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Conserved domains on  [gi|2105563033|ref|WP_225305368|]
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MULTISPECIES: thioredoxin family protein [Blautia]

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, ...
 115-254 3.67e-24

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


:

Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 93.99  E-value: 3.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 115 EFKTKTLDGKDVNQDIFAEaDLTMVNIWGTFCGPCIREMPDLGELSREYadKGFRMVGIISDvsqPEDETALEIVDKTEA 194
Cdd:COG0526    10 DFTLTDLDGKPLSLADLKG-KPVLVNFWATWCPPCRAEMPVLKELAEEY--GGVVFVGVDVD---ENPEAVKAFLKELGL 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 195 DYTHLVipdDANMQYRILRNAQVVPTTIFLDKNGNQVGeTYPGAKSKKQWIAVIDKMLEK 254
Cdd:COG0526    84 PYPVLL---DPDGELAKAYGVRGIPTTVLIDKDGKIVA-RHVGPLSPEELEEALEKLLAK 139
2A1904 super family cl36772
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 57-135 3.95e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


The actual alignment was detected with superfamily member TIGR00927:

Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 38.44  E-value: 3.95e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105563033   57 GEDAADKAQTDGQQENKDSAKEDGQKADYQDQQTESQEKSQDQQADAENETDKNEIFGEFKTKTlDGKDVNQDIFAEAD 135
Cdd:TIGR00927  660 GEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEA-EGTEDEGEIETGEE 737
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 115-254 3.67e-24

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 93.99  E-value: 3.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 115 EFKTKTLDGKDVNQDIFAEaDLTMVNIWGTFCGPCIREMPDLGELSREYadKGFRMVGIISDvsqPEDETALEIVDKTEA 194
Cdd:COG0526    10 DFTLTDLDGKPLSLADLKG-KPVLVNFWATWCPPCRAEMPVLKELAEEY--GGVVFVGVDVD---ENPEAVKAFLKELGL 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 195 DYTHLVipdDANMQYRILRNAQVVPTTIFLDKNGNQVGeTYPGAKSKKQWIAVIDKMLEK 254
Cdd:COG0526    84 PYPVLL---DPDGELAKAYGVRGIPTTVLIDKDGKIVA-RHVGPLSPEELEEALEKLLAK 139
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 115-231 3.79e-23

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: 90.76  E-value: 3.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 115 EFKTKTLDGKDVNQDIFAEaDLTMVNIWGTFCGPCIREMPDLGELSREYADKGFRMVGIisDVSQPEDETALEIVDKTEA 194
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKG-KVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGV--NVDDDDPAAVKAFLKKYGI 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2105563033 195 DYTHLVIPDDA-NMQYRIlrnaQVVPTTIFLDKNGNQV 231
Cdd:cd02966    78 TFPVLLDPDGElAKAYGV----RGLPTTFLIDRDGRIR 111
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 115-229 1.72e-12

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 63.16  E-value: 1.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 115 EFKTKTLDGKDVNQDIFAEADLtMVNIW-GTFCGPCIREMPDLGELSREYADKGFRMVGIISD-----VSQPEDETALEI 188
Cdd:pfam08534  10 TLPDAATDGNTVSLSDFKGKKV-VLNFWpGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDndaffVKRFWGKEGLPF 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2105563033 189 V---DkTEADYTH---LVIPDDANMQYRIlrnaqvvPTTIFLDKNGN 229
Cdd:pfam08534  89 PflsD-GNAAFTKalgLPIEEDASAGLRS-------PRYAVIDEDGK 127
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
115-243 5.02e-10

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 56.94  E-value: 5.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 115 EFKTKTLDGKDVnqdifaeadltMVNIWGTFCGPCIREMPDLGELSREYADKGFRMVGIisDVSQPedetalEIVDKTEA 194
Cdd:PRK03147   53 KIELKDLKGKGV-----------FLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAV--NVDET------ELAVKNFV 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2105563033 195 DYTHLVIPDDANMQYRILRNAQV--VPTTIFLDKNGnQVGETYPGAKSKKQ 243
Cdd:PRK03147  114 NRYGLTFPVAIDKGRQVIDAYGVgpLPTTFLIDKDG-KVVKVITGEMTEEQ 163
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 98-254 1.98e-06

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: 46.69  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033  98 DQQADAENETDKNEifgefktktlDGKDVNQDIFAEADLTMVNIWGTFCGPCIREMPDLGELSREyadkGFRMVGIisDV 177
Cdd:TIGR00385  37 GKPVPAFRLASLDE----------PGQFYTADVLTQGKPVLLNVWASWCPPCRAEHPYLNELAKQ----GLPIVGV--DY 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105563033 178 SQPEDEtALEIVdKTEADYTHLVIpDDANMQYRILRNAQVVPTTIFLDKNGnQVGETYPGAKSKKQWIAVIDKMLEK 254
Cdd:TIGR00385 101 KDDRQN-AIKFL-KELGNPYQLSL-FDPDGMLGLDLGVYGAPETFLVDGNG-VIRYRHAGPLNPEVWTEEFLPLWEK 173
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 57-135 3.95e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 38.44  E-value: 3.95e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105563033   57 GEDAADKAQTDGQQENKDSAKEDGQKADYQDQQTESQEKSQDQQADAENETDKNEIFGEFKTKTlDGKDVNQDIFAEAD 135
Cdd:TIGR00927  660 GEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEA-EGTEDEGEIETGEE 737
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 115-254 3.67e-24

