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Conserved domains on  [gi|6755114|ref|NP_036151|]
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peroxiredoxin-5, mitochondrial isoform 1 precursor [Mus musculus]

Protein Classification

peroxiredoxin family protein( domain architecture ID 10122413)

peroxiredoxin family protein such as peroxiredoxin 5, a thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively, playing a role in cell protection against oxidative stress by detoxifying peroxides

CATH:  3.40.30.10
EC:  1.11.1.-
Gene Ontology:  GO:0004601
PubMed:  15518547|12517450|15558583|10049365
SCOP:  4000042

Graphical summary

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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, ...
 54-208 3.71e-68

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: 205.49  E-value: 3.71e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114   54 VGDAIPSVEVFE--GEPGKKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAGALKAKGAQVVACLSVNDVFVIE 131
Cdd:cd03013   1 VGDKLPNVTLFEyvPGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVICVSVNDPFVMK 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755114  132 EWGRAHQAEGKVRLLADPTGAFGKAtdLLLDDSLVSLFGNRRLKRFSMVIDNGIVKALNVEPDGTGLTCSLAPNILS 208
Cdd:cd03013  81 AWGKALGAKDKIRFLADGNGEFTKA--LGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVEEDPGDVEVSSAENVLK 155
 
Name Accession Description Interval E-value
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 54-208 3.71e-68

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: 205.49  E-value: 3.71e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114   54 VGDAIPSVEVFE--GEPGKKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAGALKAKGAQVVACLSVNDVFVIE 131
Cdd:cd03013   1 VGDKLPNVTLFEyvPGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVICVSVNDPFVMK 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755114  132 EWGRAHQAEGKVRLLADPTGAFGKAtdLLLDDSLVSLFGNRRLKRFSMVIDNGIVKALNVEPDGTGLTCSLAPNILS 208
Cdd:cd03013  81 AWGKALGAKDKIRFLADGNGEFTKA--LGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVEEDPGDVEVSSAENVLK 155
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
51-210 4.12e-63

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 193.00  E-value: 4.12e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114   51 PIKVGDAIPSV---EVFEGEPgKKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAGALKAKGAQVVACLSVNDV 127
Cdd:COG0678   1 TIKVGDKLPDVtfkTRTADGP-EDVTTDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAKGVDEIACVSVNDA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114  128 FVIEEWGRAHQAEGKVRLLADPTGAFGKATdLLLDDSLVSLFGNRRlKRFSMVIDNGIVKALNVEPDGTGLTCSLAPNIL 207
Cdd:COG0678  80 FVMNAWGKAQGAEGKITMLADGNGEFTKAL-GLEVDKSALGFGKRS-QRYAMLVEDGVVKKLNVEPAPGPFEVSDAETLL 157


                ...
gi 6755114  208 SQL 210
Cdd:COG0678 158 AQL 160
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 53-196 2.16e-28

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 103.99  E-value: 2.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114     53 KVGDAIPSVEVFE-GEPGKKVNLAElFKGKKGVLFGVPGAFTPGCSKTHLpgFVEQAGAL-KAKGAQVVACLSVNDVF-V 129
Cdd:pfam08534   1 KAGDKAPDFTLPDaATDGNTVSLSD-FKGKKVVLNFWPGAFCPTCSAEHP--YLEKLNELyKEKGVDVVAVNSDNDAFfV 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755114    130 IEEWGRAHqaeGKVRLLADPTGAFGKATDLLLDDSLVSLFgnrRLKRFSMVIDNGIVKALNVEPDGT 196
Cdd:pfam08534  78 KRFWGKEG---LPFPFLSDGNAAFTKALGLPIEEDASAGL---RSPRYAVIDEDGKVVYLFVGPEPG 138
PRK13599 PRK13599
peroxiredoxin;
54-133 3.51e-04

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 40.08  E-value: 3.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114    54 VGDAIPSVEVFEGEPGKKvnLAELFKGKKGVLFGVPGAFTPGCSkTHLPGFVEQAGALKAKGAQVVAcLSVNDVFVIEEW 133
Cdd:PRK13599   4 LGEKFPSMEVVTTQGVKR--LPEDYAGKWFVLFSHPADFTPVCT-TEFVEFARKANDFKELNTELIG-LSVDQVFSHIKW 79
 
Name Accession Description Interval E-value
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 54-208 3.71e-68

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: 205.49  E-value: 3.71e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114   54 VGDAIPSVEVFE--GEPGKKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAGALKAKGAQVVACLSVNDVFVIE 131
Cdd:cd03013   1 VGDKLPNVTLFEyvPGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVICVSVNDPFVMK 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755114  132 EWGRAHQAEGKVRLLADPTGAFGKAtdLLLDDSLVSLFGNRRLKRFSMVIDNGIVKALNVEPDGTGLTCSLAPNILS 208
Cdd:cd03013  81 AWGKALGAKDKIRFLADGNGEFTKA--LGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVEEDPGDVEVSSAENVLK 155
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
51-210 4.12e-63

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 193.00  E-value: 4.12e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114   51 PIKVGDAIPSV---EVFEGEPgKKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAGALKAKGAQVVACLSVNDV 127
Cdd:COG0678   1 TIKVGDKLPDVtfkTRTADGP-EDVTTDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAKGVDEIACVSVNDA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114  128 FVIEEWGRAHQAEGKVRLLADPTGAFGKATdLLLDDSLVSLFGNRRlKRFSMVIDNGIVKALNVEPDGTGLTCSLAPNIL 207
Cdd:COG0678  80 FVMNAWGKAQGAEGKITMLADGNGEFTKAL-GLEVDKSALGFGKRS-QRYAMLVEDGVVKKLNVEPAPGPFEVSDAETLL 157


                ...
gi 6755114  208 SQL 210
Cdd:COG0678 158 AQL 160
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 58-197 2.90e-33

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: 116.11  E-value: 2.90e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114   58 IPSVEVFeGEPGKKVNLAElFKGKKGVLFGVPGAFTPGCSkTHLPGFVEQAGALKAKGAQVVaCLSVNDVFVIEEWGRAH 137
Cdd:cd02971   2 APDFTLP-ATDGGEVSLSD-FKGKWVVLFFYPKDFTPVCT-TELCAFRDLAEEFAKGGAEVL-GVSVDSPFSHKAWAEKE 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755114  138 QaEGKVRLLADPTGAFGKATdlllDDSLVSLFGNRRLKRFSMVID-NGIVKALNVEPDGTG 197
Cdd:cd02971  78 G-GLNFPLLSDPDGEFAKAY----GVLIEKSAGGGLAARATFIIDpDGKIRYVEVEPLPTG 133
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 53-196 2.16e-28

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 103.99  E-value: 2.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114     53 KVGDAIPSVEVFE-GEPGKKVNLAElFKGKKGVLFGVPGAFTPGCSKTHLpgFVEQAGAL-KAKGAQVVACLSVNDVF-V 129
Cdd:pfam08534   1 KAGDKAPDFTLPDaATDGNTVSLSD-FKGKKVVLNFWPGAFCPTCSAEHP--YLEKLNELyKEKGVDVVAVNSDNDAFfV 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755114    130 IEEWGRAHqaeGKVRLLADPTGAFGKATDLLLDDSLVSLFgnrRLKRFSMVIDNGIVKALNVEPDGT 196
Cdd:pfam08534  78 KRFWGKEG---LPFPFLSDGNAAFTKALGLPIEEDASAGL---RSPRYAVIDEDGKVVYLFVGPEPG 138
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 54-156 2.06e-20

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: 82.66  E-value: 2.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114     54 VGDAIPSVEVFEGEpGKKVNLAElFKGKKGVLFGVPGAFTPGCsKTHLPGFVEQAGALKAKGAQVVAcLSVNDVFVIEEW 133
Cdd:pfam00578   1 VGDKAPDFELPDGD-GGTVSLSD-YRGKWVVLFFYPADWTPVC-TTELPALADLYEEFKKLGVEVLG-VSVDSPESHKAF 76

                          90       100
                  ....*....|....*....|...
gi 6755114    134 GRAHQAegKVRLLADPTGAFGKA 156
Cdd:pfam00578  77 AEKYGL--PFPLLSDPDGEVARA 97
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
52-197 3.44e-12

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 62.40  E-value: 3.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114   52 IKVGDAIPSVEV--FEGEPGKKVNLAElFKGKKGVLFGVPGAFTPGCSkTHLPGFVEQAGALKAKGAQVVAcLSVNDVFV 129
Cdd:COG0450   3 PLIGDKAPDFTAeaTHGGEFKKISLSD-YKGKWVVLFFHPADFTFVCP-TELGAFAKRYEEFKKLGVEVIG-LSVDSVFS 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755114  130 IEEWGRA---HQAEGKVR--LLADPTGAFGKAtdlllddslvslFGNRRLK-----RFSMVID-NGIVKALNVEPDGTG 197
Cdd:COG0450  80 HKAWHETikeKGGIVKIKfpIIADPTGKIARA------------YGMLHPEdgvavRGVFIIDpDGKIRAIEVYPLSVG 146
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
69-188 8.83e-11

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 57.57  E-value: 8.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114   69 GKKVNLAElFKGKKGVLFgVPGAFTPGCsKTHLPGFVEQAGALKAKGAQVVAcLSVNDVFVIEEWGRAHQAEgkVRLLAD 148
Cdd:COG1225  11 GKTVSLSD-LRGKPVVLY-FYATWCPGC-TAELPELRDLYEEFKDKGVEVLG-VSSDSDEAHKKFAEKYGLP--FPLLSD 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6755114  149 PTGAFGKAtdlllddslvslFGNRRLkRFSMVID-NGIVKA 188
Cdd:COG1225  85 PDGEVAKA------------YGVRGT-PTTFLIDpDGKIRY 112
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 52-195 1.01e-10

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: 57.67  E-value: 1.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114   52 IKVGDAIPSVEVfEGEPGKKVNLAELFKGKKGVLFGVPGAFTPGCSKtHLPGFVEQAGALKAKGAQVVAcLSVNDVFVIE 131
Cdd:cd03018   1 LEVGDKAPDFEL-PDQNGQEVRLSEFRGRKPVVLVFFPLAFTPVCTK-ELCALRDSLELFEAAGAEVLG-ISVDSPFSLR 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755114  132 EWGRAHQAEgkVRLLAD--PTGAFGKAtdlllddslvslFG----NRRL-KRFSMVID-NGIVKALNVEPDG 195
Cdd:cd03018  78 AWAEENGLT--FPLLSDfwPHGEVAKA------------YGvfdeDLGVaERAVFVIDrDGIIRYAWVSDDG 135
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 56-195 2.12e-09

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: 53.71  E-value: 2.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114   56 DAIPSVEVfEGEPGKKVNLAElFKGKKGVLFGVPGAFTPGCSKtHLPGFVEQAGALKAKGAQVVAcLSVNDVFVIEEWGR 135
Cdd:cd03017   1 DKAPDFTL-PDQDGETVSLSD-LRGKPVVLYFYPKDDTPGCTK-EACDFRDLYEEFKALGAVVIG-VSPDSVESHAKFAE 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755114  136 AHQAegKVRLLADPTGAFGKATDLLLDDSLVSLFgnrrLKRFSMVID-NGIVKAL--NVEPDG 195
Cdd:cd03017  77 KYGL--PFPLLSDPDGKLAKAYGVWGEKKKKYMG----IERSTFLIDpDGKIVKVwrKVKPKG 133
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 54-156 6.63e-08

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: 50.20  E-value: 6.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114   54 VGDAIPSVE---VFEGEPGKKVNLAElFKGKKGVLFGVPGAFTPGCSkTHLPGFVEQAGALKAKGAQVVAClSVNDVFVI 130
Cdd:cd03015   1 VGKKAPDFKataVVPNGEFKEISLSD-YKGKWVVLFFYPLDFTFVCP-TEIIAFSDRYEEFKKLNAEVLGV-STDSHFSH 77

                        90       100       110
                ....*....|....*....|....*....|.
gi 6755114  131 EEWGRAHQAEGKVR-----LLADPTGAFGKA 156
Cdd:cd03015  78 LAWRNTPRKEGGLGkinfpLLADPKKKISRD 108
PRK13599 PRK13599
peroxiredoxin;
54-133 3.51e-04

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 40.08  E-value: 3.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114    54 VGDAIPSVEVFEGEPGKKvnLAELFKGKKGVLFGVPGAFTPGCSkTHLPGFVEQAGALKAKGAQVVAcLSVNDVFVIEEW 133
Cdd:PRK13599   4 LGEKFPSMEVVTTQGVKR--LPEDYAGKWFVLFSHPADFTPVCT-TEFVEFARKANDFKELNTELIG-LSVDQVFSHIKW 79
PRK13189 PRK13189
peroxiredoxin; Provisional
 54-128 4.82e-04

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 39.58  E-value: 4.82e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755114    54 VGDAIPSVEVF--EGepgkKVNLAELFKGKKGVLFGVPGAFTPGCSkTHLPGFVEQAGALKAKGAQVVAcLSVNDVF 128
Cdd:PRK13189  11 IGDKFPEFEVKttHG----PIKLPDDYKGKWFVLFSHPADFTPVCT-TEFVAFQKRYDEFRELNTELIG-LSIDQVF 81
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 49-96 6.61e-04

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 38.77  E-value: 6.61e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 6755114    49 MAPIKVGDAIPSVEVFEgEPGKKVNLAElFKGKKGVLFGVPGAFTPGC 96
Cdd:PRK09437   1 MNPLKAGDIAPKFSLPD-QDGEQVSLTD-FQGQRVLVYFYPKAMTPGC 46
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 55-152 1.11e-03

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: 38.68  E-value: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114   55 GDAIPSVEV--FEGepgkKVNLAELFKGKKGVLFGVPGAFTPGCSkTHLPGFVEQAGALKAKGAQVVAcLSVNDVFVIEE 132
Cdd:cd03016   2 GDTAPNFEAdtTHG----PIKFHDYLGDSWGILFSHPADFTPVCT-TELGAFAKLAPEFKKRNVKLIG-LSVDSVESHIK 75

                        90       100
                ....*....|....*....|....
gi 6755114  133 WGRAHQAEGKVRL----LADPTGA 152
Cdd:cd03016  76 WIEDIEEYTGVEIpfpiIADPDRE 99
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 54-155 7.49e-03

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 36.36  E-value: 7.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755114    54 VGDAIPSVEVFEGEpgKKVNLAELFKGKKGVLFGVPGAFTPGCSkTHLPGFVEQAGALKAKGAQVVAcLSVNDVFVIEEW 133
Cdd:PRK13191   9 IGEKFPEMEVITTH--GKIKLPDDYKGRWFVLFSHPGDFTPVCT-TEFYSFAKKYEEFKKLNTELIG-LSVDSNISHIEW 84

                         90       100
                 ....*....|....*....|....*.
gi 6755114   134 GRAHQAEGKVR----LLADPTGAFGK 155
Cdd:PRK13191  85 VMWIEKNLKVEvpfpIIADPMGNVAK 110
 
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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