NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446369686|ref|WP_000447541|]
View 

MULTISPECIES: Grx4 family monothiol glutaredoxin [Vibrio]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-110 3.79e-71

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 PRK10824:

Pssm-ID: 469754  Cd Length: 115  Bit Score: 207.45  E-value: 3.79e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446369686   1 METIDKIKQQIAENPILLYMKGSPKLPSCGFSSQAAQALMACGEKFAYVDILQNPDIRAELPVYAQWPTFPQLWIEGELI 80
Cdd:PRK10824   2 STTIEKIQRQIAENPILLYMKGSPKLPSCGFSAQAVQALSACGERFAYVDILQNPDIRAELPKYANWPTFPQLWVDGELV 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 446369686  81 GGCDIMLEMFQKGELQTLVKEAAARSASQE 110
Cdd:PRK10824  82 GGCDIVIEMYQRGELQQLIKETAAKYKSEE 111
 
Name Accession Description Interval E-value
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
1-110 3.79e-71

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 207.45  E-value: 3.79e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446369686   1 METIDKIKQQIAENPILLYMKGSPKLPSCGFSSQAAQALMACGEKFAYVDILQNPDIRAELPVYAQWPTFPQLWIEGELI 80
Cdd:PRK10824   2 STTIEKIQRQIAENPILLYMKGSPKLPSCGFSAQAVQALSACGERFAYVDILQNPDIRAELPKYANWPTFPQLWVDGELV 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 446369686  81 GGCDIMLEMFQKGELQTLVKEAAARSASQE 110
Cdd:PRK10824  82 GGCDIVIEMYQRGELQQLIKETAAKYKSEE 111
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
1-104 2.85e-70

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


Pssm-ID: 440047  Cd Length: 105  Bit Score: 204.96  E-value: 2.85e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446369686   1 METIDKIKQQIAENPILLYMKGSPKLPSCGFSSQAAQALMACGEKFAYVDILQNPDIRAELPVYAQWPTFPQLWIEGELI 80
Cdd:COG0278    2 MDVQERIKQQIKSNPVVLFMKGTPQFPQCGFSARAVQILNACGVDFATVNVLEDPEIRQGLKEYSNWPTIPQLYVKGEFI 81

                         90       100
                 ....*....|....*....|....
gi 446369686  81 GGCDIMLEMFQKGELQTLVKEAAA 104
Cdd:COG0278   82 GGCDIIREMYESGELQKLLEEAGA 105
TIGR00365 TIGR00365
monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. ...
 3-99 4.28e-67

monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. coli, originally designated ydhD, is now designated grxD. Its protein, Grx4, is a monothiol glutaredoxin similar to Grx5 of yeast, which is involved in iron-sulfur cluster formation. [Energy metabolism, Electron transport]


Pssm-ID: 188046  Cd Length: 97  Bit Score: 196.53  E-value: 4.28e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446369686    3 TIDKIKQQIAENPILLYMKGSPKLPSCGFSSQAAQALMACGEKFAYVDILQNPDIRAELPVYAQWPTFPQLWIEGELIGG 82
Cdd:TIGR00365   1 TIERIKEQIAENPVVLYMKGTPQFPQCGFSARAVQILNACGVPFAYVNVLEDPEIRQGIKEYSNWPTIPQLYVKGEFVGG 80

                          90
                  ....*....|....*..
gi 446369686   83 CDIMLEMFQKGELQTLV 99
Cdd:TIGR00365  81 CDIIMEMYQSGELQTLL 97
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 7-96 1.64e-50

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: 154.57  E-value: 1.64e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446369686   7 IKQQIAENPILLYMKGSPKLPSCGFSSQAAQALMACGEKFAYVDILQNPDIRAELPVYAQWPTFPQLWIEGELIGGCDIM 86
Cdd:cd03028    1 IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDIV 80

                         90
                 ....*....|
gi 446369686  87 LEMFQKGELQ 96
Cdd:cd03028   81 KEMHESGELQ 90
Glutaredoxin pfam00462
Glutaredoxin;
16-80 1.10e-20

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 77.93  E-value: 1.10e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446369686   16 ILLYMKgspklPSCGFSSQAAQALMACGEKFAYVDILQNPDIRAELPVYAQWPTFPQLWIEGELI 80
Cdd:pfam00462   1 VVLYTK-----PTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTVPQVFIDGEHI 60
 
