NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2420736723|gb|KAJ2259226|]
View 

hypothetical protein GGI13_000009 [Coemansia sp. RSA 455]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 308-393 2.47e-31

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: 114.17  E-value: 2.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723 308 RVMVFSKTYCPYSSMAKRLLAKLkeqrGLQFAVLEADKEADPMEVKAALGKISGRLTFPNIFVDGRSIGGSDDLQAQHTS 387
Cdd:cd03419     1 PVVVFSKSYCPYCKRAKSLLKEL----GVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKS 76


                  ....*.
gi 2420736723 388 GELVKL 393
Cdd:cd03419    77 GKLVKL 82
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 82-167 1.07e-24

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: 96.45  E-value: 1.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723  82 RIVVFSKTTCPHCKATKALLEryheQYGLGYMVVEADLRKDMDNVKHALASLCSHSTFPSVFVDAKCIGGNDDMYAKHAN 161
Cdd:cd03419     1 PVVVFSKSYCPYCKRAKSLLK----ELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKS 76


                  ....*.
gi 2420736723 162 GNLQQI 167
Cdd:cd03419    77 GKLVKL 82
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 226-283 2.99e-09

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 cd03419:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 82  Bit Score: 53.31  E-value: 2.99e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2420736723 226 GFAYRFVDLDERADHLQLAEVVREISGQPGLPVIFVGGSEVGGYKGLQSLHASGELSK 283
Cdd:cd03419    24 GVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLVK 81
 
Name Accession Description Interval E-value
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 308-393 2.47e-31

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: 114.17  E-value: 2.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723 308 RVMVFSKTYCPYSSMAKRLLAKLkeqrGLQFAVLEADKEADPMEVKAALGKISGRLTFPNIFVDGRSIGGSDDLQAQHTS 387
Cdd:cd03419     1 PVVVFSKSYCPYCKRAKSLLKEL----GVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKS 76


                  ....*.
gi 2420736723 388 GELVKL 393
Cdd:cd03419    77 GKLVKL 82
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
 309-394 1.51e-26

Glutaredoxin; 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 represents eukaryotic glutaredoxins and includes sequences from fungi, plants and metazoans as well as viruses.


Pssm-ID: 274016 [Multi-domain]  Cd Length: 83  Bit Score: 101.55  E-value: 1.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723 309 VMVFSKTYCPYSSMAKRLLAKLKEQrglQFAVLEADKEADPMEVKAALGKISGRLTFPNIFVDGRSIGGSDDLQAQHTSG 388
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLNVK---PYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNG 77


                  ....*.
gi 2420736723 389 ELVKLL 394
Cdd:TIGR02180  78 KLAELL 83
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 82-167 1.07e-24

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: 96.45  E-value: 1.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723  82 RIVVFSKTTCPHCKATKALLEryheQYGLGYMVVEADLRKDMDNVKHALASLCSHSTFPSVFVDAKCIGGNDDMYAKHAN 161
Cdd:cd03419     1 PVVVFSKSYCPYCKRAKSLLK----ELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKS 76


                  ....*.
gi 2420736723 162 GNLQQI 167
Cdd:cd03419    77 GKLVKL 82
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
 83-168 1.41e-20

Glutaredoxin; 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 represents eukaryotic glutaredoxins and includes sequences from fungi, plants and metazoans as well as viruses.


Pssm-ID: 274016 [Multi-domain]  Cd Length: 83  Bit Score: 85.37  E-value: 1.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723  83 IVVFSKTTCPHCKATKALLERYheqYGLGYMVVEADLRKDMDNVKHALASLCSHSTFPSVFVDAKCIGGNDDMYAKHANG 162
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKL---NVKPYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNG 77


                  ....*.
gi 2420736723 163 NLQQIL 168
Cdd:TIGR02180  78 KLAELL 83
Glutaredoxin pfam00462
Glutaredoxin;
309-375 7.59e-16

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 71.38  E-value: 7.59e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2420736723 309 VMVFSKTYCPYSSMAKRLLaklkEQRGLQFAVLEADKEAdpmEVKAALGKISGRLTFPNIFVDGRSI 375
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLL----KSLGVDFEEIDVDEDP---EIREELKELSGWPTVPQVFIDGEHI 60
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
308-395 1.80e-12

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 62.14  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723 308 RVMVFSKTYCPYSSMAKRLLaklkEQRGLQFAVLEADKeaDPmEVKAALGKISGRLTFPNIFVDGRSIGGSDDlqaqhts 387
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLL----DEKGIPYEEIDVDE--DP-EAREELRERSGRRTVPVIFIGGEHLGGFDE------- 66


