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Conserved domains on  [gi|18397457|ref|NP_566268|]
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peroxiredoxin IIF [Arabidopsis thaliana]

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, ...
 67-198 3.22e-71

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: 212.81  E-value: 3.22e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457  67 LSDIFKGKKVVIFGLPGAYTGVCSQQHVPSYKSHIDKFKAKGIDSVICVSVNDPFAINGWAEKLGAKDAIEFYGDFDGKF 146
Cdd:cd03013  23 LSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVICVSVNDPFVMKAWGKALGAKDKIRFLADGNGEF 102

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 18397457 147 HKSLGLDKDLSAALLGPRSERWSAYVEDGKVKAVNVEEAPSDFKVTGAEVIL 198
Cdd:cd03013 103 TKALGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVEEDPGDVEVSSAENVL 154
 
Name Accession Description Interval E-value
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 67-198 3.22e-71

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: 212.81  E-value: 3.22e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457  67 LSDIFKGKKVVIFGLPGAYTGVCSQQHVPSYKSHIDKFKAKGIDSVICVSVNDPFAINGWAEKLGAKDAIEFYGDFDGKF 146
Cdd:cd03013  23 LSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVICVSVNDPFVMKAWGKALGAKDKIRFLADGNGEF 102

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 18397457 147 HKSLGLDKDLSAALLGPRSERWSAYVEDGKVKAVNVEEAPSDFKVTGAEVIL 198
Cdd:cd03013 103 TKALGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVEEDPGDVEVSSAENVL 154
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
67-201 1.05e-66

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 201.86  E-value: 1.05e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457  67 LSDIFKGKKVVIFGLPGAYTGVCSQQHVPSYKSHIDKFKAKGIDSVICVSVNDPFAINGWAEKLGAKDAIEFYGDFDGKF 146
Cdd:COG0678  26 TDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAKGVDEIACVSVNDAFVMNAWGKAQGAEGKITMLADGNGEF 105

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18397457 147 HKSLGLDKDLSAALLGPRSERWSAYVEDGKVKAVNVEEAPSDFKVTGAEVILGQI 201
Cdd:COG0678 106 TKALGLEVDKSALGFGKRSQRYAMLVEDGVVKKLNVEPAPGPFEVSDAETLLAQL 160
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 55-198 1.06e-22

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 88.97  E-value: 1.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457    55 DEGVSSKFSTTPLSDiFKGKKVVIFGLPGAYTGVCSQQHVpsYKSHIDK-FKAKGIDSVICVSVNDPFAINGWAEKLGAK 133
Cdd:pfam08534  11 LPDAATDGNTVSLSD-FKGKKVVLNFWPGAFCPTCSAEHP--YLEKLNElYKEKGVDVVAVNSDNDAFFVKRFWGKEGLP 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18397457   134 daIEFYGDFDGKFHKSLGLDkDLSAALLGPRSERWSAYVEDGKVKAVNVEEAPsDFKVTGAEVIL 198
Cdd:pfam08534  88 --FPFLSDGNAAFTKALGLP-IEEDASAGLRSPRYAVIDEDGKVVYLFVGPEP-GVDVSDAEAVL 148
tpx PRK00522
thiol peroxidase;
58-153 2.61e-06

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 45.66  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457   58 VSSKFSTTPLSDiFKGKKVVIFGLPGAYTGVCSQQhvpsykshIDKF--KAKGID--SVICVSVNDPFAINGWAEKLGAK 133
Cdd:PRK00522  30 VANDLSDVSLAD-FAGKRKVLNIFPSIDTGVCATS--------VRKFnqEAAELDntVVLCISADLPFAQKRFCGAEGLE 100

                         90       100
                 ....*....|....*....|
gi 18397457  134 DAIEFYGDFDGKFHKSLGLD 153
Cdd:PRK00522 101 NVITLSDFRDHSFGKAYGVA 120
 
Name Accession Description Interval E-value
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 67-198 3.22e-71

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: 212.81  E-value: 3.22e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457  67 LSDIFKGKKVVIFGLPGAYTGVCSQQHVPSYKSHIDKFKAKGIDSVICVSVNDPFAINGWAEKLGAKDAIEFYGDFDGKF 146
Cdd:cd03013  23 LSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVICVSVNDPFVMKAWGKALGAKDKIRFLADGNGEF 102

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 18397457 147 HKSLGLDKDLSAALLGPRSERWSAYVEDGKVKAVNVEEAPSDFKVTGAEVIL 198
Cdd:cd03013 103 TKALGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVEEDPGDVEVSSAENVL 154
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
67-201 1.05e-66

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 201.86  E-value: 1.05e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457  67 LSDIFKGKKVVIFGLPGAYTGVCSQQHVPSYKSHIDKFKAKGIDSVICVSVNDPFAINGWAEKLGAKDAIEFYGDFDGKF 146
Cdd:COG0678  26 TDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAKGVDEIACVSVNDAFVMNAWGKAQGAEGKITMLADGNGEF 105

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18397457 147 HKSLGLDKDLSAALLGPRSERWSAYVEDGKVKAVNVEEAPSDFKVTGAEVILGQI 201
Cdd:COG0678 106 TKALGLEVDKSALGFGKRSQRYAMLVEDGVVKKLNVEPAPGPFEVSDAETLLAQL 160
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 56-198 1.21e-29

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: 106.48  E-value: 1.21e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457  56 EGVSSKFSTTPLSDiFKGKKVVIFGLPGAYTGVCSQQhVPSYKSHIDKFKaKGIDSVICVSVNDPFAINGWAEKLGaKDA 135
Cdd:cd02971   6 TLPATDGGEVSLSD-FKGKWVVLFFYPKDFTPVCTTE-LCAFRDLAEEFA-KGGAEVLGVSVDSPFSHKAWAEKEG-GLN 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18397457 136 IEFYGDFDGKFHKSLGLDKDLSAalLGPRSERWSAYV-EDGKVKAVNVEEAPsdfKVTGAEVIL 198
Cdd:cd02971  82 FPLLSDPDGEFAKAYGVLIEKSA--GGGLAARATFIIdPDGKIRYVEVEPLP---TGRNAEELL 140
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 55-198 1.06e-22

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 88.97  E-value: 1.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457    55 DEGVSSKFSTTPLSDiFKGKKVVIFGLPGAYTGVCSQQHVpsYKSHIDK-FKAKGIDSVICVSVNDPFAINGWAEKLGAK 133
Cdd:pfam08534  11 LPDAATDGNTVSLSD-FKGKKVVLNFWPGAFCPTCSAEHP--YLEKLNElYKEKGVDVVAVNSDNDAFFVKRFWGKEGLP 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18397457   134 daIEFYGDFDGKFHKSLGLDkDLSAALLGPRSERWSAYVEDGKVKAVNVEEAPsDFKVTGAEVIL 198
Cdd:pfam08534  88 --FPFLSDGNAAFTKALGLP-IEEDASAGLRSPRYAVIDEDGKVVYLFVGPEP-GVDVSDAEAVL 148
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 67-152 2.51e-10

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: 55.69  E-value: 2.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457    67 LSDiFKGKKVVIFGLPGAYTGVCSQQhVPSYKSHIDKFKAKGIDsVICVSVNDPFAINGWAEKLGakdaIEF--YGDFDG 144
Cdd:pfam00578  20 LSD-YRGKWVVLFFYPADWTPVCTTE-LPALADLYEEFKKLGVE-VLGVSVDSPESHKAFAEKYG----LPFplLSDPDG 92


                  ....*...
gi 18397457   145 KFHKSLGL 152
Cdd:pfam00578  93 EVARAYGV 100
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 66-131 8.31e-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: 54.97  E-value: 8.31e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18397457  66 PLSDIFKGKKVVIFGLPGAYTGVCSQQhVPSYKSHIDKFKAKGIDsVICVSVNDPFAINGWAEKLG 131
Cdd:cd03018  21 RLSEFRGRKPVVLVFFPLAFTPVCTKE-LCALRDSLELFEAAGAE-VLGISVDSPFSLRAWAEENG 84
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
67-182 1.93e-07

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 48.32  E-value: 1.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457  67 LSDiFKGKKVVI-FGlpGAYTGVCsQQHVPSYKSHIDKFKAKGIDsVICVSVNDPFAINGWAEKLGAKdaIEFYGDFDGK 145
Cdd:COG1225  16 LSD-LRGKPVVLyFY--ATWCPGC-TAELPELRDLYEEFKDKGVE-VLGVSSDSDEAHKKFAEKYGLP--FPLLSDPDGE 88

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 18397457 146 FHKSLGLdkdlsaallgpRSERwSAYV--EDGKVKAVNV 182
Cdd:COG1225  89 VAKAYGV-----------RGTP-TTFLidPDGKIRYVWV 115
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 67-180 2.16e-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: 48.31  E-value: 2.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457  67 LSDiFKGKKVVIFGLPGAYTGVCSQQhVPSYKSHIDKFKAKGIdSVICVSVNDPFAINGWAEKLGAKdaIEFYGDFDGKF 146
Cdd:cd03017  18 LSD-LRGKPVVLYFYPKDDTPGCTKE-ACDFRDLYEEFKALGA-VVIGVSPDSVESHAKFAEKYGLP--FPLLSDPDGKL 92

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 18397457 147 HKSLGLDKDLSAALLGPrsERwSAYV--EDGKVKAV 180
Cdd:cd03017  93 AKAYGVWGEKKKKYMGI--ER-STFLidPDGKIVKV 125
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 58-153 1.96e-06

Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing peroxidatic and resolving cysteines, similar to the homodimeric thiol specific antioxidant (TSA) protein also known as TRX-dependent thiol peroxidase (Tpx). Tpx is a bacterial periplasmic peroxidase which differs from other PRXs in that it shows substrate specificity toward alkyl hydroperoxides over hydrogen peroxide. As with all other PRXs, the peroxidatic cysteine (N-terminal) of Tpx is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Tpx is able to resolve this intermediate by forming an intramolecular disulfide bond with a conserved C-terminal cysteine (the resolving cysteine), which can then be reduced by thioredoxin. This differs from the typical 2-cys PRX which resolves the oxidized cysteine by forming an intermolecular disulfide bond with the resolving cysteine from the other subunit of the homodimer. Atypical 2-cys PRX homodimers have a loop-based interface (A-type for alternate), in contrast with the B-type interface of typical 2-cys and 1-cys PRXs.


Pssm-ID: 239312 [Multi-domain]  Cd Length: 143  Bit Score: 45.65  E-value: 1.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457  58 VSSKFSTTPLSDiFKGKKVVIFGLPGAYTGVCSQQHVpsyksHIDKFKAKGID-SVICVSVNDPFAINGWAEKLGAKDaI 136
Cdd:cd03014  12 VTSDLSEVSLAD-FAGKVKVISVFPSIDTPVCATQTK-----RFNKEAAKLDNtVVLTISADLPFAQKRWCGAEGVDN-V 84

                        90
                ....*....|....*...
gi 18397457 137 EFYGDF-DGKFHKSLGLD 153
Cdd:cd03014  85 TTLSDFrDHSFGKAYGVL 102
tpx PRK00522
thiol peroxidase;
58-153 2.61e-06

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 45.66  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457   58 VSSKFSTTPLSDiFKGKKVVIFGLPGAYTGVCSQQhvpsykshIDKF--KAKGID--SVICVSVNDPFAINGWAEKLGAK 133
Cdd:PRK00522  30 VANDLSDVSLAD-FAGKRKVLNIFPSIDTGVCATS--------VRKFnqEAAELDntVVLCISADLPFAQKRFCGAEGLE 100

                         90       100
                 ....*....|....*....|
gi 18397457  134 DAIEFYGDFDGKFHKSLGLD 153
Cdd:PRK00522 101 NVITLSDFRDHSFGKAYGVA 120
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
58-152 6.57e-06

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 44.31  E-value: 6.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457  58 VSSKFSTTPLSDiFKGKKVVIFGLPGAYTGVCSQQhvpsykshIDKF--KAKGID--SVICVSVNDPFAINGW--AEKLg 131
Cdd:COG2077  30 VDTDLSDVTLSD-FAGKRKVLNIVPSLDTPVCATS--------TRKFneEAAKLDnvVVLTISADLPFAQKRFcgAEGI- 99

                        90       100
                ....*....|....*....|..
gi 18397457 132 akDAIEFYGDF-DGKFHKSLGL 152
Cdd:COG2077 100 --DNVVTLSDFrDRSFGKDYGV 119
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
67-184 4.02e-04

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 39.67  E-value: 4.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457  67 LSDiFKGKKVVIFGLPGAYTGVCsqqhvPS----YKSHIDKFKAKGIDsVICVSVNDPFAINGWA----EKLGAKDaIEF 138
Cdd:COG0450  27 LSD-YKGKWVVLFFHPADFTFVC-----PTelgaFAKRYEEFKKLGVE-VIGLSVDSVFSHKAWHetikEKGGIVK-IKF 98

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457 139 Y--GDFDGKFHKSLG-LDKDLSAALlgpRserwSAYV--EDGKVKAV---------NVEE 184
Cdd:COG0450  99 PiiADPTGKIARAYGmLHPEDGVAV---R----GVFIidPDGKIRAIevyplsvgrNVDE 151
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 61-162 5.13e-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: 39.02  E-value: 5.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457  61 KFSTTPLSDiFKGKKVVIFGLPGAYTGVCsqqhvPS----YKSHIDKFKAKGIDsVICVSVNDPFAINGWAE---KLGAK 133
Cdd:cd03015  18 EFKEISLSD-YKGKWVVLFFYPLDFTFVC-----PTeiiaFSDRYEEFKKLNAE-VLGVSTDSHFSHLAWRNtprKEGGL 90

                        90       100       110
                ....*....|....*....|....*....|..
gi 18397457 134 DAIEFY--GDFDGKFHKSLG-LDKDLSAALLG 162
Cdd:cd03015  91 GKINFPllADPKKKISRDYGvLDEEEGVALRG 122
PRK13189 PRK13189
peroxiredoxin; Provisional
 67-152 2.13e-03

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 37.65  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457   67 LSDIFKGKKVVIFGLPGAYTGVCSQQHVpSYKSHIDKFKAKGIDsVICVSVNDPFAINGWA----EKLGAKdaIEF--YG 140
Cdd:PRK13189  29 LPDDYKGKWFVLFSHPADFTPVCTTEFV-AFQKRYDEFRELNTE-LIGLSIDQVFSHIKWVewikEKLGVE--IEFpiIA 104

                         90
                 ....*....|..
gi 18397457  141 DFDGKFHKSLGL 152
Cdd:PRK13189 105 DDRGEIAKKLGM 116
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 67-152 7.46e-03

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 35.98  E-value: 7.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397457   67 LSDIFKGKKVVIFGLPGAYTGVCSQQHVpSYKSHIDKFKAKGIDsVICVSVNDPFA----INgWAEK-LGAKDAIEFYGD 141
Cdd:PRK13191  27 LPDDYKGRWFVLFSHPGDFTPVCTTEFY-SFAKKYEEFKKLNTE-LIGLSVDSNIShiewVM-WIEKnLKVEVPFPIIAD 103

                         90
                 ....*....|.
gi 18397457  142 FDGKFHKSLGL 152
Cdd:PRK13191 104 PMGNVAKRLGM 114
 
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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