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Conserved domains on  [gi|502820717|ref|WP_013055693|]
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MULTISPECIES: TlpA disulfide reductase family protein [Bacillaceae]

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

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List of domain hits

 Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 1-146 6.66e-26

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


:

Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 95.14  E-value: 6.66e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820717   1 MK-LREQMPELTGATSwINDEVTKEDLVGdKATLIHFWSVSCHLCKEAMPEVNDLRDEYDDqLNVVAVHMPRSEDDldmg 79
Cdd:COG0526    1 MKaVGKPAPDFTLTDL-DGKPLSLADLKG-KPVLVNFWATWCPPCRAEMPVLKELAEEYGG-VVFVGVDVDENPEA---- 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502820717  80 vIEAMAMGHDITQPIYVDSEHKLTDAFENKYVPAYYVFDKEGQLRHFQAGGNGMPMLRKRINRVLGE 146
Cdd:COG0526   74 -VKAFLKELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 1-146 6.66e-26

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 95.14  E-value: 6.66e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820717   1 MK-LREQMPELTGATSwINDEVTKEDLVGdKATLIHFWSVSCHLCKEAMPEVNDLRDEYDDqLNVVAVHMPRSEDDldmg 79
Cdd:COG0526    1 MKaVGKPAPDFTLTDL-DGKPLSLADLKG-KPVLVNFWATWCPPCRAEMPVLKELAEEYGG-VVFVGVDVDENPEA---- 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502820717  80 vIEAMAMGHDITQPIYVDSEHKLTDAFENKYVPAYYVFDKEGQLRHFQAGGNGMPMLRKRINRVLGE 146
Cdd:COG0526   74 -VKAFLKELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 6-129 8.09e-24

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: 89.22  E-value: 8.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820717   6 QMPELTGATswindeVTKEDLVGdKATLIHFWSVSCHLCKEAMPEVNDLRDEY-DDQLNVVAVHMPRSEDDldmgVIEAM 84
Cdd:cd02966    3 SLPDLDGKP------VSLSDLKG-KVVLVNFWASWCPPCRAEMPELEALAKEYkDDGVEVVGVNVDDDDPA----AVKAF 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 502820717  85 AMGHDITQPIYVDSEHKLTDAFENKYVPAYYVFDKEGQLRHFQAG 129
Cdd:cd02966   72 LKKYGITFPVLLDPDGELAKAYGVRGLPTTFLIDRDGRIRARHVG 116
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 5-125 1.44e-08

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: 49.92  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820717    5 EQMPELTgATSWINDEVTKEDLVGdKATLIHFW-SVSCHLCKEAMPEVNDLRDEYDDQ-LNVVAVhmprSEDDLDmgVIE 82
Cdd:pfam00578   3 DKAPDFE-LPDGDGGTVSLSDYRG-KWVVLFFYpADWTPVCTTELPALADLYEEFKKLgVEVLGV----SVDSPE--SHK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 502820717   83 AMAMGHDITQPIYVDSEHKLTDAF------ENKYVPAYYVFDKEGQLRH 125
Cdd:pfam00578  75 AFAEKYGLPFPLLSDPDGEVARAYgvlneeEGGALRATFVIDPDGKVRY 123
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
24-143 9.87e-08

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 48.46  E-value: 9.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820717  24 EDLVGdKATLIHFWSVSCHLCKEAMPEVNDLRDEYDDQ-LNVVAVHMprSEDDLdmgVIEAMAMGHDITQPIYVDSEHKL 102
Cdd:PRK03147  57 KDLKG-KGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKgVEIIAVNV--DETEL---AVKNFVNRYGLTFPVAIDKGRQV 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 502820717 103 TDAFENKYVPAYYVFDKEGQLRHFQAGGNGMPMLRKRINRV 143
Cdd:PRK03147 131 IDAYGVGPLPTTFLIDKDGKVVKVITGEMTEEQLEEYLEKI 171
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 1-146 6.66e-26

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 95.14  E-value: 6.66e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820717   1 MK-LREQMPELTGATSwINDEVTKEDLVGdKATLIHFWSVSCHLCKEAMPEVNDLRDEYDDqLNVVAVHMPRSEDDldmg 79
Cdd:COG0526    1 MKaVGKPAPDFTLTDL-DGKPLSLADLKG-KPVLVNFWATWCPPCRAEMPVLKELAEEYGG-VVFVGVDVDENPEA---- 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502820717  80 vIEAMAMGHDITQPIYVDSEHKLTDAFENKYVPAYYVFDKEGQLRHFQAGGNGMPMLRKRINRVLGE 146
Cdd:COG0526   74 -VKAFLKELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 6-129 8.09e-24

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: 89.22  E-value: 8.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820717   6 QMPELTGATswindeVTKEDLVGdKATLIHFWSVSCHLCKEAMPEVNDLRDEY-DDQLNVVAVHMPRSEDDldmgVIEAM 84
Cdd:cd02966    3 SLPDLDGKP------VSLSDLKG-KVVLVNFWASWCPPCRAEMPELEALAKEYkDDGVEVVGVNVDDDDPA----AVKAF 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 502820717  85 AMGHDITQPIYVDSEHKLTDAFENKYVPAYYVFDKEGQLRHFQAG 129
Cdd:cd02966   72 LKKYGITFPVLLDPDGELAKAYGVRGLPTTFLIDRDGRIRARHVG 116
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 8-129 2.00e-23

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: 88.52  E-value: 2.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820717   8 PELTGATSWINDE--VTKEDLVGdKATLIHFWSVSCHLCKEAMPEVNDLRDEY-DDQLNVVAVHMPRSEDDLDMGVIEAM 84
Cdd:cd03012    1 PEFEGILQWLNTDkpLSLAQLRG-KVVLLDFWTYCCINCLHTLPYLTDLEQKYkDDGLVVIGVHSPEFAFERDLANVKSA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 502820717  85 AMGHDITQPIYVDSEHKLTDAFENKYVPAYYVFDKEGQLRHFQAG 129
Cdd:cd03012   80 VLRYGITYPVANDNDYATWRAYGNQYWPALYLIDPTGNVRHVHFG 124
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
20-125 6.45e-15

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 66.81  E-value: 6.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820717  20 EVTKEDLVGdKATLIHFWSVSCHLCKEAMPEVNDLRDEYDDQ-LNVVAVHMPRSEDdldmgvIEAMAMGHDITQPIYVDS 98
Cdd:COG1225   13 TVSLSDLRG-KPVVLYFYATWCPGCTAELPELRDLYEEFKDKgVEVLGVSSDSDEA------HKKFAEKYGLPFPLLSDP 85

                         90       100
                 ....*....|....*....|....*..
gi 502820717  99 EHKLTDAFENKYVPAYYVFDKEGQLRH 125
Cdd:COG1225   86 DGEVAKAYGVRGTPTTFLIDPDGKIRY 112
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 9-144 6.61e-09

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: 50.20  E-value: 6.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820717   9 ELTGATswINDEVTKEDlvgdKATLIHFWSVSCHLCKEAMPEVNDLRDEYDDQLNVVAVhmprseDdldmgvieamamgh 88
Cdd:COG3118    4 ELTDEN--FEEEVLESD----KPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKV------D-------------- 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 502820717  89 ditqpiyVDSEHKLTDAFENKYVPAYYVFdKEGQLRHFQAGGNGMPMLRKRINRVL 144
Cdd:COG3118   58 -------VDENPELAAQFGVRSIPTLLLF-KDGQPVDRFVGALPKEQLREFLDKVL 105
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 5-125 1.44e-08

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: 49.92  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820717    5 EQMPELTgATSWINDEVTKEDLVGdKATLIHFW-SVSCHLCKEAMPEVNDLRDEYDDQ-LNVVAVhmprSEDDLDmgVIE 82
Cdd:pfam00578   3 DKAPDFE-LPDGDGGTVSLSDYRG-KWVVLFFYpADWTPVCTTELPALADLYEEFKKLgVEVLGV----SVDSPE--SHK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 502820717   83 AMAMGHDITQPIYVDSEHKLTDAF------ENKYVPAYYVFDKEGQLRH 125
Cdd:pfam00578  75 AFAEKYGLPFPLLSDPDGEVARAYgvlneeEGGALRATFVIDPDGKVRY 123
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
24-143 9.87e-08

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 48.46  E-value: 9.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820717  24 EDLVGdKATLIHFWSVSCHLCKEAMPEVNDLRDEYDDQ-LNVVAVHMprSEDDLdmgVIEAMAMGHDITQPIYVDSEHKL 102
Cdd:PRK03147  57 KDLKG-KGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKgVEIIAVNV--DETEL---AVKNFVNRYGLTFPVAIDKGRQV 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 502820717 103 TDAFENKYVPAYYVFDKEGQLRHFQAGGNGMPMLRKRINRV 143
Cdd:PRK03147 131 IDAYGVGPLPTTFLIDKDGKVVKVITGEMTEEQLEEYLEKI 171
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 7-99 2.87e-07

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 48.31  E-value: 2.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820717    7 MPELTGATSWINDEVT--KEDLVGdKATLIHFWSVSCHLCKEAMPEVNDLRDEYDDQ-LNVVAVHMPRSEDDLDMGVIEA 83
Cdd:PLN02919  397 VPEFPPKLDWLNTAPLqfRRDLKG-KVVILDFWTYCCINCMHVLPDLEFLEKKYKDQpFTVVGVHSAKFDNEKDLEAIRN 475

                          90
                  ....*....|....*.
gi 502820717   84 MAMGHDITQPIYVDSE 99
Cdd:PLN02919  476 AVLRYNISHPVVNDGD 491
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 29-122 1.62e-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: 43.84  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820717   29 DKATLIHFWSVSCHLCKEAMPEVNDLRDEY--DDQLNVVAVHMPRSEDDLDMgVIEAMAMgHDITQPIYVDSEHKLTDAF 106
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLkkKKNVEIVFVSLDRDLEEFKD-YLKKMPK-DWLSVPFDDDERNELKRKY 78

                          90
                  ....*....|....*.
gi 502820717  107 ENKYVPAYYVFDKEGQ 122
Cdd:pfam13905  79 GVNAIPTLVLLDPNGE 94
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 6-124 2.21e-06

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: 44.92  E-value: 2.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820717   6 QMPELTGATswindeVTKEDLVGDKATLIHFWSVSCHLCKEAMPEVNDLRDEYDDQ-LNVVAVhMPRSEDDLDMGVIEAM 84
Cdd:cd02969    8 SLPDTDGKT------YSLADFADGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKgVAVVAI-NSNDIEAYPEDSPENM 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 502820717  85 ---AMGHDITQPIYVDSEHKLTDAFENKYVPAYYVFDKEGQLR 124
Cdd:cd02969   81 kakAKEHGYPFPYLLDETQEVAKAYGAACTPDFFLFDPDGKLV 123
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 30-121 6.14e-06

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: 42.67  E-value: 6.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820717  30 KATLIHFWSVSCHLCKEAMPEVNDLRDEYddqlNVVAVHMpRSEDDLDMgvIEAMAmGHDITQPIYVDSEHKLTDAFENK 109
Cdd:cd03011   21 KPVLVYFWATWCPVCRFTSPTVNQLAADY----PVVSVAL-RSGDDGAV--ARFMQ-KKGYGFPVINDPDGVISARWGVS 92

                         90
                 ....*....|..
gi 502820717 110 YVPAYYVFDKEG 121
Cdd:cd03011   93 VTPAIVIVDPGG 104
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 26-77 6.96e-05

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: 40.40  E-value: 6.96e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502820717  26 LVGDKATLIHFWSVSCHLCKEAMPEVNDLRDEYDDQLNVVAVHM--PRSEDDLD 77
Cdd:cd02950   17 LSNGKPTLVEFYADWCTVCQEMAPDVAKLKQKYGDQVNFVMLNVdnPKWLPEID 70
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 23-141 1.89e-03

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: 35.61  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820717  23 KEDLVGDKATLIHFWSVSCHLCKEAMPEVNDLRDEYDDqLNVVAVhmprseDdldmgvieamamghditqpiyVDSEHKL 102
Cdd:cd02947    4 EELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK-VKFVKV------D---------------------VDENPEL 55

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 502820717 103 TDAFENKYVPAYYVFdKEGQLRHFQAGGNGMPMLRKRIN 141
Cdd:cd02947   56 AEEYGVRSIPTFLFF-KNGKEVDRVVGADPKEELEEFLE 93
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 30-71 6.87e-03

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 34.97  E-value: 6.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 502820717  30 KATLIHFWSVSCHLCKEAMPEVNDLRDEY-DDQLNVVAVHMPR 71
Cdd:COG1651    1 KVTVVEFFDYQCPYCARFHPELPELLKKYvDGKVRVVYRPFPL 43
 
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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