHIGGFTD 70
Cdd:cd02976    3 TVYTKPDCPYCKATKRFLDERGIPFEEVDVDEDPEALEELKklnGYRSVPVVVIGD----EHLSGFRP 66
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 6-75 3.55e-09

Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of uncharacterized proteins containing a GRX domain and additional domains DEP and DUF547, both of which have unknown functions. GRX is a glutathione (GSH) dependent reductase containing a redox active CXXC motif in a TRX fold. It has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. By altering the redox state of target proteins, GRX is involved in many cellular functions.


Pssm-ID: 239325 [Multi-domain]  Cd Length: 73  Bit Score: 48.18  E-value: 3.55e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631943158  6 TIYTMPNCPHCVAAKELFKRDGLQFTEIT----EFTKEELIGRVGPvRTLPQILIENgegvHHIGGFTDLQAFR 75
Cdd:cd03027    4 TIYSRLGCEDCTAVRLFLREKGLPYVEINidifPERKAELEERTGS-SVVPQIFFNE----KLVGGLTDLKSLE 72
Uxx_star NF041212
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ...
 6-60 5.03e-09

Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like folds, a length of about 75 amino acids, and a CxxC, C/UxxT, or CxxS motif near the N-terminus end with a UXX-COOH motif. That final motif typically is missed during coding region feature prediction by genome annotation pipelines. This HMM covers proteins from several distinctive families with this feature. The seed alignment illustrates the final selenocysteine or aligned Cys or Ser residues, but the HMM also hits proteins that lack an equivalent motif at the C-terminus. This C-terminal selenocysteine-containing motif has not yet been described in the literature.


Pssm-ID: 469116 [Multi-domain]  Cd Length: 70  Bit Score: 47.84  E-value: 5.03e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 1631943158  6 TIYTMPNCPHCVAAKELFKRDGLQFTEI----TEFTKEELIGRVGPVRTLPqILIENGE 60
Cdd:NF041212   2 VIYTKPGCPYCAAAKEDLARRGIPFEEIdvskDPEALEEMLRLTGGERIVP-VIVEGGE 59
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 6-82 5.22e-07

Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the conserved CxxC motif and includes the Clostridium pasteurianum protein YruB which has been cloned from a rubredoxin operon. Somewhat related to NrdH, it is unknown whether this protein actually interacts with glutathione/glutathione reducatase, or, like NrdH, some other reductant system.


Pssm-ID: 274027 [Multi-domain]  Cd Length: 74  Bit Score: 42.75  E-value: 5.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631943158  6 TIYTMPNCPHCVAAKELFKRDGLQFTEIT----EFTKEELIGRVGPvRTLPQILIengegvhhigGFTDLQAFRAGKLDT 81
Cdd:TIGR02196  3 KVYTTPWCPPCVKAKEYLTSKGVAFEEIDvekdAAAREELLKVYGQ-RGVPVIVI----------GHKIVVGFDPEKLDQ 71


                 .
gi 1631943158 82 L 82
Cdd:TIGR02196 72 L 72
PRK12759 PRK12759
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
 2-79 1.23e-06

bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional


Pssm-ID: 139206 [Multi-domain]  Cd Length: 410  Bit Score: 44.25  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631943158   2 MNHYTIYTMPNCPHCVAAKELFKRDGLQFTEIT---EFTKEELIGRVGP--------VRTLPQILIengeGVHHIGGFTD 70
Cdd:PRK12759    1 MVEVRIYTKTNCPFCDLAKSWFGANDIPFTQISlddDVKRAEFYAEVNKnillveehIRTVPQIFV----GDVHIGGYDN 76


                  ....*....
gi 1631943158  71 LQAfRAGKL 79
Cdd:PRK12759   77 LMA-RAGEV 84
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 6-66 4.36e-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: 37.68  E-value: 4.36e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1631943158  6 TIYTMPNCPHCVAAKELFKR-----DGLQFTEI--TEFTKEELIGRVGPVRTLPQILIENGEGVHHIG 66
Cdd:cd01659    2 VLFYAPWCPFCQALRPVLAElallnKGVKFEAVdvDEDPALEKELKRYGVGGVPTLVVFGPGIGVKYG 69
GlrX_NrdH TIGR02194
Glutaredoxin-like protein NrdH; NrdH-redoxin is a representative of a class of small redox ...
 6-68 7.51e-04

Glutaredoxin-like protein NrdH; NrdH-redoxin is a representative of a class of small redox proteins that contain a conserved CXXC motif and are characterized by a glutaredoxin-like amino acid sequence and thioredoxin-like activity profile. Unlike other the glutaredoxins to which it is most closely related, NrdH aparrently does not interact with glutathione/glutathione reductase, but rather with thioredoxin reductase to catalyze the reduction of ribonucleotide reductase.


Pssm-ID: 131249  Cd Length: 72  Bit Score: 34.70  E-value: 7.51e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1631943158  6 TIYTMPNCPHCVAAKELFKRDGLQFTEITEFTKEELIGRVGPV--RTLPQILIengEGVHHIGGF 68
Cdd:TIGR02194  2 TVYSKNNCVQCKMTKKALEEHGIAFEEINIDEQPEAIDYVKAQgfRQVPVIVA---DGDLSWSGF 63
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
6-76 4.44e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 33.17  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631943158   6 TIYTMPNCPHCVA-AKELFKRDGLQF--------------------TEITEFTKEELIGRVGPVRTLPQILIENGEG-VH 63
Cdd:pfam13098   9 VVFTDPDCPYCKKlKKELLEDPDVTVylgpnfvfiavniwcakevaKAFTDILENKELGRKYGVRGTPTIVFFDGKGeLL 88

                          90
                  ....*....|...
gi 1631943158  64 HIGGFTDLQAFRA 76
Cdd:pfam13098  89 RLPGYVPAEEFLA 101
 
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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