NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|495964247|ref|WP_008688826|]
View 

MULTISPECIES: thioredoxin-dependent thiol peroxidase [Longicatena]

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|GO:0008379
PubMed:  15518547|12517450|10644761|15558583
SCOP:  4000042

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 8-148 6.50e-72

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: 212.41  E-value: 6.50e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   8 AIDFTLPDEQGNLISLHSFKGKKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRFKEKYDLPF 87
Cdd:cd03017    3 APDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYGLPF 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495964247  88 ILLSDEEHKVIEAYDVWKEKKlygKTYMGITRSTYVIDEEGTIIKTFEKANPATNAQDILE 148
Cdd:cd03017   83 PLLSDPDGKLAKAYGVWGEKK---KKYMGIERSTFLIDPDGKIVKVWRKVKPKGHAEEVLE 140
 
Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 8-148 6.50e-72

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: 212.41  E-value: 6.50e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   8 AIDFTLPDEQGNLISLHSFKGKKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRFKEKYDLPF 87
Cdd:cd03017    3 APDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYGLPF 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495964247  88 ILLSDEEHKVIEAYDVWKEKKlygKTYMGITRSTYVIDEEGTIIKTFEKANPATNAQDILE 148
Cdd:cd03017   83 PLLSDPDGKLAKAYGVWGEKK---KKYMGIERSTFLIDPDGKIVKVWRKVKPKGHAEEVLE 140
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 2-152 2.26e-53

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 165.88  E-value: 2.26e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   2 LEIGTTAIDFTLPDEQGNLISLHSFKGKKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRFKE 81
Cdd:PRK09437   4 LKAGDIAPKFSLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLSRFAE 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495964247  82 KYDLPFILLSDEEHKVIEAYDVWKEKKLYGKTYMGITRSTYVIDEEGTIIKTFEKANPATNAQDILEYLAQ 152
Cdd:PRK09437  84 KELLNFTLLSDEDHQVAEQFGVWGEKKFMGKTYDGIHRISFLIDADGKIEHVFDKFKTSNHHDVVLDYLKE 154
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 4-130 1.75e-48

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: 152.38  E-value: 1.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247    4 IGTTAIDFTLPDEQGNLISLHSFKGKKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRFKEKY 83
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 495964247   84 DLPFILLSDEEHKVIEAYDVWKEKklygktYMGITRSTYVIDEEGTI 130
Cdd:pfam00578  81 GLPFPLLSDPDGEVARAYGVLNEE------EGGALRATFVIDPDGKV 121
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
8-152 2.71e-48

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 152.33  E-value: 2.71e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   8 AIDFTLPDEQGNLISLHSFKGKKIVLYFYpKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRFKEKYDLPF 87
Cdd:COG1225    1 APDFTLPDLDGKTVSLSDLRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYGLPF 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495964247  88 ILLSDEEHKVIEAYDVWKekklygktymgiTRSTYVIDEEGTIIKTFE-KANPATNAQDILEYLAQ 152
Cdd:COG1225   80 PLLSDPDGEVAKAYGVRG------------TPTTFLIDPDGKIRYVWVgPVDPRPHLEEVLEALLA 133
 
Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 8-148 6.50e-72

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: 212.41  E-value: 6.50e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   8 AIDFTLPDEQGNLISLHSFKGKKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRFKEKYDLPF 87
Cdd:cd03017    3 APDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYGLPF 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495964247  88 ILLSDEEHKVIEAYDVWKEKKlygKTYMGITRSTYVIDEEGTIIKTFEKANPATNAQDILE 148
Cdd:cd03017   83 PLLSDPDGKLAKAYGVWGEKK---KKYMGIERSTFLIDPDGKIVKVWRKVKPKGHAEEVLE 140
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 2-152 2.26e-53

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 165.88  E-value: 2.26e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   2 LEIGTTAIDFTLPDEQGNLISLHSFKGKKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRFKE 81
Cdd:PRK09437   4 LKAGDIAPKFSLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLSRFAE 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495964247  82 KYDLPFILLSDEEHKVIEAYDVWKEKKLYGKTYMGITRSTYVIDEEGTIIKTFEKANPATNAQDILEYLAQ 152
Cdd:PRK09437  84 KELLNFTLLSDEDHQVAEQFGVWGEKKFMGKTYDGIHRISFLIDADGKIEHVFDKFKTSNHHDVVLDYLKE 154
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 7-148 1.07e-51

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: 161.18  E-value: 1.07e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   7 TAIDFTLPDEQGNLISLHSFKGKKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRFKEKY-DL 85
Cdd:cd02971    1 KAPDFTLPATDGGEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEKEgGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495964247  86 PFILLSDEEHKVIEAYDVWKEKKlygKTYMGITRSTYVIDEEGTIIKTFEKANPATNAQDILE 148
Cdd:cd02971   81 NFPLLSDPDGEFAKAYGVLIEKS---AGGGLAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 4-130 1.75e-48

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: 152.38  E-value: 1.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247    4 IGTTAIDFTLPDEQGNLISLHSFKGKKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRFKEKY 83
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 495964247   84 DLPFILLSDEEHKVIEAYDVWKEKklygktYMGITRSTYVIDEEGTI 130
Cdd:pfam00578  81 GLPFPLLSDPDGEVARAYGVLNEE------EGGALRATFVIDPDGKV 121
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
8-152 2.71e-48

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 152.33  E-value: 2.71e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   8 AIDFTLPDEQGNLISLHSFKGKKIVLYFYpKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRFKEKYDLPF 87
Cdd:COG1225    1 APDFTLPDLDGKTVSLSDLRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYGLPF 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495964247  88 ILLSDEEHKVIEAYDVWKekklygktymgiTRSTYVIDEEGTIIKTFE-KANPATNAQDILEYLAQ 152
Cdd:COG1225   80 PLLSDPDGEVAKAYGVRG------------TPTTFLIDPDGKIRYVWVgPVDPRPHLEEVLEALLA 133
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 2-153 3.16e-32

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: 111.98  E-value: 3.16e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   2 LEIGTTAIDFTLPDEQGNLISLHSFKG-KKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRFK 80
Cdd:cd03018    1 LEVGDKAPDFELPDQNGQEVRLSEFRGrKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAWA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495964247  81 EKYDLPFILLSD--EEHKVIEAYDVWKEKKlygktymGIT-RSTYVIDEEGTIikTFEKANPATNAQDILEYLAQL 153
Cdd:cd03018   81 EENGLTFPLLSDfwPHGEVAKAYGVFDEDL-------GVAeRAVFVIDRDGII--RYAWVSDDGEPRDLPDYDEAL 147
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-147 5.50e-25

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 94.76  E-value: 5.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   1 MLEIGTTAIDFTLPDEQGNL---ISLHSFKGKKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHL 77
Cdd:COG0450    2 MPLIGDKAPDFTAEATHGGEfkkISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247  78 RF----KEKY---DLPFILLSDEEHKVIEAYDVWKEKklygktyMGIT-RSTYVIDEEGtIIKTFEkANPAT---NAQDI 146
Cdd:COG0450   82 AWhetiKEKGgivKIKFPIIADPTGKIARAYGMLHPE-------DGVAvRGVFIIDPDG-KIRAIE-VYPLSvgrNVDEI 152


                 .
gi 495964247 147 L 147
Cdd:COG0450  153 L 153
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 5-150 5.91e-24

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 90.89  E-value: 5.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247    5 GTTAIDFTLPD--EQGNLISLHSFKGKKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSH-LRFKE 81
Cdd:pfam08534   3 GDKAPDFTLPDaaTDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAFFvKRFWG 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   82 KYDLPFILLSDEEHKVIEAYDV-WKEKKLYGKTymgiTRSTYVIDEEGTIIKTFEKANPATNAQDILEYL 150
Cdd:pfam08534  83 KEGLPFPFLSDGNAAFTKALGLpIEEDASAGLR----SPRYAVIDEDGKVVYLFVGPEPGVDVSDAEAVL 148
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 1-156 2.98e-18

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 75.88  E-value: 2.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   1 MLEIGTTAIDFTLPDEQGNLISLHSFKGKKIVLYFYpkdNT--PGCSKQACAFKAAYDVYKrnDIIVIGISKDSSRSHLR 78
Cdd:COG0526    1 MKAVGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFW---ATwcPPCRAEMPVLKELAEEYG--GVVFVGVDVDENPEAVK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247  79 -FKEKYDLPFILLSDEEHKVIEAYDVwkekklygktyMGI-TrsTYVIDEEGTIIKTFEkanPATNAQDILEYLAQLSNE 156
Cdd:COG0526   76 aFLKELGLPYPVLLDPDGELAKAYGV-----------RGIpT--TVLIDKDGKIVARHV---GPLSPEELEEALEKLLAK 139
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 4-130 1.67e-17

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: 74.85  E-value: 1.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   4 IGTTAIDFT----LPDEQGNLISLHSFKGKKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRF 79
Cdd:cd03015    1 VGKKAPDFKatavVPNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495964247  80 KEKY-------DLPFILLSDEEHKVIEAYDVWKEKKlygktymGIT-RSTYVIDEEGTI 130
Cdd:cd03015   81 RNTPrkegglgKINFPLLADPKKKISRDYGVLDEEE-------GVAlRGTFIIDPEGII 132
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 1-150 1.16e-14

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 67.96  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   1 MLEIGTTAIDFTLPDEQGnLISLHSFKGKKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRF- 79
Cdd:PRK13190   1 PVKLGQKAPDFTVNTTKG-PIDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHIAWl 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495964247  80 ---KEKY--DLPFILLSDEEHKVIEAYDVWKEKKlyGKTymgiTRSTYVIDEEGTIikTFEKANPATNAQDILEYL 150
Cdd:PRK13190  80 rdiEERFgiKIPFPVIADIDKELAREYNLIDENS--GAT----VRGVFIIDPNQIV--RWMIYYPAETGRNIDEII 147
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 10-134 2.81e-14

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: 64.95  E-value: 2.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247  10 DFTLPDEQGNLISLHSFKGKKIVLYFY-----PkdntpgCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSH--LRFKEK 82
Cdd:cd02966    1 DFSLPDLDGKPVSLSDLKGKVVLVNFWaswcpP------CRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAavKAFLKK 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495964247  83 YDLPFILLSDEEHKVIEAYDVwkekklygktyMGITrSTYVIDEEGTIIKTF 134
Cdd:cd02966   75 YGITFPVLLDPDGELAKAYGV-----------RGLP-TTFLIDRDGRIRARH 114
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
2-131 2.65e-13

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 63.57  E-value: 2.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   2 LEIGTTAIDFTLPDEQGNLISLHSFKGKKIVLYFYPKDNTPGCSKQACAF--KAAydvyKRNDIIVIGISKdssrshlrf 79
Cdd:COG2077   18 PKVGDKAPDFTLVDTDLSDVTLSDFAGKRKVLNIVPSLDTPVCATSTRKFneEAA----KLDNVVVLTISA--------- 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495964247  80 kekyDLPF--------------ILLSD-EEHKVIEAYDVW-KEKKLYGKTymgiTRSTYVIDEEGTII 131
Cdd:COG2077   85 ----DLPFaqkrfcgaegidnvVTLSDfRDRSFGKDYGVLiKEGPLLGLL----ARAVFVLDENGKVV 144
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 4-130 7.16e-13

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: 62.94  E-value: 7.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   4 IGTTAIDFTLPDEQGNlISLHSFKGKKIVLYF-YPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRFKE- 81
Cdd:cd03016    1 LGDTAPNFEADTTHGP-IKFHDYLGDSWGILFsHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIEd 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495964247  82 -----KYDLPFILLSDEEHKVIEAYDVWKEKKlygktymGIT---RSTYVIDEEGTI 130
Cdd:cd03016   80 ieeytGVEIPFPIIADPDREVAKLLGMIDPDA-------GSTltvRAVFIIDPDKKI 129
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 3-131 1.43e-12

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: 61.06  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   3 EIGTTAIDFTLPDEQGNLISLHSFKGKKIVLYFYPKDNTPGCSKQACAFKAAYDvyKRNDIIVIGISKDSSRSHLRFKEK 82
Cdd:cd03014    1 KVGDKAPDFTLVTSDLSEVSLADFAGKVKVISVFPSIDTPVCATQTKRFNKEAA--KLDNTVVLTISADLPFAQKRWCGA 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495964247  83 YDLP-FILLSD-EEHKVIEAYDVW-KEKKLYgktymgiTRSTYVIDEEGTII 131
Cdd:cd03014   79 EGVDnVTTLSDfRDHSFGKAYGVLiKDLGLL-------ARAVFVIDENGKVI 123
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
3-132 3.10e-11

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 58.09  E-value: 3.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   3 EIGTTAIDFTLPDEQGNLISLHSFKGKKIVLYFYPKDNTPgCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHL-RFKE 81
Cdd:PRK03147  36 QVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKP-CEKEMPYMNELYPKYKEKGVEIIAVNVDETELAVkNFVN 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495964247  82 KYDLPFILLSDEEHKVIEAYDVwkekklygktymGITRSTYVIDEEGTIIK 132
Cdd:PRK03147 115 RYGLTFPVAIDKGRQVIDAYGV------------GPLPTTFLIDKDGKVVK 153
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 13-130 1.32e-10

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 57.22  E-value: 1.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247  13 LPDEQGNLISLHSFKGKKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRF----KEKYDLPFI 88
Cdd:PTZ00253  21 MPNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQWtlqeRKKGGLGTM 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 495964247  89 ---LLSDEEHKVIEAYDVWKEKKlyGKTYMGItrstYVIDEEGTI 130
Cdd:PTZ00253 101 aipMLADKTKSIARSYGVLEEEQ--GVAYRGL----FIIDPKGML 139
tpx PRK00522
thiol peroxidase;
4-133 1.00e-09

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 54.14  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   4 IGTTAIDFTLPDEQGNLISLHSFKGKKIVLYFYPKDNTPGCSKQACAF--KAAydvyKRNDIIVIGISKdssrshlrfke 81
Cdd:PRK00522  20 VGDKAPDFTLVANDLSDVSLADFAGKRKVLNIFPSIDTGVCATSVRKFnqEAA----ELDNTVVLCISA----------- 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495964247  82 kyDLPF--------------ILLSD-EEHKVIEAYDVW-KEKKLYGKTymgiTRSTYVIDEEGTIIKT 133
Cdd:PRK00522  85 --DLPFaqkrfcgaeglenvITLSDfRDHSFGKAYGVAiAEGPLKGLL----ARAVFVLDENNKVVYS 146
PRK13189 PRK13189
peroxiredoxin; Provisional
 1-130 4.79e-09

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 53.06  E-value: 4.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   1 MLEIGTTAIDFTLPDEQGNL-ISLHsFKGKKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRF 79
Cdd:PRK13189   8 MPLIGDKFPEFEVKTTHGPIkLPDD-YKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSHIKW 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495964247  80 ----KEKYDL--PFILLSDEEHKVIEAYDVWKEKKlyGKTymgITRSTYVIDEEGTI 130
Cdd:PRK13189  87 vewiKEKLGVeiEFPIIADDRGEIAKKLGMISPGK--GTN---TVRAVFIIDPKGII 138
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 5-101 1.04e-08

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: 51.47  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   5 GTTAIDFTLPDEQGNLISLHSFKGKKIVLYFYPkdntpgCSKqaCAF-KAAYDV-------YKRNDIIVIGISKDSSRSH 76
Cdd:cd02969    1 GSPAPDFSLPDTDGKTYSLADFADGKALVVMFI------CNH--CPYvKAIEDRlnrlakeYGAKGVAVVAINSNDIEAY 72

                         90       100       110
                 ....*....|....*....|....*....|...
gi 495964247  77 --------LRFKEKYDLPFILLSDEEHKVIEAY 101
Cdd:cd02969   73 pedspenmKAKAKEHGYPFPYLLDETQEVAKAY 105
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 2-130 1.57e-08

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 51.39  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   2 LEIGTTAIDFTLPDEqgnlislhsFKGKKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRF-- 79
Cdd:PRK13191  16 MEVITTHGKIKLPDD---------YKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWvm 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495964247  80 ----KEKYDLPFILLSDEEHKVIEaydvwKEKKLYGKTYMGITRSTYVIDEEGTI 130
Cdd:PRK13191  87 wiekNLKVEVPFPIIADPMGNVAK-----RLGMIHAESSTATVRAVFIVDDKGTV 136
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 12-156 3.40e-08

Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441602  Cd Length: 156  Bit Score: 49.90  E-value: 3.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247  12 TLPDEQGNLISLHSFKGKKIVLYF-YpkdnT--PG-CSKQACAFKAAYDVYK---RNDIIVIGISKDSSR---SHLR-FK 80
Cdd:COG1999    4 TLTDQDGKPVTLADLRGKPVLVFFgY----TscPDvCPTTLANLAQVQEALGedgGDDVQVLFISVDPERdtpEVLKaYA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247  81 EKYDLP-FILLS-DEE--HKVIEAYDVWKEKKLYGKTYMGITRSTYVIDEEGTIIKTFekaNPATNAQDILEYLAQLSNE 156
Cdd:COG1999   80 EAFGAPrWIGLTgDPEeiAALAKAFGVYYEKVPDGDYTFDHSAAVYLVDPDGRLRGYY---PAGEDPEELAADLKALLEE 156
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 7-101 3.77e-06

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: 44.27  E-value: 3.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   7 TAIDFTLPDEQGNLISLHSFKG-KKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDsSRSHLR-FKEKYD 84
Cdd:cd02970    1 TAPDFELPDAGGETVTLSALLGeGPVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGPE-SPEKLEaFDKGKF 79

                         90
                 ....*....|....*..
gi 495964247  85 LPFILLSDEEHKVIEAY 101
Cdd:cd02970   80 LPFPVYADPDRKLYRAL 96
PRK13599 PRK13599
peroxiredoxin;
26-153 4.40e-06

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 44.70  E-value: 4.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247  26 FKGKKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRFKE------KYDLPFILLSDEEHKVIE 99
Cdd:PRK13599  26 YAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEwikdntNIAIPFPVIADDLGKVSN 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495964247 100 AYDVwkekkLYGKTYMGITRSTYVIDEEGTI-IKTFEKANPATNAQDILEYLAQL 153
Cdd:PRK13599 106 QLGM-----IHPGKGTNTVRAVFIVDDKGTIrLIMYYPQEVGRNVDEILRALKAL 155
PRK15000 PRK15000
peroxiredoxin C;
1-130 2.88e-05

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 42.35  E-value: 2.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247   1 MLEIGTTAIDFTLPDEQGN--LISLHSFK----GKKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSR 74
Cdd:PRK15000   1 MVLVTRQAPDFTAAAVLGSgeIVDKFNFKqhtnGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495964247  75 SHLRFKEKY-------DLPFILLSDEEHKVIEAYDVWKEKKlygktymGIT-RSTYVIDEEGTI 130
Cdd:PRK15000  81 VHNAWRNTPvdkggigPVKYAMVADVKREIQKAYGIEHPDE-------GVAlRGSFLIDANGIV 137
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 10-134 3.43e-05

SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II.


Pssm-ID: 239266  Cd Length: 142  Bit Score: 41.43  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247  10 DFTLPDEQGNLISLHSFKGKKIVLYF-YpkdnT--PG-CSKQACAFKAAYDVYK---RNDIIVIGISKDSSR---SHLR- 78
Cdd:cd02968    4 DFTLTDQDGRPVTLSDLKGKPVLVYFgY----ThcPDvCPTTLANLAQALKQLGadgGDDVQVVFISVDPERdtpEVLKa 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495964247  79 FKEKYDLPFILL---SDEEHKVIEAYDV--WKEKKLYGKTYMGITRSTYVIDEEGTIIKTF 134
Cdd:cd02968   80 YAKAFGPGWIGLtgtPEEIEALAKAFGVyyEKVPEDDGDYLVDHSAAIYLVDPDGKLVRYY 140
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 18-130 2.19e-04

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 39.93  E-value: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495964247  18 GNLISLHS---FKGKKIVLYFYPKDNTPGCSKQACAFKAAYDVYKRNDIIVIGISKDSSRSHLRFKEK-------YDLPF 87
Cdd:PTZ00137  85 DDLVQFNSsdyFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHKAWKELdvrqggvSPLKF 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 495964247  88 ILLSDEEHKVIEAYDVWKEKKLYgktymgiTRSTYVIDEEGTI 130
Cdd:PTZ00137 165 PLFSDISREVSKSFGLLRDEGFS-------HRASVLVDKAGVV 200
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH