NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|937117545|ref|WP_054554876|]
View 

MULTISPECIES: peroxiredoxin-like family protein [Pseudoalteromonas]

Protein Classification

peroxiredoxin-like family protein( domain architecture ID 10121943)

peroxiredoxin (PRX)-like family protein containing a CXXC motif, with the second cysteine in the motif corresponding to the peroxidatic cysteine of PRX, however, it does not contain the other two residues of the catalytic triad of PRXs; similar to vertebrate peroxiredoxin-like 2A, 2B (prostamide/prostaglandin F synthase) and 2C

CATH:  3.40.30.10
PubMed:  15518547|12517450|10049365
SCOP:  3000031

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 41-185 2.17e-27

Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs 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. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.


:

Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 101.28  E-value: 2.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545  41 VPNIELKDQYGKTVSLAERFKEKTTVLIVYRGGWCPYCSKQLANVQKIEKELADLGAQIIAVSPDSPEKL-AESKITSPN 119
Cdd:cd02970    2 APDFELPDAGGETVTLSALLGEGPVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGPESPEKLeAFDKGKFLP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937117545 120 YQLLSDDSLLLAQKLGLAFYLDDKTAKIY--RNKLGVNFVSLEGEVkvaLPVPAVFVIDTNGLVNFQY 185
Cdd:cd02970   82 FPVYADPDRKLYRALGLVRSLPWSNTPRAlwKNAAIGFRGNDEGDG---LQLPGVFVIGPDGTILFAH 146
 
Name Accession Description Interval E-value
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 41-185 2.17e-27

Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs 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. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.


Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 101.28  E-value: 2.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545  41 VPNIELKDQYGKTVSLAERFKEKTTVLIVYRGGWCPYCSKQLANVQKIEKELADLGAQIIAVSPDSPEKL-AESKITSPN 119
Cdd:cd02970    2 APDFELPDAGGETVTLSALLGEGPVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGPESPEKLeAFDKGKFLP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937117545 120 YQLLSDDSLLLAQKLGLAFYLDDKTAKIY--RNKLGVNFVSLEGEVkvaLPVPAVFVIDTNGLVNFQY 185
Cdd:cd02970   82 FPVYADPDRKLYRALGLVRSLPWSNTPRAlwKNAAIGFRGNDEGDG---LQLPGVFVIGPDGTILFAH 146
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 37-181 7.62e-25

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 94.21  E-value: 7.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545   37 PGLAVPNIELKDQYGKTVSLAErFKEKTTVLIVYRGGWCPYCSKQLANVQKIEKELADLGAQIIAVSPDSPEKLAEskit 116
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSD-YRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKA---- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937117545  117 spnyqllsddsllLAQKLGLAF-YLDDKTAKIYRnKLGVNFvslegeVKVALPVPAVFVIDTNGLV 181
Cdd:pfam00578  76 -------------FAEKYGLPFpLLSDPDGEVAR-AYGVLN------EEEGGALRATFVIDPDGKV 121
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
41-205 1.02e-24

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 94.16  E-value: 1.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545  41 VPNIELKDQYGKTVSLAErFKEKTTVLIVYrGGWCPYCSKQLANVQKIEKELADLGAQIIAVSPDSPEKLAEskitspny 120
Cdd:COG1225    1 APDFTLPDLDGKTVSLSD-LRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKK-------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545 121 qllsddsllLAQKLGLAF-YLDDKTAKIYRnKLGVNFvslegevkvalpVPAVFVIDTNGLVNFQYANPNYKVRLTEDLL 199
Cdd:COG1225   71 ---------FAEKYGLPFpLLSDPDGEVAK-AYGVRG------------TPTTFLIDPDGKIRYVWVGPVDPRPHLEEVL 128


                 ....*.
gi 937117545 200 LAAVKS 205
Cdd:COG1225  129 EALLAE 134
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 33-111 7.05e-09

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 52.63  E-value: 7.05e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937117545  33 SPLLPGLAVPNIELKDQYGKTVSLAErFKEKTTVLIVYRGGWCPYCSKQLANVQKIEKELADLGAQIIAVSPDSPEKLA 111
Cdd:PRK09437   2 NPLKAGDIAPKFSLPDQDGEQVSLTD-FQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLS 79
 
Name Accession Description Interval E-value
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 41-185 2.17e-27

Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs 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. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.


Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 101.28  E-value: 2.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545  41 VPNIELKDQYGKTVSLAERFKEKTTVLIVYRGGWCPYCSKQLANVQKIEKELADLGAQIIAVSPDSPEKL-AESKITSPN 119
Cdd:cd02970    2 APDFELPDAGGETVTLSALLGEGPVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGPESPEKLeAFDKGKFLP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937117545 120 YQLLSDDSLLLAQKLGLAFYLDDKTAKIY--RNKLGVNFVSLEGEVkvaLPVPAVFVIDTNGLVNFQY 185
Cdd:cd02970   82 FPVYADPDRKLYRALGLVRSLPWSNTPRAlwKNAAIGFRGNDEGDG---LQLPGVFVIGPDGTILFAH 146
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 37-181 7.62e-25

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 94.21  E-value: 7.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545   37 PGLAVPNIELKDQYGKTVSLAErFKEKTTVLIVYRGGWCPYCSKQLANVQKIEKELADLGAQIIAVSPDSPEKLAEskit 116
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSD-YRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKA---- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937117545  117 spnyqllsddsllLAQKLGLAF-YLDDKTAKIYRnKLGVNFvslegeVKVALPVPAVFVIDTNGLV 181
Cdd:pfam00578  76 -------------FAEKYGLPFpLLSDPDGEVAR-AYGVLN------EEEGGALRATFVIDPDGKV 121
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
41-205 1.02e-24

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 94.16  E-value: 1.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545  41 VPNIELKDQYGKTVSLAErFKEKTTVLIVYrGGWCPYCSKQLANVQKIEKELADLGAQIIAVSPDSPEKLAEskitspny 120
Cdd:COG1225    1 APDFTLPDLDGKTVSLSD-LRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKK-------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545 121 qllsddsllLAQKLGLAF-YLDDKTAKIYRnKLGVNFvslegevkvalpVPAVFVIDTNGLVNFQYANPNYKVRLTEDLL 199
Cdd:COG1225   71 ---------FAEKYGLPFpLLSDPDGEVAK-AYGVRG------------TPTTFLIDPDGKIRYVWVGPVDPRPHLEEVL 128


                 ....*.
gi 937117545 200 LAAVKS 205
Cdd:COG1225  129 EALLAE 134
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 41-199 6.13e-16

Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins originally known as bacterioferritin comigratory proteins (BCP), based on their electrophoretic mobility before their function was identified. PRXs are thiol-specific antioxidant (TSA) proteins also known as TRX peroxidases and alkyl hydroperoxide reductase C22 (AhpC) proteins. They 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 TRX, glutathione, trypanothione and AhpF. They are distinct from other peroxidases in that they have no cofactors such as metals or prosthetic groups. The first step of catalysis, common to all PRXs, is the nucleophilic attack by the catalytic cysteine (also known as the peroxidatic cysteine) on the peroxide leading to cleavage of the oxygen-oxygen bond and the formation of a cysteine sulfenic acid intermediate. The second step of the reaction, the resolution of the intermediate, distinguishes the different types of PRXs. The presence or absence of a second cysteine (the resolving cysteine) classifies PRXs as either belonging to the 2-cys or 1-cys type. The resolving cysteine of 2-cys PRXs is either on the same chain (atypical) or on the second chain (typical) of a functional homodimer. Structural and motif analysis of this growing family supports the need for a new classification system. The peroxidase activity of PRXs is regulated in vivo by irreversible cysteine over-oxidation into a sulfinic acid, phosphorylation and limited proteolysis.