                  ....*...
gi 2420736723 388 GELVKLLQ 395
Cdd:COG0695    67 GELDALLA 74
PRK10638 PRK10638
glutaredoxin 3; Provisional
 309-395 5.85e-12

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 60.99  E-value: 5.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723 309 VMVFSKTYCPYSSMAKRLLaklkEQRGLQFAVLEADKEADPMEVkaaLGKISGRLTFPNIFVDGRSIGGSDDLQAQHTSG 388
Cdd:PRK10638    4 VEIYTKATCPFCHRAKALL----NSKGVSFQEIPIDGDAAKREE---MIKRSGRTTVPQIFIDAQHIGGCDDLYALDARG 76


                  ....*..
gi 2420736723 389 ELVKLLQ 395
Cdd:PRK10638   77 GLDPLLK 83
Glutaredoxin pfam00462
Glutaredoxin;
83-149 5.22e-10

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 54.82  E-value: 5.22e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2420736723  83 IVVFSKTTCPHCKATKALLERyheqYGLGYMVVEADlrkDMDNVKHALASLCSHSTFPSVFVDAKCI 149
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKS----LGVDFEEIDVD---EDPEIREELKELSGWPTVPQVFIDGEHI 60
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 226-283 2.99e-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: 53.31  E-value: 2.99e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2420736723 226 GFAYRFVDLDERADHLQLAEVVREISGQPGLPVIFVGGSEVGGYKGLQSLHASGELSK 283
Cdd:cd03419    24 GVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLVK 81
PRK10638 PRK10638
glutaredoxin 3; Provisional
 83-168 4.30e-09

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 52.90  E-value: 4.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723  83 IVVFSKTTCPHCKATKALLEryheQYGLGY--MVVEADLRKDMDNVKHAlaslcSHSTFPSVFVDAKCIGGNDDMYAKHA 160
Cdd:PRK10638    4 VEIYTKATCPFCHRAKALLN----SKGVSFqeIPIDGDAAKREEMIKRS-----GRTTVPQIFIDAQHIGGCDDLYALDA 74


                  ....*...
gi 2420736723 161 NGNLQQIL 168
Cdd:PRK10638   75 RGGLDPLL 82
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
82-154 4.31e-08

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 49.81  E-value: 4.31e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2420736723  82 RIVVFSKTTCPHCKATKALLERyheqYGLGYmvVEADLRKDMDNVKhALASLCSHSTFPSVFVDAKCIGGNDD 154
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDE----KGIPY--EEIDVDEDPEARE-ELRERSGRRTVPVIFIGGEHLGGFDE 66
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
223-269 2.25e-06

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 44.80  E-value: 2.25e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2420736723 223 ERTGFAYRFVDLDERADHlqlAEVVREISGQPGLPVIFVGGSEVGGY 269
Cdd:COG0695    21 DEKGIPYEEIDVDEDPEA---REELRERSGRRTVPVIFIGGEHLGGF 64
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 232-285 3.50e-06

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: 45.14  E-value: 3.50e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2420736723 232 VDLDERADHLQLAEVVREISGQPGLPVIFVGGSEVGGYKGLQSLHASGELSKRL 285
Cdd:TIGR02189  38 HEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMALHISGSLVPML 91
Glutaredoxin pfam00462
Glutaredoxin;
223-266 1.12e-04

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 39.80  E-value: 1.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2420736723 223 ERTGFAYRFVDLDEradHLQLAEVVREISGQPGLPVIFVGGSEV 266
Cdd:pfam00462  20 KSLGVDFEEIDVDE---DPEIREELKELSGWPTVPQVFIDGEHI 60
 
Name Accession Description Interval E-value
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 308-393 2.47e-31

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: 114.17  E-value: 2.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723 308 RVMVFSKTYCPYSSMAKRLLAKLkeqrGLQFAVLEADKEADPMEVKAALGKISGRLTFPNIFVDGRSIGGSDDLQAQHTS 387
Cdd:cd03419     1 PVVVFSKSYCPYCKRAKSLLKEL----GVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKS 76


                  ....*.
gi 2420736723 388 GELVKL 393
Cdd:cd03419    77 GKLVKL 82
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
 309-394 1.51e-26

Glutaredoxin; 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 represents eukaryotic glutaredoxins and includes sequences from fungi, plants and metazoans as well as viruses.


