NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2038578253|emb|CAG6124777|]
View 

transcriptional regulator Spx [Streptococcus pneumoniae]

Protein Classification

glutathione S-transferase; glutathione S-transferase omega family protein( domain architecture ID 10793784)

glutathione S-transferase catalyzes the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress| glutathione S-transferase (GST) omega family protein such as class-omega GSTs, which catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins than GSTs

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
spxA PRK13344
transcriptional regulator Spx; Reviewed
 1-132 2.13e-90

transcriptional regulator Spx; Reviewed


:

Pssm-ID: 183988  Cd Length: 132  Bit Score: 257.97  E-value: 2.13e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578253   1 MIKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELLDILTKTDNGIASIVSSKNRYAKALGVDIEDLSVNEVL 80
Cdd:PRK13344    1 MIKIYTISSCTSCKKAKTWLNAHQLSYKEQNLGKEPLTKEEILAILTKTENGIESIVSSKNRYAKALDCDIEELSVNEVI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2038578253  81 NLIMETPRILKSPILVDEKRLQVGYKEDDIRAFLPRSVRNVENAEARLRAAL 132
Cdd:PRK13344   81 DLIQENPRILKSPILIDDKRLQVGYKEDDIRAFLPRSIRNVENAEARLRAAL 132
 
Name Accession Description Interval E-value
spxA PRK13344
transcriptional regulator Spx; Reviewed
 1-132 2.13e-90

transcriptional regulator Spx; Reviewed


Pssm-ID: 183988  Cd Length: 132  Bit Score: 257.97  E-value: 2.13e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578253   1 MIKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELLDILTKTDNGIASIVSSKNRYAKALGVDIEDLSVNEVL 80
Cdd:PRK13344    1 MIKIYTISSCTSCKKAKTWLNAHQLSYKEQNLGKEPLTKEEILAILTKTENGIESIVSSKNRYAKALDCDIEELSVNEVI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2038578253  81 NLIMETPRILKSPILVDEKRLQVGYKEDDIRAFLPRSVRNVENAEARLRAAL 132
Cdd:PRK13344   81 DLIQENPRILKSPILIDDKRLQVGYKEDDIRAFLPRSIRNVENAEARLRAAL 132
ArsC_Spx cd03032
Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding ...
 1-115 1.00e-57

Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding protein present in bacilli and some mollicutes. It inhibits transcription by binding to the C-terminal domain of the alpha subunit of RNAP, disrupting complex formation between RNAP and certain transcriptional activator proteins like ResD and ComA. In response to oxidative stress, Spx can also activate transcription, making it a general regulator that exerts both positive and negative control over transcription initiation. Spx has been shown to exert redox-sensitive transcriptional control over genes like trxA (TRX) and trxB (TRX reductase), genes that function in thiol homeostasis. This redox-sensitive activity is dependent on the presence of a CXXC motif, present in some members of the Spx subfamily, that acts as a thiol/disulfide switch. Spx has also been shown to repress genes in a sulfate-dependent manner independent of the presence of the CXXC motif.


Pssm-ID: 239330  Cd Length: 115  Bit Score: 174.35  E-value: 1.00e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578253   1 MIKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELLDILTKTDNGIASIVSSKNRYAKALGVDIEDLSVNEVL 80
Cdd:cd03032     1 MIKLYTSPSCSSCRKAKQWLEEHQIPFEERNLFKQPLTKEELKEILSLTENGVEDIISTRSKAFKNLNIDIDELSLSELI 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2038578253  81 NLIMETPRILKSPILVDEKRLQVGYKEDDIRAFLP 115
Cdd:cd03032    81 RLISEHPSLLRRPIIIDEKRLQIGYNEDEIRQFLP 115
ArsC pfam03960
ArsC family; This family is related to glutaredoxins pfam00462.
 5-113 6.58e-37

ArsC family; This family is related to glutaredoxins pfam00462.


