NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1519314757|ref|NP_036226|]
View 

peroxiredoxin-5, mitochondrial isoform L precursor [Homo sapiens]

Protein Classification

peroxiredoxin( domain architecture ID 10122413)

peroxiredoxin, also called thioredoxin peroxidase or alkyl hydroperoxide reductase, is a thiol-specific antioxidant protein that protects cells against reactive oxygen species

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 58-212 1.61e-73

Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs.


:

Pssm-ID: 239311 [Multi-domain]  Cd Length: 155  Bit Score: 219.36  E-value: 1.61e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  58 VGDAIPAVEVFE--GEPGNKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAEALKAKGVQVVACLSVNDAFVTG 135
Cdd:cd03013     1 VGDKLPNVTLFEyvPGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVICVSVNDPFVMK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519314757 136 EWGRAHKAEGKVRLLADPTGAFGKETDLLLDDSLvsIFGNRRLKRFSMVVQDGIVKALNVEPDGTGLTCSLAPNIIS 212
Cdd:cd03013    81 AWGKALGAKDKIRFLADGNGEFTKALGLTLDLSA--AGGGIRSKRYALIVDDGKVKYLFVEEDPGDVEVSSAENVLK 155
 
Name Accession Description Interval E-value
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 58-212 1.61e-73

Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs.


Pssm-ID: 239311 [Multi-domain]  Cd Length: 155  Bit Score: 219.36  E-value: 1.61e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  58 VGDAIPAVEVFE--GEPGNKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAEALKAKGVQVVACLSVNDAFVTG 135
Cdd:cd03013     1 VGDKLPNVTLFEyvPGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVICVSVNDPFVMK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519314757 136 EWGRAHKAEGKVRLLADPTGAFGKETDLLLDDSLvsIFGNRRLKRFSMVVQDGIVKALNVEPDGTGLTCSLAPNIIS 212
Cdd:cd03013    81 AWGKALGAKDKIRFLADGNGEFTKALGLTLDLSA--AGGGIRSKRYALIVDDGKVKYLFVEEDPGDVEVSSAENVLK 155
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
55-214 5.31e-68

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 205.32  E-value: 5.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  55 PIKVGDAIPAV---EVFEGEPgNKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAEALKAKGVQVVACLSVNDA 131
Cdd:COG0678     1 TIKVGDKLPDVtfkTRTADGP-EDVTTDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAKGVDEIACVSVNDA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757 132 FVTGEWGRAHKAEGKVRLLADPTGAFGKETDLLLDdslVSIFGN-RRLKRFSMVVQDGIVKALNVEPDGTGLTCSLAPNI 210
Cdd:COG0678    80 FVMNAWGKAQGAEGKITMLADGNGEFTKALGLEVD---KSALGFgKRSQRYAMLVEDGVVKKLNVEPAPGPFEVSDAETL 156


                  ....
gi 1519314757 211 ISQL 214
Cdd:COG0678   157 LAQL 160
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 57-200 3.45e-31

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 111.31  E-value: 3.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  57 KVGDAIPAVEVFE-GEPGNKVNLAElFKGKKGVLFGVPGAFTPGCSKTHlPGFVEQAEALKAKGVQVVACLSVNDAF-VT 134
Cdd:pfam08534   1 KAGDKAPDFTLPDaATDGNTVSLSD-FKGKKVVLNFWPGAFCPTCSAEH-PYLEKLNELYKEKGVDVVAVNSDNDAFfVK 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519314757 135 GEWGRAHkaeGKVRLLADPTGAFGKETDLLLDDSLVSifgNRRLKRFSMVVQDGIVKALNVEPDGT 200
Cdd:pfam08534  79 RFWGKEG---LPFPFLSDGNAAFTKALGLPIEEDASA---GLRSPRYAVIDEDGKVVYLFVGPEPG 138
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 53-123 1.39e-05

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 43.39  E-value: 1.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519314757  53 MAPIKVGDAIPAVEVFEgEPGNKVNLAElFKGKKGVLFGVPGAFTPGCSkTHLPGFVEQAEALKAKGVQVV 123
Cdd:PRK09437    1 MNPLKAGDIAPKFSLPD-QDGEQVSLTD-FQGQRVLVYFYPKAMTPGCT-VQACGLRDNMDELKKAGVVVL 68
 
Name Accession Description Interval E-value
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 58-212 1.61e-73

Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs.


Pssm-ID: 239311 [Multi-domain]  Cd Length: 155  Bit Score: 219.36  E-value: 1.61e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  58 VGDAIPAVEVFE--GEPGNKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAEALKAKGVQVVACLSVNDAFVTG 135
Cdd:cd03013     1 VGDKLPNVTLFEyvPGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVICVSVNDPFVMK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519314757 136 EWGRAHKAEGKVRLLADPTGAFGKETDLLLDDSLvsIFGNRRLKRFSMVVQDGIVKALNVEPDGTGLTCSLAPNIIS 212
Cdd:cd03013    81 AWGKALGAKDKIRFLADGNGEFTKALGLTLDLSA--AGGGIRSKRYALIVDDGKVKYLFVEEDPGDVEVSSAENVLK 155
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
55-214 5.31e-68

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 205.32  E-value: 5.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  55 PIKVGDAIPAV---EVFEGEPgNKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAEALKAKGVQVVACLSVNDA 131
Cdd:COG0678     1 TIKVGDKLPDVtfkTRTADGP-EDVTTDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAKGVDEIACVSVNDA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757 132 FVTGEWGRAHKAEGKVRLLADPTGAFGKETDLLLDdslVSIFGN-RRLKRFSMVVQDGIVKALNVEPDGTGLTCSLAPNI 210
Cdd:COG0678    80 FVMNAWGKAQGAEGKITMLADGNGEFTKALGLEVD---KSALGFgKRSQRYAMLVEDGVVKKLNVEPAPGPFEVSDAETL 156


                  ....
gi 1519314757 211 ISQL 214
Cdd:COG0678   157 LAQL 160
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 62-201 3.76e-35

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: 121.12  E-value: 3.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  62 IPAVEVFeGEPGNKVNLAElFKGKKGVLFGVPGAFTPGCSkTHLPGFVEQAEALKAKGVQVVaCLSVNDAFVTGEWGRAH 141
Cdd:cd02971     2 APDFTLP-ATDGGEVSLSD-FKGKWVVLFFYPKDFTPVCT-TELCAFRDLAEEFAKGGAEVL-GVSVDSPFSHKAWAEKE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519314757 142 KaEGKVRLLADPTGAFGKETDLLLDDSlvsiFGNRRLKRFSMVV-QDGIVKALNVEPDGTG 201
Cdd:cd02971    78 G-GLNFPLLSDPDGEFAKAYGVLIEKS----AGGGLAARATFIIdPDGKIRYVEVEPLPTG 133
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 57-200 3.45e-31

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 111.31  E-value: 3.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  57 KVGDAIPAVEVFE-GEPGNKVNLAElFKGKKGVLFGVPGAFTPGCSKTHlPGFVEQAEALKAKGVQVVACLSVNDAF-VT 134
Cdd:pfam08534   1 KAGDKAPDFTLPDaATDGNTVSLSD-FKGKKVVLNFWPGAFCPTCSAEH-PYLEKLNELYKEKGVDVVAVNSDNDAFfVK 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519314757 135 GEWGRAHkaeGKVRLLADPTGAFGKETDLLLDDSLVSifgNRRLKRFSMVVQDGIVKALNVEPDGT 200
Cdd:pfam08534  79 RFWGKEG---LPFPFLSDGNAAFTKALGLPIEEDASA---GLRSPRYAVIDEDGKVVYLFVGPEPG 138
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 58-172 5.00e-19

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: 79.19  E-value: 5.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  58 VGDAIPAVEVFEGEpGNKVNLAElFKGKKGVLFGVPGAFTPGCsKTHLPGFVEQAEALKAKGVQVVAcLSVNDAFVTGEW 137
Cdd:pfam00578   1 VGDKAPDFELPDGD-GGTVSLSD-YRGKWVVLFFYPADWTPVC-TTELPALADLYEEFKKLGVEVLG-VSVDSPESHKAF 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1519314757 138 GRAHKAegKVRLLADPTGAFGKETDLLLDDSLVSI 172
Cdd:pfam00578  77 AEKYGL--PFPLLSDPDGEVARAYGVLNEEEGGAL 109
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
56-201 2.52e-12

Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];


Pssm-ID: 440219  Cd Length: 196  Bit Score: 63.17  E-value: 2.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  56 IKVGDAIPAVEV--FEGEPGNKVNLAElFKGKKGVLFGVPGAFTPGCSkTHLPGFVEQAEALKAKGVQVVAcLSVNDAFV 133
Cdd:COG0450     3 PLIGDKAPDFTAeaTHGGEFKKISLSD-YKGKWVVLFFHPADFTFVCP-TELGAFAKRYEEFKKLGVEVIG-LSVDSVFS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757 134 tgewgraHKA----------EGKVR--LLADPTGAFGKETDLLLDDSLVSIfgnrrlkRFSMVV-QDGIVKALNVEPDGT 200
Cdd:COG0450    80 -------HKAwhetikekggIVKIKfpIIADPTGKIARAYGMLHPEDGVAV-------RGVFIIdPDGKIRAIEVYPLSV 145