Pssm-ID: 274016 [Multi-domain]  Cd Length: 83  Bit Score: 101.55  E-value: 1.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723 309 VMVFSKTYCPYSSMAKRLLAKLKEQrglQFAVLEADKEADPMEVKAALGKISGRLTFPNIFVDGRSIGGSDDLQAQHTSG 388
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLNVK---PYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNG 77


                  ....*.
gi 2420736723 389 ELVKLL 394
Cdd:TIGR02180  78 KLAELL 83
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 82-167 1.07e-24

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: 96.45  E-value: 1.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723  82 RIVVFSKTTCPHCKATKALLEryheQYGLGYMVVEADLRKDMDNVKHALASLCSHSTFPSVFVDAKCIGGNDDMYAKHAN 161
Cdd:cd03419     1 PVVVFSKSYCPYCKRAKSLLK----ELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKS 76


                  ....*.
gi 2420736723 162 GNLQQI 167
Cdd:cd03419    77 GKLVKL 82
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 308-385 7.68e-21

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: 85.60  E-value: 7.68e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2420736723 308 RVMVFSKTYCPYSSMAKRLLAKLKeqrglqFAVLEADKEADPmEVKAALGKISGRLTFPNIFVDGRSIGGSDDLQAQH 385
Cdd:cd02066     1 KVVVFSKSTCPYCKRAKRLLESLG------IEFEEIDILEDG-ELREELKELSGWPTVPQIFINGEFIGGYDDLKALH 71
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
 83-168 1.41e-20

Glutaredoxin; 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 represents eukaryotic glutaredoxins and includes sequences from fungi, plants and metazoans as well as viruses.


Pssm-ID: 274016 [Multi-domain]  Cd Length: 83  Bit Score: 85.37  E-value: 1.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723  83 IVVFSKTTCPHCKATKALLERYheqYGLGYMVVEADLRKDMDNVKHALASLCSHSTFPSVFVDAKCIGGNDDMYAKHANG 162
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKL---NVKPYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNG 77


                  ....*.
gi 2420736723 163 NLQQIL 168
Cdd:TIGR02180  78 KLAELL 83
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 300-398 1.19e-16

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: 74.80  E-value: 1.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723 300 VRQLIQRNRVMVFSKTYCPYSSMAKRLLAKLkeqrGLQFAVLEADKEADPMEVKAALGKISGRLTFPNIFVDGRSIGGSD 379
Cdd:TIGR02189   1 VRRMVSEKAVVIFSRSSCCMCHVVKRLLLTL----GVNPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLE 76

                          90
                  ....*....|....*....
gi 2420736723 380 DLQAQHTSGELVKLLQKAG 398
Cdd:TIGR02189  77 NVMALHISGSLVPMLKQAG 95
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 309-394 1.55e-16

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: 73.83  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723 309 VMVFSKTYCPYSSMAKRLLaklkEQRGLQFAVLEADkeADPmEVKAALGKISGRLTFPNIFVDGRSIGGSDDLQAQHTSG 388
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALL----SSKGVTFTEIRVD--GDP-ALRDEMMQRSGRRTVPQIFIGDVHVGGCDDLYALDREG 73


                  ....*.
gi 2420736723 389 ELVKLL 394
Cdd:TIGR02181  74 KLDPLL 79
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 82-157 5.21e-16

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: 72.11  E-value: 5.21e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2420736723  82 RIVVFSKTTCPHCKATKALLEryheqyGLGYMVVEADLRKDMDNVKhALASLCSHSTFPSVFVDAKCIGGNDDMYA 157
Cdd:cd02066     1 KVVVFSKSTCPYCKRAKRLLE------SLGIEFEEIDILEDGELRE-ELKELSGWPTVPQIFINGEFIGGYDDLKA 69
Glutaredoxin pfam00462
Glutaredoxin;
309-375 7.59e-16

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 71.38  E-value: 7.59e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2420736723 309 VMVFSKTYCPYSSMAKRLLaklkEQRGLQFAVLEADKEAdpmEVKAALGKISGRLTFPNIFVDGRSI 375
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLL----KSLGVDFEEIDVDEDP---EIREELKELSGWPTVPQVFIDGEHI 60
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 309-383 7.54e-14

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: 66.07  E-value: 7.54e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2420736723 309 VMVFSKTYCPYSSMAKRLLaklkEQRGLQFAvlEADKEADPmEVKAALGKISG-RLTFPNIFVDGRSIGGSDDLQA 383
Cdd:cd03418     2 VEIYTKPNCPYCVRAKALL----DKKGVDYE--EIDVDGDP-ALREEMINRSGgRRTVPQIFIGDVHIGGCDDLYA 70
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 74-174 5.22e-13