Name Accession Description Interval E-value
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
1-110 3.79e-71

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 207.45  E-value: 3.79e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446369686   1 METIDKIKQQIAENPILLYMKGSPKLPSCGFSSQAAQALMACGEKFAYVDILQNPDIRAELPVYAQWPTFPQLWIEGELI 80
Cdd:PRK10824   2 STTIEKIQRQIAENPILLYMKGSPKLPSCGFSAQAVQALSACGERFAYVDILQNPDIRAELPKYANWPTFPQLWVDGELV 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 446369686  81 GGCDIMLEMFQKGELQTLVKEAAARSASQE 110
Cdd:PRK10824  82 GGCDIVIEMYQRGELQQLIKETAAKYKSEE 111
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
1-104 2.85e-70

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


Pssm-ID: 440047  Cd Length: 105  Bit Score: 204.96  E-value: 2.85e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446369686   1 METIDKIKQQIAENPILLYMKGSPKLPSCGFSSQAAQALMACGEKFAYVDILQNPDIRAELPVYAQWPTFPQLWIEGELI 80
Cdd:COG0278    2 MDVQERIKQQIKSNPVVLFMKGTPQFPQCGFSARAVQILNACGVDFATVNVLEDPEIRQGLKEYSNWPTIPQLYVKGEFI 81

                         90       100
                 ....*....|....*....|....
gi 446369686  81 GGCDIMLEMFQKGELQTLVKEAAA 104
Cdd:COG0278   82 GGCDIIREMYESGELQKLLEEAGA 105
TIGR00365 TIGR00365
monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. ...
 3-99 4.28e-67

monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. coli, originally designated ydhD, is now designated grxD. Its protein, Grx4, is a monothiol glutaredoxin similar to Grx5 of yeast, which is involved in iron-sulfur cluster formation. [Energy metabolism, Electron transport]


Pssm-ID: 188046  Cd Length: 97  Bit Score: 196.53  E-value: 4.28e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446369686    3 TIDKIKQQIAENPILLYMKGSPKLPSCGFSSQAAQALMACGEKFAYVDILQNPDIRAELPVYAQWPTFPQLWIEGELIGG 82
Cdd:TIGR00365   1 TIERIKEQIAENPVVLYMKGTPQFPQCGFSARAVQILNACGVPFAYVNVLEDPEIRQGIKEYSNWPTIPQLYVKGEFVGG 80

                          90
                  ....*....|....*..
gi 446369686   83 CDIMLEMFQKGELQTLV 99
Cdd:TIGR00365  81 CDIIMEMYQSGELQTLL 97
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 7-96 1.64e-50

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: 154.57  E-value: 1.64e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446369686   7 IKQQIAENPILLYMKGSPKLPSCGFSSQAAQALMACGEKFAYVDILQNPDIRAELPVYAQWPTFPQLWIEGELIGGCDIM 86
Cdd:cd03028    1 IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDIV 80

                         90
                 ....*....|
gi 446369686  87 LEMFQKGELQ 96
Cdd:cd03028   81 KEMHESGELQ 90
PTZ00062 PTZ00062
glutaredoxin; Provisional
 3-101 1.83e-34

glutaredoxin; Provisional


Pssm-ID: 240250 [Multi-domain]  Cd Length: 204  Bit Score: 117.59  E-value: 1.83e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446369686   3 TIDKIKQQIAENPILLYMKGSPKLPSCGFSSQAAQALMACGEKFAYVDILQNPDIRAELPVYAQWPTFPQLWIEGELIGG 82
Cdd:PTZ00062 102 TVEKIERLIRNHKILLFMKGSKTFPFCRFSNAVVNMLNSSGVKYETYNIFEDPDLREELKVYSNWPTYPQLYVNGELIGG 181

                         90
                 ....*....|....*....
gi 446369686  83 CDIMLEMFQKGELQTLVKE 101
Cdd:PTZ00062 182 HDIIKELYESNSLRKVIPD 200
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 15-91 1.07e-24

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: 1.07e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446369686  15 PILLYMKGSpklpsCGFSSQAAQALMACGEKFAYVDILQNPDIRAELPVYAQWPTFPQLWIEGELIGGCDIMLEMFQ 91
Cdd:cd02066    1 KVVVFSKST-----CPYCKRAKRLLESLGIEFEEIDILEDGELREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
Glutaredoxin pfam00462
Glutaredoxin;
16-80 1.10e-20

