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Conserved domains on  [gi|1676319623|ref|NP_001345440|]
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peroxiredoxin-5, mitochondrial isoform d precursor [Homo sapiens]

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

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, ...
 57-167 2.09e-48

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: 153.87  E-value: 2.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319623  57 KTHLPGFVEQAEALKAKGVQVVACLSVNDAFVTGEWGRAHKAEGKVRLLADPTGAFGKETDLLLDDSLvsIFGNRRLKRF 136
Cdd:cd03013    47 AQHLPGYVENADELKAKGVDEVICVSVNDPFVMKAWGKALGAKDKIRFLADGNGEFTKALGLTLDLSA--AGGGIRSKRY 124

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1676319623 137 SMVVQDGIVKALNVEPDGTGLTCSLAPNIIS 167
Cdd:cd03013   125 ALIVDDGKVKYLFVEEDPGDVEVSSAENVLK 155
 
Name Accession Description Interval E-value
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 57-167 2.09e-48

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: 153.87  E-value: 2.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319623  57 KTHLPGFVEQAEALKAKGVQVVACLSVNDAFVTGEWGRAHKAEGKVRLLADPTGAFGKETDLLLDDSLvsIFGNRRLKRF 136
Cdd:cd03013    47 AQHLPGYVENADELKAKGVDEVICVSVNDPFVMKAWGKALGAKDKIRFLADGNGEFTKALGLTLDLSA--AGGGIRSKRY 124

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1676319623 137 SMVVQDGIVKALNVEPDGTGLTCSLAPNIIS 167
Cdd:cd03013   125 ALIVDDGKVKYLFVEEDPGDVEVSSAENVLK 155
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
57-169 7.79e-44

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 142.15  E-value: 7.79e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319623  57 KTHLPGFVEQAEALKAKGVQVVACLSVNDAFVTGEWGRAHKAEGKVRLLADPTGAFGKETDLLLDdslVSIFGN-RRLKR 135
Cdd:COG0678    50 SAHLPGFVELADAFKAKGVDEIACVSVNDAFVMNAWGKAQGAEGKITMLADGNGEFTKALGLEVD---KSALGFgKRSQR 126

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1676319623 136 FSMVVQDGIVKALNVEPDGTGLTCSLAPNIISQL 169
Cdd:COG0678   127 YAMLVEDGVVKKLNVEPAPGPFEVSDAETLLAQL 160
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 67-155 4.90e-15

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 68.17  E-value: 4.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319623  67 AEALKAKGVQVVACLSVNDAF-VTGEWGRAHkaeGKVRLLADPTGAFGKETDLLLDDSLVSifgNRRLKRFSMVVQDGIV 145
Cdd:pfam08534  55 NELYKEKGVDVVAVNSDNDAFfVKRFWGKEG---LPFPFLSDGNAAFTKALGLPIEEDASA---GLRSPRYAVIDEDGKV 128

                          90
                  ....*....|
gi 1676319623 146 KALNVEPDGT 155
Cdd:pfam08534 129 VYLFVGPEPG 138
 
Name Accession Description Interval E-value
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 57-167 2.09e-48

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: 153.87  E-value: 2.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319623  57 KTHLPGFVEQAEALKAKGVQVVACLSVNDAFVTGEWGRAHKAEGKVRLLADPTGAFGKETDLLLDDSLvsIFGNRRLKRF 136
Cdd:cd03013    47 AQHLPGYVENADELKAKGVDEVICVSVNDPFVMKAWGKALGAKDKIRFLADGNGEFTKALGLTLDLSA--AGGGIRSKRY 124

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1676319623 137 SMVVQDGIVKALNVEPDGTGLTCSLAPNIIS 167
Cdd:cd03013   125 ALIVDDGKVKYLFVEEDPGDVEVSSAENVLK 155
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
57-169 7.79e-44

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 142.15  E-value: 7.79e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319623  57 KTHLPGFVEQAEALKAKGVQVVACLSVNDAFVTGEWGRAHKAEGKVRLLADPTGAFGKETDLLLDdslVSIFGN-RRLKR 135
Cdd:COG0678    50 SAHLPGFVELADAFKAKGVDEIACVSVNDAFVMNAWGKAQGAEGKITMLADGNGEFTKALGLEVD---KSALGFgKRSQR 126

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1676319623 136 FSMVVQDGIVKALNVEPDGTGLTCSLAPNIISQL 169
Cdd:COG0678   127 YAMLVEDGVVKKLNVEPAPGPFEVSDAETLLAQL 160
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 67-155 4.90e-15

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 68.17  E-value: 4.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676319623  67 AEALKAKGVQVVACLSVNDAF-VTGEWGRAHkaeGKVRLLADPTGAFGKETDLLLDDSLVSifgNRRLKRFSMVVQDGIV 145
Cdd:pfam08534  55 NELYKEKGVDVVAVNSDNDAFfVKRFWGKEG---LPFPFLSDGNAAFTKALGLPIEEDASA---GLRSPRYAVIDEDGKV 128

                          90
                  ....*....|
gi 1676319623 146 KALNVEPDGT 155
Cdd:pfam08534 129 VYLFVGPEPG 138
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 57-127 3.75e-06

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: 43.75  E-value: 3.75e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1676319623  57 KTHLPGFVEQAEALKAKGVQVVAcLSVNDAFVTGEWGRAHKAegKVRLLADPTGAFGKETDLLLDDSLVSI 127
Cdd:pfam00578  42 TTELPALADLYEEFKKLGVEVLG-VSVDSPESHKAFAEKYGL--PFPLLSDPDGEVARAYGVLNEEEGGAL 109
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
51-114 5.98e-03

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 35.23  E-value: 5.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1676319623  51 AAMAPI-KTHLPGFVEQAEALKAKGVQVVAcLSVNDAFVTGEWGRAHKAEgkVRLLADPTGAFGK 114
Cdd:COG1225    30 ATWCPGcTAELPELRDLYEEFKDKGVEVLG-VSSDSDEAHKKFAEKYGLP--FPLLSDPDGEVAK 91
 
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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