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: 64.78  E-value: 5.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723  74 VQSVLRKHRIVVFSKTTCPHCKATKALLeryheqYGLGY--MVVEADLRKDMDNVKHALASLCSHSTFPSVFVDAKCIGG 151
Cdd:TIGR02189   1 VRRMVSEKAVVIFSRSSCCMCHVVKRLL------LTLGVnpAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGG 74

                          90       100
                  ....*....|....*....|...
gi 2420736723 152 NDDMYAKHANGNLQQILVDAGLL 174
Cdd:TIGR02189  75 LENVMALHISGSLVPMLKQAGAL 97
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
308-395 1.80e-12

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 62.14  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723 308 RVMVFSKTYCPYSSMAKRLLaklkEQRGLQFAVLEADKeaDPmEVKAALGKISGRLTFPNIFVDGRSIGGSDDlqaqhts 387
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLL----DEKGIPYEEIDVDE--DP-EAREELRERSGRRTVPVIFIGGEHLGGFDE------- 66


                  ....*...
gi 2420736723 388 GELVKLLQ 395
Cdd:COG0695    67 GELDALLA 74
PRK10638 PRK10638
glutaredoxin 3; Provisional
 309-395 5.85e-12

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 60.99  E-value: 5.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723 309 VMVFSKTYCPYSSMAKRLLaklkEQRGLQFAVLEADKEADPMEVkaaLGKISGRLTFPNIFVDGRSIGGSDDLQAQHTSG 388
Cdd:PRK10638    4 VEIYTKATCPFCHRAKALL----NSKGVSFQEIPIDGDAAKREE---MIKRSGRTTVPQIFIDAQHIGGCDDLYALDARG 76


                  ....*..
gi 2420736723 389 ELVKLLQ 395
Cdd:PRK10638   77 GLDPLLK 83
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
293-399 9.92e-12

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


Pssm-ID: 440047  Cd Length: 105  Bit Score: 61.29  E-value: 9.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723 293 QSAAEQKVRQLIQRNRVMVFSK-T----YCPYSSMAKRLLAKLkeqrGLQFA---VLEADkeadpmEVKAALGKISGRLT 364
Cdd:COG0278     1 MMDVQERIKQQIKSNPVVLFMKgTpqfpQCGFSARAVQILNAC----GVDFAtvnVLEDP------EIRQGLKEYSNWPT 70

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2420736723 365 FPNIFVDGRSIGGSDDLQAQHTSGELVKLLQKAGL 399
Cdd:COG0278    71 IPQLYVKGEFIGGCDIIREMYESGELQKLLEEAGA 105
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 83-168 2.86e-11

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: 59.20  E-value: 2.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723  83 IVVFSKTTCPHCKATKALLEryheQYGLGYMVVEAD----LRKDMdnvkhalASLCSHSTFPSVFVDAKCIGGNDDMYAK 158
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALLS----SKGVTFTEIRVDgdpaLRDEM-------MQRSGRRTVPQIFIGDVHVGGCDDLYAL 69

                          90
                  ....*....|
gi 2420736723 159 HANGNLQQIL 168
Cdd:TIGR02181  70 DREGKLDPLL 79
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 300-391 3.18e-11

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: 59.04  E-value: 3.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723 300 VRQLIQRNRVMVFSK-----TYCPYSSMAKRLLaklkEQRGLQFA---VLEADkeadpmEVKAALGKISGRLTFPNIFVD 371
Cdd:cd03028     1 IKKLIKENPVVLFMKgtpeePRCGFSRKVVQIL----NQLGVDFGtfdILEDE------EVRQGLKEYSNWPTFPQLYVN 70

                          90       100
                  ....*....|....*....|
gi 2420736723 372 GRSIGGSDDLQAQHTSGELV 391
Cdd:cd03028    71 GELVGGCDIVKEMHESGELQ 90
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 83-162 9.59e-11

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: 57.21  E-value: 9.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723  83 IVVFSKTTCPHCKATKALLERYheqyGLGYMVVEAD----LRKDMDNVKHALaslcshSTFPSVFVDAKCIGGNDDMYAK 158
Cdd:cd03418     2 VEIYTKPNCPYCVRAKALLDKK----GVDYEEIDVDgdpaLREEMINRSGGR------RTVPQIFIGDVHIGGCDDLYAL 71


                  ....
gi 2420736723 159 HANG 162
Cdd:cd03418    72 ERKG 75
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 309-383 2.04e-10

