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Conserved domains on  [gi|488215050|ref|WP_002286258|]
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MULTISPECIES: Spx/MgsR family RNA polymerase-binding regulatory protein [Enterococcus]

Protein Classification

Spx/MgsR family RNA polymerase-binding regulatory protein( domain architecture ID 10122542)

Spx/MgsR family RNA polymerase-binding regulatory protein similar to Bacillus subtilis MgsR that regulates transcription of a subregulon within the general stress response; belongs to the thioredoxin superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ArsC_Spx cd03032
Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding ...
 1-115 6.93e-62

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: 185.14  E-value: 6.93e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050   1 MIKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAATEGGVQDIISTRSKIYEKLGIDFNELTLKQMI 80
Cdd:cd03032    1 MIKLYTSPSCSSCRKAKQWLEEHQIPFEERNLFKQPLTKEELKEILSLTENGVEDIISTRSKAFKNLNIDIDELSLSELI 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488215050  81 VLFKEYPSLLRRPILIDEKRILIGFNEDEIRSFVP 115
Cdd:cd03032   81 RLISEHPSLLRRPIIIDEKRLQIGYNEDEIRQFLP 115
 
Name Accession Description Interval E-value
ArsC_Spx cd03032
Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding ...
 1-115 6.93e-62

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: 185.14  E-value: 6.93e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050   1 MIKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAATEGGVQDIISTRSKIYEKLGIDFNELTLKQMI 80
Cdd:cd03032    1 MIKLYTSPSCSSCRKAKQWLEEHQIPFEERNLFKQPLTKEELKEILSLTENGVEDIISTRSKAFKNLNIDIDELSLSELI 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488215050  81 VLFKEYPSLLRRPILIDEKRILIGFNEDEIRSFVP 115
Cdd:cd03032   81 RLISEHPSLLRRPIIIDEKRLQIGYNEDEIRQFLP 115
spxA PRK01655
transcriptional regulator Spx; Reviewed
 1-119 4.19e-61

transcriptional regulator Spx; Reviewed


Pssm-ID: 179316  Cd Length: 131  Bit Score: 183.73  E-value: 4.19e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050   1 MIKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAATEGGVQDIISTRSKIYEKLGIDFNELTLKQMI 80
Cdd:PRK01655   1 MVTLFTSPSCTSCRKAKAWLEEHDIPFTERNIFSSPLTIDEIKQILRMTEDGTDEIISTRSKVFQKLNVDVESLSLQDLI 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488215050  81 VLFKEYPSLLRRPILIDEKRILIGFNEDEIRSFVPREIR 119
Cdd:PRK01655  81 KLISDNPGLLRRPIIIDEKRLQVGYNEDEIRAFLPRKVR 119
ArsC pfam03960
ArsC family; This family is related to glutaredoxins pfam00462.
 5-113 9.89e-44

ArsC family; This family is related to glutaredoxins pfam00462.


Pssm-ID: 427617  Cd Length: 109  Bit Score: 138.89  E-value: 9.89e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050    5 YTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAATEGGVQDIISTRSKIYEKLGIDFNELTLKQMIVLFK 84
Cdd:pfam03960   1 YGSPNCSTCRKALAWLEEHGIEYQEIDYLETPPSKEELKDILAKLGDGVEALLNTRGTTYRELNLDKEDLSEDELLELIL 80

                          90       100
                  ....*....|....*....|....*....
gi 488215050   85 EYPSLLRRPILIDEKRILIGFNEDEIRSF 113
Cdd:pfam03960  81 EHPSLIRRPIVVDGGKLLVGFNEEEIRAF 109
ArsC COG1393
Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and ...
 1-115 9.98e-41

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


Pssm-ID: 441003  Cd Length: 115  Bit Score: 131.75  E-value: 9.98e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050   1 MIKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAATEGGVQDIISTRSKIYEKLGIDFNELTLKQMI 80
Cdd:COG1393    1 MITIYGNPNCSTSRKALAWLEEAGIEYEFIDYLKTPPTAEELKELLAKLGLGVEELLNTRGTTYRELGLKDKALSEEEAL 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488215050  81 VLFKEYPSLLRRPILIDEKRILIGFNEDEIRSFVP 115
Cdd:COG1393   81 ALMLEHPSLIKRPIVVTGDKALVGFPPEEVLALLG 115
arsC_related TIGR01617
transcriptional regulator, Spx/MgsR family; This model represents a portion of the proteins ...
 2-115 6.14e-37

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: 122.15  E-value: 6.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050    2 IKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAATEGGVQDIISTRSKIYEKLGI--DFNELTLKQM 79
Cdd:TIGR01617   1 IKVYGSPNCTTCKKARRWLEANGIEYQFIDIGEDGPTREELLDILSLLEDGIDPLLNTRGQSYRALNTsnTFLDLSDKEA 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 488215050   80 IVLFKEYPSLLRRPILIDEK-RILIGFNEDEIRSFVP 115
Cdd:TIGR01617  81 LELLAEDPALLRRPLIVDTKnRLLIGFKSESIEEFKL 117
Uxx_star NF041212
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ...
 2-45 1.49e-04

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


Pssm-ID: 469116 [Multi-domain]  Cd Length: 70  Bit Score: 37.83  E-value: 1.49e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488215050   2 IKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKI 45
Cdd:NF041212   1 VVIYTKPGCPYCAAAKEDLARRGIPFEEIDVSKDPEALEEMLRL 44
 
Name Accession Description Interval E-value
ArsC_Spx cd03032
Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding ...
 1-115 6.93e-62

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: 185.14  E-value: 6.93e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050   1 MIKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAATEGGVQDIISTRSKIYEKLGIDFNELTLKQMI 80
Cdd:cd03032    1 MIKLYTSPSCSSCRKAKQWLEEHQIPFEERNLFKQPLTKEELKEILSLTENGVEDIISTRSKAFKNLNIDIDELSLSELI 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488215050  81 VLFKEYPSLLRRPILIDEKRILIGFNEDEIRSFVP 115
Cdd:cd03032   81 RLISEHPSLLRRPIIIDEKRLQIGYNEDEIRQFLP 115
spxA PRK01655
transcriptional regulator Spx; Reviewed
 1-119 4.19e-61

transcriptional regulator Spx; Reviewed


Pssm-ID: 179316  Cd Length: 131  Bit Score: 183.73  E-value: 4.19e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050   1 MIKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAATEGGVQDIISTRSKIYEKLGIDFNELTLKQMI 80
Cdd:PRK01655   1 MVTLFTSPSCTSCRKAKAWLEEHDIPFTERNIFSSPLTIDEIKQILRMTEDGTDEIISTRSKVFQKLNVDVESLSLQDLI 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488215050  81 VLFKEYPSLLRRPILIDEKRILIGFNEDEIRSFVPREIR 119
Cdd:PRK01655  81 KLISDNPGLLRRPIIIDEKRLQVGYNEDEIRAFLPRKVR 119
ArsC pfam03960
ArsC family; This family is related to glutaredoxins pfam00462.
 5-113 9.89e-44

ArsC family; This family is related to glutaredoxins pfam00462.


Pssm-ID: 427617  Cd Length: 109  Bit Score: 138.89  E-value: 9.89e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050    5 YTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAATEGGVQDIISTRSKIYEKLGIDFNELTLKQMIVLFK 84
Cdd:pfam03960   1 YGSPNCSTCRKALAWLEEHGIEYQEIDYLETPPSKEELKDILAKLGDGVEALLNTRGTTYRELNLDKEDLSEDELLELIL 80

                          90       100
                  ....*....|....*....|....*....
gi 488215050   85 EYPSLLRRPILIDEKRILIGFNEDEIRSF 113
Cdd:pfam03960  81 EHPSLIRRPIVVDGGKLLVGFNEEEIRAF 109
spxA PRK13344
transcriptional regulator Spx; Reviewed
 1-121 1.82e-41

transcriptional regulator Spx; Reviewed


Pssm-ID: 183988  Cd Length: 132  Bit Score: 134.32  E-value: 1.82e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050   1 MIKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAATEGGVQDIISTRSKIYEKLGIDFNELTLKQMI 80
Cdd:PRK13344   1 MIKIYTISSCTSCKKAKTWLNAHQLSYKEQNLGKEPLTKEEILAILTKTENGIESIVSSKNRYAKALDCDIEELSVNEVI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 488215050  81 VLFKEYPSLLRRPILIDEKRILIGFNEDEIRSFVPREIRCV 121
Cdd:PRK13344  81 DLIQENPRILKSPILIDDKRLQVGYKEDDIRAFLPRSIRNV 121
ArsC COG1393
Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and ...
 1-115 9.98e-41

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


Pssm-ID: 441003  Cd Length: 115  Bit Score: 131.75  E-value: 9.98e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050   1 MIKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAATEGGVQDIISTRSKIYEKLGIDFNELTLKQMI 80
Cdd:COG1393    1 MITIYGNPNCSTSRKALAWLEEAGIEYEFIDYLKTPPTAEELKELLAKLGLGVEELLNTRGTTYRELGLKDKALSEEEAL 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488215050  81 VLFKEYPSLLRRPILIDEKRILIGFNEDEIRSFVP 115
Cdd:COG1393   81 ALMLEHPSLIKRPIVVTGDKALVGFPPEEVLALLG 115
ArsC_family cd02977
Arsenate Reductase (ArsC) family; composed of TRX-fold arsenic reductases and similar proteins ...
 2-105 6.97e-40

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: 129.15  E-value: 6.97e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050   2 IKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAATEGGVQDIISTRSKIYEKLGI-DFNELTLKQMI 80
Cdd:cd02977    1 ITIYGNPNCSTSRKALAWLEEHGIEYEFIDYLKEPPTKEELKELLAKLGLGVEDLFNTRGTPYRKLGLaDKDELSDEEAL 80

                         90       100
                 ....*....|....*....|....*
gi 488215050  81 VLFKEYPSLLRRPILIDEKRILIGF 105
Cdd:cd02977   81 ELMAEHPKLIKRPIVVDGDRLLVGF 105
PRK12559 PRK12559
transcriptional regulator Spx; Provisional
 1-119 8.39e-40

transcriptional regulator Spx; Provisional


Pssm-ID: 79035  Cd Length: 131  Bit Score: 129.84  E-value: 8.39e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050   1 MIKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAATEGGVQDIISTRSKIYEKLGIDFNELTLKQMI 80
Cdd:PRK12559   1 MVVLYTTASCASCRKAKAWLEENQIDYTEKNIVSNSMTVDELKSILRLTEEGATEIISTRSKTFQDLNINIEELSLNEFY 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488215050  81 VLFKEYPSLLRRPILIDEKRILIGFNEDEIRSFVPREIR 119
Cdd:PRK12559  81 KLIIEHPLMLRRPIMLDEKRLQIGFNDEEIRKFLPRSVR 119
arsC_related TIGR01617
transcriptional regulator, Spx/MgsR family; This model represents a portion of the proteins ...
 2-115 6.14e-37

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: 122.15  E-value: 6.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050    2 IKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAATEGGVQDIISTRSKIYEKLGI--DFNELTLKQM 79
Cdd:TIGR01617   1 IKVYGSPNCTTCKKARRWLEANGIEYQFIDIGEDGPTREELLDILSLLEDGIDPLLNTRGQSYRALNTsnTFLDLSDKEA 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 488215050   80 IVLFKEYPSLLRRPILIDEK-RILIGFNEDEIRSFVP 115
Cdd:TIGR01617  81 LELLAEDPALLRRPLIVDTKnRLLIGFKSESIEEFKL 117
ArsC_like cd03036
Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a ...
 2-109 8.32e-23

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: 86.14  E-value: 8.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050   2 IKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAATEGGVQDIISTRSKIYEKLGID--FNELTLKQM 79
Cdd:cd03036    1 LKFYEYPKCSTCRKAKKWLDEHGVDYTAIDIVEEPPSKEELKKWLEKSGLPLKKFFNTSGKSYRELGLKdkLPSLSEEEA 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 488215050  80 IVLFKEYPSLLRRPILIDEKRILIGFNEDE 109
Cdd:cd03036   81 LELLSSDGMLIKRPFVVDDDKVLVGFKEEE 110
ArsC_ArsC cd03034
Arsenate Reductase (ArsC) family, ArsC subfamily; arsenic reductases similar to that encoded ...
 2-104 5.13e-15

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: 66.07  E-value: 5.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050   2 IKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAATEGGVQDIISTRSKIYEKLGIDFNELTLKQMIV 81
Cdd:cd03034    1 ITIYHNPRCSKSRNALALLEEAGIEPEIVEYLKTPPTAAELRELLAKLGISPRDLLRTKEAPYKELGLADPELSDEELID 80

                         90       100
                 ....*....|....*....|...
gi 488215050  82 LFKEYPSLLRRPILIDEKRILIG 104
Cdd:cd03034   81 AMAAHPILIERPIVVTGDGAVLG 103
ArsC_Yffb cd03035
Arsenate Reductase (ArsC) family, Yffb subfamily; Yffb is an uncharacterized bacterial protein ...
 2-107 1.33e-13

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: 62.23  E-value: 1.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050   2 IKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAATegGVQDIISTRSKIYEKLG-IDFNELTLKQMI 80
Cdd:cd03035    1 ITLYGIKNCDTVKKARKWLEARGVAYTFHDYRKDGLDAATLERWLAKV--GWETLLNKRGTTWRKLDdAQKAALDAAKAI 78

