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Conserved domains on  [gi|17537401|ref|NP_494757|]
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protein-disulfide reductase [Caenorhabditis elegans]

Protein Classification

thioredoxin family protein( domain architecture ID 10121823)

thioredoxin family protein may function as a thiol disulfide reductase that catalyzes the reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif; similar to human nucleoredoxin-like protein 2 that may be involved in the maintenance of both the function and the viability of sensory neurons, including photoreceptors and olfactory neurons

CATH:  3.40.30.10
EC:  1.8.-.-
Gene Ontology:  GO:0015036
PubMed:  11441809|12074972|9099998|10049365|15558583|30367780
SCOP:  4000237

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 10-144 8.76e-55

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


:

Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 168.56  E-value: 8.76e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401  10 LENREGDELPAEEHLKGKIIGLYFSASWCPPCRAFTPKLKEFFEEIKKTHPEFEIIFVSRDRNSSDLVTYFKEHqGEWTY 89
Cdd:cd02964   1 LFLLDGEGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGKNFEIVFVSRDRSEESFNEYFSEM-PPWLA 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17537401  90 IPFGSDKIMS-LMQKYEVKTIPAMRIVNDQGEVIVQDARTEIQNKGenvEGLWAEW 144
Cdd:cd02964  80 VPFEDEELRElLEKQFKVEGIPTLVVLKPDGDVVTTNARDEVEEDP---GACAFPW 132
 
Name Accession Description Interval E-value
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 10-144 8.76e-55

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 168.56  E-value: 8.76e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401  10 LENREGDELPAEEHLKGKIIGLYFSASWCPPCRAFTPKLKEFFEEIKKTHPEFEIIFVSRDRNSSDLVTYFKEHqGEWTY 89
Cdd:cd02964   1 LFLLDGEGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGKNFEIVFVSRDRSEESFNEYFSEM-PPWLA 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17537401  90 IPFGSDKIMS-LMQKYEVKTIPAMRIVNDQGEVIVQDARTEIQNKGenvEGLWAEW 144
Cdd:cd02964  80 VPFEDEELRElLEKQFKVEGIPTLVVLKPDGDVVTTNARDEVEEDP---GACAFPW 132
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 26-121 7.94e-32

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 108.93  E-value: 7.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401    26 GKIIGLYFSASWCPPCRAFTPKLKEFFEEIKKTHPeFEIIFVSRDRNSSDLVTYFKEHQGEWTYIPFGSDKIMSLMQKYE 105
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKKKN-VEIVFVSLDRDLEEFKDYLKKMPKDWLSVPFDDDERNELKRKYG 79

                          90
                  ....*....|....*.
gi 17537401   106 VKTIPAMRIVNDQGEV 121
Cdd:pfam13905  80 VNAIPTLVLLDPNGEV 95
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 1-122 2.86e-21

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 83.20  E-value: 2.86e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401   1 MPQFlkgvTLENREGDELPAEEhLKGKIIGLYFSASWCPPCRAFTPKLKEFFEEikktHPEFEIIFVSRDRNSSDLVTYF 80
Cdd:COG0526   8 APDF----TLTDLDGKPLSLAD-LKGKPVLVNFWATWCPPCRAEMPVLKELAEE----YGGVVFVGVDVDENPEAVKAFL 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 17537401  81 KEHQGEWtyiPFGSDKIMSLMQKYEVKTIPAMRIVNDQGEVI 122
Cdd:COG0526  79 KELGLPY---PVLLDPDGELAKAYGVRGIPTTVLIDKDGKIV 117
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
10-149 3.63e-07

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 46.92  E-value: 3.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401   10 LENREGDELPAEEhLKGKIIGLYFSASWCPPCRAFTPKLKEFFEEIKKThpEFEIIFVSRDRNSSDLVTYFKEHQgewTY 89
Cdd:PRK03147  46 LTDLEGKKIELKD-LKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEK--GVEIIAVNVDETELAVKNFVNRYG---LT 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17537401   90 IPFGSDKIMSLMQKYEVKTIPAMRIVNDQGEV--IVQDARTEiqnkgENVEglwaEWMALIK 149
Cdd:PRK03147 120 FPVAIDKGRQVIDAYGVGPLPTTFLIDKDGKVvkVITGEMTE-----EQLE----EYLEKIK 172
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 20-50 5.59e-04

periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the biogenesis of c-type cytochromes as well as in disulfide bond formation in some periplasmic proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 129481 [Multi-domain]  Cd Length: 173  Bit Score: 38.22  E-value: 5.59e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 17537401    20 AEEHLKGKIIGLYFSASWCPPCRAFTPKLKE 50
Cdd:TIGR00385  57 ADVLTQGKPVLLNVWASWCPPCRAEHPYLNE 87
 
Name Accession Description Interval E-value
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 10-144 8.76e-55

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 168.56  E-value: 8.76e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401  10 LENREGDELPAEEHLKGKIIGLYFSASWCPPCRAFTPKLKEFFEEIKKTHPEFEIIFVSRDRNSSDLVTYFKEHqGEWTY 89
Cdd:cd02964   1 LFLLDGEGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGKNFEIVFVSRDRSEESFNEYFSEM-PPWLA 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17537401  90 IPFGSDKIMS-LMQKYEVKTIPAMRIVNDQGEVIVQDARTEIQNKGenvEGLWAEW 144
Cdd:cd02964  80 VPFEDEELRElLEKQFKVEGIPTLVVLKPDGDVVTTNARDEVEEDP---GACAFPW 132
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 15-134 6.60e-40

Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 130.48  E-value: 6.60e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401  15 GDELPAEEhLKGKIIGLYFSASWCPPCRAFTPKLKEFFEEIKKTHPEFEIIFVSRDRNSSDLVTYFKEHqgEWTYIPFGS 94
Cdd:cd03009   8 GGKVPVSS-LEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKESGKNFEIVFISWDRDEESFNDYFSKM--PWLAVPFSD 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17537401  95 DKIMS-LMQKYEVKTIPAMRIVNDQGEVIVQDARTEIQNKG 134
Cdd:cd03009  85 RERRSrLNRTFKIEGIPTLIILDADGEVVTTDARELVLEYG 125
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 26-121 7.94e-32

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 108.93  E-value: 7.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401    26 GKIIGLYFSASWCPPCRAFTPKLKEFFEEIKKTHPeFEIIFVSRDRNSSDLVTYFKEHQGEWTYIPFGSDKIMSLMQKYE 105
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKKKN-VEIVFVSLDRDLEEFKDYLKKMPKDWLSVPFDDDERNELKRKYG 79

                          90
                  ....*....|....*.
gi 17537401   106 VKTIPAMRIVNDQGEV 121
Cdd:pfam13905  80 VNAIPTLVLLDPNGEV 95
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 1-122 2.86e-21

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 83.20  E-value: 2.86e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401   1 MPQFlkgvTLENREGDELPAEEhLKGKIIGLYFSASWCPPCRAFTPKLKEFFEEikktHPEFEIIFVSRDRNSSDLVTYF 80
Cdd:COG0526   8 APDF----TLTDLDGKPLSLAD-LKGKPVLVNFWATWCPPCRAEMPVLKELAEE----YGGVVFVGVDVDENPEAVKAFL 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 17537401  81 KEHQGEWtyiPFGSDKIMSLMQKYEVKTIPAMRIVNDQGEVI 122
Cdd:COG0526  79 KELGLPY---PVLLDPDGELAKAYGVRGIPTTVLIDKDGKIV 117
TryX_like_RdCVF cd03008
Tryparedoxin (TryX)-like family, Rod-derived cone viability factor (RdCVF) subfamily; RdCVF is ...
 12-134 3.15e-17

Tryparedoxin (TryX)-like family, Rod-derived cone viability factor (RdCVF) subfamily; RdCVF is a thioredoxin (TRX)-like protein specifically expressed in photoreceptors. RdCVF was isolated and identified as a factor that supports cone survival in retinal cultures. Cone photoreceptor loss is responsible for the visual handicap resulting from the inherited disease, retinitis pigmentosa. RdCVF shows 33% similarity to TRX but does not exhibit any detectable thiol oxidoreductase activity.


Pssm-ID: 239306  Cd Length: 146  Bit Score: 73.31  E-value: 3.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401  12 NREGDELPAE----EHLKGKIIGLYFSASWCPPCRAFTPKLKEFFeeiKKTHPEFEI--------IFVSRDRNSSDLVTY 79
Cdd:cd03008   7 NSDRDELDTEreivARLENRVLLLFFGAVVSPQCQLFAPKLKDFF---VRLTDEFYVdrsaqlalVYVSMDQSEQQQESF 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17537401  80 FKEHQGEWTYIPFGSDKIMSLMQKYEVKTIPAMRIVNDQGEVIVQDARTEIQNKG 134
Cdd:cd03008  84 LKDMPKKWLFLPFEDEFRRELEAQFSVEELPTVVVLKPDGDVLAANAVDEILRLG 138
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 8-124 2.95e-16

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: 69.96  E-value: 2.95e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401   8 VTLENREGDELPAEEhLKGKIIGLYFSASWCPPCRAFTPKLKEFFEEIKKthPEFEIIFVS-RDRNSSDLVTYFKEHQge 86
Cdd:cd02966   2 FSLPDLDGKPVSLSD-LKGKVVLVNFWASWCPPCRAEMPELEALAKEYKD--DGVEVVGVNvDDDDPAAVKAFLKKYG-- 76

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 17537401  87 wTYIPFGSDKIMSLMQKYEVKTIPAMRIVNDQGEVIVQ 124
Cdd:cd02966  77 -ITFPVLLDPDGELAKAYGVRGLPTTFLIDRDGRIRAR 113
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
24-122 5.68e-14

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 64.50  E-value: 5.68e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401  24 LKGKIIGLYFSASWCPPCRAFTPKLKEFFEEIKKthPEFEIIFVSRDrnSSDLVTYFKEHQGeWTYiPFGSDKIMSLMQK 103
Cdd:COG1225  19 LRGKPVVLYFYATWCPGCTAELPELRDLYEEFKD--KGVEVLGVSSD--SDEAHKKFAEKYG-LPF-PLLSDPDGEVAKA 92

                        90
                ....*....|....*....
gi 17537401 104 YEVKTIPAMRIVNDQGEVI 122
Cdd:COG1225  93 YGVRGTPTTFLIDPDGKIR 111
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 24-123 1.03e-08

TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c.


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 50.37  E-value: 1.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401  24 LKGKIIGLYFSASWCPPCRAFTPKLkeffEEIKKTHPefeiiFVS---RDRNSSDLVTYFKEHQGEWTYIPfgsDKIMSL 100
Cdd:cd03011  18 LSGKPVLVYFWATWCPVCRFTSPTV----NQLAADYP-----VVSvalRSGDDGAVARFMQKKGYGFPVIN---DPDGVI 85

                        90       100
                ....*....|....*....|...
gi 17537401 101 MQKYEVKTIPAMRIVNDQGEVIV 123
Cdd:cd03011  86 SARWGVSVTPAIVIVDPGGIVFV 108
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 31-121 2.05e-08

TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 48.71  E-value: 2.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401  31 LYFSASWCPPCRAFTPKlkefFEEIKKTHPEFEIIFVSRDRNssdlvtyfkehqgewtyipfgsdkiMSLMQKYEVKTIP 110
Cdd:cd02947  15 VDFWAPWCGPCKAIAPV----LEELAEEYPKVKFVKVDVDEN-------------------------PELAEEYGVRSIP 65

                        90
                ....*....|.
gi 17537401 111 AMRIVNDQGEV 121
Cdd:cd02947  66 TFLFFKNGKEV 76
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 31-122 3.68e-08

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 48.28  E-value: 3.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401  31 LYFSASWCPPCRAFTPKLKEFFEEIKkthPEFEIIFVSRDRNssdlvtyfkehqgewtyipfgsdkiMSLMQKYEVKTIP 110
Cdd:COG3118  23 VDFWAPWCGPCKMLAPVLEELAAEYG---GKVKFVKVDVDEN-------------------------PELAAQFGVRSIP 74

                        90
                ....*....|..
gi 17537401 111 AMRIVNDqGEVI 122
Cdd:COG3118  75 TLLLFKD-GQPV 85
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
10-149 3.63e-07

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 46.92  E-value: 3.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401   10 LENREGDELPAEEhLKGKIIGLYFSASWCPPCRAFTPKLKEFFEEIKKThpEFEIIFVSRDRNSSDLVTYFKEHQgewTY 89
Cdd:PRK03147  46 LTDLEGKKIELKD-LKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEK--GVEIIAVNVDETELAVKNFVNRYG---LT 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17537401   90 IPFGSDKIMSLMQKYEVKTIPAMRIVNDQGEV--IVQDARTEiqnkgENVEglwaEWMALIK 149
Cdd:PRK03147 120 FPVAIDKGRQVIDAYGVGPLPTTFLIDKDGKVvkVITGEMTE-----EQLE----EYLEKIK 172
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
25-121 8.98e-07

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 44.72  E-value: 8.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401    25 KGKIIGLYFSASWCPPCRAFTPKLKEFFEEIKKTHPEFEIIFVSrdrnssdlVTYFKEHQGEWTYIpfgsDKIMSLMQKY 104
Cdd:pfam13098   3 NGKPVLVVFTDPDCPYCKKLKKELLEDPDVTVYLGPNFVFIAVN--------IWCAKEVAKAFTDI----LENKELGRKY 70

                          90
                  ....*....|....*..
gi 17537401   105 EVKTIPAMRIVNDQGEV 121
Cdd:pfam13098  71 GVRGTPTIVFFDGKGEL 87
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 9-121 2.13e-06

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 44.14  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401     9 TLENREGDELPAEEhLKGKIIGLYF-SASWCPPCRAFTPKLKEFFEEIKKThpEFEIIFVSRDrnSSDLVTYFKEHQGEW 87
Cdd:pfam00578   9 ELPDGDGGTVSLSD-YRGKWVVLFFyPADWTPVCTTELPALADLYEEFKKL--GVEVLGVSVD--SPESHKAFAEKYGLP 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 17537401    88 tyIPFGSDKIMSLMQKYEVK------TIPAMRIVNDQGEV 121
Cdd:pfam00578  84 --FPLLSDPDGEVARAYGVLneeeggALRATFVIDPDGKV 121
PTZ00051 PTZ00051
thioredoxin; Provisional
 33-122 1.46e-04

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 38.70  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401   33 FSASWCPPCRAFTPklkeFFEEIKKTHPefEIIFVSRDrnssdlvtyfkehqgewtyipfgSDKIMSLMQKYEVKTIPAM 112
Cdd:PTZ00051  25 FYAEWCGPCKRIAP----FYEECSKEYT--KMVFVKVD-----------------------VDELSEVAEKENITSMPTF 75

                         90
                 ....*....|
gi 17537401  113 RiVNDQGEVI 122
Cdd:PTZ00051  76 K-VFKNGSVV 84
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 27-129 2.91e-04

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 37.98  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401    27 KIIGLYFSASWCPPCRAFTPKLKEFFEEIKKThpefeIIFVSRDrnssdlvtyfkehqgewtyipfgSDKIMSLMQKYEV 106
Cdd:pfam00085  19 KPVLVDFYAPWCGPCKMLAPEYEELAQEYKGN-----VVFAKVD-----------------------VDENPDLASKYGV 70

                          90       100
                  ....*....|....*....|...
gi 17537401   107 KTIPAMRIVNDQGEVIVQDARTE 129
Cdd:pfam00085  71 RGYPTLIFFKNGQPVDDYVGARP 93
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 20-50 5.59e-04

periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the biogenesis of c-type cytochromes as well as in disulfide bond formation in some periplasmic proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 129481 [Multi-domain]  Cd Length: 173  Bit Score: 38.22  E-value: 5.59e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 17537401    20 AEEHLKGKIIGLYFSASWCPPCRAFTPKLKE 50
Cdd:TIGR00385  57 ADVLTQGKPVLLNVWASWCPPCRAEHPYLNE 87
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 33-56 1.74e-03

PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is composed of the three TRX domains located at the C-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation. Also included in the alignment is the single complete TRX domain of an uncharacterized protein from Tetraodon nigroviridis, which also contains a DnaJ domain at its N-terminus.


Pssm-ID: 239302 [Multi-domain]  Cd Length: 104  Bit Score: 35.73  E-value: 1.74e-03
                        10        20
                ....*....|....*....|....
gi 17537401  33 FSASWCPPCRAFTPKLKEFFEEIK 56
Cdd:cd03004  26 FYAPWCGPCQALLPELRKAARALK 49
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 21-68 1.87e-03

TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli.


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 35.71  E-value: 1.87e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 17537401  21 EEHLKG---KIIGLYFSASWCPPCRAFtpklKEFFEEI-KKTHPefEIIFVS 68
Cdd:cd02984   6 EELLKSdasKLLVLHFWAPWAEPCKQM----NQVFEELaKEAFP--SVLFLS 51
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 33-60 1.92e-03

PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein containing an N-terminal redox active TRX domain, similar to that of PDI, and a small C-terminal flavin adenine dinucleotide (FAD)-binding domain homologous to the yeast ERV1p protein. QSOX oxidizes thiol groups to disulfides like PDI, however, unlike PDI, this oxidation is accompanied by the reduction of oxygen to hydrogen peroxide. QSOX is localized in high concentrations in cells with heavy secretory load and prefers peptides and proteins as substrates, not monothiols like glutathione. Inside the cell, QSOX is found in the endoplasmic reticulum and Golgi. The flow of reducing equivalents in a QSOX-catalyzed reaction goes from the dithiol substrate -> dithiol of the QSOX TRX domain -> dithiols of the QSOX ERV1p domain -> FAD -> oxygen.


Pssm-ID: 239290 [Multi-domain]  Cd Length: 114  Bit Score: 36.09  E-value: 1.92e-03
                        10        20
                ....*....|....*....|....*...
gi 17537401  33 FSASWCPPCRAFTPKLKEFFEEIKKTHP 60
Cdd:cd02992  26 FYASWCGHCRAFAPTWKKLARDLRKWRP 53
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 24-122 2.84e-03

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 35.81  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401    24 LKGKIIGLYFSAS-WCPPCRAFTPKLKEFFEEIKKThpEFEIIFVSRDRNSSDLVTYFKEHQGewtYIPFGSDKIMSLMQ 102
Cdd:pfam08534  26 FKGKKVVLNFWPGaFCPTCSAEHPYLEKLNELYKEK--GVDVVAVNSDNDAFFVKRFWGKEGL---PFPFLSDGNAAFTK 100

                          90       100
                  ....*....|....*....|....*....
gi 17537401   103 KYEVKT---------IPAMRIVNDQGEVI 122
Cdd:pfam08534 101 ALGLPIeedasaglrSPRYAVIDEDGKVV 129
Thioredoxin_9 pfam14595
Thioredoxin;
1-122 2.95e-03

Thioredoxin;


Pssm-ID: 434059 [Multi-domain]  Cd Length: 129  Bit Score: 35.71  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537401     1 MPQFLKGVTLENRE------------GDELPAEEHLKGKIIGLYFSASWCPPCRAFTPklkeFFEEIKKTHPEFEIIFVS 68
Cdd:pfam14595   4 FSEYLEGMTKLNKErmlriydkfelsEELIEKIKSIEKPLRILVITEDWCGDAAQNVP----VLAKIAELNPNIELRILL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17537401    69 RDRNSsdlvtyfkehqgewtyipfgsdkimSLMQKY---EVKTIPAMRIVNDQGEVI 122
Cdd:pfam14595  80 RDENL-------------------------ELMDQYltgGGRAIPTFIFLDEDGEEL 111
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 1-54 5.41e-03

TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c.


Pssm-ID: 239308 [Multi-domain]  Cd Length: 127  Bit Score: 34.86  E-value: 5.41e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17537401   1 MPQFlkgvTLENREGDELP-AEEHLKGKIIGLYFSASWCPPCRAFTPKLKEFFEE 54
Cdd:cd03010   3 APAF----SLPALPGPDKTlTSADLKGKPYLLNVWASWCAPCREEHPVLMALARQ 53
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 31-80 6.39e-03

Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 33.83  E-value: 6.39e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 17537401  31 LYFSASWCPPCRAFTPKLKEFFEEIKKThpEFEIIFVSRDRNSSDLVTYF 80
Cdd:cd01659   2 VLFYAPWCPFCQALRPVLAELALLNKGV--KFEAVDVDEDPALEKELKRY 49
 
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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