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Conserved domains on  [gi|1779109092|ref|WP_155162398|]
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glutaredoxin 3 [Sansalvadorimonas verongulae]

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 ...
 4-82 4.10e-36

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 TIGR02181:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 79  Bit Score: 116.59  E-value: 4.10e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1779109092  4 VVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSGRTSVPQIWIGKTHVGGCDDLYALEARGELDSLL 82
Cdd:TIGR02181  1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVDGDPALRDEMMQRSGRRTVPQIFIGDVHVGGCDDLYALDREGKLDPLL 79
 
Name Accession Description Interval E-value
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 4-82 4.10e-36

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: 116.59  E-value: 4.10e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1779109092  4 VVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSGRTSVPQIWIGKTHVGGCDDLYALEARGELDSLL 82
Cdd:TIGR02181  1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVDGDPALRDEMMQRSGRRTVPQIFIGDVHVGGCDDLYALDREGKLDPLL 79
PRK10638 PRK10638
glutaredoxin 3; Provisional
 1-82 6.07e-32

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 106.44  E-value: 6.07e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779109092  1 MQEVVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSGRTSVPQIWIGKTHVGGCDDLYALEARGELDS 80
Cdd:PRK10638   1 MANVEIYTKATCPFCHRAKALLNSKGVSFQEIPIDGDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARGGLDP 80


                 ..
gi 1779109092 81 LL 82
Cdd:PRK10638  81 LL 82
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 3-76 2.27e-28

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: 96.89  E-value: 2.27e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1779109092  3 EVVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSG-RTSVPQIWIGKTHVGGCDDLYALEARG 76
Cdd:cd03418    1 KVEIYTKPNCPYCVRAKALLDKKGVDYEEIDVDGDPALREEMINRSGgRRTVPQIFIGDVHIGGCDDLYALERKG 75
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
3-83 1.78e-24

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 87.18  E-value: 1.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779109092  3 EVVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSGRTSVPQIWIGKTHVGGCDDlyalearGELDSLL 82
Cdd:COG0695    1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDEDPEAREELRERSGRRTVPVIFIGGEHLGGFDE-------GELDALL 73


                 .
gi 1779109092 83 A 83
Cdd:COG0695   74 A 74
Glutaredoxin pfam00462
Glutaredoxin;
4-63 1.56e-18

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 71.77  E-value: 1.56e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779109092  4 VVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSGRTSVPQIWIGKTHV 63
Cdd:pfam00462  1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTVPQVFIDGEHI 60
 
Name Accession Description Interval E-value
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 4-82 4.10e-36

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: 116.59  E-value: 4.10e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1779109092  4 VVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSGRTSVPQIWIGKTHVGGCDDLYALEARGELDSLL 82
Cdd:TIGR02181  1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVDGDPALRDEMMQRSGRRTVPQIFIGDVHVGGCDDLYALDREGKLDPLL 79
PRK10638 PRK10638
glutaredoxin 3; Provisional
 1-82 6.07e-32

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 106.44  E-value: 6.07e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779109092  1 MQEVVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSGRTSVPQIWIGKTHVGGCDDLYALEARGELDS 80
Cdd:PRK10638   1 MANVEIYTKATCPFCHRAKALLNSKGVSFQEIPIDGDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARGGLDP 80


                 ..
gi 1779109092 81 LL 82
Cdd:PRK10638  81 LL 82
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 3-76 2.27e-28

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: 96.89  E-value: 2.27e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1779109092  3 EVVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSG-RTSVPQIWIGKTHVGGCDDLYALEARG 76
Cdd:cd03418    1 KVEIYTKPNCPYCVRAKALLDKKGVDYEEIDVDGDPALREEMINRSGgRRTVPQIFIGDVHIGGCDDLYALERKG 75
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 4-73 4.16e-25

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: 88.68  E-value: 4.16e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779109092  4 VVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSGRTSVPQIWIGKTHVGGCDDLYALE 73
Cdd:cd02066    2 VVVFSKSTCPYCKRAKRLLESLGIEFEEIDILEDGELREELKELSGWPTVPQIFINGEFIGGYDDLKALH 71
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
3-83 1.78e-24

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 87.18  E-value: 1.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779109092  3 EVVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSGRTSVPQIWIGKTHVGGCDDlyalearGELDSLL 82
Cdd:COG0695    1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDEDPEAREELRERSGRRTVPVIFIGGEHLGGFDE-------GELDALL 73


                 .
gi 1779109092 83 A 83
Cdd:COG0695   74 A 74
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 4-81 1.85e-21

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: 79.51  E-value: 1.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779109092  4 VVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKPD---VRKLMTERSGRTSVPQIWIGKTHVGGCDDLYALEARGELDS 80
Cdd:cd03419    2 VVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDgseIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLVK 81


                 .
gi 1779109092 81 L 81
Cdd:cd03419   82 L 82
Glutaredoxin pfam00462
Glutaredoxin;
4-63 1.56e-18

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 71.77  E-value: 1.56e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779109092  4 VVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSGRTSVPQIWIGKTHV 63
Cdd:pfam00462  1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTVPQVFIDGEHI 60
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 4-69 1.24e-12

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: 57.14  E-value: 1.24e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1779109092  4 VVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTeRSGRTSVPQIWIGKTHVGGCDDL 69
Cdd:cd03029    3 VSLFTKPGCPFCARAKAALQENGISYEEIPLGKDITGRSLRA-VTGAMTVPQVFIDGELIGGSDDL 67
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 3-65 1.99e-11

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: 53.77  E-value: 1.99e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1779109092  3 EVVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSGRTSVPQIWIGKTHVGG 65
Cdd:cd02976    1 EVTVYTKPDCPYCKATKRFLDERGIPFEEVDVDEDPEALEELKKLNGYRSVPVVVIGDEHLSG 63
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 4-73 3.34e-10

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: 50.87  E-value: 3.34e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779109092  4 VVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSGRTSVPQIWIGKTHVGGCDDLYALE 73
Cdd:cd03027    3 VTIYSRLGCEDCTAVRLFLREKGLPYVEINIDIFPERKAELEERTGSSVVPQIFFNEKLVGGLTDLKSLE 72
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 4-67 1.83e-09

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: 48.91  E-value: 1.83e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1779109092  4 VVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSGRTSVPQIWIGKTHVGGCD 67
Cdd:TIGR02196  2 VKVYTTPWCPPCVKAKEYLTSKGVAFEEIDVEKDAAAREELLKVYGQRGVPVIVIGHKIVVGFD 65
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
12-83 4.88e-09

Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440047  Cd Length: 105  Bit Score: 48.57  E-value: 4.88e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1779109092  12 CPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSGRTSVPQIWIGKTHVGGCDDLYALEARGELDSLLA 83
Cdd:COG0278    30 CGFSARAVQILNACGVDFATVNVLEDPEIRQGLKEYSNWPTIPQLYVKGEFIGGCDIIREMYESGELQKLLE 101
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 3-78 9.05e-09

Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of PICOT and GRX-PICOT-like proteins. The non-PICOT members of this family contain only the GRX-like domain, whereas PICOT contains an N-terminal TRX-like domain followed by one to three GRX-like domains. It is interesting to note that PICOT from plants contain three repeats of the GRX-like domain, metazoan proteins (except for insect) have two repeats, while fungal sequences contain only one copy of the domain. PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli. Both GRX and TRX domains of PICOT are required for its activity. Characterized non-PICOT members of this family include CXIP1, a CAX-interacting protein in Arabidopsis thaliana, and PfGLP-1, a GRX-like protein from Plasmodium falciparum.


Pssm-ID: 239326  Cd Length: 90  Bit Score: 47.49  E-value: 9.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779109092  3 EVVVF-----SSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSGRTSVPQIWIGKTHVGGCDDLYALEARGE 77
Cdd:cd03028    9 PVVLFmkgtpEEPRCGFSRKVVQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDIVKEMHESGE 88


                 .
gi 1779109092 78 L 78
Cdd:cd03028   89 L 89
grxA PRK11200
glutaredoxin 1; Provisional
 4-72 2.43e-07

glutaredoxin 1; Provisional


Pssm-ID: 183036 [Multi-domain]  Cd Length: 85  Bit Score: 43.87  E-value: 2.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779109092  4 VVVFSSALCPFCQQALGL---LKEKGVPAKIFSVD------GKPDVRKlmteRSGRT--SVPQIWIGKTHVGGCDDLYAL 72
Cdd:PRK11200   3 VVIFGRPGCPYCVRAKELaekLSEERDDFDYRYVDihaegiSKADLEK----TVGKPveTVPQIFVDQKHIGGCTDFEAY 78
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 4-82 3.98e-07

Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to plants. Multiple isoforms are found in A. thaliana and O.sativa.


Pssm-ID: 274023 [Multi-domain]  Cd Length: 99  Bit Score: 43.60  E-value: 3.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779109092  4 VVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKP---DVRKLMTERSGRTSVPQIWIGKTHVGGCDDLYALEARGELDS 80
Cdd:TIGR02189 10 VVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPagkDIENALSRLGCSPAVPAVFVGGKLVGGLENVMALHISGSLVP 89


                 ..
gi 1779109092 81 LL 82
Cdd:TIGR02189 90 ML 91
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
12-82 9.58e-07

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 42.97  E-value: 9.58e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1779109092  12 CPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSGRTSVPQIWIGKTHVGGCDDLYALEARGELDSLL 82
Cdd:PRK10824   30 CGFSAQAVQALSACGERFAYVDILQNPDIRAELPKYANWPTFPQLWVDGELVGGCDIVIEMYQRGELQQLI 100
PHA03050 PHA03050
glutaredoxin; Provisional
 3-83 1.50e-06

glutaredoxin; Provisional


Pssm-ID: 165343 [Multi-domain]  Cd Length: 108  Bit Score: 42.31  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779109092   3 EVVVFSSALCPFCQQALGLLKEKGVPAKIFSV----DGKPD--VRKLMTERSGRTSVPQIWIGKTHVGGCDDLYALEARG 76
Cdd:PHA03050   14 KVTIFVKFTCPFCRNALDILNKFSFKRGAYEIvdikEFKPEneLRDYFEQITGGRTVPRIFFGKTSIGGYSDLLEIDNMD 93


                  ....*..
gi 1779109092  77 ELDSLLA 83
Cdd:PHA03050   94 ALGDILS 100
PRK12759 PRK12759
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
 1-71 6.60e-06

bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional


Pssm-ID: 139206 [Multi-domain]  Cd Length: 410  Bit Score: 41.94  E-value: 6.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779109092   1 MQEVVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGK-------PDVRK--LMTERSGRTsVPQIWIGKTHVGGCDDLYA 71
Cdd:PRK12759    1 MVEVRIYTKTNCPFCDLAKSWFGANDIPFTQISLDDDvkraefyAEVNKniLLVEEHIRT-VPQIFVGDVHIGGYDNLMA 79
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 12-63 8.68e-04

Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 34.14  E-value: 8.68e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 1779109092 12 CPFCQQALGLLKEKGVPAKIFSVDGKPDVRK-LMTERSGRTSVPQIWIGKTHV 63
Cdd:pfam13409  2 SPFSHRVRLALEEKGLPYEIELVDLDPKDKPpELLALNPLGTVPVLVLPDGTV 54
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 4-63 6.26e-03

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: 32.16  E-value: 6.26e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779109092  4 VVVFSSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLMTERSGRTSVPQIWIGKTHV 63
Cdd:cd00570    1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEEFLALNPLGKVPVLEDGGLVL 60
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
 7-44 7.76e-03

GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP)-associated protein required for the lytic development of phage P1 and for stationary phase-induced acid tolerance of E. coli. It is implicated in survival during nutrient starvation. SspA adopts the GST fold with an N-terminal TRX-fold domain and a C-terminal alpha helical domain, but it does not bind glutathione (GSH) and lacks GST activity. SspA is highly conserved among gram-negative bacteria. Related proteins found in Neisseria (called RegF), Francisella and Vibrio regulate the expression of virulence factors necessary for pathogenesis.


Pssm-ID: 239357 [Multi-domain]  Cd Length: 73  Bit Score: 31.92  E-value: 7.76e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 1779109092  7 FSSALCPFCQQALGLLKEKGVPAKIFSVDGKPDVRKLM 44
Cdd:cd03059    4 YSGPDDVYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLA 41
GRXA TIGR02183
Glutaredoxin, GrxA family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 4-72 8.40e-03

Glutaredoxin, GrxA 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 model includes the E. coli glyutaredoxin GrxA which appears to have primary responsibility for the reduction of ribonucleotide reductase.


Pssm-ID: 131238 [Multi-domain]  Cd Length: 86  Bit Score: 32.11  E-value: 8.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779109092  4 VVVFSSALCPFCQQALGL---LKEKGVPAKIFSVD------GKPDVRKlmteRSGRT--SVPQIWIGKTHVGGCDDLYAL 72
Cdd:TIGR02183  2 VVIFGRPGCPYCVRAKQLaekLAIERADFEFRYIDihaegiSKADLEK----TVGKPveTVPQIFVDEKHVGGCTDFEQL 77
 
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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