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: 56.37  E-value: 2.04e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2420736723 309 VMVFSKTYCPYSSMAKRLLAklkeQRGLQFAVLEADKEADPMEVKAalgkISGRLTFPNIFVDGRSIGGSDDLQA 383
Cdd:cd03029     3 VSLFTKPGCPFCARAKAALQ----ENGISYEEIPLGKDITGRSLRA----VTGAMTVPQVFIDGELIGGSDDLEK 69
Glutaredoxin pfam00462
Glutaredoxin;
83-149 5.22e-10

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 54.82  E-value: 5.22e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2420736723  83 IVVFSKTTCPHCKATKALLERyheqYGLGYMVVEADlrkDMDNVKHALASLCSHSTFPSVFVDAKCI 149
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKS----LGVDFEEIDVD---EDPEIREELKELSGWPTVPQVFIDGEHI 60
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 226-283 2.99e-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: 53.31  E-value: 2.99e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2420736723 226 GFAYRFVDLDERADHLQLAEVVREISGQPGLPVIFVGGSEVGGYKGLQSLHASGELSK 283
Cdd:cd03419    24 GVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLVK 81
PRK10638 PRK10638
glutaredoxin 3; Provisional
 83-168 4.30e-09

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 52.90  E-value: 4.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723  83 IVVFSKTTCPHCKATKALLEryheQYGLGY--MVVEADLRKDMDNVKHAlaslcSHSTFPSVFVDAKCIGGNDDMYAKHA 160
Cdd:PRK10638    4 VEIYTKATCPFCHRAKALLN----SKGVSFqeIPIDGDAAKREEMIKRS-----GRTTVPQIFIDAQHIGGCDDLYALDA 74


                  ....*...
gi 2420736723 161 NGNLQQIL 168
Cdd:PRK10638   75 RGGLDPLL 82
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
82-154 4.31e-08

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 49.81  E-value: 4.31e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2420736723  82 RIVVFSKTTCPHCKATKALLERyheqYGLGYmvVEADLRKDMDNVKhALASLCSHSTFPSVFVDAKCIGGNDD 154
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDE----KGIPY--EEIDVDEDPEARE-ELRERSGRRTVPVIFIGGEHLGGFDE 66
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 83-155 4.65e-08

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: 49.82  E-value: 4.65e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2420736723  83 IVVFSKTTCPHCKATKALLERyheqYGLGYmvVEADLRKDMDNVkhALASLCSHSTFPSVFVDAKCIGGNDDM 155
Cdd:cd03029     3 VSLFTKPGCPFCARAKAALQE----NGISY--EEIPLGKDITGR--SLRAVTGAMTVPQVFIDGELIGGSDDL 67
grxA PRK11200
glutaredoxin 1; Provisional
 309-383 1.56e-06

glutaredoxin 1; Provisional


Pssm-ID: 183036 [Multi-domain]  Cd Length: 85  Bit Score: 45.79  E-value: 1.56e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2420736723 309 VMVFSKTYCPYSSMAKRLLAKLKEQR-GLQFAVLeaDKEADPMEvKAALGKISGR--LTFPNIFVDGRSIGGSDDLQA 383
Cdd:PRK11200    3 VVIFGRPGCPYCVRAKELAEKLSEERdDFDYRYV--DIHAEGIS-KADLEKTVGKpvETVPQIFVDQKHIGGCTDFEA 77
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
223-269 2.25e-06

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 44.80  E-value: 2.25e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2420736723 223 ERTGFAYRFVDLDERADHlqlAEVVREISGQPGLPVIFVGGSEVGGY 269
Cdd:COG0695    21 DEKGIPYEEIDVDEDPEA---REELRERSGRRTVPVIFIGGEHLGGF 64
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 82-155 2.76e-06

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: 44.71  E-value: 2.76e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2420736723  82 RIVVFSKTTCPHCKATKALLERyheqygLGYMVVEADLRKdMDNVKHALASLCSHSTFPSVFVDAKCIGGNDDM 155
Cdd:cd03027     2 RVTIYSRLGCEDCTAVRLFLRE------KGLPYVEINIDI-FPERKAELEERTGSSVVPQIFFNEKLVGGLTDL 68
PHA03050 PHA03050
glutaredoxin; Provisional
 296-400 3.01e-06

glutaredoxin; Provisional


Pssm-ID: 165343 [Multi-domain]  Cd Length: 108  Bit Score: 45.78  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723 296 AEQKVRQLIQRNRVMVFSKTYCPYSSMAKRLLAKLKEQRGlQFAVLEADKEADPMEVKAALGKISGRLTFPNIFVDGRSI 375
Cdd:PHA03050    2 AEEFVQQRLANNKVTIFVKFTCPFCRNALDILNKFSFKRG-AYEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSI 80

