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Conserved domains on  [gi|1958719812|ref|XP_038951915|]
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peroxiredoxin-like 2C isoform X1 [Rattus norvegicus]

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

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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. ...
 34-192 4.87e-43

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: 142.50  E-value: 4.87e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958719812  34 VAELPVLDASGRRVTFGALFRERRAVVVFVRHFLCYVCKEYVEDLAKIpKSVLQEADVTLIVIGQSSYHHIEPFCKLTGY 113
Cdd:cd02970     2 APDFELPDAGGETVTLSALLGEGPVVVVFYRGFGCPFCREYLRALSKL-LPELDALGVELVAVGPESPEKLEAFDKGKFL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958719812 114 SHEIYVDPEREIYKRLGMKRGEEISSSGQSPHiksnllsgslqslWRAVTGPLFDFQGDPAQQGGTLILGPESTSHRSQ 192
Cdd:cd02970    81 PFPVYADPDRKLYRALGLVRSLPWSNTPRALW-------------KNAAIGFRGNDEGDGLQLPGVFVIGPDGTILFAH 146
 
Name Accession Description Interval E-value
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 34-192 4.87e-43

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: 142.50  E-value: 4.87e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958719812  34 VAELPVLDASGRRVTFGALFRERRAVVVFVRHFLCYVCKEYVEDLAKIpKSVLQEADVTLIVIGQSSYHHIEPFCKLTGY 113
Cdd:cd02970     2 APDFELPDAGGETVTLSALLGEGPVVVVFYRGFGCPFCREYLRALSKL-LPELDALGVELVAVGPESPEKLEAFDKGKFL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958719812 114 SHEIYVDPEREIYKRLGMKRGEEISSSGQSPHiksnllsgslqslWRAVTGPLFDFQGDPAQQGGTLILGPESTSHRSQ 192
Cdd:cd02970    81 PFPVYADPDRKLYRALGLVRSLPWSNTPRALW-------------KNAAIGFRGNDEGDGLQLPGVFVIGPDGTILFAH 146
AhpC-TSA_2 pfam13911
AhpC/TSA antioxidant enzyme; This family contains proteins related to alkyl hydro-peroxide ...
 83-185 4.87e-22

AhpC/TSA antioxidant enzyme; This family contains proteins related to alkyl hydro-peroxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 433575  Cd Length: 114  Bit Score: 87.36  E-value: 4.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958719812  83 KSVLQEADVTLIVIGQSSYHHIEPFCKLTGYSHEIYVDPEREIYKRLGMKRGEEISSsgQSPHIKsNLLSGSLQSLWRAv 162
Cdd:pfam13911   6 KPELDAAGIRLVAIGCGTPGRIEEFIKLTGFPFPVYVDPSRKLYRALGLKRGLSGGL--LPGFLG-KGLRNMTRRAKAI- 81

                          90       100
                  ....*....|....*....|...
gi 1958719812 163 tGPLFDFQGDPAQQGGTLILGPE 185
Cdd:pfam13911  82 -GIPGNLGGDGTQLGGTFVFDKG 103
SelL_rel_redox NF040769
SelL-related redox protein; Members of this family are related to the C-terminal region of ...
 34-191 2.11e-12

SelL-related redox protein; Members of this family are related to the C-terminal region of selenoprotein L (SelL), found in many non-mammalian animals. But while SelL itself has a pair of selenocysteine (U) residues (e.g. XP_029705782.1), typically in the motif ULPU, this family is defined more broadly. Most members of the seed alignment for this HMM are bacterial proteins that have one or zero selenocysteine residues, and are shorter than SelU, although SelU members are also included.


Pssm-ID: 468728  Cd Length: 172  Bit Score: 63.10  E-value: 2.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958719812  34 VAELPVLDASGRRVTFGALFRERRAVVVFVRHFLCYVCKEYVEDLAKIpKSVLQEADVTLIVIGQSSYHHIEPFCKLTGY 113
Cdd:NF040769    3 APEVELLDPDGTLVRLLEFLPQGPLLLVFLRHLGUIPCREHLAQLREH-QEEFAARGCRVLVVSFASPEFAEKYLERTWL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958719812 114 S-HEIYVDPEREIYKRLGMKRGEEISSSGQSphiksnllsgSLQSLWRAVTG---PLFDFQGDPAQQGGTLILGPEST-- 187
Cdd:NF040769   82 SwPLVVSDPDRKLYRAFGLKRATFLELWGPK----------VLVGYLRALLKggnFYGKPGGDILQLGGDFILDRDGRil 151


                  ....*
gi 1958719812 188 -SHRS 191
Cdd:NF040769  152 fAHRS 156
 
Name Accession Description Interval E-value
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 34-192 4.87e-43

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: 142.50  E-value: 4.87e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958719812  34 VAELPVLDASGRRVTFGALFRERRAVVVFVRHFLCYVCKEYVEDLAKIpKSVLQEADVTLIVIGQSSYHHIEPFCKLTGY 113
Cdd:cd02970     2 APDFELPDAGGETVTLSALLGEGPVVVVFYRGFGCPFCREYLRALSKL-LPELDALGVELVAVGPESPEKLEAFDKGKFL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958719812 114 SHEIYVDPEREIYKRLGMKRGEEISSSGQSPHiksnllsgslqslWRAVTGPLFDFQGDPAQQGGTLILGPESTSHRSQ 192
Cdd:cd02970    81 PFPVYADPDRKLYRALGLVRSLPWSNTPRALW-------------KNAAIGFRGNDEGDGLQLPGVFVIGPDGTILFAH 146
AhpC-TSA_2 pfam13911
AhpC/TSA antioxidant enzyme; This family contains proteins related to alkyl hydro-peroxide ...
 83-185 4.87e-22

AhpC/TSA antioxidant enzyme; This family contains proteins related to alkyl hydro-peroxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 433575  Cd Length: 114  Bit Score: 87.36  E-value: 4.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958719812  83 KSVLQEADVTLIVIGQSSYHHIEPFCKLTGYSHEIYVDPEREIYKRLGMKRGEEISSsgQSPHIKsNLLSGSLQSLWRAv 162
Cdd:pfam13911   6 KPELDAAGIRLVAIGCGTPGRIEEFIKLTGFPFPVYVDPSRKLYRALGLKRGLSGGL--LPGFLG-KGLRNMTRRAKAI- 81

                          90       100
                  ....*....|....*....|...
gi 1958719812 163 tGPLFDFQGDPAQQGGTLILGPE 185
Cdd:pfam13911  82 -GIPGNLGGDGTQLGGTFVFDKG 103
SelL_rel_redox NF040769
SelL-related redox protein; Members of this family are related to the C-terminal region of ...
 34-191 2.11e-12

SelL-related redox protein; Members of this family are related to the C-terminal region of selenoprotein L (SelL), found in many non-mammalian animals. But while SelL itself has a pair of selenocysteine (U) residues (e.g. XP_029705782.1), typically in the motif ULPU, this family is defined more broadly. Most members of the seed alignment for this HMM are bacterial proteins that have one or zero selenocysteine residues, and are shorter than SelU, although SelU members are also included.


Pssm-ID: 468728  Cd Length: 172  Bit Score: 63.10  E-value: 2.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958719812  34 VAELPVLDASGRRVTFGALFRERRAVVVFVRHFLCYVCKEYVEDLAKIpKSVLQEADVTLIVIGQSSYHHIEPFCKLTGY 113
Cdd:NF040769    3 APEVELLDPDGTLVRLLEFLPQGPLLLVFLRHLGUIPCREHLAQLREH-QEEFAARGCRVLVVSFASPEFAEKYLERTWL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958719812 114 S-HEIYVDPEREIYKRLGMKRGEEISSSGQSphiksnllsgSLQSLWRAVTG---PLFDFQGDPAQQGGTLILGPEST-- 187
Cdd:NF040769   82 SwPLVVSDPDRKLYRAFGLKRATFLELWGPK----------VLVGYLRALLKggnFYGKPGGDILQLGGDFILDRDGRil 151


                  ....*
gi 1958719812 188 -SHRS 191
Cdd:NF040769  152 fAHRS 156
 
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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