Pssm-ID: 239269 [Multi-domain]  Cd Length: 140  Bit Score: 71.43  E-value: 6.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545  41 VPNIELKDQYGKTVSLAErFKEKTTVLIVYRGGWCPYCSKQLANVQKIEKELADLGAQIIAVSPDSPEKLAE--SKITSP 118
Cdd:cd02971    2 APDFTLPATDGGEVSLSD-FKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAwaEKEGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545 119 NYQLlsddslllaqklglafyLDDKTAKIyRNKLGVNFvslEGEVKVALPVPAVFVIDTNGLVNFQYANPNYKVRLTEDL 198
Cdd:cd02971   81 NFPL-----------------LSDPDGEF-AKAYGVLI---EKSAGGGLAARATFIIDPDGKIRYVEVEPLPTGRNAEEL 139


                 .
gi 937117545 199 L 199
Cdd:cd02971  140 L 140
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 35-193 1.09e-13

Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium tuberculosis AhpE. AhpE is described as a 1-cys PRX because of the absence of a resolving cysteine. The structure and sequence of AhpE, however, show greater similarity to 2-cys PRXs than 1-cys PRXs. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective 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. The first step of catalysis is the nucleophilic attack by the peroxidatic cysteine on the peroxide leading to the formation of a cysteine sulfenic acid intermediate. The absence of a resolving cysteine suggests that functional AhpE is regenerated by an external reductant. The solution behavior and crystal structure of AhpE show that it forms dimers and octamers.


Pssm-ID: 239316 [Multi-domain]  Cd Length: 149  Bit Score: 65.76  E-value: 1.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545  35 LLPGLAVPNIELKDQYGKTVSLAERFKEKTTVLIVYRGGWCPYCSKQLANVQKIEKELADLGAQIIAVSPDSPEKLAEsk 114
Cdd:cd03018    1 LEVGDKAPDFELPDQNGQEVRLSEFRGRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRA-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545 115 itspnyqllsddsllLAQKLGLAF-YLDD-----KTAKIYrnklGVnFVSLEGevkvaLPVPAVFVIDTNGLVNFQYANP 188
Cdd:cd03018   79 ---------------WAEENGLTFpLLSDfwphgEVAKAY----GV-FDEDLG-----VAERAVFVIDRDGIIRYAWVSD 133


                 ....*
gi 937117545 189 NYKVR 193
Cdd:cd03018  134 DGEPR 138
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 37-192 1.42e-13

Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 65.08  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545   37 PGLAVPNIELKD--QYGKTVSLAErFKEKTTVLIVYRGGWCPYCSKQLANVQKIEKELADLGAQIIAVSPDSPEKLAESK 114
Cdd:pfam08534   2 AGDKAPDFTLPDaaTDGNTVSLSD-FKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAFFVKRF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937117545  115 ITspnyqllsddslllaqKLGLAF-YLDDKTAKIYRNkLGVNFVSLEGEVKVAlpvPAVFVIDTNGLVNFQYANPNYKV 192
Cdd:pfam08534  81 WG----------------KEGLPFpFLSDGNAAFTKA-LGLPIEEDASAGLRS---PRYAVIDEDGKVVYLFVGPEPGV 139
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 40-181 1.10e-12

Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of thioredoxin-dependent thiol peroxidases, widely expressed in pathogenic bacteria, that protect cells against toxicity from reactive oxygen species by reducing and detoxifying hydroperoxides. The protein was named BCP based on its electrophoretic mobility before its function was known. BCP shows substrate selectivity toward fatty acid hydroperoxides rather than hydrogen peroxide or alkyl hydroperoxides. BCP contains the peroxidatic cysteine but appears not to possess a resolving cysteine (some sequences, not all, contain a second cysteine but its role is still unknown). Unlike other PRXs, BCP exists as a monomer. The plant homolog of BCP is PRX Q, which is expressed only in leaves and is cellularly localized in the chloroplasts and the guard cells of stomata. Also included in this subfamily is the fungal nuclear protein, Dot5p (for disrupter of telomere silencing protein 5), which functions as an alkyl-hydroperoxide reductase during post-diauxic growth.


Pssm-ID: 239315  Cd Length: 140  Bit Score: 62.57  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545  40 AVPNIELKDQYGKTVSLAErFKEKTTVLIVYRGGWCPYCSKQLANVQKIEKELADLGAQIIAVSPDSPEKLAEskitspn 119
Cdd:cd03017    2 KAPDFTLPDQDGETVSLSD-LRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAK------- 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937117545 120 yqllsddsllLAQKLGLAF-YLDDKTAKIyRNKLGvnfVSLEGEVKVALPVPAVFVIDTNGLV 181
Cdd:cd03017   74 ----------FAEKYGLPFpLLSDPDGKL-AKAYG---VWGEKKKKYMGIERSTFLIDPDGKI 122
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 38-206 7.78e-11

Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a conserved cysteine that aligns to the first cysteine in the CXXC motif of TRX. This does not correspond to the peroxidatic cysteine found in PRXs, which aligns to the second cysteine in the CXXC motif of TRX. In addition, these proteins do not contain the other two conserved residues of the catalytic triad of PRX. PRXs 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.


Pssm-ID: 239267 [Multi-domain]  Cd Length: 171  Bit Score: 58.40  E-value: 7.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545  38 GLAVPNIELKDQYGKTVSLAErFKEKTTVLIVYRGGWCPYcskqlanVQKIEKELADL-------GAQIIAVSP------ 104
Cdd:cd02969    1 GSPAPDFSLPDTDGKTYSLAD-FADGKALVVMFICNHCPY-------VKAIEDRLNRLakeygakGVAVVAINSndieay 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545 105 --DSPEKLAEskitspnyqllsddsllLAQKLGLAF-YLDDKT---AKIYRnklgvnfvslegevkvALPVPAVFVIDTN 178
Cdd:cd02969   73 peDSPENMKA-----------------KAKEHGYPFpYLLDETqevAKAYG----------------AACTPDFFLFDPD 119

                        170       180       190
                 ....*....|....*....|....*....|....
gi 937117545 179 GLVnfQY------ANPNYKVRLTEDLLLAAVKSV 206
Cdd:cd02969  120 GKL--VYrgriddSRPGNDPPVTGRDLRAALDAL 151
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 37-179 9.79e-11

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 57.39  E-value: 9.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545  37 PGLAVPNIELKDQYGKTVSLAErFKEKTTVLIVYrGGWCPYCSKQLANVQKIEKELADLgaQIIAVSPDSPEKLAESKIt 116
Cdd:COG0526    4 VGKPAPDFTLTDLDGKPLSLAD-LKGKPVLVNFW-ATWCPPCRAEMPVLKELAEEYGGV--VFVGVDVDENPEAVKAFL- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 937117545 117 spnyqllsddslllaQKLGLAF-YLDDKTAKIYRnKLGVNFvslegevkvalpVPAVFVIDTNG 179
Cdd:COG0526   79 ---------------KELGLPYpVLLDPDGELAK-AYGVRG------------IPTTVLIDKDG 114
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 33-111 7.05e-09

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 52.63  E-value: 7.05e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937117545  33 SPLLPGLAVPNIELKDQYGKTVSLAErFKEKTTVLIVYRGGWCPYCSKQLANVQKIEKELADLGAQIIAVSPDSPEKLA 111
Cdd:PRK09437   2 NPLKAGDIAPKFSLPDQDGEQVSLTD-FQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLS 79
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 43-186 2.16e-08

