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Conserved domains on  [gi|221234884|ref|YP_002517320|]
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thioredoxin peroxidase [Caulobacter vibrioides NA1000]

Protein Classification

peroxiredoxin( domain architecture ID 10122458)

peroxiredoxin belonging to the bacterioferritin comigratory protein (BCP) subfamily is a thioredoxin-dependent thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively

CATH:  3.40.30.10
EC:  1.11.1.24
Gene Ontology:  GO:0051920
PubMed:  15518547|12517450|10644761
SCOP:  4000042

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 6-147 4.37e-73

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: 215.10  E-value: 4.37e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   6 DKAPDFDLPTDTGR-VSLSALKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFRAKHDL 84
Cdd:cd03017    1 DKAPDFTLPDQDGEtVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221234884  85 TIELAADTLGDVVESYGAWVEKSmygRKYMGIDRSTFLIDREGVIREIWRKVKVPGHIKAVMN 147
Cdd:cd03017   81 PFPLLSDPDGKLAKAYGVWGEKK---KKYMGIERSTFLIDPDGKIVKVWRKVKPKGHAEEVLE 140
 
Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 6-147 4.37e-73

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: 215.10  E-value: 4.37e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   6 DKAPDFDLPTDTGR-VSLSALKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFRAKHDL 84
Cdd:cd03017    1 DKAPDFTLPDQDGEtVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221234884  85 TIELAADTLGDVVESYGAWVEKSmygRKYMGIDRSTFLIDREGVIREIWRKVKVPGHIKAVMN 147
Cdd:cd03017   81 PFPLLSDPDGKLAKAYGVWGEKK---KKYMGIERSTFLIDPDGKIVKVWRKVKPKGHAEEVLE 140
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 4-132 3.59e-47

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: 148.91  E-value: 3.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884    4 PGDKAPDFDLPTDTGR-VSLSALKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFRAKH 82
Cdd:pfam00578   1 VGDKAPDFELPDGDGGtVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEKY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 221234884   83 DLTIELAADTLGDVVESYGAWVEksmygrKYMGIDRSTFLIDREGVIREI 132
Cdd:pfam00578  81 GLPFPLLSDPDGEVARAYGVLNE------EEGGALRATFVIDPDGKVRYI 124
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
8-149 3.14e-44

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 141.93  E-value: 3.14e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   8 APDFDLPTDTGR-VSLSALKGKNVVLYFYpKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFRAKHDLTI 86
Cdd:COG1225    1 APDFTLPDLDGKtVSLSDLRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYGLPF 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221234884  87 ELAADTLGDVVESYGAWVEksmygrkymgidRSTFLIDREGVIREIW-RKVKVPGHIKAVMNAA 149
Cdd:COG1225   80 PLLSDPDGEVAKAYGVRGT------------PTTFLIDPDGKIRYVWvGPVDPRPHLEEVLEAL 131
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 2-147 1.89e-38

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 127.75  E-value: 1.89e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   2 LQPGDKAPDFDLPTDTGR-VSLSALKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFRA 80
Cdd:PRK09437   4 LKAGDIAPKFSLPDQDGEqVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLSRFAE 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221234884  81 KHDLTIELAADTLGDVVESYGAWVEKSMYGRKYMGIDRSTFLIDREGVIREIWRKVKVPGHIKAVMN 147
Cdd:PRK09437  84 KELLNFTLLSDEDHQVAEQFGVWGEKKFMGKTYDGIHRISFLIDADGKIEHVFDKFKTSNHHDVVLD 150
 
Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 6-147 4.37e-73

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: 215.10  E-value: 4.37e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   6 DKAPDFDLPTDTGR-VSLSALKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFRAKHDL 84
Cdd:cd03017    1 DKAPDFTLPDQDGEtVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221234884  85 TIELAADTLGDVVESYGAWVEKSmygRKYMGIDRSTFLIDREGVIREIWRKVKVPGHIKAVMN 147
Cdd:cd03017   81 PFPLLSDPDGKLAKAYGVWGEKK---KKYMGIERSTFLIDPDGKIVKVWRKVKPKGHAEEVLE 140
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 7-141 2.58e-53

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: 165.03  E-value: 2.58e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   7 KAPDFDLPTDTG-RVSLSALKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFRAKH-DL 84
Cdd:cd02971    1 KAPDFTLPATDGgEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEKEgGL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 221234884  85 TIELAADTLGDVVESYGAWVEKSMygrKYMGIDRSTFLIDREGVIREIWRKVKVPGH 141
Cdd:cd02971   81 NFPLLSDPDGEFAKAYGVLIEKSA---GGGLAARATFIIDPDGKIRYVEVEPLPTGR 134
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 4-132 3.59e-47

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: 148.91  E-value: 3.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884    4 PGDKAPDFDLPTDTGR-VSLSALKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFRAKH 82
Cdd:pfam00578   1 VGDKAPDFELPDGDGGtVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEKY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 221234884   83 DLTIELAADTLGDVVESYGAWVEksmygrKYMGIDRSTFLIDREGVIREI 132
Cdd:pfam00578  81 GLPFPLLSDPDGEVARAYGVLNE------EEGGALRATFVIDPDGKVRYI 124
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
8-149 3.14e-44

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 141.93  E-value: 3.14e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   8 APDFDLPTDTGR-VSLSALKGKNVVLYFYpKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFRAKHDLTI 86
Cdd:COG1225    1 APDFTLPDLDGKtVSLSDLRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYGLPF 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221234884  87 ELAADTLGDVVESYGAWVEksmygrkymgidRSTFLIDREGVIREIW-RKVKVPGHIKAVMNAA 149
Cdd:COG1225   80 PLLSDPDGEVAKAYGVRGT------------PTTFLIDPDGKIRYVWvGPVDPRPHLEEVLEAL 131
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 2-147 1.89e-38

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 127.75  E-value: 1.89e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   2 LQPGDKAPDFDLPTDTGR-VSLSALKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFRA 80
Cdd:PRK09437   4 LKAGDIAPKFSLPDQDGEqVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLSRFAE 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221234884  81 KHDLTIELAADTLGDVVESYGAWVEKSMYGRKYMGIDRSTFLIDREGVIREIWRKVKVPGHIKAVMN 147
Cdd:PRK09437  84 KELLNFTLLSDEDHQVAEQFGVWGEKKFMGKTYDGIHRISFLIDADGKIEHVFDKFKTSNHHDVVLD 150
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-137 1.27e-30

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 109.01  E-value: 1.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   1 MLQPGDKAPDFDLPTDTG----RVSLSALKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHA 76
Cdd:COG0450    2 MPLIGDKAPDFTAEATHGgefkKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884  77 KFRA--KHDLTIE-----LAADTLGDVVESYGAWVEKSmygrkymGI-DRSTFLIDREGVIR--------------EIWR 134
Cdd:COG0450   82 AWHEtiKEKGGIVkikfpIIADPTGKIARAYGMLHPED-------GVaVRGVFIIDPDGKIRaievyplsvgrnvdEILR 154


                 ...
gi 221234884 135 KVK 137
Cdd:COG0450  155 VVD 157
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 5-132 4.68e-30

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: 106.82  E-value: 4.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   5 GDKAPDFDLPT-----DTGRVSLSALKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFR 79
Cdd:cd03015    2 GKKAPDFKATAvvpngEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAWR 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221234884  80 AKH-------DLTIELAADTLGDVVESYGAWVEKSmygrkymGI-DRSTFLIDREGVIREI 132
Cdd:cd03015   82 NTPrkegglgKINFPLLADPKKKISRDYGVLDEEE-------GVaLRGTFIIDPEGIIRHI 135
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 2-134 8.31e-30

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: 105.82  E-value: 8.31e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   2 LQPGDKAPDFDLPTDTG-RVSLSALKG-KNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFR 79
Cdd:cd03018    1 LEVGDKAPDFELPDQNGqEVRLSEFRGrKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAWA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 221234884  80 AKHDLTIELAAD--TLGDVVESYGAWVEKSMYGRkymgidRSTFLIDREGVIREIWR 134
Cdd:cd03018   81 EENGLTFPLLSDfwPHGEVAKAYGVFDEDLGVAE------RAVFVIDRDGIIRYAWV 131
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 3-132 3.17e-21

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 83.57  E-value: 3.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884    3 QPGDKAPDFDLP---TDTGRVSLSALKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAK-F 78
Cdd:pfam08534   1 KAGDKAPDFTLPdaaTDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAFFVKrF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 221234884   79 RAKHDLTIELAADTLGDVVESYGAWVEKSMYGRKYMgidRSTFLIDREGVIREI 132
Cdd:pfam08534  81 WGKEGLPFPFLSDGNAAFTKALGLPIEEDASAGLRS---PRYAVIDEDGKVVYL 131
PRK13189 PRK13189
peroxiredoxin; Provisional
 1-132 8.69e-20

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 81.57  E-value: 8.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   1 MLQPGDKAPDFDLPTDTGRVSLSA-LKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKF- 78
Cdd:PRK13189   8 MPLIGDKFPEFEVKTTHGPIKLPDdYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSHIKWv 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 221234884  79 ---RAKHDLTIE--LAADTLGDVVESYGAWVEKsmygrKYMGIDRSTFLIDREGVIREI 132
Cdd:PRK13189  88 ewiKEKLGVEIEfpIIADDRGEIAKKLGMISPG-----KGTNTVRAVFIIDPKGIIRAI 141
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 5-130 1.27e-19

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: 80.66  E-value: 1.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   5 GDKAPDFDLPTDTGRVSLSALKGKN-VVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKF----- 78
Cdd:cd03016    2 GDTAPNFEADTTHGPIKFHDYLGDSwGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWiedie 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221234884  79 -RAKHDLTIELAADTLGDVVESYGawveksMygrkymgID---------RSTFLIDREGVIR 130
Cdd:cd03016   82 eYTGVEIPFPIIADPDREVAKLLG------M-------IDpdagstltvRAVFIIDPDKKIR 130
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 1-130 2.05e-18

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 77.59  E-value: 2.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   1 MLQPGDKAPDFDLPTDTGRVSLSALKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFra 80
Cdd:PRK13190   1 PVKLGQKAPDFTVNTTKGPIDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHIAW-- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221234884  81 khdltielaadtLGDVVESYG--------AWVEKSMyGRKYMGID-------RSTFLIDREGVIR 130
Cdd:PRK13190  79 ------------LRDIEERFGikipfpviADIDKEL-AREYNLIDensgatvRGVFIIDPNQIVR 130
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 8-132 7.08e-18

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 76.10  E-value: 7.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   8 APDFD----LPTDT-GRVSLSALKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKF---- 78
Cdd:PTZ00253  12 APSFEevalMPNGSfKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQWtlqe 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 221234884  79 RAKHDL---TIELAADTLGDVVESYGAWVEKSmyGRKYMGIdrstFLIDREGVIREI 132
Cdd:PTZ00253  92 RKKGGLgtmAIPMLADKTKSIARSYGVLEEEQ--GVAYRGL----FIIDPKGMLRQI 142
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 5-153 6.82e-14

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 66.02  E-value: 6.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   5 GDKAPDFDLPTDTGRVSL-SALKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFRA--K 81
Cdd:PRK13191  10 GEKFPEMEVITTHGKIKLpDDYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWVMwiE 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221234884  82 HDLTIELA----ADTLGDVVESYGAwveksMYGRKYMGIDRSTFLIDREGVIREI-WRKVKVPGHIKAVMNAAKAIK 153
Cdd:PRK13191  90 KNLKVEVPfpiiADPMGNVAKRLGM-----IHAESSTATVRAVFIVDDKGTVRLIlYYPMEIGRNIDEILRAIRALQ 161
PRK13599 PRK13599
peroxiredoxin;
5-153 2.54e-12

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 61.65  E-value: 2.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   5 GDKAPDFDLPTDTGRVSLSA-LKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFRA--K 81
Cdd:PRK13599   5 GEKFPSMEVVTTQGVKRLPEdYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEwiK 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221234884  82 HDLTIELA----ADTLGDVVESYGAwveksMYGRKYMGIDRSTFLIDREGVIREI-WRKVKVPGHIKAVMNAAKAIK 153
Cdd:PRK13599  85 DNTNIAIPfpviADDLGKVSNQLGM-----IHPGKGTNTVRAVFIVDDKGTIRLImYYPQEVGRNVDEILRALKALQ 156
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 1-136 3.91e-12

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 59.70  E-value: 3.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   1 MLQPGDKAPDFDLPTDTGR-VSLSALKGKNVVLYFY-----PkddtagCTSEALQFSSEVEEFQklGAVIIGVS-KDSAA 73
Cdd:COG0526    1 MKAVGKPAPDFTLTDLDGKpLSLADLKGKPVLVNFWatwcpP------CRAEMPVLKELAEEYG--GVVFVGVDvDENPE 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221234884  74 SHAKFRAKHDLTIELAADTLGDVVESYGAwveksmygrkyMGIDrSTFLIDREGviREIWRKV 136
Cdd:COG0526   73 AVKAFLKELGLPYPVLLDPDGELAKAYGV-----------RGIP-TTVLIDKDG--KIVARHV 121
PRK15000 PRK15000
peroxiredoxin C;
27-130 1.75e-10

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 56.61  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884  27 GKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFRAK-------HDLTIELAADTLGDVVES 99
Cdd:PRK15000  34 GKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHNAWRNTpvdkggiGPVKYAMVADVKREIQKA 113

                         90       100       110
                 ....*....|....*....|....*....|.
gi 221234884 100 YGawVEKSMYGRKYmgidRSTFLIDREGVIR 130
Cdd:PRK15000 114 YG--IEHPDEGVAL----RGSFLIDANGIVR 138
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 7-134 1.82e-10

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: 55.44  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   7 KAPDFDLPTDTG-RVSLSALKGKN-VVLYFY-----PKddtagCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFR 79
Cdd:cd02970    1 TAPDFELPDAGGeTVTLSALLGEGpVVVVFYrgfgcPF-----CREYLRALSKLLPELDALGVELVAVGPESPEKLEAFD 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221234884  80 AKHDLTIELAADT-------LGdvVESYGAWVEKSMYGRKYMGIDRS------------TFLIDREGVIREIWR 134
Cdd:cd02970   76 KGKFLPFPVYADPdrklyraLG--LVRSLPWSNTPRALWKNAAIGFRgndegdglqlpgVFVIGPDGTILFAHV 147
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 20-132 1.87e-10

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 56.53  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884  20 VSLSALKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFRAKHDLTIELAADTLGDVVes 99
Cdd:PRK10382  24 VTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHKAWHSSSETIAKIKYAMIGDPT-- 101

                         90       100       110
                 ....*....|....*....|....*....|....
gi 221234884 100 yGAWVEKSMYGRKYMGI-DRSTFLIDREGVIREI 132
Cdd:PRK10382 102 -GALTRNFDNMREDEGLaDRATFVVDPQGIIQAI 134
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 10-132 6.05e-10

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 53.39  E-value: 6.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884  10 DFDLPTDTGR-VSLSALKGKNVVLYFY-----PkddtagCTSEALQFSSEVEEFQKLGAVIIGVS--KDSAASHAKFRAK 81
Cdd:cd02966    1 DFSLPDLDGKpVSLSDLKGKVVLVNFWaswcpP------CRAEMPELEALAKEYKDDGVEVVGVNvdDDDPAAVKAFLKK 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 221234884  82 HDLTIELAADTLGDVVESYGAwveksmygrkyMGIDrSTFLIDREGVIREI 132
Cdd:cd02966   75 YGITFPVLLDPDGELAKAYGV-----------RGLP-TTFLIDRDGRIRAR 113
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 3-130 1.44e-09

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: 52.97  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   3 QPGDKAPDFDLPT-DTGRVSLSALKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQklGAVIIGVSKDSAASHAKFRAK 81
Cdd:cd03014    1 KVGDKAPDFTLVTsDLSEVSLADFAGKVKVISVFPSIDTPVCATQTKRFNKEAAKLD--NTVVLTISADLPFAQKRWCGA 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 221234884  82 HDLT-IELAADT-LGDVVESYGAWVEKsmygrkyMGID-RSTFLIDREGVIR 130
Cdd:cd03014   79 EGVDnVTTLSDFrDHSFGKAYGVLIKD-------LGLLaRAVFVIDENGKVI 123
tpx PRK00522
thiol peroxidase;
2-78 7.45e-09

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 51.44  E-value: 7.45e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221234884   2 LQPGDKAPDFDL-PTDTGRVSLSALKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQklGAVIIGVSKDSAASHAKF 78
Cdd:PRK00522  18 PQVGDKAPDFTLvANDLSDVSLADFAGKRKVLNIFPSIDTGVCATSVRKFNQEAAELD--NTVVLCISADLPFAQKRF 93
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 31-132 1.03e-08

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 52.26  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884  31 VLYFYPKDDTAGCTSEALQFSSEVEEFQKLGAVIIGVSKDSAASHAKFR-------AKHDLTIELAADTLGDVVESYGAW 103
Cdd:PTZ00137 102 LLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHKAWKeldvrqgGVSPLKFPLFSDISREVSKSFGLL 181

                         90       100
                 ....*....|....*....|....*....
gi 221234884 104 VEKSMYgrkymgiDRSTFLIDREGVIREI 132
Cdd:PTZ00137 182 RDEGFS-------HRASVLVDKAGVVKHV 203
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
5-132 1.26e-08

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 51.16  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   5 GDKAPDFDLP-TDTGRVSLSALKGKNVVLYFY-----PkddtagCTSEALQFSSEVEEFQKLGAVIIGVSKDSAA-SHAK 77
Cdd:PRK03147  38 GKEAPNFVLTdLEGKKIELKDLKGKGVFLNFWgtwckP------CEKEMPYMNELYPKYKEKGVEIIAVNVDETElAVKN 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 221234884  78 FRAKHDLTIELAADTLGDVVESYGawveksmygrkyMGIDRSTFLIDREGVIREI 132
Cdd:PRK03147 112 FVNRYGLTFPVAIDKGRQVIDAYG------------VGPLPTTFLIDKDGKVVKV 154
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
2-130 1.74e-08

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 50.47  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   2 LQPGDKAPDFDLpTDTG--RVSLSALKGKNVVLYFYPKDDTAGCTSEALQFSSEVEEFQklGAVIIGVSKDSAASHAKFR 79
Cdd:COG2077   18 PKVGDKAPDFTL-VDTDlsDVTLSDFAGKRKVLNIVPSLDTPVCATSTRKFNEEAAKLD--NVVVLTISADLPFAQKRFC 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 221234884  80 AKHDLTielAADTLGDVVES-----YGAWVEKSmygrKYMGID-RSTFLIDREGVIR 130
Cdd:COG2077   95 GAEGID---NVVTLSDFRDRsfgkdYGVLIKEG----PLLGLLaRAVFVLDENGKVV 144
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 5-102 2.35e-03

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: 36.45  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221234884   5 GDKAPDFDLP-TDTGRVSLSAL-KGKNVVLYFYpkddTAGCTSEALQFSSEV---EEFQKLGAVIIGVSKDSAASH---- 75
Cdd:cd02969    1 GSPAPDFSLPdTDGKTYSLADFaDGKALVVMFI----CNHCPYVKAIEDRLNrlaKEYGAKGVAVVAINSNDIEAYpeds 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 221234884  76 ----AKFRAKHDLTIELAADTLGDVVESYGA 102
Cdd:cd02969   77 penmKAKAKEHGYPFPYLLDETQEVAKAYGA 107
 
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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