                          90       100
                  ....*....|....*....|....*
gi 2420736723 376 GGSDDLQAQHTSGELVKLLQKAGLI 400
Cdd:PHA03050   81 GGYSDLLEIDNMDALGDILSSIGVL 105
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 232-285 3.50e-06

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: 45.14  E-value: 3.50e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2420736723 232 VDLDERADHLQLAEVVREISGQPGLPVIFVGGSEVGGYKGLQSLHASGELSKRL 285
Cdd:TIGR02189  38 HEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMALHISGSLVPML 91
PHA03050 PHA03050
glutaredoxin; Provisional
 70-174 5.55e-06

glutaredoxin; Provisional


Pssm-ID: 165343 [Multi-domain]  Cd Length: 108  Bit Score: 45.01  E-value: 5.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723  70 AARFVQSVLRKHRIVVFSKTTCPHCKATKALLERYHEQYGlGYMVVEADLRKDMDNVKHALASLCSHSTFPSVFVDAKCI 149
Cdd:PHA03050    2 AEEFVQQRLANNKVTIFVKFTCPFCRNALDILNKFSFKRG-AYEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSI 80

                          90       100
                  ....*....|....*....|....*
gi 2420736723 150 GGNDDMYAKHANGNLQQILVDAGLL 174
Cdd:PHA03050   81 GGYSDLLEIDNMDALGDILSSIGVL 105
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 308-380 4.22e-05

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: 41.44  E-value: 4.22e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2420736723 308 RVMVFSKTYCPYSSMAKRLLaklkEQRGLQFAvlEADKEADPmEVKAALGKISGRLTFPNIFVDGRSIGGSDD 380
Cdd:cd02976     1 EVTVYTKPDCPYCKATKRFL----DERGIPFE--EVDVDEDP-EALEELKKLNGYRSVPVVVIGDEHLSGFRP 66
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
298-397 5.65e-05

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 42.20  E-value: 5.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723 298 QKVRQLIQRNRVMVFSK-----TYCPYSSMAKRLLAKLKEQrglqFAVLEADKEADpmeVKAALGKISGRLTFPNIFVDG 372
Cdd:PRK10824    6 EKIQRQIAENPILLYMKgspklPSCGFSAQAVQALSACGER----FAYVDILQNPD---IRAELPKYANWPTFPQLWVDG 78

                          90       100
                  ....*....|....*....|....*
gi 2420736723 373 RSIGGSDDLQAQHTSGELVKLLQKA 397
Cdd:PRK10824   79 ELVGGCDIVIEMYQRGELQQLIKET 103
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 226-276 6.74e-05

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: 40.91  E-value: 6.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2420736723 226 GFAYRFVDLDERADHLQlaeVVREISGQPGLPVIFVGGSEVGGYKGLQSLH 276
Cdd:cd02066    24 GIEFEEIDILEDGELRE---ELKELSGWPTVPQIFINGEFIGGYDDLKALH 71
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 351-398 8.99e-05

Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of uncharacterized eukaryotic proteins containing a GRX-like domain having only one conserved cysteine, aligning to the C-terminal cysteine of the CXXC motif of GRXs. This subfamily is predominantly composed of plant proteins. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins via a redox active CXXC motif using a similar dithiol mechanism employed by TRXs. GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. Proteins containing only the C-terminal cysteine are generally redox inactive.


Pssm-ID: 239329 [Multi-domain]  Cd Length: 147  Bit Score: 42.22  E-value: 8.99e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2420736723 351 EVKAALGKISGRLTFPNIFVDGRSIGGSDDLQAQHTSGELVKLLQKAG 398
Cdd:cd03031    47 ELRELLGAELKAVSLPRVFVDGRYLGGAEEVLRLNESGELRKLLKGIR 94
Glutaredoxin pfam00462
Glutaredoxin;
223-266 1.12e-04

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 39.80  E-value: 1.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2420736723 223 ERTGFAYRFVDLDEradHLQLAEVVREISGQPGLPVIFVGGSEV 266
Cdd:pfam00462  20 KSLGVDFEEIDVDE---DPEIREELKELSGWPTVPQVFIDGEHI 60
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 94-172 1.12e-04

Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of uncharacterized eukaryotic proteins containing a GRX-like domain having only one conserved cysteine, aligning to the C-terminal cysteine of the CXXC motif of GRXs. This subfamily is predominantly composed of plant proteins. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins via a redox active CXXC motif using a similar dithiol mechanism employed by TRXs. GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. Proteins containing only the C-terminal cysteine are generally redox inactive.