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 50.31  E-value: 2.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545  43 NIELKDQYGKTVSLAErFKEKTtVLIVYRGGWCPYCSKQLANVQKIEKELADLGAQIIAVS--PDSPEKLAEskitspny 120
Cdd:cd02966    1 DFSLPDLDGKPVSLSD-LKGKV-VLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNvdDDDPAAVKA-------- 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937117545 121 qllsddsllLAQKLGLAF-YLDDKTAKIYRnKLGVNfvslegevkvalPVPAVFVIDTNGLVNFQYA 186
Cdd:cd02966   71 ---------FLKKYGITFpVLLDPDGELAK-AYGVR------------GLPTTFLIDRDGRIRARHV 115
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
10-181 5.76e-06

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 44.99  E-value: 5.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545  10 LFVLSSQVIAATATNIAESAEQVSPllpGLAVPNIELKDQYGKTVSLAErFKEKTtVLIVYRGGWCPYCSKQLANVQKIE 89
Cdd:PRK03147  13 LLILLAAVGYTIYSNFFADKEKVQV---GKEAPNFVLTDLEGKKIELKD-LKGKG-VFLNFWGTWCKPCEKEMPYMNELY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545  90 KELADLGAQIIAVSPDspeklaESKITSPNYqllsddslllAQKLGLAFYLD-DKTAKIyRNKLGVNfvslegevkvalP 168
Cdd:PRK03147  88 PKYKEKGVEIIAVNVD------ETELAVKNF----------VNRYGLTFPVAiDKGRQV-IDAYGVG------------P 138

                        170
                 ....*....|...
gi 937117545 169 VPAVFVIDTNGLV 181
Cdd:PRK03147 139 LPTTFLIDKDGKV 151
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 41-112 8.63e-06

SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II.


Pssm-ID: 239266  Cd Length: 142  Bit Score: 43.75  E-value: 8.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545  41 VPNIELKDQYGKTVSLAErFKEKTTVL--IVYRggwCPY-CSKQLANVQKIEKELADLGA---QIIAVS--P--DSPEKL 110
Cdd:cd02968    2 GPDFTLTDQDGRPVTLSD-LKGKPVLVyfGYTH---CPDvCPTTLANLAQALKQLGADGGddvQVVFISvdPerDTPEVL 77


                 ..
gi 937117545 111 AE 112
Cdd:cd02968   78 KA 79
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 46-187 3.25e-04

Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. The functional unit of typical 2-cys PRX is a homodimer. A unique intermolecular redox-active disulfide center is utilized for its activity. Upon reaction with peroxides, its peroxidatic cysteine is oxidized into a sulfenic acid intermediate which is resolved by bonding with the resolving cysteine from the other subunit of the homodimer. This intermolecular disulfide bond is then reduced by thioredoxin, tryparedoxin or AhpF. Typical 2-cys PRXs, like 1-cys PRXs, form decamers which are stabilized by reduction of the active site cysteine. Typical 2-cys PRX interacts through beta strands at one edge of the monomer (B-type interface) to form the functional homodimer, and uses an A-type interface (similar to the dimeric interface in atypical 2-cys PRX and PRX5) at the opposite end of the monomer to form the stable decameric (pentamer of dimers) structure.


Pssm-ID: 239313  Cd Length: 173  Bit Score: 39.80  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117545  46 LKDQYGKTVSLAErFKEKTTVLIVYrggwcPY-----CSKQLANVQKIEKELADLGAQIIAVSPDSP-EKLAESKiTSPN 119
Cdd:cd03015   14 VPNGEFKEISLSD-YKGKWVVLFFY-----PLdftfvCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHfSHLAWRN-TPRK 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937117545 120 YQLLSddslllaqklGLAFYL-DDKTAKIYRNkLGVnfvsLEGEVKVALpvPAVFVIDTNGLVNFQYAN 187
Cdd:cd03015   87 EGGLG----------KINFPLlADPKKKISRD-YGV----LDEEEGVAL--RGTFIIDPEGIIRHITVN 138
 
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