                         90       100
                 ....*....|....*....|....*..
gi 488215050  81 VLFKEYPSLLRRPILIDEKRILIGFNE 107
Cdd:cd03035   79 ALMLEHPSLIKRPVLETGGKVLVGFSE 105
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
1-32 4.06e-08

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 47.11  E-value: 4.06e-08
                         10        20        30
                 ....*....|....*....|....*....|..
gi 488215050   1 MIKVYTSPSCTSCRKARAWLQANQLEFEEKNI 32
Cdd:COG0695    1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDV 32
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 1-46 2.20e-07

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: 45.29  E-value: 2.20e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 488215050   1 MIKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKIL 46
Cdd:cd02976    1 EVTVYTKPDCPYCKATKRFLDERGIPFEEVDVDEDPEALEELKKLN 46
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 1-36 2.47e-07

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


Pssm-ID: 274027 [Multi-domain]  Cd Length: 74  Bit Score: 45.06  E-value: 2.47e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 488215050    1 MIKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEP 36
Cdd:TIGR02196   1 KVKVYTTPWCPPCVKAKEYLTSKGVAFEEIDVEKDA 36
PRK10853 PRK10853
putative reductase; Provisional
 1-113 2.60e-07

putative reductase; Provisional


Pssm-ID: 182780  Cd Length: 118  Bit Score: 46.19  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050   1 MIKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAatEGGVQDIISTRSKIYEKL------GIDFNEL 74
Cdd:PRK10853   1 MVTLYGIKNCDTIKKARRWLEAQGIDYRFHDYRVDGLDSELLQGFID--ELGWEALLNTRGTTWRKLdetqrnAITDAAS 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488215050  75 TLKQMIvlfkEYPSLLRRPILIDE-KRILIGFNEDEIRSF 113
Cdd:PRK10853  79 AAALML----EQPAIIKRPLLCAPgKPMLLGFSESSYQQF 114
Glutaredoxin pfam00462
Glutaredoxin;
2-45 7.04e-06

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 40.95  E-value: 7.04e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 488215050    2 IKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKI 45
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKEL 44
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 2-45 1.10e-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: 1.10e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488215050   2 IKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKI 45
Cdd:cd02066    2 VVVFSKSTCPYCKRAKRLLESLGIEFEEIDILEDGELREELKEL 45
Uxx_star NF041212
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ...
 2-45 1.49e-04

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


Pssm-ID: 469116 [Multi-domain]  Cd Length: 70  Bit Score: 37.83  E-value: 1.49e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488215050   2 IKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKI 45
Cdd:NF041212   1 VVIYTKPGCPYCAAAKEDLARRGIPFEEIDVSKDPEALEEMLRL 44
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 2-32 1.79e-04

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: 37.57  E-value: 1.79e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 488215050   2 IKVYTSPSCTSCRKARAWLQANQLEFEEKNI 32
Cdd:cd03418    2 VEIYTKPNCPYCVRAKALLDKKGVDYEEIDV 32
PRK10026 PRK10026
arsenate reductase (glutaredoxin);
2-96 4.88e-04

arsenate reductase (glutaredoxin);


Pssm-ID: 182200  Cd Length: 141  Bit Score: 37.88  E-value: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215050   2 IKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKILAATEGGVQDIISTRSKIYEKLGIDFNELTLKQMIV 81
Cdd:PRK10026   4 ITIYHNPACGTSRNTLEMIRNSGTEPTIIHYLETPPTRDELVKLIADMGISVRALLRKNVEPYEELGLAEDKFTDDQLID 83

                         90
                 ....*....|....*
gi 488215050  82 LFKEYPSLLRRPILI 96
Cdd:PRK10026  84 FMLQHPILINRPIVV 98
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 2-29 2.87e-03

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: 34.41  E-value: 2.87e-03
                         10        20
                 ....*....|....*....|....*...
gi 488215050   2 IKVYTSPSCTSCRKARAWLQANQLEFEE 29
Cdd:cd03029    3 VSLFTKPGCPFCARAKAALQENGISYEE 30
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 2-45 6.11e-03

Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK subfamily, a member of the DsbA family). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxin 2 and stringent starvation protein A.


Pssm-ID: 238319 [Multi-domain]  Cd Length: 71  Bit Score: 33.31  E-value: 6.11e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488215050   2 IKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKI 45
Cdd:cd00570    1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEEFLAL 44
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 2-45 9.20e-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: 33.15  E-value: 9.20e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488215050   2 IKVYTSPSCTSCRKARAWLQANQLEFEEKNIFAEPLTESEIKKI 45
Cdd:cd03027    3 VTIYSRLGCEDCTAVRLFLREKGLPYVEINIDIFPERKAELEER 46
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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