Pssm-ID: 239329 [Multi-domain]  Cd Length: 147  Bit Score: 41.84  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723  94 CKATKALLEryheqyGLGYMVVEADLrkDMDNV-----KHALASLCSHSTFPSVFVDAKCIGGNDDMYAKHANGNLQQIL 168
Cdd:cd03031    19 CNNVRAILE------SFRVKFDERDV--SMDSGfreelRELLGAELKAVSLPRVFVDGRYLGGAEEVLRLNESGELRKLL 90


                  ....
gi 2420736723 169 VDAG 172
Cdd:cd03031    91 KGIR 94
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
 24-126 1.88e-04

DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active CXXC motif imbedded in a TRX fold. They function as protein disulfide isomerases and chaperones in the bacterial periplasm to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins. DsbC and DsbG are kept in their reduced state by the cytoplasmic membrane protein DsbD, which utilizes the TRX/TRX reductase system in the cytosol as a source of reducing equivalents. DsbG differ from DsbC in that it has a more limited substrate specificity, and it may preferentially act later in the folding process to catalyze disulfide rearrangements in folded or partially folded proteins. Also included in the alignment is the predicted protein TrbB, whose gene was sequenced from the enterohemorrhagic E. coli type IV pilus gene cluster, which is required for efficient plasmid transfer.


Pssm-ID: 239318 [Multi-domain]  Cd Length: 197  Bit Score: 42.30  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723  24 FLLVGRSFHVDGMLDALGDDSRdrprgginrhwpEAPLPIDAAQGPAARFVQSVLR--KHRIVVFSKTTCPHCKAtkall 101
Cdd:cd03020    32 YLIQGNLYDAKGRKDDLTEARL------------AQLNAIDLSALPLDDAIVYGKGngKRVVYVFTDPDCPYCRK----- 94

                          90       100
                  ....*....|....*....|....*
gi 2420736723 102 eryheqyglgymvVEADLRKDMDNV 126
Cdd:cd03020    95 -------------LEKELKPNADGV 106
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 82-103 1.04e-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: 37.59  E-value: 1.04e-03
                          10        20
                  ....*....|....*....|..
gi 2420736723  82 RIVVFSKTTCPHCKATKALLER 103
Cdd:cd02976     1 EVTVYTKPDCPYCKATKRFLDE 22
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 232-285 1.48e-03

Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of uncharacterized eukaryotic proteins containing a GRX-like domain having only one conserved cysteine, aligning to the C-terminal cysteine of the CXXC motif of GRXs. This subfamily is predominantly composed of plant proteins. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins via a redox active CXXC motif using a similar dithiol mechanism employed by TRXs. GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. Proteins containing only the C-terminal cysteine are generally redox inactive.


Pssm-ID: 239329 [Multi-domain]  Cd Length: 147  Bit Score: 38.76  E-value: 1.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723 232 VDLDER-----ADHL-QLAEVVREISGQPGLPVIFVGGSEVGGYKGLQSLHASGELSKRL 285
Cdd:cd03031    31 VKFDERdvsmdSGFReELRELLGAELKAVSLPRVFVDGRYLGGAEEVLRLNESGELRKLL 90
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 308-382 1.72e-03

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: 37.01  E-value: 1.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2420736723 308 RVMVFSKTYCPYSSMAKRLLaklkEQRGLQFAVLEADKEAdpmEVKAALGKISGRLTFPNIFVDGRSIGGSDDLQ 382
Cdd:cd03027     2 RVTIYSRLGCEDCTAVRLFL----REKGLPYVEINIDIFP---ERKAELEERTGSSVVPQIFFNEKLVGGLTDLK 69
PTZ00062 PTZ00062
glutaredoxin; Provisional
 223-392 2.17e-03

glutaredoxin; Provisional


Pssm-ID: 240250 [Multi-domain]  Cd Length: 204  Bit Score: 39.01  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723 223 ERTGFAYRFVDLDERADHLQLAEVVREISGQ-PGLPVIFVGGSEVGGYKGLQSLHASGELSKRLIDTKTS---------- 291
Cdd:PTZ00062   15 SNTGKLVLYVKSSKEPEYEQLMDVCNALVEDfPSLEFYVVNLADANNEYGVFEFYQNSQLINSLEGCNTStlvsfirgwa 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723 292 ---EQSAAEQKVRQLIQRNRVMVF---SKT--YCPYSSMAKRLLAKLKeQRGLQFAVLEadkeaDPmEVKAALGKISGRL 363
Cdd:PTZ00062   95 qkgSSEDTVEKIERLIRNHKILLFmkgSKTfpFCRFSNAVVNMLNSSG-VKYETYNIFE-----DP-DLREELKVYSNWP 167