Pssm-ID: 427617  Cd Length: 109  Bit Score: 121.55  E-value: 6.58e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578253   5 YTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELLDILTKTDNGIASIVSSKNRYAKALGVDIEDLSVNEVLNLIM 84
Cdd:pfam03960   1 YGSPNCSTCRKALAWLEEHGIEYQEIDYLETPPSKEELKDILAKLGDGVEALLNTRGTTYRELNLDKEDLSEDELLELIL 80

                          90       100
                  ....*....|....*....|....*....
gi 2038578253  85 ETPRILKSPILVDEKRLQVGYKEDDIRAF 113
Cdd:pfam03960  81 EHPSLIRRPIVVDGGKLLVGFNEEEIRAF 109
arsC_related TIGR01617
transcriptional regulator, Spx/MgsR family; This model represents a portion of the proteins ...
 2-115 1.09e-34

transcriptional regulator, Spx/MgsR family; This model represents a portion of the proteins within the larger set covered by pfam03960. That larger family includes a glutaredoxin-dependent arsenate reductase (TIGR00014). Characterized members of this family include Spx and MgsR from Bacillus subtili. Spx is a global regulator for response to thiol-specific oxidative stress. It interacts with RNA polymerase. MgsR (modulator of the general stress response, also called YqgZ) provides a second level of regulation for more than a third of the proteins in the B. subtilis general stress regulon controlled by Sigma-B. [Regulatory functions, DNA interactions]


Pssm-ID: 273720  Cd Length: 117  Bit Score: 116.38  E-value: 1.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578253   2 IKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELLDILTKTDNGIASIVSSKNRYAKALGV--DIEDLSVNEV 79
Cdd:TIGR01617   1 IKVYGSPNCTTCKKARRWLEANGIEYQFIDIGEDGPTREELLDILSLLEDGIDPLLNTRGQSYRALNTsnTFLDLSDKEA 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2038578253  80 LNLIMETPRILKSPILVDEK-RLQVGYKEDDIRAFLP 115
Cdd:TIGR01617  81 LELLAEDPALLRRPLIVDTKnRLLIGFKSESIEEFKL 117
ArsC COG1393
Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and ...
 1-115 1.22e-33

Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and metabolism];


Pssm-ID: 441003  Cd Length: 115  Bit Score: 113.65  E-value: 1.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578253   1 MIKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELLDILTKTDNGIASIVSSKNRYAKALGVDIEDLSVNEVL 80
Cdd:COG1393     1 MITIYGNPNCSTSRKALAWLEEAGIEYEFIDYLKTPPTAEELKELLAKLGLGVEELLNTRGTTYRELGLKDKALSEEEAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2038578253  81 NLIMETPRILKSPILVDEKRLQVGYKEDDIRAFLP 115
Cdd:COG1393    81 ALMLEHPSLIKRPIVVTGDKALVGFPPEEVLALLG 115
 
Name Accession Description Interval E-value
spxA PRK13344
transcriptional regulator Spx; Reviewed
 1-132 2.13e-90

transcriptional regulator Spx; Reviewed


Pssm-ID: 183988  Cd Length: 132  Bit Score: 257.97  E-value: 2.13e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578253   1 MIKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELLDILTKTDNGIASIVSSKNRYAKALGVDIEDLSVNEVL 80
Cdd:PRK13344    1 MIKIYTISSCTSCKKAKTWLNAHQLSYKEQNLGKEPLTKEEILAILTKTENGIESIVSSKNRYAKALDCDIEELSVNEVI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2038578253  81 NLIMETPRILKSPILVDEKRLQVGYKEDDIRAFLPRSVRNVENAEARLRAAL 132
Cdd:PRK13344   81 DLIQENPRILKSPILIDDKRLQVGYKEDDIRAFLPRSIRNVENAEARLRAAL 132
ArsC_Spx cd03032
Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding ...
 1-115 1.00e-57

Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding protein present in bacilli and some mollicutes. It inhibits transcription by binding to the C-terminal domain of the alpha subunit of RNAP, disrupting complex formation between RNAP and certain transcriptional activator proteins like ResD and ComA. In response to oxidative stress, Spx can also activate transcription, making it a general regulator that exerts both positive and negative control over transcription initiation. Spx has been shown to exert redox-sensitive transcriptional control over genes like trxA (TRX) and trxB (TRX reductase), genes that function in thiol homeostasis. This redox-sensitive activity is dependent on the presence of a CXXC motif, present in some members of the Spx subfamily, that acts as a thiol/disulfide switch. Spx has also been shown to repress genes in a sulfate-dependent manner independent of the presence of the CXXC motif.


Pssm-ID: 239330  Cd Length: 115  Bit Score: 174.35  E-value: 1.00e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578253   1 MIKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELLDILTKTDNGIASIVSSKNRYAKALGVDIEDLSVNEVL 80
Cdd:cd03032     1 MIKLYTSPSCSSCRKAKQWLEEHQIPFEERNLFKQPLTKEELKEILSLTENGVEDIISTRSKAFKNLNIDIDELSLSELI 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2038578253  81 NLIMETPRILKSPILVDEKRLQVGYKEDDIRAFLP 115
Cdd:cd03032    81 RLISEHPSLLRRPIIIDEKRLQIGYNEDEIRQFLP 115
spxA PRK01655
transcriptional regulator Spx; Reviewed
 1-131 4.48e-53

transcriptional regulator Spx; Reviewed


Pssm-ID: 179316  Cd Length: 131  Bit Score: 163.32  E-value: 4.48e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578253   1 MIKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELLDILTKTDNGIASIVSSKNRYAKALGVDIEDLSVNEVL 80
Cdd:PRK01655    1 MVTLFTSPSCTSCRKAKAWLEEHDIPFTERNIFSSPLTIDEIKQILRMTEDGTDEIISTRSKVFQKLNVDVESLSLQDLI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2038578253  81 NLIMETPRILKSPILVDEKRLQVGYKEDDIRAFLPRSVRNVENAEARLRAA 131
Cdd:PRK01655   81 KLISDNPGLLRRPIIIDEKRLQVGYNEDEIRAFLPRKVRTFELREAQRRAN 131
ArsC pfam03960
ArsC family; This family is related to glutaredoxins pfam00462.
 5-113 6.58e-37

ArsC family; This family is related to glutaredoxins pfam00462.


Pssm-ID: 427617  Cd Length: 109  Bit Score: 121.55  E-value: 6.58e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578253   5 YTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELLDILTKTDNGIASIVSSKNRYAKALGVDIEDLSVNEVLNLIM 84
Cdd:pfam03960   1 YGSPNCSTCRKALAWLEEHGIEYQEIDYLETPPSKEELKDILAKLGDGVEALLNTRGTTYRELNLDKEDLSEDELLELIL 80

                          90       100
                  ....*....|....*....|....*....
gi 2038578253  85 ETPRILKSPILVDEKRLQVGYKEDDIRAF 113
Cdd:pfam03960  81 EHPSLIRRPIVVDGGKLLVGFNEEEIRAF 109
PRK12559 PRK12559
transcriptional regulator Spx; Provisional
 1-125 2.94e-35

transcriptional regulator Spx; Provisional


Pssm-ID: 79035  Cd Length: 131  Bit Score: 118.28  E-value: 2.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578253   1 MIKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELLDILTKTDNGIASIVSSKNRYAKALGVDIEDLSVNEVL 80
Cdd:PRK12559    1 MVVLYTTASCASCRKAKAWLEENQIDYTEKNIVSNSMTVDELKSILRLTEEGATEIISTRSKTFQDLNINIEELSLNEFY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2038578253  81 NLIMETPRILKSPILVDEKRLQVGYKEDDIRAFLPRSVRNVENAE 125
Cdd:PRK12559   81 KLIIEHPLMLRRPIMLDEKRLQIGFNDEEIRKFLPRSVRTFLNIE 125
arsC_related TIGR01617
transcriptional regulator, Spx/MgsR family; This model represents a portion of the proteins ...
 2-115 1.09e-34

transcriptional regulator, Spx/MgsR family; This model represents a portion of the proteins within the larger set covered by pfam03960. That larger family includes a glutaredoxin-dependent arsenate reductase (TIGR00014). Characterized members of this family include Spx and MgsR from Bacillus subtili. Spx is a global regulator for response to thiol-specific oxidative stress. It interacts with RNA polymerase. MgsR (modulator of the general stress response, also called YqgZ) provides a second level of regulation for more than a third of the proteins in the B. subtilis general stress regulon controlled by Sigma-B. [Regulatory functions, DNA interactions]


Pssm-ID: 273720  Cd Length: 117  Bit Score: 116.38  E-value: 1.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578253   2 IKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELLDILTKTDNGIASIVSSKNRYAKALGV--DIEDLSVNEV 79
Cdd:TIGR01617   1 IKVYGSPNCTTCKKARRWLEANGIEYQFIDIGEDGPTREELLDILSLLEDGIDPLLNTRGQSYRALNTsnTFLDLSDKEA 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2038578253  80 LNLIMETPRILKSPILVDEK-RLQVGYKEDDIRAFLP 115
Cdd:TIGR01617  81 LELLAEDPALLRRPLIVDTKnRLLIGFKSESIEEFKL 117
ArsC COG1393
Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and ...
 1-115 1.22e-33

Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and metabolism];


