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Conserved domains on  [gi|1039542075|ref|WP_064872232|]
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TlpA disulfide reductase family protein [Mycolicibacterium monacense]

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 ...
 56-176 4.56e-37

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: 125.04  E-value: 4.56e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  56 ALSGPDLldPAKTLSLDDFAGQVVVINVWGQWCAPCRTEIGELQQVHDATRAKGVAFLGIDVRDNNREAAVDFVRDRGIT 135
Cdd:cd02966     1 DFSLPDL--DGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAAVKAFLKKYGIT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1039542075 136 FPSIYDPPMRTMIAFGGkyptTVIPSTVVLDREHRVAAVFL 176
Cdd:cd02966    79 FPVLLDPDGELAKAYGV----RGLPTTFLIDRDGRIRARHV 115
UgpB super family cl43481
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-46 9.38e-03

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


The actual alignment was detected with superfamily member COG1653:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 36.18  E-value: 9.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1039542075   1 MRRWWIVLASVAVVALAGCSTGDDAV---AQGGTFEFVAPGGKTDIFYD 46
Cdd:COG1653     1 MRRLALALAAALALALAACGGGGSGAaaaAGKVTLTVWHTGGGEAAALE 49
 
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 ...
 56-176 4.56e-37

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: 125.04  E-value: 4.56e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  56 ALSGPDLldPAKTLSLDDFAGQVVVINVWGQWCAPCRTEIGELQQVHDATRAKGVAFLGIDVRDNNREAAVDFVRDRGIT 135
Cdd:cd02966     1 DFSLPDL--DGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAAVKAFLKKYGIT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1039542075 136 FPSIYDPPMRTMIAFGGkyptTVIPSTVVLDREHRVAAVFL 176
Cdd:cd02966    79 FPVLLDPDGELAKAYGV----RGLPTTFLIDRDGRIRARHV 115
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 49-191 1.07e-34

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 119.79  E-value: 1.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  49 ADRGRPGALSGPDLLDpaKTLSLDDFAGQVVVINVWGQWCAPCRTEIGELQQVHDatRAKGVAFLGIDVrDNNREAAVDF 128
Cdd:COG0526     3 AVGKPAPDFTLTDLDG--KPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAE--EYGGVVFVGVDV-DENPEAVKAF 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039542075 129 VRDRGITFPSIYDPPMRTMIAFGgkypTTVIPSTVVLDREHRVAAVFLRELLAEDLQPVVERL 191
Cdd:COG0526    78 LKELGLPYPVLLDPDGELAKAYG----VRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKL 136
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 67-174 6.41e-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: 78.42  E-value: 6.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  67 KTLSLDDFAGQVVVINVW-GQWCAPCRTEIGELQQVHDATRAKGVAFLGIDVrdNNREAAVDFVRDRGITFPSIYDPPMR 145
Cdd:pfam00578  16 GTVSLSDYRGKWVVLFFYpADWTPVCTTELPALADLYEEFKKLGVEVLGVSV--DSPESHKAFAEKYGLPFPLLSDPDGE 93

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1039542075 146 TMIAFGGKYP--TTVIPSTVVLDREHRVAAV 174
Cdd:pfam00578  94 VARAYGVLNEeeGGALRATFVIDPDGKVRYI 124
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
67-157 3.52e-12

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 61.94  E-value: 3.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  67 KTLSLDDFAGQVVVINVWGQWCAPCRTEIGELQQVHDATRAKGVAFLGIDVrdNNREAAVD-FVRDRGITFPSIYDPPMR 145
Cdd:PRK03147   52 KKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNV--DETELAVKnFVNRYGLTFPVAIDKGRQ 129

                          90
                  ....*....|...
gi 1039542075 146 TMIAFG-GKYPTT 157
Cdd:PRK03147  130 VIDAYGvGPLPTT 142
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 54-190 1.62e-10