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 77.93  E-value: 1.10e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446369686   16 ILLYMKgspklPSCGFSSQAAQALMACGEKFAYVDILQNPDIRAELPVYAQWPTFPQLWIEGELI 80
Cdd:pfam00462   1 VVLYTK-----PTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTVPQVFIDGEHI 60
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
15-84 1.19e-10

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 52.89  E-value: 1.19e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446369686  15 PILLYMKgspklPSCGFSSQAAQALMACGEKFAYVDILQNPDIRAELPVYAQWPTFPQLWIEGELIGGCD 84
Cdd:COG0695    1 KVTLYTT-----PGCPYCARAKRLLDEKGIPYEEIDVDEDPEAREELRERSGRRTVPVIFIGGEHLGGFD 65
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 27-98 7.09e-09

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: 48.41  E-value: 7.09e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446369686   27 PSCGFSSQAAQALMACGEKFAYVDILQNPDIRAELPVYAQWPTFPQLWIEGELIGGCDIMLEMFQKGELQTL 98
Cdd:TIGR02181   7 PYCPYCTRAKALLSSKGVTFTEIRVDGDPALRDEMMQRSGRRTVPQIFIGDVHVGGCDDLYALDREGKLDPL 78
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 27-98 6.72e-07

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: 43.30  E-value: 6.72e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446369686  27 PSCGFSSQAAQALMACGEKFAYVDILQNPD---IRAELpvyAQW---PTFPQLWIEGELIGGCDIMLEMFQKGELQTL 98
Cdd:cd03419    8 SYCPYCKRAKSLLKELGVKPAVVELDQHEDgseIQDYL---QELtgqRTVPNVFIGGKFIGGCDDLMALHKSGKLVKL 82
PRK10638 PRK10638
glutaredoxin 3; Provisional
 28-100 2.75e-06

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 42.11  E-value: 2.75e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446369686  28 SCGFSSQAAQALMACGEKFAYVDILQNPDIRAELPVYAQWPTFPQLWIEGELIGGCDIMLEMFQKGELQTLVK 100
Cdd:PRK10638  11 TCPFCHRAKALLNSKGVSFQEIPIDGDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARGGLDPLLK 83
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 15-93 2.79e-05

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: 39.11  E-value: 2.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446369686  15 PILLYMKgspklPSCGFSSQAAQALMACGEKFAYVDILQNPDIRAELPVYAQ-WPTFPQLWIEGELIGGCDIMLEMFQKG 93
Cdd:cd03418    1 KVEIYTK-----PNCPYCVRAKALLDKKGVDYEEIDVDGDPALREEMINRSGgRRTVPQIFIGDVHIGGCDDLYALERKG 75
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 27-84 7.57e-05

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: 37.88  E-value: 7.57e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446369686  27 PSCGFSSQAAQALMACGekFAYVDILQNPDIRAE-LPVYAQWPTFPQLWIEGELIGGCD 84
Cdd:cd03029    9 PGCPFCARAKAALQENG--ISYEEIPLGKDITGRsLRAVTGAMTVPQVFIDGELIGGSD 65
grxA PRK11200
glutaredoxin 1; Provisional
 27-101 9.23e-04

glutaredoxin 1; Provisional


Pssm-ID: 183036 [Multi-domain]  Cd Length: 85  Bit Score: 35.39  E-value: 9.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446369686  27 PSCGFSSQA---AQALMACGE--KFAYVDILQNPDIRAEL------PVYaqwpTFPQLWIEGELIGGCDimlemfqkgEL 95
Cdd:PRK11200   9 PGCPYCVRAkelAEKLSEERDdfDYRYVDIHAEGISKADLektvgkPVE----TVPQIFVDQKHIGGCT---------DF 75


                 ....*.
gi 446369686  96 QTLVKE 101
Cdd:PRK11200  76 EAYVKE 81
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 50-105 1.49e-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: 35.67  E-value: 1.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446369686  50 DILQNPDIRAEL----PVYAQWPTFPQLWIEGELIGGCDIMLEMFQKGELQTLVKEAAAR 105
Cdd:cd03031   37 DVSMDSGFREELrellGAELKAVSLPRVFVDGRYLGGAEEVLRLNESGELRKLLKGIRAR 96
 
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