Pssm-ID: 441003  Cd Length: 115  Bit Score: 113.65  E-value: 1.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578253   1 MIKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELLDILTKTDNGIASIVSSKNRYAKALGVDIEDLSVNEVL 80
Cdd:COG1393     1 MITIYGNPNCSTSRKALAWLEEAGIEYEFIDYLKTPPTAEELKELLAKLGLGVEELLNTRGTTYRELGLKDKALSEEEAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2038578253  81 NLIMETPRILKSPILVDEKRLQVGYKEDDIRAFLP 115
Cdd:COG1393    81 ALMLEHPSLIKRPIVVTGDKALVGFPPEEVLALLG 115
ArsC_family cd02977
Arsenate Reductase (ArsC) family; composed of TRX-fold arsenic reductases and similar proteins ...
 2-105 6.46e-32

Arsenate Reductase (ArsC) family; composed of TRX-fold arsenic reductases and similar proteins including the transcriptional regulator, Spx. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from glutathione (GSH) via glutaredoxin (GRX), through a single catalytic cysteine. This family of predominantly bacterial enzymes is unrelated to two other families of arsenate reductases which show similarity to low-molecular-weight acid phosphatases and phosphotyrosyl phosphatases. Spx is a general regulator that exerts negative and positive control over transcription initiation by binding to the C-terminal domain of the alpha subunit of RNA polymerase.


Pssm-ID: 239275  Cd Length: 105  Bit Score: 108.73  E-value: 6.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578253   2 IKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELLDILTKTDNGIASIVSSKNRYAKALG-VDIEDLSVNEVL 80
Cdd:cd02977     1 ITIYGNPNCSTSRKALAWLEEHGIEYEFIDYLKEPPTKEELKELLAKLGLGVEDLFNTRGTPYRKLGlADKDELSDEEAL 80

                          90       100
                  ....*....|....*....|....*
gi 2038578253  81 NLIMETPRILKSPILVDEKRLQVGY 105
Cdd:cd02977    81 ELMAEHPKLIKRPIVVDGDRLLVGF 105
ArsC_like cd03036
Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a ...
 2-109 3.40e-16

Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a CXXC motif with similarity to thioredoxin (TRX)-fold arsenic reductases, ArsC. Proteins containing a redox active CXXC motif like TRX and glutaredoxin (GRX) function as protein disulfide oxidoreductases, altering the redox state of target proteins via the reversible oxidation of the active site dithiol. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from glutathione via GRX, through a single catalytic cysteine.


Pssm-ID: 239334  Cd Length: 111  Bit Score: 68.81  E-value: 3.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578253   2 IKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELLDILTKTDNGIASIV-SSKNRYaKALGVD--IEDLSVNE 78
Cdd:cd03036     1 LKFYEYPKCSTCRKAKKWLDEHGVDYTAIDIVEEPPSKEELKKWLEKSGLPLKKFFnTSGKSY-RELGLKdkLPSLSEEE 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2038578253  79 VLNLIMETPRILKSPILVDEKRLQVGYKEDD 109
Cdd:cd03036    80 ALELLSSDGMLIKRPFVVDDDKVLVGFKEEE 110
ArsC_Yffb cd03035
Arsenate Reductase (ArsC) family, Yffb subfamily; Yffb is an uncharacterized bacterial protein ...
 2-107 2.61e-11

Arsenate Reductase (ArsC) family, Yffb subfamily; Yffb is an uncharacterized bacterial protein encoded by the yffb gene, related to the thioredoxin-fold arsenic reductases, ArsC. The structure of Yffb and the conservation of the catalytic cysteine suggest that it is likely to function as a glutathione (GSH)-dependent thiol reductase. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from GSH via glutaredoxin, through a single catalytic cysteine.


Pssm-ID: 239333  Cd Length: 105  Bit Score: 56.06  E-value: 2.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578253   2 IKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELLDILTKTdnGIASIVSSKNRYAKALGVDIE-DLSVNEVL 80
Cdd:cd03035     1 ITLYGIKNCDTVKKARKWLEARGVAYTFHDYRKDGLDAATLERWLAKV--GWETLLNKRGTTWRKLDDAQKaALDAAKAI 78

                          90       100
                  ....*....|....*....|....*..
gi 2038578253  81 NLIMETPRILKSPILVDEKRLQVGYKE 107
Cdd:cd03035    79 ALMLEHPSLIKRPVLETGGKVLVGFSE 105
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 1-43 2.09e-06

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


Pssm-ID: 274027 [Multi-domain]  Cd Length: 74  Bit Score: 42.75  E-value: 2.09e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2038578253   1 MIKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELL 43
Cdd:TIGR02196   1 KVKVYTTPWCPPCVKAKEYLTSKGVAFEEIDVEKDAAAREELL 43
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
1-42 5.95e-06

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 41.34  E-value: 5.95e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2038578253   1 MIKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREEL 42
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDEDPEAREEL 42
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 1-56 2.45e-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: 39.90  E-value: 2.45e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2038578253   1 MIKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKegitREELLDILTKTdNGIASI 56
Cdd:cd02976     1 EVTVYTKPDCPYCKATKRFLDERGIPFEEVDVDE----DPEALEELKKL-NGYRSV 51
ArsC_ArsC cd03034
Arsenate Reductase (ArsC) family, ArsC subfamily; arsenic reductases similar to that encoded ...
 34-104 4.08e-05

Arsenate Reductase (ArsC) family, ArsC subfamily; arsenic reductases similar to that encoded by arsC on the R733 plasmid of Escherichia coli. E. coli ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], the first step in the detoxification of arsenic, using reducing equivalents derived from glutathione (GSH) via glutaredoxin (GRX). ArsC contains a single catalytic cysteine, within a thioredoxin fold, that forms a covalent thiolate-As(V) intermediate, which is reduced by GRX through a mixed GSH-arsenate intermediate. This family of predominantly bacterial enzymes is unrelated to two other families of arsenate reductases which show similarity to low-molecular-weight acid phosphatases and phosphotyrosyl phosphatases.


Pssm-ID: 239332  Cd Length: 112  Bit Score: 39.88  E-value: 4.08e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038578253  34 KEGITREELLDILTKTDNGIASIVSSKNRYAKALGVDIEDLSVNEVLNLIMETPRILKSPILVDEKRLQVG 104
Cdd:cd03034    33 KTPPTAAELRELLAKLGISPRDLLRTKEAPYKELGLADPELSDEELIDAMAAHPILIERPIVVTGDGAVLG 103
Glutaredoxin pfam00462
Glutaredoxin;
2-45 1.14e-04

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 37.48  E-value: 1.14e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2038578253   2 IKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELLDI 45
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKEL 44
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 2-42 2.75e-04

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: 37.06  E-value: 2.75e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2038578253   2 IKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREEL 42
Cdd:cd02066     2 VVVFSKSTCPYCKRAKRLLESLGIEFEEIDILEDGELREEL 42
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 2-43 1.42e-03

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: 35.26  E-value: 1.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2038578253   2 IKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELL 43
Cdd:cd03418     2 VEIYTKPNCPYCVRAKALLDKKGVDYEEIDVDGDPALREEMI 43
PRK10638 PRK10638
glutaredoxin 3; Provisional
 2-43 2.32e-03

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 34.80  E-value: 2.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2038578253   2 IKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELL 43
Cdd:PRK10638    4 VEIYTKATCPFCHRAKALLNSKGVSFQEIPIDGDAAKREEMI 45
ArsC_15kD cd03033
Arsenate Reductase (ArsC) family, 15kD protein subfamily; composed of proteins of unknown ...
 2-115 5.14e-03

Arsenate Reductase (ArsC) family, 15kD protein subfamily; composed of proteins of unknown function with similarity to thioredoxin-fold arsenic reductases, ArsC. It is encoded by an ORF present in a gene cluster associated with nitrogen fixation that also encodes dinitrogenase reductase ADP-ribosyltransferase (DRAT) and dinitrogenase reductase activating glycohydrolase (DRAG). ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from glutathione via glutaredoxin, through a single catalytic cysteine.


Pssm-ID: 239331  Cd Length: 113  Bit Score: 34.56  E-value: 5.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038578253   2 IKIYTVSSCTSCKKAKTWLNAHQLSYKEQNLGKEGITREELLDILTktDNGIASIVsskNRYA---KALGVDIEDLSVNE 78
Cdd:cd03033     2 IIFYEKPGCANNARQKALLEAAGHEVEVRDLLTEPWTAETLRPFFG--DLPVAEWF---NPAAprvKSGEVVPEALDEEE 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2038578253  79 VLNLIMETPRILKSPIL-VDEKRLqVGYKEDDIRAFLP 115
Cdd:cd03033    77 ALALMIADPLLIRRPLMqVGDRRM-VGFDTARVDAWIG 113
 
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