                  .
gi 1519314757 201 G 201
Cdd:COG0450   146 G 146
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 56-199 2.69e-11

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: 59.21  E-value: 2.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  56 IKVGDAIPAVEVfEGEPGNKVNLAELFKGKKGVLFGVPGAFTPGCSKtHLPGFVEQAEALKAKGVQVVAcLSVNDAFVTG 135
Cdd:cd03018     1 LEVGDKAPDFEL-PDQNGQEVRLSEFRGRKPVVLVFFPLAFTPVCTK-ELCALRDSLELFEAAGAEVLG-ISVDSPFSLR 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519314757 136 EWGRAHKAEgkVRLLAD--PTGAFGKETDLLLDDSLVSifgnrrlKRFSMVV-QDGIVKALNVEPDG 199
Cdd:cd03018    78 AWAEENGLT--FPLLSDfwPHGEVAKAYGVFDEDLGVA-------ERAVFVIdRDGIIRYAWVSDDG 135
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
73-159 1.20e-08

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 51.79  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  73 GNKVNLAElFKGKKGVLFgVPGAFTPGCsKTHLPGFVEQAEALKAKGVQVVAcLSVNDAFVTGEWGRAHKAEgkVRLLAD 152
Cdd:COG1225    11 GKTVSLSD-LRGKPVVLY-FYATWCPGC-TAELPELRDLYEEFKDKGVEVLG-VSSDSDEAHKKFAEKYGLP--FPLLSD 84


                  ....*..
gi 1519314757 153 PTGAFGK 159
Cdd:COG1225    85 PDGEVAK 91
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 58-201 1.05e-07

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: 49.81  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  58 VGDAIPAVE---VFEGEPGNKVNLAElFKGKKGVLFGVPGAFTPGCSkTHLPGFVEQAEALKAKGVQVVAClSVNDAFVT 134
Cdd:cd03015     1 VGKKAPDFKataVVPNGEFKEISLSD-YKGKWVVLFFYPLDFTFVCP-TEIIAFSDRYEEFKKLNAEVLGV-STDSHFSH 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519314757 135 GEWGRAHKAEGKVR-----LLADPTGAFGKETDLLLDDSLVSIfgnrrlkRFSMVV-QDGIVKALNVEPDGTG 201
Cdd:cd03015    78 LAWRNTPRKEGGLGkinfpLLADPKKKISRDYGVLDEEEGVAL-------RGTFIIdPEGIIRHITVNDLPVG 143
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 60-199 1.60e-07

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: 48.70  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  60 DAIPAVEVfEGEPGNKVNLAElFKGKKGVLFGVPGAFTPGCSKtHLPGFVEQAEALKAKGVQVVAcLSVNDAFVTGEWGR 139
Cdd:cd03017     1 DKAPDFTL-PDQDGETVSLSD-LRGKPVVLYFYPKDDTPGCTK-EACDFRDLYEEFKALGAVVIG-VSPDSVESHAKFAE 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519314757 140 AHKAegKVRLLADPTGAFGKETDLLLDDSLVSIFgnrrLKRFSMVV-QDGIVKAL--NVEPDG 199
Cdd:cd03017    77 KYGL--PFPLLSDPDGKLAKAYGVWGEKKKKYMG----IERSTFLIdPDGKIVKVwrKVKPKG 133
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 75-164 9.24e-06

Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one conserved cysteine, which serves as the peroxidatic cysteine. They are homodimeric thiol-specific antioxidant (TSA) proteins that confer a protective role in cells by reducing and detoxifying hydrogen peroxide, peroxynitrite, and organic hydroperoxides. As with all other PRXs, a cysteine sulfenic acid intermediate is formed upon reaction of 1-cys PRX with its substrates. Having no resolving cysteine, the oxidized enzyme is resolved by an external small-molecule or protein reductant such as thioredoxin or glutaredoxin. Similar to typical 2-cys PRX, 1-cys PRX forms a functional dimeric unit with a B-type interface, as well as a decameric structure which is stabilized in the reduced form of the enzyme. Other oligomeric forms, tetramers and hexamers, have also been reported. Mammalian 1-cys PRX is localized cellularly in the cytosol and is expressed at high levels in brain, eye, testes and lung. The seed-specific plant 1-cys PRXs protect tissues from reactive oxygen species during desiccation and are also called rehydrins.


Pssm-ID: 239314  Cd Length: 203  Bit Score: 44.84  E-value: 9.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  75 KVNLAELFKGKKGVLFGVPGAFTPGCSkTHLPGFVEQAEALKAKGVQVVAcLSVNDAFVTGEWGRAHKAEGKVRL----L 150
Cdd:cd03016    16 PIKFHDYLGDSWGILFSHPADFTPVCT-TELGAFAKLAPEFKKRNVKLIG-LSVDSVESHIKWIEDIEEYTGVEIpfpiI 93

                          90
                  ....*....|....
gi 1519314757 151 ADPTGAFGKETDLL 164
Cdd:cd03016    94 ADPDREVAKLLGMI 107
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 53-123 1.39e-05

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 43.39  E-value: 1.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519314757  53 MAPIKVGDAIPAVEVFEgEPGNKVNLAElFKGKKGVLFGVPGAFTPGCSkTHLPGFVEQAEALKAKGVQVV 123
Cdd:PRK09437    1 MNPLKAGDIAPKFSLPD-QDGEQVSLTD-FQGQRVLVYFYPKAMTPGCT-VQACGLRDNMDELKKAGVVVL 68
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 84-201 4.57e-05

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 42.67  E-value: 4.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  84 GKKGVLFGVPGAFTPGCSkTHLPGFVEQAEALKAKGVQVVAcLSVNDAFVTGEWGRAHKAEGKVR--LLADPTGAFGKET 161
Cdd:PRK10382   31 GRWSVFFFYPADFTFVCP-TELGDVADHYEELQKLGVDVYS-VSTDTHFTHKAWHSSSETIAKIKyaMIGDPTGALTRNF 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1519314757 162 DLLLDDSLVSifgnrrlKRFSMVVQ-DGIVKALNVEPDGTG 201
Cdd:PRK10382  109 DNMREDEGLA-------DRATFVVDpQGIIQAIEVTAEGIG 142
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 55-174 9.06e-05

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 41.76  E-value: 9.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  55 PIKVGDAIPAVEVFEGEpgNKVNLAElFKGKKGVLFGVPGAFTPGCSkTHLPGFVEQAEALKAKGVQVVAcLSVNDAFVT 134
Cdd:PRK13190    1 PVKLGQKAPDFTVNTTK--GPIDLSK-YKGKWVLLFSHPADFTPVCT-TEFIAFSRRYEDFKKLGVELVG-LSVDSIYSH 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1519314757 135 GEWGRAHKAEGKVRL----LADPTGAFGKETDLLLDDSLVSIFG 174
Cdd:PRK13190   76 IAWLRDIEERFGIKIpfpvIADIDKELAREYNLIDENSGATVRG 119
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 58-171 9.17e-05

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 41.76  E-value: 9.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  58 VGDAIPAVEVFEGEpgNKVNLAELFKGKKGVLFGVPGAFTPGCSkTHLPGFVEQAEALKAKGVQVVAcLSVNDAFVTGEW 137
Cdd:PRK13191    9 IGEKFPEMEVITTH--GKIKLPDDYKGRWFVLFSHPGDFTPVCT-TEFYSFAKKYEEFKKLNTELIG-LSVDSNISHIEW 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1519314757 138 ----GRAHKAEGKVRLLADPTGAFGKETDLLLDDSLVS 171
Cdd:PRK13191   85 vmwiEKNLKVEVPFPIIADPMGNVAKRLGMIHAESSTA 122
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 73-159 5.52e-04

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: 39.14  E-value: 5.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  73 GNKVNLAElFKGKKGVLFgvpgAFT-PGC--SKTHLPGFVEQAEALKAKGVQVVAcLSVNDA----FVTGEWGRAHKAEG 145
Cdd:cd02969    14 GKTYSLAD-FADGKALVV----MFIcNHCpyVKAIEDRLNRLAKEYGAKGVAVVA-INSNDIeaypEDSPENMKAKAKEH 87

                          90
                  ....*....|....*.
gi 1519314757 146 KVR--LLADPTGAFGK 159
Cdd:cd02969    88 GYPfpYLLDETQEVAK 103
PRK13189 PRK13189
peroxiredoxin; Provisional
 58-132 6.47e-04

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 39.58  E-value: 6.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519314757  58 VGDAIPAVEVF--EGepgnKVNLAELFKGKKGVLFGVPGAFTPGCSkTHLPGFVEQAEALKAKGVQVVAcLSVNDAF 132
Cdd:PRK13189   11 IGDKFPEFEVKttHG----PIKLPDDYKGKWFVLFSHPADFTPVCT-TEFVAFQKRYDEFRELNTELIG-LSIDQVF 81
PRK13599 PRK13599
peroxiredoxin;
58-137 1.07e-03

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 38.93  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314757  58 VGDAIPAVEVFEGEpGNKvNLAELFKGKKGVLFGVPGAFTPGCSkTHLPGFVEQAEALKAKGVQVVAcLSVNDAFVTGEW 137
Cdd:PRK13599    4 LGEKFPSMEVVTTQ-GVK-RLPEDYAGKWFVLFSHPADFTPVCT-TEFVEFARKANDFKELNTELIG-LSVDQVFSHIKW 79
 
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