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Conserved domains on  [gi|1248243682|ref|WP_096739706|]
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MULTISPECIES: ArsC family reductase [Pseudoalteromonas]

Protein Classification

arsenate reductase( domain architecture ID 10122554)

glutathione dependent arsenate reductase family, Yffb subfamily protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ArsC_Yffb cd03035
Arsenate Reductase (ArsC) family, Yffb subfamily; Yffb is an uncharacterized bacterial protein ...
 2-106 2.57e-56

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: 169.70  E-value: 2.57e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248243682   2 ITLYGISNCDTIKKAKKYLADNNIDFTFHDYRKDGVNEQLVSEFAEHIDWEQLVNKRGTTYRALADEQKQNLNKDTAITL 81
Cdd:cd03035     1 ITLYGIKNCDTVKKARKWLEARGVAYTFHDYRKDGLDAATLERWLAKVGWETLLNKRGTTWRKLDDAQKAALDAAKAIAL 80

                          90       100
                  ....*....|....*....|....*
gi 1248243682  82 LVEQPAMIKRPVLVNNNSYHLGFKA 106
Cdd:cd03035    81 MLEHPSLIKRPVLETGGKVLVGFSE 105
 
Name Accession Description Interval E-value
ArsC_Yffb cd03035
Arsenate Reductase (ArsC) family, Yffb subfamily; Yffb is an uncharacterized bacterial protein ...
 2-106 2.57e-56

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: 169.70  E-value: 2.57e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248243682   2 ITLYGISNCDTIKKAKKYLADNNIDFTFHDYRKDGVNEQLVSEFAEHIDWEQLVNKRGTTYRALADEQKQNLNKDTAITL 81
Cdd:cd03035     1 ITLYGIKNCDTVKKARKWLEARGVAYTFHDYRKDGLDAATLERWLAKVGWETLLNKRGTTWRKLDDAQKAALDAAKAIAL 80

                          90       100
                  ....*....|....*....|....*
gi 1248243682  82 LVEQPAMIKRPVLVNNNSYHLGFKA 106
Cdd:cd03035    81 MLEHPSLIKRPVLETGGKVLVGFSE 105
PRK10853 PRK10853
putative reductase; Provisional
 1-113 7.64e-47

putative reductase; Provisional


Pssm-ID: 182780  Cd Length: 118  Bit Score: 146.35  E-value: 7.64e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248243682   1 MITLYGISNCDTIKKAKKYLADNNIDFTFHDYRKDGVNEQLVSEFAEHIDWEQLVNKRGTTYRALADEQKQNLNK-DTAI 79
Cdd:PRK10853    1 MVTLYGIKNCDTIKKARRWLEAQGIDYRFHDYRVDGLDSELLQGFIDELGWEALLNTRGTTWRKLDETQRNAITDaASAA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1248243682  80 TLLVEQPAMIKRPVLVN-NNSYHLGFKAAQYDEIF 113
Cdd:PRK10853   81 ALMLEQPAIIKRPLLCApGKPMLLGFSESSYQQFF 115
ArsC COG1393
Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and ...
 1-114 4.75e-44

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


Pssm-ID: 441003  Cd Length: 115  Bit Score: 139.07  E-value: 4.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248243682   1 MITLYGISNCDTIKKAKKYLADNNIDFTFHDYRKDGVNEQLVSEFAE--HIDWEQLVNKRGTTYRALADEQKqNLNKDTA 78
Cdd:COG1393     1 MITIYGNPNCSTSRKALAWLEEAGIEYEFIDYLKTPPTAEELKELLAklGLGVEELLNTRGTTYRELGLKDK-ALSEEEA 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1248243682  79 ITLLVEQPAMIKRPVLVNNNSYHLGFKAAQYDEIFK 114
Cdd:COG1393    80 LALMLEHPSLIKRPIVVTGDKALVGFPPEEVLALLG 115
ArsC pfam03960
ArsC family; This family is related to glutaredoxins pfam00462.
 5-112 9.34e-33

ArsC family; This family is related to glutaredoxins pfam00462.