                         170       180
                  ....*....|....*....|....*....
gi 2420736723 364 TFPNIFVDGRSIGGSDDLQAQHTSGELVK 392
Cdd:PTZ00062  168 TYPQLYVNGELIGGHDIIKELYESNSLRK 196
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 74-165 2.26e-03

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: 37.09  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723  74 VQSVLRKHRIVVFSKTT--CPHCKATKA---LLERYHEQYGlgYMVVEADlrkdmDNVKHALASLCSHSTFPSVFVDAKC 148
Cdd:cd03028     1 IKKLIKENPVVLFMKGTpeEPRCGFSRKvvqILNQLGVDFG--TFDILED-----EEVRQGLKEYSNWPTFPQLYVNGEL 73

                          90
                  ....*....|....*..
gi 2420736723 149 IGGNDDMYAKHANGNLQ 165
Cdd:cd03028    74 VGGCDIVKEMHESGELQ 90
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 80-143 2.55e-03

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 38.13  E-value: 2.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2420736723  80 KHRIVVFSKTTCPHCKATKALLERYHEQYGlGYMVVEADLRKDMDNVKHALASLcsHSTFPSVF 143
Cdd:COG0526    29 KPVLVNFWATWCPPCRAEMPVLKELAEEYG-GVVFVGVDVDENPEAVKAFLKEL--GLPYPVLL 89
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 223-285 2.96e-03

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: 36.47  E-value: 2.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2420736723 223 ERTGFAYRFVDLDerADHLQLAEVVrEISGQPGLPVIFVGGSEVGGYKGLQSLHASGELSKRL 285
Cdd:TIGR02181  20 SSKGVTFTEIRVD--GDPALRDEMM-QRSGRRTVPQIFIGDVHVGGCDDLYALDREGKLDPLL 79
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 82-153 3.10e-03

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: 36.20  E-value: 3.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2420736723  82 RIVVFSKTTCPHCKATKalleRYHEQYGLGYmvVEADLRKDMDNVKHALASLCSHSTfPSVFVDAKCIGGND 153
Cdd:TIGR02196   1 KVKVYTTPWCPPCVKAK----EYLTSKGVAF--EEIDVEKDAAAREELLKVYGQRGV-PVIVIGHKIVVGFD 65
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
73-173 4.87e-03

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


Pssm-ID: 440047  Cd Length: 105  Bit Score: 36.25  E-value: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736723  73 FVQSVLRKHRIVVFSKTT--CPHC----KATKALleryhEQYGLGYMVV----EADLRkdmdnvkhalASLCSHS---TF 139
Cdd:COG0278     7 RIKQQIKSNPVVLFMKGTpqFPQCgfsaRAVQIL-----NACGVDFATVnvleDPEIR----------QGLKEYSnwpTI 71

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2420736723 140 PSVFVDAKCIGGNDDMYAKHANGNLQQILVDAGL 173
Cdd:COG0278    72 PQLYVKGEFIGGCDIIREMYESGELQKLLEEAGA 105
TrbB TIGR02738
type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein ...
 60-118 5.88e-03

type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein is part of a large group of proteins involved in conjugative transfer of plasmid DNA, specifically the F-type system. This protein has been predicted to contain a thioredoxin fold, contains a conserved pair of cysteines and has been shown to function as a thiol disulfide isomerase by complementation of an Ecoli DsbA defect. The protein is believed to be involved in pilin assembly. The protein is closely related to TraF (TIGR02739) which is somewhat longer, lacks the cysteine motif and is apparently not functional as a disulfide bond isomerase.


Pssm-ID: 131785  Cd Length: 153  Bit Score: 37.09  E-value: 5.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2420736723  60 PLPIDAAQGPAARFVQSVLRKHRIVVFSKTTCPHCKATKALLERYHEQYGLGYMVVEAD 118
Cdd:TIGR02738  31 PQGLTAATDNAPQGRHANQDDYALVFFYQSTCPYCHQFAPVLKRFSQQFGLPVYAFSLD 89
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 83-145 7.71e-03

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: 34.98  E-value: 7.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2420736723  83 IVVFSKTTCPHCKATKALLERYHEQYgLGYMVVEADLrkDMDNVKHALASLCSHSTFPSVFVD 145
Cdd:cd01659     1 LVLFYAPWCPFCQALRPVLAELALLN-KGVKFEAVDV--DEDPALEKELKRYGVGGVPTLVVF 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH