NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488914205|ref|WP_002825280|]
View 

MULTISPECIES: TlpA disulfide reductase family protein [Campylobacter]

Protein Classification

TlpA family protein disulfide reductase( domain architecture ID 10001660)

TlpA family protein disulfide reductase such as Bradyrhizobium japonicum thiol:disulfide interchange protein TlpA, an unusual thioredoxin which has been implicated in the biogenesis of cytochrome aa3 and also characterized as a reductant for the copper metallochaperone ScoI, and similar to ResA and DsbE, which are essential proteins in cytochrome c maturation

CATH:  3.40.30.10
Gene Ontology:  GO:0016491
PubMed:  11531338|15667290

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 46-184 3.52e-28

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


:

Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 102.46  E-value: 3.52e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205  46 FNLNLIDGNSIFIKKDNenlnfadgDKATLFVFFTTWCSPCIAEIPHLNKLQEKYEEqFNIVGVLLeDKSDEELRAFAQK 125
Cdd:COG0526   11 FTLTDLDGKPLSLADLK--------GKPVLVNFWATWCPPCRAEMPVLKELAEEYGG-VVFVGVDV-DENPEAVKAFLKE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488914205 126 NQILYKIANgENNYLLAKILgGVNGIPTMFLYDKNSQLVNQYLGLIPEEMLEIDIQKAI 184
Cdd:COG0526   81 LGLPYPVLL-DPDGELAKAY-GVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLL 137
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 46-184 3.52e-28

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 102.46  E-value: 3.52e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205  46 FNLNLIDGNSIFIKKDNenlnfadgDKATLFVFFTTWCSPCIAEIPHLNKLQEKYEEqFNIVGVLLeDKSDEELRAFAQK 125
Cdd:COG0526   11 FTLTDLDGKPLSLADLK--------GKPVLVNFWATWCPPCRAEMPVLKELAEEYGG-VVFVGVDV-DENPEAVKAFLKE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488914205 126 NQILYKIANgENNYLLAKILgGVNGIPTMFLYDKNSQLVNQYLGLIPEEMLEIDIQKAI 184
Cdd:COG0526   81 LGLPYPVLL-DPDGELAKAY-GVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLL 137
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 46-169 3.98e-25

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: 93.84  E-value: 3.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205  46 FNLNLIDGNSIfikkDNENLNfadgDKATLFVFFTTWCSPCIAEIPHLNKLQEKYEEQ-FNIVGVLLEDKSDEELRAFAQ 124
Cdd:cd02966    2 FSLPDLDGKPV----SLSDLK----GKVVLVNFWASWCPPCRAEMPELEALAKEYKDDgVEVVGVNVDDDDPAAVKAFLK 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 488914205 125 KNQILYKIANGENNYLLAKIlgGVNGIPTMFLYDKNSQLVNQYLG 169
Cdd:cd02966   74 KYGITFPVLLDPDGELAKAY--GVRGLPTTFLIDRDGRIRARHVG 116
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 46-160 2.36e-09

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: 53.00  E-value: 2.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205   46 FNLNLIDGNSIfikkdneNLNFADGDKATLFVFFTTWCSPCIAEIPHLNKLQEKYEEQ-FNIVGVLLEdkSDEELRAFAQ 124
Cdd:pfam00578   8 FELPDGDGGTV-------SLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLgVEVLGVSVD--SPESHKAFAE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 488914205  125 KNQILYKIANGENNyLLAKILGGVN-----GIPTMFLYDKN 160
Cdd:pfam00578  79 KYGLPFPLLSDPDG-EVARAYGVLNeeeggALRATFVIDPD 118
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
78-177 2.95e-09

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 53.47  E-value: 2.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205  78 FFTTWCSPCIAEIPHLNKLQEKYEEQ-FNIVGVLLeDKSDEELRAFAQKNQILYKIANGENNYLLAkiLGGVNGIPTMFL 156
Cdd:PRK03147  68 FWGTWCKPCEKEMPYMNELYPKYKEKgVEIIAVNV-DETELAVKNFVNRYGLTFPVAIDKGRQVID--AYGVGPLPTTFL 144

                         90       100
                 ....*....|....*....|.
gi 488914205 157 YDKNSQLVNQYLGLIPEEMLE 177
Cdd:PRK03147 145 IDKDGKVVKVITGEMTEEQLE 165
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 67-184 3.49e-06

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 43.82  E-value: 3.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205   67 FADGDKATLFVFFTTWCSPCIAEIPHLNKLQEKYEEQFNIVgvlledKSD-EELRAFAQKNqilykiangennyllakil 145
Cdd:TIGR01068  10 IASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFV------KLNvDENPDIAAKY------------------- 64

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 488914205  146 gGVNGIPTMFLYdKNSQLVNQYLGLIPEEMLEIDIQKAI 184
Cdd:TIGR01068  65 -GIRSIPTLLLF-KNGKEVDRSVGALPKAALKQLINKNL 101
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 46-184 3.52e-28

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 102.46  E-value: 3.52e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205  46 FNLNLIDGNSIFIKKDNenlnfadgDKATLFVFFTTWCSPCIAEIPHLNKLQEKYEEqFNIVGVLLeDKSDEELRAFAQK 125
Cdd:COG0526   11 FTLTDLDGKPLSLADLK--------GKPVLVNFWATWCPPCRAEMPVLKELAEEYGG-VVFVGVDV-DENPEAVKAFLKE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488914205 126 NQILYKIANgENNYLLAKILgGVNGIPTMFLYDKNSQLVNQYLGLIPEEMLEIDIQKAI 184
Cdd:COG0526   81 LGLPYPVLL-DPDGELAKAY-GVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLL 137
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 46-169 3.98e-25

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: 93.84  E-value: 3.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205  46 FNLNLIDGNSIfikkDNENLNfadgDKATLFVFFTTWCSPCIAEIPHLNKLQEKYEEQ-FNIVGVLLEDKSDEELRAFAQ 124
Cdd:cd02966    2 FSLPDLDGKPV----SLSDLK----GKVVLVNFWASWCPPCRAEMPELEALAKEYKDDgVEVVGVNVDDDDPAAVKAFLK 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 488914205 125 KNQILYKIANGENNYLLAKIlgGVNGIPTMFLYDKNSQLVNQYLG 169
Cdd:cd02966   74 KYGITFPVLLDPDGELAKAY--GVRGLPTTFLIDRDGRIRARHVG 116
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
71-183 1.57e-18

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 77.21  E-value: 1.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205  71 DKATLFVFFTTWCSPCIAEIPHLNKLQEKYEEQ-FNIVGVLLEDksDEELRAFAQKNQILYKIANGENNYlLAKILgGVN 149
Cdd:COG1225   21 GKPVVLYFYATWCPGCTAELPELRDLYEEFKDKgVEVLGVSSDS--DEAHKKFAEKYGLPFPLLSDPDGE-VAKAY-GVR 96

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488914205 150 GIPTMFLYDKNSQLVNQYLGLIP-----EEMLEIDIQKA 183
Cdd:COG1225   97 GTPTTFLIDPDGKIRYVWVGPVDprphlEEVLEALLAEL 135
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 69-184 2.57e-12

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: 60.22  E-value: 2.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205  69 DGDKATLFVFFTTWCSPCIAEIPHLNKLQEKYEEQFNIVGVlledksdeelrafaqknqilykiaNGENNYLLAKILgGV 148
Cdd:COG3118   16 ESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKV------------------------DVDENPELAAQF-GV 70

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488914205 149 NGIPTMFLYdKNSQLVNQYLGLIPEEMLEIDIQKAI 184
Cdd:COG3118   71 RSIPTLLLF-KDGQPVDRFVGALPKEQLREFLDKVL 105
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 46-160 2.36e-09

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: 53.00  E-value: 2.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205   46 FNLNLIDGNSIfikkdneNLNFADGDKATLFVFFTTWCSPCIAEIPHLNKLQEKYEEQ-FNIVGVLLEdkSDEELRAFAQ 124
Cdd:pfam00578   8 FELPDGDGGTV-------SLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLgVEVLGVSVD--SPESHKAFAE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 488914205  125 KNQILYKIANGENNyLLAKILGGVN-----GIPTMFLYDKN 160
Cdd:pfam00578  79 KYGLPFPLLSDPDG-EVARAYGVLNeeeggALRATFVIDPD 118
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
78-177 2.95e-09

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 53.47  E-value: 2.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205  78 FFTTWCSPCIAEIPHLNKLQEKYEEQ-FNIVGVLLeDKSDEELRAFAQKNQILYKIANGENNYLLAkiLGGVNGIPTMFL 156
Cdd:PRK03147  68 FWGTWCKPCEKEMPYMNELYPKYKEKgVEIIAVNV-DETELAVKNFVNRYGLTFPVAIDKGRQVID--AYGVGPLPTTFL 144

                         90       100
                 ....*....|....*....|.
gi 488914205 157 YDKNSQLVNQYLGLIPEEMLE 177
Cdd:PRK03147 145 IDKDGKVVKVITGEMTEEQLE 165
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 71-160 1.05e-08

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: 50.38  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205   71 DKATLFVFFTTWCSPCIAEIPHLNKLQEKYEE--QFNIVGVLLeDKSDEELRAFAQKNQ---ILYKIANGENNYLLAKIl 145
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKkkNVEIVFVSL-DRDLEEFKDYLKKMPkdwLSVPFDDDERNELKRKY- 78

                          90
                  ....*....|....*
gi 488914205  146 gGVNGIPTMFLYDKN 160
Cdd:pfam13905  79 -GVNAIPTLVLLDPN 92
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 71-177 3.70e-08

TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport.


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 50.03  E-value: 3.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205  71 DKATLFVFFTTWCSPCIAEIPHLNKLQEKYEEQFNIVGVlledksdeelrafaqknqilykiaNGENNYLLAKILG-GVN 149
Cdd:cd02950   20 GKPTLVEFYADWCTVCQEMAPDVAKLKQKYGDQVNFVML------------------------NVDNPKWLPEIDRyRVD 75

                         90       100
                 ....*....|....*....|....*...
gi 488914205 150 GIPTMFLYDKNSQLVNQYLGLIPEEMLE 177
Cdd:cd02950   76 GIPHFVFLDREGNEEGQSIGLQPKQVLA 103
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 66-177 1.09e-07

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: 47.55  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205  66 NFADGDKATLFVFFTTWCSPCIAEIPHLNKLQEKYeEQFNIVGVlledkSDEELRAFAQKNqilykiangennyllakil 145
Cdd:cd02947    5 ELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEY-PKVKFVKV-----DVDENPELAEEY------------------- 59

                         90       100       110
                 ....*....|....*....|....*....|..
gi 488914205 146 gGVNGIPTMFLYdKNSQLVNQYLGLIPEEMLE 177
Cdd:cd02947   60 -GVRSIPTFLFF-KNGKEVDRVVGADPKEELE 89
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 71-177 8.06e-07

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: 46.03  E-value: 8.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205  71 DKATLFVFFTTWCSPCIAEIPHLNKLQEkyEEQFNIVGVLLEDKSDEELRAFAQKNQILYKIANGENNYLLAKIlgGVNG 150
Cdd:cd03010   25 GKPYLLNVWASWCAPCREEHPVLMALAR--QGRVPIYGINYKDNPENALAWLARHGNPYAAVGFDPDGRVGIDL--GVYG 100

                         90       100
                 ....*....|....*....|....*..
gi 488914205 151 IPTMFLYDKNSQLVNQYLGLIPEEMLE 177
Cdd:cd03010  101 VPETFLIDGDGIIRYKHVGPLTPEVWE 127
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
72-177 1.01e-06

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 45.11  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205   72 KATLFVFFTTWCSPCI---AEIPHLNKLQEKYEEQFNIVGVLLeDKSDEELRAFAQKnqilykiangENNYLLAKILGgV 148
Cdd:pfam13098   5 KPVLVVFTDPDCPYCKklkKELLEDPDVTVYLGPNFVFIAVNI-WCAKEVAKAFTDI----------LENKELGRKYG-V 72

                          90       100
                  ....*....|....*....|....*....
gi 488914205  149 NGIPTMFLYDKNSQLvNQYLGLIPEEMLE 177
Cdd:pfam13098  73 RGTPTIVFFDGKGEL-LRLPGYVPAEEFL 100
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 67-184 3.49e-06

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 43.82  E-value: 3.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205   67 FADGDKATLFVFFTTWCSPCIAEIPHLNKLQEKYEEQFNIVgvlledKSD-EELRAFAQKNqilykiangennyllakil 145
Cdd:TIGR01068  10 IASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFV------KLNvDENPDIAAKY------------------- 64

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 488914205  146 gGVNGIPTMFLYdKNSQLVNQYLGLIPEEMLEIDIQKAI 184
Cdd:TIGR01068  65 -GIRSIPTLLLF-KNGKEVDRSVGALPKAALKQLINKNL 101
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 68-182 1.28e-05

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: 42.22  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205   68 ADGDKATLFVFFTTWCSPCIAEIPHLNKLQEKYEEQFnivgvlledksdeelrafaqknqILYKIANGENNYLLAKilGG 147
Cdd:pfam00085  15 QKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNV-----------------------VFAKVDVDENPDLASK--YG 69

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 488914205  148 VNGIPTMFLYdKNSQLVNQYLGLIPEEMLEIDIQK 182
Cdd:pfam00085  70 VRGYPTLIFF-KNGQPVDDYVGARPKDALAAFLKA 103
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 60-185 1.72e-05

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 42.74  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205   60 KDNENLNFAD--GDKATLFVFFTTWCSPCIAEIPHLNKLQEKYEEQ-FNIVGVLLeDKSDEELRAFAQKNQILYKIANGE 136
Cdd:pfam08534  16 TDGNTVSLSDfkGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKgVDVVAVNS-DNDAFFVKRFWGKEGLPFPFLSDG 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 488914205  137 N-------NYLLAKILGGVNGIPTMFLYDKNSQLVnqYLGLIPEEMLEIDIQKAIL 185
Cdd:pfam08534  95 NaaftkalGLPIEEDASAGLRSPRYAVIDEDGKVV--YLFVGPEPGVDVSDAEAVL 148
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 75-177 2.21e-05

Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 42.58  E-value: 2.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205  75 LFVFFTT-WCSPCI---AEIPHLNKLQEKYEEQFNIVGVLLEdkSDEELRAFAQKnqilyKIANGEnnylLAKILgGVNG 150
Cdd:COG2143   43 ILLFFESdWCPYCKklhKEVFSDPEVAAYLKENFVVVQLDAE--GDKEVTDFDGE-----TLTEKE----LARKY-GVRG 110

                         90       100
                 ....*....|....*....|....*..
gi 488914205 151 IPTMFLYDKNSQLVNQYLGLIPEEMLE 177
Cdd:COG2143  111 TPTLVFFDAEGKEIARIPGYLKPETFL 137
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 72-169 1.50e-04

TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a TlpA-like TRX domain. Some members show domain architectures similar to that of E. coli DipZ protein (also known as DsbD). The only eukaryotic members of the TlpA family belong to this subfamily. TlpA is a disulfide reductase known to have a crucial role in the biogenesis of cytochrome aa3.


Pssm-ID: 239310 [Multi-domain]  Cd Length: 126  Bit Score: 39.60  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205  72 KATLFVFFTTWCSPCIAEIPHLNKLQEKYEEQ-FNIVGV----LLEDKSDEELRAFAQKNQILYKIANgENNYLLAKILg 146
Cdd:cd03012   24 KVVLLDFWTYCCINCLHTLPYLTDLEQKYKDDgLVVIGVhspeFAFERDLANVKSAVLRYGITYPVAN-DNDYATWRAY- 101

                         90       100
                 ....*....|....*....|...
gi 488914205 147 GVNGIPTMFLYDKNSQLVNQYLG 169
Cdd:cd03012  102 GNQYWPALYLIDPTGNVRHVHFG 124
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 46-169 8.88e-04

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: 38.37  E-value: 8.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205  46 FNLNLIDGNSIfikkdneNL-NFADGdKATLFVFFTTWCSPCIAEIPHLNKLQEKYEEQ-FNIVGVLLEDKSD------E 117
Cdd:cd02969    7 FSLPDTDGKTY-------SLaDFADG-KALVVMFICNHCPYVKAIEDRLNRLAKEYGAKgVAVVAINSNDIEAypedspE 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488914205 118 ELRAFAQKNQILYKiangennYLL------AKILGGVNgIPTMFLYDKNSQLVnqYLG 169
Cdd:cd02969   79 NMKAKAKEHGYPFP-------YLLdetqevAKAYGAAC-TPDFFLFDPDGKLV--YRG 126
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 72-169 2.63e-03

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 37.91  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205   72 KATLFVFFTTWCSPCIAEIPHLNKLQEKYEEQ-FNIVGVlLEDKSDEELRAFAQKNQIL-YKIA----NGENNYLLAKIl 145
Cdd:PLN02919  421 KVVILDFWTYCCINCMHVLPDLEFLEKKYKDQpFTVVGV-HSAKFDNEKDLEAIRNAVLrYNIShpvvNDGDMYLWREL- 498

                          90       100
                  ....*....|....*....|....
gi 488914205  146 gGVNGIPTMFLYDKNSQLVNQYLG 169
Cdd:PLN02919  499 -GVSSWPTFAVVSPNGKLIAQLSG 521
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 66-169 5.80e-03

Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29.


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 34.89  E-value: 5.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488914205  66 NFAD---GDKATLFVFFTTWCSPCIAEIPHLNKLQEKYEEQFNIVgvlledksdeelrafaqknqiLYKIaNGENNYLLA 142
Cdd:cd02961    7 NFDElvkDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVV---------------------VAKV-DCTANNDLC 64

                         90       100
                 ....*....|....*....|....*..
gi 488914205 143 KILgGVNGIPTMFLYDKNSQLVNQYLG 169
Cdd:cd02961   65 SEY-GVRGYPTIKLFPNGSKEPVKYEG 90
 
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