Pssm-ID: 427617  Cd Length: 109  Bit Score: 110.38  E-value: 9.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248243682   5 YGISNCDTIKKAKKYLADNNIDFTFHDYRKDGVNEQLVSEFAE--HIDWEQLVNKRGTTYRALaDEQKQNLNKDTAITLL 82
Cdd:pfam03960   1 YGSPNCSTCRKALAWLEEHGIEYQEIDYLETPPSKEELKDILAklGDGVEALLNTRGTTYREL-NLDKEDLSEDELLELI 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1248243682  83 VEQPAMIKRPVLVNNNSYHLGFKAAQYDEI 112
Cdd:pfam03960  80 LEHPSLIRRPIVVDGGKLLVGFNEEEIRAF 109
arsC_related TIGR01617
transcriptional regulator, Spx/MgsR family; This model represents a portion of the proteins ...
 2-114 3.34e-26

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: 94.03  E-value: 3.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248243682   2 ITLYGISNCDTIKKAKKYLADNNIDFTFHDYRKDGVNEQLVSEFAE--HIDWEQLVNKRGTTYRALADEQK-QNLNKDTA 78
Cdd:TIGR01617   1 IKVYGSPNCTTCKKARRWLEANGIEYQFIDIGEDGPTREELLDILSllEDGIDPLLNTRGQSYRALNTSNTfLDLSDKEA 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1248243682  79 ITLLVEQPAMIKRPVLV-NNNSYHLGFKAAQYdEIFK 114
Cdd:TIGR01617  81 LELLAEDPALLRRPLIVdTKNRLLIGFKSESI-EEFK 116
 
Name Accession Description Interval E-value
ArsC_Yffb cd03035
Arsenate Reductase (ArsC) family, Yffb subfamily; Yffb is an uncharacterized bacterial protein ...
 2-106 2.57e-56

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: 169.70  E-value: 2.57e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248243682   2 ITLYGISNCDTIKKAKKYLADNNIDFTFHDYRKDGVNEQLVSEFAEHIDWEQLVNKRGTTYRALADEQKQNLNKDTAITL 81
Cdd:cd03035     1 ITLYGIKNCDTVKKARKWLEARGVAYTFHDYRKDGLDAATLERWLAKVGWETLLNKRGTTWRKLDDAQKAALDAAKAIAL 80

                          90       100
                  ....*....|....*....|....*
gi 1248243682  82 LVEQPAMIKRPVLVNNNSYHLGFKA 106
Cdd:cd03035    81 MLEHPSLIKRPVLETGGKVLVGFSE 105
PRK10853 PRK10853
putative reductase; Provisional
 1-113 7.64e-47

putative reductase; Provisional


Pssm-ID: 182780  Cd Length: 118  Bit Score: 146.35  E-value: 7.64e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248243682   1 MITLYGISNCDTIKKAKKYLADNNIDFTFHDYRKDGVNEQLVSEFAEHIDWEQLVNKRGTTYRALADEQKQNLNK-DTAI 79
Cdd:PRK10853    1 MVTLYGIKNCDTIKKARRWLEAQGIDYRFHDYRVDGLDSELLQGFIDELGWEALLNTRGTTWRKLDETQRNAITDaASAA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1248243682  80 TLLVEQPAMIKRPVLVN-NNSYHLGFKAAQYDEIF 113
Cdd:PRK10853   81 ALMLEQPAIIKRPLLCApGKPMLLGFSESSYQQFF 115
ArsC COG1393
Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and ...
 1-114 4.75e-44

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


Pssm-ID: 441003  Cd Length: 115  Bit Score: 139.07  E-value: 4.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248243682   1 MITLYGISNCDTIKKAKKYLADNNIDFTFHDYRKDGVNEQLVSEFAE--HIDWEQLVNKRGTTYRALADEQKqNLNKDTA 78
Cdd:COG1393     1 MITIYGNPNCSTSRKALAWLEEAGIEYEFIDYLKTPPTAEELKELLAklGLGVEELLNTRGTTYRELGLKDK-ALSEEEA 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1248243682  79 ITLLVEQPAMIKRPVLVNNNSYHLGFKAAQYDEIFK 114
Cdd:COG1393    80 LALMLEHPSLIKRPIVVTGDKALVGFPPEEVLALLG 115
ArsC_family cd02977
Arsenate Reductase (ArsC) family; composed of TRX-fold arsenic reductases and similar proteins ...
 2-104 6.97e-38

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: 123.37  E-value: 6.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248243682   2 ITLYGISNCDTIKKAKKYLADNNIDFTFHDYRKDGVNEQLVSEFAE--HIDWEQLVNKRGTTYRALADEQKQNLNKDTAI 79
Cdd:cd02977     1 ITIYGNPNCSTSRKALAWLEEHGIEYEFIDYLKEPPTKEELKELLAklGLGVEDLFNTRGTPYRKLGLADKDELSDEEAL 80

                          90       100
                  ....*....|....*....|....*
gi 1248243682  80 TLLVEQPAMIKRPVLVNNNSYHLGF 104
Cdd:cd02977    81 ELMAEHPKLIKRPIVVDGDRLLVGF 105
ArsC pfam03960
ArsC family; This family is related to glutaredoxins pfam00462.
 5-112 9.34e-33

ArsC family; This family is related to glutaredoxins pfam00462.


Pssm-ID: 427617  Cd Length: 109  Bit Score: 110.38  E-value: 9.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248243682   5 YGISNCDTIKKAKKYLADNNIDFTFHDYRKDGVNEQLVSEFAE--HIDWEQLVNKRGTTYRALaDEQKQNLNKDTAITLL 82
Cdd:pfam03960   1 YGSPNCSTCRKALAWLEEHGIEYQEIDYLETPPSKEELKDILAklGDGVEALLNTRGTTYREL-NLDKEDLSEDELLELI 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1248243682  83 VEQPAMIKRPVLVNNNSYHLGFKAAQYDEI 112
Cdd:pfam03960  80 LEHPSLIRRPIVVDGGKLLVGFNEEEIRAF 109
arsC_related TIGR01617
transcriptional regulator, Spx/MgsR family; This model represents a portion of the proteins ...
 2-114 3.34e-26

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: 94.03  E-value: 3.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248243682   2 ITLYGISNCDTIKKAKKYLADNNIDFTFHDYRKDGVNEQLVSEFAE--HIDWEQLVNKRGTTYRALADEQK-QNLNKDTA 78
Cdd:TIGR01617   1 IKVYGSPNCTTCKKARRWLEANGIEYQFIDIGEDGPTREELLDILSllEDGIDPLLNTRGQSYRALNTSNTfLDLSDKEA 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1248243682  79 ITLLVEQPAMIKRPVLV-NNNSYHLGFKAAQYdEIFK 114
Cdd:TIGR01617  81 LELLAEDPALLRRPLIVdTKNRLLIGFKSESI-EEFK 116
ArsC_like cd03036
Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a ...
 2-109 7.38e-15

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: 64.96  E-value: 7.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248243682   2 ITLYGISNCDTIKKAKKYLADNNIDFTFHDYRKDGVNEQLVSEFAEHIDWE--QLVNKRGTTYRAL-ADEQKQNLNKDTA 78
Cdd:cd03036     1 LKFYEYPKCSTCRKAKKWLDEHGVDYTAIDIVEEPPSKEELKKWLEKSGLPlkKFFNTSGKSYRELgLKDKLPSLSEEEA 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1248243682  79 ITLLVEQPAMIKRPVLVNNNSYHLGFKAAQY 109
Cdd:cd03036    81 LELLSSDGMLIKRPFVVDDDKVLVGFKEEEW 111
ArsC_Spx cd03032
Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding ...
 1-112 7.73e-12

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: 57.25  E-value: 7.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248243682   1 MITLYGISNCDTIKKAKKYLADNNIDFTFHDYRKDGVNEQLVSE---FAEHiDWEQLVNKRGTTYRALA---DEqkqnLN 74
Cdd:cd03032     1 MIKLYTSPSCSSCRKAKQWLEEHQIPFEERNLFKQPLTKEELKEilsLTEN-GVEDIISTRSKAFKNLNidiDE----LS 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1248243682  75 KDTAITLLVEQPAMIKRPVLVNNNSYHLGFKAaqyDEI 112
Cdd:cd03032    76 LSELIRLISEHPSLLRRPIIIDEKRLQIGYNE---DEI 110
ArsC_ArsC cd03034
Arsenate Reductase (ArsC) family, ArsC subfamily; arsenic reductases similar to that encoded ...
 2-103 4.44e-09

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: 49.89  E-value: 4.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248243682   2 ITLYGISNCDTIKKAKKYLADNNIDFTFHDYRKDGVN-EQLVSEFAE-HIDWEQLVNKRGTTY--RALADeqkQNLNKDT 77
Cdd:cd03034     1 ITIYHNPRCSKSRNALALLEEAGIEPEIVEYLKTPPTaAELRELLAKlGISPRDLLRTKEAPYkeLGLAD---PELSDEE 77

                          90       100
                  ....*....|....*....|....*.
gi 1248243682  78 AITLLVEQPAMIKRPVLVNNNSYHLG 103
Cdd:cd03034    78 LIDAMAAHPILIERPIVVTGDGAVLG 103
spxA PRK13344
transcriptional regulator Spx; Reviewed
 1-105 5.11e-08

transcriptional regulator Spx; Reviewed


Pssm-ID: 183988  Cd Length: 132  Bit Score: 47.65  E-value: 5.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248243682   1 MITLYGISNCDTIKKAKKYLADNNIDFTFHDYRKDGVNEQLVSEFAEHID--WEQLVNKRGTTYRALaDEQKQNLNKDTA 78
Cdd:PRK13344    1 MIKIYTISSCTSCKKAKTWLNAHQLSYKEQNLGKEPLTKEEILAILTKTEngIESIVSSKNRYAKAL-DCDIEELSVNEV 79

                          90       100
                  ....*....|....*....|....*..
gi 1248243682  79 ITLLVEQPAMIKRPVLVNNNSYHLGFK 105
Cdd:PRK13344   80 IDLIQENPRILKSPILIDDKRLQVGYK 106
PRK12559 PRK12559
transcriptional regulator Spx; Provisional
 1-104 9.84e-08

transcriptional regulator Spx; Provisional


Pssm-ID: 79035  Cd Length: 131  Bit Score: 47.02  E-value: 9.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248243682   1 MITLYGISNCDTIKKAKKYLADNNIDFTfhdyRKDGVNEQLVSEFAEHI------DWEQLVNKRGTTYRALaDEQKQNLN 74
Cdd:PRK12559    1 MVVLYTTASCASCRKAKAWLEENQIDYT----EKNIVSNSMTVDELKSIlrlteeGATEIISTRSKTFQDL-NINIEELS 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 1248243682  75 KDTAITLLVEQPAMIKRPVLVNNNSYHLGF 104
Cdd:PRK12559   76 LNEFYKLIIEHPLMLRRPIMLDEKRLQIGF 105
spxA PRK01655
transcriptional regulator Spx; Reviewed
 1-112 1.18e-07

transcriptional regulator Spx; Reviewed


Pssm-ID: 179316  Cd Length: 131  Bit Score: 46.60  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248243682   1 MITLYGISNCDTIKKAKKYLADNNIDFTFHDYRKDGVNEQLVSEFAEHID--WEQLVNKRGTTYraladeQKQNLNKD-- 76
Cdd:PRK01655    1 MVTLFTSPSCTSCRKAKAWLEEHDIPFTERNIFSSPLTIDEIKQILRMTEdgTDEIISTRSKVF------QKLNVDVEsl 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1248243682  77 ---TAITLLVEQPAMIKRPVLVNNNSYHLGFKAaqyDEI 112
Cdd:PRK01655   75 slqDLIKLISDNPGLLRRPIIIDEKRLQVGYNE---DEI 110
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 1-35 5.70e-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: 5.70e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1248243682   1 MITLYGISNCDTIKKAKKYLADNNIDFTFHDYRKD 35
Cdd:cd02976     1 EVTVYTKPDCPYCKATKRFLDERGIPFEEVDVDED 35
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
1-35 2.79e-03

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 34.02  E-value: 2.79e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1248243682   1 MITLYGISNCDTIKKAKKYLADNNIDFTFHDYRKD 35
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDED 35
 
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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