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: 57.48  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  54 PGALSG--------PDLLDPAKTLSLDDF-AGQVVVINVWGQWCAPCRTEIGELQQVhdatRAKGVAFLGIDVRDnNREA 124
Cdd:TIGR00385  32 PSALIGkpvpafrlASLDEPGQFYTADVLtQGKPVLLNVWASWCPPCRAEHPYLNEL----AKQGLPIVGVDYKD-DRQN 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039542075 125 AVDFVRDRGITFP-SIYDPPMRTMIAFGgkypTTVIPSTVVLDRE----HRVAAVFLRELLAEDLQPVVER 190
Cdd:TIGR00385 107 AIKFLKELGNPYQlSLFDPDGMLGLDLG----VYGAPETFLVDGNgvirYRHAGPLNPEVWTEEFLPLWEK 173
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-46 9.38e-03

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 36.18  E-value: 9.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1039542075   1 MRRWWIVLASVAVVALAGCSTGDDAV---AQGGTFEFVAPGGKTDIFYD 46
Cdd:COG1653     1 MRRLALALAAALALALAACGGGGSGAaaaAGKVTLTVWHTGGGEAAALE 49
 
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 ...
 56-176 4.56e-37

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: 125.04  E-value: 4.56e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  56 ALSGPDLldPAKTLSLDDFAGQVVVINVWGQWCAPCRTEIGELQQVHDATRAKGVAFLGIDVRDNNREAAVDFVRDRGIT 135
Cdd:cd02966     1 DFSLPDL--DGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAAVKAFLKKYGIT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1039542075 136 FPSIYDPPMRTMIAFGGkyptTVIPSTVVLDREHRVAAVFL 176
Cdd:cd02966    79 FPVLLDPDGELAKAYGV----RGLPTTFLIDRDGRIRARHV 115
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 49-191 1.07e-34

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 119.79  E-value: 1.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  49 ADRGRPGALSGPDLLDpaKTLSLDDFAGQVVVINVWGQWCAPCRTEIGELQQVHDatRAKGVAFLGIDVrDNNREAAVDF 128
Cdd:COG0526     3 AVGKPAPDFTLTDLDG--KPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAE--EYGGVVFVGVDV-DENPEAVKAF 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039542075 129 VRDRGITFPSIYDPPMRTMIAFGgkypTTVIPSTVVLDREHRVAAVFLRELLAEDLQPVVERL 191
Cdd:COG0526    78 LKELGLPYPVLLDPDGELAKAYG----VRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKL 136
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
67-191 2.31e-27

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 100.71  E-value: 2.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  67 KTLSLDDFAGQVVVINVWGQWCAPCRTEIGELQQVHDATRAKGVAFLGIDVrdNNREAAVDFVRDRGITFPSIYDPPMRT 146
Cdd:COG1225    12 KTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSS--DSDEAHKKFAEKYGLPFPLLSDPDGEV 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1039542075 147 MIAFGgkypTTVIPSTVVLDREHRVAAVFLREL-LAEDLQPVVERL 191
Cdd:COG1225    90 AKAYG----VRGTPTTFLIDPDGKIRYVWVGPVdPRPHLEEVLEAL 131
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 56-171 8.97e-21

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: 83.40  E-value: 8.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  56 ALSGPDLLDPAKTLSLDDFAGQVVVINVWGQWCAPCRTEIGELQQVHdatRAKGVAFLGIDVRDnNREAAVDFVRDRGIT 135
Cdd:cd03010     5 AFSLPALPGPDKTLTSADLKGKPYLLNVWASWCAPCREEHPVLMALA---RQGRVPIYGINYKD-NPENALAWLARHGNP 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039542075 136 F-PSIYDPPMRTMIAFGgkypTTVIPSTVVLDREHRV 171
Cdd:cd03010    81 YaAVGFDPDGRVGIDLG----VYGVPETFLIDGDGII 113
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 67-174 6.41e-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: 78.42  E-value: 6.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  67 KTLSLDDFAGQVVVINVW-GQWCAPCRTEIGELQQVHDATRAKGVAFLGIDVrdNNREAAVDFVRDRGITFPSIYDPPMR 145
Cdd:pfam00578  16 GTVSLSDYRGKWVVLFFYpADWTPVCTTELPALADLYEEFKKLGVEVLGVSV--DSPESHKAFAEKYGLPFPLLSDPDGE 93

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1039542075 146 TMIAFGGKYP--TTVIPSTVVLDREHRVAAV 174
Cdd:pfam00578  94 VARAYGVLNEeeGGALRATFVIDPDGKVRYI 124
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 56-176 1.62e-15

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 70.48  E-value: 1.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  56 ALSGPDLLDPAKTLSLDDFAGQVVVINVW-GQWCAPCRTEIGELQQVHDATRAKGVAFLGIdVRDNNREAAVDFVRDRGI 134
Cdd:pfam08534   8 DFTLPDAATDGNTVSLSDFKGKKVVLNFWpGAFCPTCSAEHPYLEKLNELYKEKGVDVVAV-NSDNDAFFVKRFWGKEGL 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1039542075 135 TFPSIYDPPMRTMIAFGGKYP-----TTVIPSTVVLDREHRVAAVFL 176
Cdd:pfam08534  87 PFPFLSDGNAAFTKALGLPIEedasaGLRSPRYAVIDEDGKVVYLFV 133
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
67-157 3.52e-12

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 61.94  E-value: 3.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  67 KTLSLDDFAGQVVVINVWGQWCAPCRTEIGELQQVHDATRAKGVAFLGIDVrdNNREAAVD-FVRDRGITFPSIYDPPMR 145
Cdd:PRK03147   52 KKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNV--DETELAVKnFVNRYGLTFPVAIDKGRQ 129

                          90
                  ....*....|...
gi 1039542075 146 TMIAFG-GKYPTT 157
Cdd:PRK03147  130 VIDAYGvGPLPTT 142
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 54-190 1.62e-10

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: 57.48  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  54 PGALSG--------PDLLDPAKTLSLDDF-AGQVVVINVWGQWCAPCRTEIGELQQVhdatRAKGVAFLGIDVRDnNREA 124
Cdd:TIGR00385  32 PSALIGkpvpafrlASLDEPGQFYTADVLtQGKPVLLNVWASWCPPCRAEHPYLNEL----AKQGLPIVGVDYKD-DRQN 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039542075 125 AVDFVRDRGITFP-SIYDPPMRTMIAFGgkypTTVIPSTVVLDRE----HRVAAVFLRELLAEDLQPVVER 190
Cdd:TIGR00385 107 AIKFLKELGNPYQlSLFDPDGMLGLDLG----VYGAPETFLVDGNgvirYRHAGPLNPEVWTEEFLPLWEK 173
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 68-166 1.63e-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: 50.76  E-value: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  68 TLSLDDFAGQVVVINVWGQWCAPCRTEIGELQQVhdatrAKGVAFLGIDVRDNNREAAVDFVRDRGITFPSIYDPPMRTM 147
Cdd:cd03011    12 QFDLESLSGKPVLVYFWATWCPVCRFTSPTVNQL-----AADYPVVSVALRSGDDGAVARFMQKKGYGFPVINDPDGVIS 86

                          90
                  ....*....|....*....
gi 1039542075 148 IAFGgkypTTVIPSTVVLD 166
Cdd:cd03011    87 ARWG----VSVTPAIVIVD 101
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 76-171 3.06e-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: 49.61  E-value: 3.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  76 GQVVVINVWGQWCAPCRTEIGELQQVHDATRA-KGVAFLGIDVrDNNREAAVDFVRDRGITFPSIY--DPPMRTMIAfgg 152
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKkKNVEIVFVSL-DRDLEEFKDYLKKMPKDWLSVPfdDDERNELKR--- 76

                          90
                  ....*....|....*....
gi 1039542075 153 KYPTTVIPSTVVLDREHRV 171
Cdd:pfam13905  77 KYGVNAIPTLVLLDPNGEV 95
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 5-141 5.43e-06

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 44.98  E-value: 5.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075   5 WIVLASVAVVALAGCSTGDDavaqggtfefvaPGGKTDIFYDPPADRGRPGALSGPDLLDPAKTLSlddfAGQVVVINVW 84
Cdd:PRK15412   13 FLAIAAALLWQLARNAEGDD------------PTNLESALIGKPVPKFRLESLENPGQFYQADVLT----QGKPVLLNVW 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039542075  85 GQWCAPCRTEIGELQQVhdatRAKGVAFLGIDVRDnNREAAVDFVRDRGITFP-SIYD 141
Cdd:PRK15412   77 ATWCPTCRAEHQYLNQL----SAQGIRVVGMNYKD-DRQKAISWLKELGNPYAlSLFD 129
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 60-151 2.91e-05

Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.


Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 42.35  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  60 PDLLDPAKTLSLDDFAGQVVVINVWGQWCAPCRTEIGELQQVHDATRAKGVAFLGIDVrdNNREAAVDFVRDRGITFPSI 139
Cdd:cd02970     8 PDAGGETVTLSALLGEGPVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGP--ESPEKLEAFDKGKFLPFPVY 85

                          90
                  ....*....|..
gi 1039542075 140 YDPPMRTMIAFG 151
Cdd:cd02970    86 ADPDRKLYRALG 97
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 63-178 6.38e-05

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: 41.14  E-value: 6.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  63 LDPAKTLSLDDFAGQVVVINVWGQWCAPCRTEIGELQQVHDATRAKGVAFLGIDVR--DNNREAA--VDFVRDRGITFPS 138
Cdd:cd03012    10 LNTDKPLSLAQLRGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKDDGLVVIGVHSPefAFERDLAnvKSAVLRYGITYPV 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1039542075 139 IYDPPMRTMIAFGGKYpttvIPSTVVLDREHRVAAVFLRE 178
Cdd:cd03012    90 ANDNDYATWRAYGNQY----WPALYLIDPTGNVRHVHFGE 125
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 75-128 2.83e-04

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: 38.69  E-value: 2.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039542075  75 AGQVVVINVWGQWCAPCRTEIGELQQVhdATRAKGVAFLGIDVrDNNREAAVDF 128
Cdd:cd02947     9 SAKPVVVDFWAPWCGPCKAIAPVLEEL--AEEYPKVKFVKVDV-DENPELAEEY 59
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 60-172 1.09e-03

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: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  60 PD--LLDPA-KTLSLDDFAGQVVVINVWgqWCAPC---RTEIGELQQVHDATRAKGVAFLGI------DVRDNNREAAVD 127
Cdd:cd02969     5 PDfsLPDTDgKTYSLADFADGKALVVMF--ICNHCpyvKAIEDRLNRLAKEYGAKGVAVVAInsndieAYPEDSPENMKA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1039542075 128 FVRDRGITFPSIYDPPMRTMIAFGGKypTTviPSTVVLDREHRVA 172
Cdd:cd02969    83 KAKEHGYPFPYLLDETQEVAKAYGAA--CT--PDFFLFDPDGKLV 123
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 78-159 7.75e-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: 34.57  E-value: 7.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039542075  78 VVVINVWGQWCAPCRTEIGELQQVhDATRAKGVAFLGIDVrDNNREAAVDFvrdrGITfpSIydPpmrTMIAF-GGKYPT 156
Cdd:TIGR01068  16 PVLVDFWAPWCGPCKMIAPILEEL-AKEYEGKVKFVKLNV-DENPDIAAKY----GIR--SI--P---TLLLFkNGKEVD 82


                  ...
gi 1039542075 157 TVI 159
Cdd:TIGR01068  83 RSV 85
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-46 9.38e-03

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 36.18  E-value: 9.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1039542075   1 MRRWWIVLASVAVVALAGCSTGDDAV---AQGGTFEFVAPGGKTDIFYD 46
Cdd:COG1653     1 MRRLALALAAALALALAACGGGGSGAaaaAGKVTLTVWHTGGGEAAALE 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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