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Conserved domains on  [gi|518548264|ref|WP_019718471|]
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MULTISPECIES: TlpA disulfide reductase family protein [Ralstonia solanacearum species complex]

Protein Classification

TlpA disulfide reductase family protein( domain architecture ID 10121831)

TlpA disulfide reductase family protein 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

CATH:  3.40.30.10
Gene Ontology:  GO:0015036
PubMed:  9099998|10049365|15558583
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 51-157 3.58e-28

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: 101.54  E-value: 3.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518548264  51 PLVLHTLDGHSIATDDLRGQVVVLTFWATWCEPCRKELPLLSAYAARHADRGLRVLGFCLDEPDALPAVREVAA-GLSFP 129
Cdd:cd02966    1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAAVKAFLKKyGITFP 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 518548264 130 VGLLGSpyaggyGRIWR------LPVNFTIDRKG 157
Cdd:cd02966   81 VLLDPD------GELAKaygvrgLPTTFLIDRDG 108
 
Name Accession Description Interval E-value
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 51-157 3.58e-28

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: 101.54  E-value: 3.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518548264  51 PLVLHTLDGHSIATDDLRGQVVVLTFWATWCEPCRKELPLLSAYAARHADRGLRVLGFCLDEPDALPAVREVAA-GLSFP 129
Cdd:cd02966    1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAAVKAFLKKyGITFP 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 518548264 130 VGLLGSpyaggyGRIWR------LPVNFTIDRKG 157
Cdd:cd02966   81 VLLDPD------GELAKaygvrgLPTTFLIDRDG 108
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
49-157 3.35e-25

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 94.55  E-value: 3.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518548264  49 APPLVLHTLDGHSIATDDLRGQVVVLTFWATWCEPCRKELPLLSAYAARHADRGLRVLGFCLDEPDalpAVREVAA--GL 126
Cdd:COG1225    1 APDFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDE---AHKKFAEkyGL 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 518548264 127 SFPVGL-LGSPYAGGYGrIWRLPVNFTIDRKG 157
Cdd:COG1225   78 PFPLLSdPDGEVAKAYG-VRGTPTTFLIDPDG 108
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
44-157 1.13e-21

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 86.60  E-value: 1.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518548264  44 EVGRSAPPLVLHTLDGHSIATDDLRGQVVVLTFWATWCEPCRKELPLLSAYAARHADRGLRVLGFCLDEPDAlpAVREVA 123
Cdd:PRK03147  36 QVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNVDETEL--AVKNFV 113

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 518548264 124 A--GLSFPVGL-LGSPYAGGYGrIWRLPVNFTIDRKG 157
Cdd:PRK03147 114 NryGLTFPVAIdKGRQVIDAYG-VGPLPTTFLIDKDG 149
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 45-160 1.67e-19

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: 79.58  E-value: 1.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518548264   45 VGRSAPPLVLHTLDGHSIATDDLRGQVVVLTFWAT-WCEPCRKELPLLSAYAARHADRGLRVLGFCLDEPDALPAVREvA 123
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAE-K 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 518548264  124 AGLSFPV------------GLLGSPYAGGYgriwrlPVNFTIDRKGLLA 160
Cdd:pfam00578  80 YGLPFPLlsdpdgevarayGVLNEEEGGAL------RATFVIDPDGKVR 122
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 36-138 4.61e-09

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: 53.24  E-value: 4.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518548264   36 PAAQAAGLeVGRSAPPLVLHTLDGHSIATDD---LRGQVVVLTFWATWCEPCRKELPLLSAYAArhadRGLRVLGfcLDE 112
Cdd:TIGR00385  28 PKALPSAL-IGKPVPAFRLASLDEPGQFYTAdvlTQGKPVLLNVWASWCPPCRAEHPYLNELAK----QGLPIVG--VDY 100

                          90       100
                  ....*....|....*....|....*.
gi 518548264  113 PDALPavrevaAGLSFpVGLLGSPYA 138
Cdd:TIGR00385 101 KDDRQ------NAIKF-LKELGNPYQ 119
 
Name Accession Description Interval E-value
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 51-157 3.58e-28

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: 101.54  E-value: 3.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518548264  51 PLVLHTLDGHSIATDDLRGQVVVLTFWATWCEPCRKELPLLSAYAARHADRGLRVLGFCLDEPDALPAVREVAA-GLSFP 129
Cdd:cd02966    1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAAVKAFLKKyGITFP 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 518548264 130 VGLLGSpyaggyGRIWR------LPVNFTIDRKG 157
Cdd:cd02966   81 VLLDPD------GELAKaygvrgLPTTFLIDRDG 108
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
49-157 3.35e-25

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 94.55  E-value: 3.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518548264  49 APPLVLHTLDGHSIATDDLRGQVVVLTFWATWCEPCRKELPLLSAYAARHADRGLRVLGFCLDEPDalpAVREVAA--GL 126
Cdd:COG1225    1 APDFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDE---AHKKFAEkyGL 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 518548264 127 SFPVGL-LGSPYAGGYGrIWRLPVNFTIDRKG 157
Cdd:COG1225   78 PFPLLSdPDGEVAKAYG-VRGTPTTFLIDPDG 108
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 45-184 2.09e-24

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 92.83  E-value: 2.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518548264  45 VGRSAPPLVLHTLDGHSIATDDLRGQVVVLTFWATWCEPCRKELPLLSAYAARHadRGLRVLGFCLDE--PDALPAVREv 122
Cdd:COG0526    4 VGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEY--GGVVFVGVDVDEnpEAVKAFLKE- 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518548264 123 aAGLSFPVgllgspYAGGYGRIWR------LPVNFTIDRKGLLAdngwDAREPAWTAERLDRVITPLL 184
Cdd:COG0526   81 -LGLPYPV------LLDPDGELAKaygvrgIPTTVLIDKDGKIV----ARHVGPLSPEELEEALEKLL 137
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
44-157 1.13e-21

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 86.60  E-value: 1.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518548264  44 EVGRSAPPLVLHTLDGHSIATDDLRGQVVVLTFWATWCEPCRKELPLLSAYAARHADRGLRVLGFCLDEPDAlpAVREVA 123
Cdd:PRK03147  36 QVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNVDETEL--AVKNFV 113

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 518548264 124 A--GLSFPVGL-LGSPYAGGYGrIWRLPVNFTIDRKG 157
Cdd:PRK03147 114 NryGLTFPVAIdKGRQVIDAYG-VGPLPTTFLIDKDG 149
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 45-160 1.67e-19

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: 79.58  E-value: 1.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518548264   45 VGRSAPPLVLHTLDGHSIATDDLRGQVVVLTFWAT-WCEPCRKELPLLSAYAARHADRGLRVLGFCLDEPDALPAVREvA 123
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAE-K 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 518548264  124 AGLSFPV------------GLLGSPYAGGYgriwrlPVNFTIDRKGLLA 160
Cdd:pfam00578  80 YGLPFPLlsdpdgevarayGVLNEEEGGAL------RATFVIDPDGKVR 122
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 44-157 3.10e-14

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 66.62  E-value: 3.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518548264   44 EVGRSAPPLVLHT--LDGHSIATDDLRGQVVVLTFWAT-WCEPCRKELPLLSAYAARHADRGLRVLGFCLDepDALPAVR 120
Cdd:pfam08534   1 KAGDKAPDFTLPDaaTDGNTVSLSDFKGKKVVLNFWPGaFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSD--NDAFFVK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 518548264  121 EVAA--GLSFPVGL---------LGSPYAGGYGRIWRLPVNFTIDRKG 157
Cdd:pfam08534  79 RFWGkeGLPFPFLSdgnaaftkaLGLPIEEDASAGLRSPRYAVIDEDG 126
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 47-157 5.28e-12

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: 59.90  E-value: 5.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518548264  47 RSAPPLVLHTLDGHS--IATDDLRGQVVVLTFWATWCEPCRKELPLLSAYAARHadrGLRVLGFC-LDEPDalpavreva 123
Cdd:cd03010    1 KPAPAFSLPALPGPDktLTSADLKGKPYLLNVWASWCAPCREEHPVLMALARQG---RVPIYGINyKDNPE--------- 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 518548264 124 AGLSFpVGLLGSPYA--------------GGYGriwrLPVNFTIDRKG 157
Cdd:cd03010   69 NALAW-LARHGNPYAavgfdpdgrvgidlGVYG----VPETFLIDGDG 111
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 36-138 4.61e-09

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: 53.24  E-value: 4.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518548264   36 PAAQAAGLeVGRSAPPLVLHTLDGHSIATDD---LRGQVVVLTFWATWCEPCRKELPLLSAYAArhadRGLRVLGfcLDE 112
Cdd:TIGR00385  28 PKALPSAL-IGKPVPAFRLASLDEPGQFYTAdvlTQGKPVLLNVWASWCPPCRAEHPYLNELAK----QGLPIVG--VDY 100

                          90       100
                  ....*....|....*....|....*.
gi 518548264  113 PDALPavrevaAGLSFpVGLLGSPYA 138
Cdd:TIGR00385 101 KDDRQ------NAIKF-LKELGNPYQ 119
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 50-99 1.33e-07

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: 48.06  E-value: 1.33e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 518548264  50 PPLVLHTLDGHSIATDDLRGQVVVLTFWATWCEPCRKELPLLSAYAARHA 99
Cdd:cd03011    1 PLFTATTLDGEQFDLESLSGKPVLVYFWATWCPVCRFTSPTVNQLAADYP 50
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 68-101 3.97e-07

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: 46.35  E-value: 3.97e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 518548264  68 RGQVVVLTFWATWCEPCRKELPLLSAYAARHADR 101
Cdd:COG3118   17 SDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGK 50
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 45-159 6.90e-07

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 47.29  E-value: 6.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518548264  45 VGRSAPPLVLHTLD--GHSIATDDL-RGQVVVLTFWATWCEPCRKELPLLSAYAArhadRGLRVLGFCL--DEPDALPAV 119
Cdd:PRK15412  41 IGKPVPKFRLESLEnpGQFYQADVLtQGKPVLLNVWATWCPTCRAEHQYLNQLSA----QGIRVVGMNYkdDRQKAISWL 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 518548264 120 REV----AAGLSFPVGLLGSPYaGGYGRiwrlPVNFTIDRKGLL 159
Cdd:PRK15412 117 KELgnpyALSLFDGDGMLGLDL-GVYGA----PETFLIDGNGII 155
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 62-107 1.23e-06

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: 45.37  E-value: 1.23e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 518548264  62 IATDDLRGQVVVLTFWATWCEPCRKELPLLSAYAARHADRGLRVLG 107
Cdd:cd03012   16 LSLAQLRGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKDDGLVVIG 61
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 69-112 5.23e-06

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: 43.07  E-value: 5.23e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 518548264   69 GQVVVLTFWATWCEPCRKELPLLSAYAARH-ADRGLRVLGFCLDE 112
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLkKKKNVEIVFVSLDR 45
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 69-100 2.26e-05

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: 41.39  E-value: 2.26e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 518548264  69 GQVVVLTFWATWCEPCRKELPLLSAYAARHAD 100
Cdd:cd02947   10 AKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK 41
PTZ00051 PTZ00051
thioredoxin; Provisional
 70-99 2.00e-03

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 36.01  E-value: 2.00e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 518548264  70 QVVVLTFWATWCEPCRKELPLLSAYAARHA 99
Cdd:PTZ00051  19 ELVIVDFYAEWCGPCKRIAPFYEECSKEYT 48
GSHPx pfam00255
Glutathione peroxidase;
56-108 2.11e-03

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 36.18  E-value: 2.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 518548264   56 TLDGHSIATDDLRGQVVVLTFWATWC--EPCRKELPLLSAyaaRHADRGLRVLGF 108
Cdd:pfam00255   8 DIDGEPVPFDQYRGKVVLIVNVASKCglTPQYTQLEELQE---RYKDRGLVILGF 59
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 72-125 2.23e-03

ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like domain. Its gene has been sequenced from several gammaproteobacteria and actinobacteria.


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 36.10  E-value: 2.23e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518548264  72 VVLTFWATWCEPCRKELPLLSAYAARHADRGLRVLGFCLDEPD--------ALPAVREVAAG 125
Cdd:cd02956   15 VVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQiaqqfgvqALPTVYLFAAG 76
PRK10996 PRK10996
thioredoxin 2; Provisional
 72-101 2.33e-03

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 36.59  E-value: 2.33e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 518548264  72 VVLTFWATWCEPCRKELPLLSAYAARHADR 101
Cdd:PRK10996  55 VVIDFWAPWCGPCRNFAPIFEDVAAERSGK 84
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 43-130 2.90e-03

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: 36.48  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518548264  43 LEVGRSAPPLVLHTLDGHSIATDDLRGQ-VVVLTFW-ATWCEPCRKELPLLSAYAARHADRGLRVLGFCLDEPDALPAVR 120
Cdd:cd03018    1 LEVGDKAPDFELPDQNGQEVRLSEFRGRkPVVLVFFpLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAWA 80

                         90
                 ....*....|
gi 518548264 121 EvAAGLSFPV 130
Cdd:cd03018   81 E-ENGLTFPL 89
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 62-102 3.57e-03

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: 36.05  E-value: 3.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 518548264  62 IATDDLRGQVVVLTFWATWCEPCRKELPLLSAYAARHADRG 102
Cdd:cd02964   10 VPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEG 50
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 56-130 3.74e-03

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


Pssm-ID: 238207 [Multi-domain]  Cd Length: 152  Bit Score: 36.34  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518548264  56 TLDGHSIATDDLRGQVVVLTFWATWC--EPCRKEL-PLLSAYAarhaDRGLRVLGF-CLD----EPDALPAVREVAA--- 124
Cdd:cd00340    9 DIDGEPVSLSKYKGKVLLIVNVASKCgfTPQYEGLeALYEKYK----DRGLVVLGFpCNQfggqEPGSNEEIKEFCEtny 84


                 ....*.
gi 518548264 125 GLSFPV 130
Cdd:cd00340   85 GVTFPM 90
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 62-85 5.23e-03

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: 34.96  E-value: 5.23e-03
                          10        20
                  ....*....|....*....|....
gi 518548264   62 IATDDLrgqVVVLTFWATWCEPCR 85
Cdd:TIGR01068  10 IASSDK---PVLVDFWAPWCGPCK 30
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 72-100 6.65e-03

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: 34.90  E-value: 6.65e-03
                          10        20
                  ....*....|....*....|....*....
gi 518548264   72 VVLTFWATWCEPCRKELPLLSAYAARHAD 100
Cdd:pfam00085  21 VLVDFYAPWCGPCKMLAPEYEELAQEYKG 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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