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Conserved domains on  [gi|492542290|ref|WP_005879220|]
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MULTISPECIES: arsenate reductase family protein [Enterococcus]

Protein Classification

arsenate reductase family protein( domain architecture ID 10122556)

arsenate reductase (ArsC) family protein similar to Bacillus subtilis uncharacterized protein YusI and Geobacillus kaustophilus ArsC3, which is involved in arsenate reduction

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ArsC_like cd03036
Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a ...
2-113 2.77e-51

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: 157.40  E-value: 2.77e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290   2 YRFYWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLTHNEIPMRRLFNTSGMKYRELGLKDQIADFSVKKA 81
Cdd:cd03036    1 LKFYEYPKCSTCRKAKKWLDEHGVDYTAIDIVEEPPSKEELKKWLEKSGLPLKKFFNTSGKSYRELGLKDKLPSLSEEEA 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 492542290  82 SAVLSTDGMLIKRPLIVKDKQlVAIGFNEKTY 113
Cdd:cd03036   81 LELLSSDGMLIKRPFVVDDDK-VLVGFKEEEW 111
 
Name Accession Description Interval E-value
ArsC_like cd03036
Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a ...
2-113 2.77e-51

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: 157.40  E-value: 2.77e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290   2 YRFYWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLTHNEIPMRRLFNTSGMKYRELGLKDQIADFSVKKA 81
Cdd:cd03036    1 LKFYEYPKCSTCRKAKKWLDEHGVDYTAIDIVEEPPSKEELKKWLEKSGLPLKKFFNTSGKSYRELGLKDKLPSLSEEEA 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 492542290  82 SAVLSTDGMLIKRPLIVKDKQlVAIGFNEKTY 113
Cdd:cd03036   81 LELLSSDGMLIKRPFVVDDDK-VLVGFKEEEW 111
ArsC COG1393
Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and ...
1-117 2.43e-42

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


Pssm-ID: 441003  Cd Length: 115  Bit Score: 134.84  E-value: 2.43e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290   1 MYRFYWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLTHNEIPMRRLFNTSGMKYRELGLKDQiaDFSVKK 80
Cdd:COG1393    1 MITIYGNPNCSTSRKALAWLEEAGIEYEFIDYLKTPPTAEELKELLAKLGLGVEELLNTRGTTYRELGLKDK--ALSEEE 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 492542290  81 ASAVLSTDGMLIKRPLIVKDKQLVaIGFNEKTYEGVL 117
Cdd:COG1393   79 ALALMLEHPSLIKRPIVVTGDKAL-VGFPPEEVLALL 114
arsC_related TIGR01617
transcriptional regulator, Spx/MgsR family; This model represents a portion of the proteins ...
3-114 4.13e-38

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: 124.46  E-value: 4.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290    3 RFYWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLTHNEIPMRRLFNTSGMKYRELGLKDQIADFSVKKAS 82
Cdd:TIGR01617   2 KVYGSPNCTTCKKARRWLEANGIEYQFIDIGEDGPTREELLDILSLLEDGIDPLLNTRGQSYRALNTSNTFLDLSDKEAL 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 492542290   83 AVLSTDGMLIKRPLIVKDKQLVAIGFNEKTYE 114
Cdd:TIGR01617  82 ELLAEDPALLRRPLIVDTKNRLLIGFKSESIE 113
ArsC pfam03960
ArsC family; This family is related to glutaredoxins pfam00462.
5-114 1.06e-34

ArsC family; This family is related to glutaredoxins pfam00462.


Pssm-ID: 427617  Cd Length: 109  Bit Score: 115.39  E-value: 1.06e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290    5 YWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLTHNEIPMRRLFNTSGMKYRELGLkdQIADFSVKKASAV 84
Cdd:pfam03960   1 YGSPNCSTCRKALAWLEEHGIEYQEIDYLETPPSKEELKDILAKLGDGVEALLNTRGTTYRELNL--DKEDLSEDELLEL 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 492542290   85 LSTDGMLIKRPLIVKDKQLVaIGFNEKTYE 114
Cdd:pfam03960  79 ILEHPSLIRRPIVVDGGKLL-VGFNEEEIR 107
spxA PRK01655
transcriptional regulator Spx; Reviewed
1-110 9.51e-16

transcriptional regulator Spx; Reviewed


Pssm-ID: 179316  Cd Length: 131  Bit Score: 67.79  E-value: 9.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290   1 MYRFYWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLTHNEIPMRRLFNTSGMKYRELGLkdQIADFSVKK 80
Cdd:PRK01655   1 MVTLFTSPSCTSCRKAKAWLEEHDIPFTERNIFSSPLTIDEIKQILRMTEDGTDEIISTRSKVFQKLNV--DVESLSLQD 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 492542290  81 ASAVLSTDGMLIKRPLIVKDKQLvAIGFNE 110
Cdd:PRK01655  79 LIKLISDNPGLLRRPIIIDEKRL-QVGYNE 107
 
Name Accession Description Interval E-value
ArsC_like cd03036
Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a ...
2-113 2.77e-51

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: 157.40  E-value: 2.77e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290   2 YRFYWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLTHNEIPMRRLFNTSGMKYRELGLKDQIADFSVKKA 81
Cdd:cd03036    1 LKFYEYPKCSTCRKAKKWLDEHGVDYTAIDIVEEPPSKEELKKWLEKSGLPLKKFFNTSGKSYRELGLKDKLPSLSEEEA 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 492542290  82 SAVLSTDGMLIKRPLIVKDKQlVAIGFNEKTY 113
Cdd:cd03036   81 LELLSSDGMLIKRPFVVDDDK-VLVGFKEEEW 111
ArsC COG1393
Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and ...
1-117 2.43e-42

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


Pssm-ID: 441003  Cd Length: 115  Bit Score: 134.84  E-value: 2.43e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290   1 MYRFYWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLTHNEIPMRRLFNTSGMKYRELGLKDQiaDFSVKK 80
Cdd:COG1393    1 MITIYGNPNCSTSRKALAWLEEAGIEYEFIDYLKTPPTAEELKELLAKLGLGVEELLNTRGTTYRELGLKDK--ALSEEE 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 492542290  81 ASAVLSTDGMLIKRPLIVKDKQLVaIGFNEKTYEGVL 117
Cdd:COG1393   79 ALALMLEHPSLIKRPIVVTGDKAL-VGFPPEEVLALL 114
ArsC_family cd02977
Arsenate Reductase (ArsC) family; composed of TRX-fold arsenic reductases and similar proteins ...
4-108 6.24e-41

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: 131.08  E-value: 6.24e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290   4 FYWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLTHNEIPMRRLFNTSGMKYRELGLKDqIADFSVKKASA 83
Cdd:cd02977    3 IYGNPNCSTSRKALAWLEEHGIEYEFIDYLKEPPTKEELKELLAKLGLGVEDLFNTRGTPYRKLGLAD-KDELSDEEALE 81
                         90       100
                 ....*....|....*....|....*
gi 492542290  84 VLSTDGMLIKRPLIVKDKQLVaIGF 108
Cdd:cd02977   82 LMAEHPKLIKRPIVVDGDRLL-VGF 105
arsC_related TIGR01617
transcriptional regulator, Spx/MgsR family; This model represents a portion of the proteins ...
3-114 4.13e-38

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: 124.46  E-value: 4.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290    3 RFYWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLTHNEIPMRRLFNTSGMKYRELGLKDQIADFSVKKAS 82
Cdd:TIGR01617   2 KVYGSPNCTTCKKARRWLEANGIEYQFIDIGEDGPTREELLDILSLLEDGIDPLLNTRGQSYRALNTSNTFLDLSDKEAL 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 492542290   83 AVLSTDGMLIKRPLIVKDKQLVAIGFNEKTYE 114
Cdd:TIGR01617  82 ELLAEDPALLRRPLIVDTKNRLLIGFKSESIE 113
ArsC pfam03960
ArsC family; This family is related to glutaredoxins pfam00462.
5-114 1.06e-34

ArsC family; This family is related to glutaredoxins pfam00462.


Pssm-ID: 427617  Cd Length: 109  Bit Score: 115.39  E-value: 1.06e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290    5 YWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLTHNEIPMRRLFNTSGMKYRELGLkdQIADFSVKKASAV 84
Cdd:pfam03960   1 YGSPNCSTCRKALAWLEEHGIEYQEIDYLETPPSKEELKDILAKLGDGVEALLNTRGTTYRELNL--DKEDLSEDELLEL 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 492542290   85 LSTDGMLIKRPLIVKDKQLVaIGFNEKTYE 114
Cdd:pfam03960  79 ILEHPSLIRRPIVVDGGKLL-VGFNEEEIR 107
ArsC_Spx cd03032
Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding ...
1-110 2.63e-23

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: 86.53  E-value: 2.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290   1 MYRFYWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLTHNEIPMRRLFNTSGMKYRELGLKdqIADFSVKK 80
Cdd:cd03032    1 MIKLYTSPSCSSCRKAKQWLEEHQIPFEERNLFKQPLTKEELKEILSLTENGVEDIISTRSKAFKNLNID--IDELSLSE 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 492542290  81 ASAVLSTDGMLIKRPLIVKDKQLVaIGFNE 110
Cdd:cd03032   79 LIRLISEHPSLLRRPIIIDEKRLQ-IGYNE 107
ArsC_Yffb cd03035
Arsenate Reductase (ArsC) family, Yffb subfamily; Yffb is an uncharacterized bacterial protein ...
5-110 6.09e-21

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: 80.33  E-value: 6.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290   5 YWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLThnEIPMRRLFNTSGMKYRELGLKDQiADFSVKKASAV 84
Cdd:cd03035    4 YGIKNCDTVKKARKWLEARGVAYTFHDYRKDGLDAATLERWLA--KVGWETLLNKRGTTWRKLDDAQK-AALDAAKAIAL 80
                         90       100
                 ....*....|....*....|....*.
gi 492542290  85 LSTDGMLIKRPLIVKDKQlVAIGFNE 110
Cdd:cd03035   81 MLEHPSLIKRPVLETGGK-VLVGFSE 105
spxA PRK01655
transcriptional regulator Spx; Reviewed
1-110 9.51e-16

transcriptional regulator Spx; Reviewed


Pssm-ID: 179316  Cd Length: 131  Bit Score: 67.79  E-value: 9.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290   1 MYRFYWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLTHNEIPMRRLFNTSGMKYRELGLkdQIADFSVKK 80
Cdd:PRK01655   1 MVTLFTSPSCTSCRKAKAWLEEHDIPFTERNIFSSPLTIDEIKQILRMTEDGTDEIISTRSKVFQKLNV--DVESLSLQD 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 492542290  81 ASAVLSTDGMLIKRPLIVKDKQLvAIGFNE 110
Cdd:PRK01655  79 LIKLISDNPGLLRRPIIIDEKRL-QVGYNE 107
PRK10853 PRK10853
putative reductase; Provisional
1-114 2.34e-14

putative reductase; Provisional


Pssm-ID: 182780  Cd Length: 118  Bit Score: 63.91  E-value: 2.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290   1 MYRFYWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLthNEIPMRRLFNTSGMKYREL--GLKDQIADFSV 78
Cdd:PRK10853   1 MVTLYGIKNCDTIKKARRWLEAQGIDYRFHDYRVDGLDSELLQGFI--DELGWEALLNTRGTTWRKLdeTQRNAITDAAS 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 492542290  79 kkASAVLSTDGMLIKRPLIVKDKQLVAIGFNEKTYE 114
Cdd:PRK10853  79 --AAALMLEQPAIIKRPLLCAPGKPMLLGFSESSYQ 112
ArsC_ArsC cd03034
Arsenate Reductase (ArsC) family, ArsC subfamily; arsenic reductases similar to that encoded ...
3-107 1.93e-12

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: 58.75  E-value: 1.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290   3 RFYWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLTHNEIPMRRLFNTSGMKYRELGLKDQiaDFSVKKAS 82
Cdd:cd03034    2 TIYHNPRCSKSRNALALLEEAGIEPEIVEYLKTPPTAAELRELLAKLGISPRDLLRTKEAPYKELGLADP--ELSDEELI 79
                         90       100
                 ....*....|....*....|....*
gi 492542290  83 AVLSTDGMLIKRPLIVKDKQlVAIG 107
Cdd:cd03034   80 DAMAAHPILIERPIVVTGDG-AVLG 103
PRK12559 PRK12559
transcriptional regulator Spx; Provisional
1-111 1.04e-11

transcriptional regulator Spx; Provisional


Pssm-ID: 79035  Cd Length: 131  Bit Score: 57.42  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290   1 MYRFYWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLTHNEIPMRRLFNTSGMKYRELGLkdQIADFSVKK 80
Cdd:PRK12559   1 MVVLYTTASCASCRKAKAWLEENQIDYTEKNIVSNSMTVDELKSILRLTEEGATEIISTRSKTFQDLNI--NIEELSLNE 78
                         90       100       110
                 ....*....|....*....|....*....|.
gi 492542290  81 ASAVLSTDGMLIKRPLIVKDKQLvAIGFNEK 111
Cdd:PRK12559  79 FYKLIIEHPLMLRRPIMLDEKRL-QIGFNDE 108
spxA PRK13344
transcriptional regulator Spx; Reviewed
1-110 6.40e-11

transcriptional regulator Spx; Reviewed


Pssm-ID: 183988  Cd Length: 132  Bit Score: 55.36  E-value: 6.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290   1 MYRFYWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLTHNEIPMRRLFNTSGMKYRELGLkdQIADFSVKK 80
Cdd:PRK13344   1 MIKIYTISSCTSCKKAKTWLNAHQLSYKEQNLGKEPLTKEEILAILTKTENGIESIVSSKNRYAKALDC--DIEELSVNE 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 492542290  81 ASAVLSTDGMLIKRPLIVKDKQLvAIGFNE 110
Cdd:PRK13344  79 VIDLIQENPRILKSPILIDDKRL-QVGYKE 107
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
5-35 3.65e-06

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 41.72  E-value: 3.65e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 492542290   5 YWYPKCSTCKKAKAWLDAHHIDYQVVDMIAD 35
Cdd:COG0695    5 YTTPGCPYCARAKRLLDEKGIPYEEIDVDED 35
ArsC_15kD cd03033
Arsenate Reductase (ArsC) family, 15kD protein subfamily; composed of proteins of unknown ...
4-108 2.78e-05

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: 40.34  E-value: 2.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542290   4 FYWYPKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLthNEIPMRRLFNTSG--MKYRELGLKdqiaDFSVKKA 81
Cdd:cd03033    4 FYEKPGCANNARQKALLEAAGHEVEVRDLLTEPWTAETLRPFF--GDLPVAEWFNPAAprVKSGEVVPE----ALDEEEA 77
                         90       100
                 ....*....|....*....|....*...
gi 492542290  82 SAVLSTDGMLIKRPLI-VKDKQLVaiGF 108
Cdd:cd03033   78 LALMIADPLLIRRPLMqVGDRRMV--GF 103
GST_N_mPGES2 cd03040
GST_N family; microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a ...
3-78 6.25e-04

GST_N family; microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a membrane-anchored dimeric protein containing a CXXC motif which catalyzes the isomerization of PGH2 to PGE2. Unlike cytosolic PGE synthase (cPGES) and microsomal PGES Type 1 (mPGES1), mPGES2 does not require glutathione (GSH) for its activity, although its catalytic rate is increased two- to four-fold in the presence of DTT, GSH or other thiol compounds. PGE2 is widely distributed in various tissues and is implicated in the sleep/wake cycle, relaxation/contraction of smooth muscle, excretion of sodium ions, maintenance of body temperature and mediation of inflammation. mPGES2 contains an N-terminal hydrophobic domain which is membrane associated, and a C-terminal soluble domain with a GST-like structure.


Pssm-ID: 239338  Cd Length: 77  Bit Score: 35.85  E-value: 6.25e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492542290   3 RFYWYPKCSTCKKAKAWLDAHHIDYQVVDMiadTPSAETIEEWLTHNEIPMrrlfntsgMKYRELGLKDQIADFSV 78
Cdd:cd03040    3 TLYQYKTCPFCCKVRAFLDYHGIPYEVVEV---NPVSRKEIKWSSYKKVPI--------LRVESGGDGQQLVDSSV 67
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
8-52 7.76e-04

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: 35.66  E-value: 7.76e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 492542290   8 PKCSTCKKAKAWLDAHHIDYQVVDMIADTPSAETIEEWLTHNEIP 52
Cdd:cd02976    8 PDCPYCKATKRFLDERGIPFEEVDVDEDPEALEELKKLNGYRSVP 52
Glutaredoxin pfam00462
Glutaredoxin;
5-31 3.11e-03

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 33.63  E-value: 3.11e-03
                          10        20
                  ....*....|....*....|....*..
gi 492542290    5 YWYPKCSTCKKAKAWLDAHHIDYQVVD 31
Cdd:pfam00462   4 YTKPTCPFCKRAKRLLKSLGVDFEEID 30
 
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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