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 93.99  E-value: 3.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 115 EFKTKTLDGKDVNQDIFAEaDLTMVNIWGTFCGPCIREMPDLGELSREYadKGFRMVGIISDvsqPEDETALEIVDKTEA 194
Cdd:COG0526    10 DFTLTDLDGKPLSLADLKG-KPVLVNFWATWCPPCRAEMPVLKELAEEY--GGVVFVGVDVD---ENPEAVKAFLKELGL 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 195 DYTHLVipdDANMQYRILRNAQVVPTTIFLDKNGNQVGeTYPGAKSKKQWIAVIDKMLEK 254
Cdd:COG0526    84 PYPVLL---DPDGELAKAYGVRGIPTTVLIDKDGKIVA-RHVGPLSPEELEEALEKLLAK 139
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 115-231 3.79e-23

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: 90.76  E-value: 3.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 115 EFKTKTLDGKDVNQDIFAEaDLTMVNIWGTFCGPCIREMPDLGELSREYADKGFRMVGIisDVSQPEDETALEIVDKTEA 194
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKG-KVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGV--NVDDDDPAAVKAFLKKYGI 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2105563033 195 DYTHLVIPDDA-NMQYRIlrnaQVVPTTIFLDKNGNQV 231
Cdd:cd02966    78 TFPVLLDPDGElAKAYGV----RGLPTTFLIDRDGRIR 111
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
115-256 2.06e-19

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 81.45  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 115 EFKTKTLDGKDVNQdifaeADL----TMVNIWGTFCGPCIREMPDLGELSREYADKGFRMVGIISDvsqpEDETALEIVD 190
Cdd:COG1225     3 DFTLPDLDGKTVSL-----SDLrgkpVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSD----SDEAHKKFAE 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105563033 191 KTEADYTHLVIPD-DANMQYrilrNAQVVPTTIFLDKNGNQVGETYPGAKSKKQWIAVIDKMLEKVQ 256
Cdd:COG1225    74 KYGLPFPLLSDPDgEVAKAY----GVRGTPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLEALLAELK 136
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 115-229 1.72e-12

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 63.16  E-value: 1.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 115 EFKTKTLDGKDVNQDIFAEADLtMVNIW-GTFCGPCIREMPDLGELSREYADKGFRMVGIISD-----VSQPEDETALEI 188
Cdd:pfam08534  10 TLPDAATDGNTVSLSDFKGKKV-VLNFWpGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDndaffVKRFWGKEGLPF 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2105563033 189 V---DkTEADYTH---LVIPDDANMQYRIlrnaqvvPTTIFLDKNGN 229
Cdd:pfam08534  89 PflsD-GNAAFTKalgLPIEEDASAGLRS-------PRYAVIDEDGK 127
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
115-243 5.02e-10

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 56.94  E-value: 5.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 115 EFKTKTLDGKDVnqdifaeadltMVNIWGTFCGPCIREMPDLGELSREYADKGFRMVGIisDVSQPedetalEIVDKTEA 194
Cdd:PRK03147   53 KIELKDLKGKGV-----------FLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAV--NVDET------ELAVKNFV 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2105563033 195 DYTHLVIPDDANMQYRILRNAQV--VPTTIFLDKNGnQVGETYPGAKSKKQ 243
Cdd:PRK03147  114 NRYGLTFPVAIDKGRQVIDAYGVgpLPTTFLIDKDG-KVVKVITGEMTEEQ 163
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 117-252 5.90e-10

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: 55.21  E-value: 5.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 117 KTKTLDGKDVNQDIFAEADLTMVNIWGTFCGPCIREMPDLGELSREYADKgFRMVGIisDVSQpEDETAleivdkteady 196
Cdd:COG3118     1 AVVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGK-VKFVKV--DVDE-NPELA----------- 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2105563033 197 thlvipddanMQYRIlrnaQVVPTTIFLdKNGNQVGeTYPGAKSKKQWIAVIDKML 252
Cdd:COG3118    66 ----------AQFGV----RSIPTLLLF-KDGQPVD-RFVGALPKEQLREFLDKVL 105
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 115-229 8.34e-10

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: 55.31  E-value: 8.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 115 EFKTKTLDGKDVN-QDIfaEADLTMVNIWGT-FCGPCIREMPDLGELSREYADKGFRMVGIISDvsqpEDETALEIVDKT 192
Cdd:pfam00578   7 DFELPDGDGGTVSlSDY--RGKWVVLFFYPAdWTPVCTTELPALADLYEEFKKLGVEVLGVSVD----SPESHKAFAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2105563033 193 EADYTHLVIPD-DANMQYRILRNAQVV--PTTIFLDKNGN 229
Cdd:pfam00578  81 GLPFPLLSDPDgEVARAYGVLNEEEGGalRATFVIDPDGK 120
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 135-229 9.12e-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: 48.84  E-value: 9.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 135 DLTMVNIWGTFCGPCIREMPDLGELSREY-ADKGFRMVGIISDVSQPEDEtalEIVDKTEADYTHLVIPDDANMQYRILR 213
Cdd:pfam13905   2 KVVLLYFGASWCKPCRRFTPLLKELYEKLkKKKNVEIVFVSLDRDLEEFK---DYLKKMPKDWLSVPFDDDERNELKRKY 78

                          90
                  ....*....|....*.
gi 2105563033 214 NAQVVPTTIFLDKNGN 229
Cdd:pfam13905  79 GVNAIPTLVLLDPNGE 94
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 115-228 1.13e-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: 49.50  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 115 EFKTKTLDGKD--VNQDIFAEaDLTMVNIWGTFCGPCIREMPDLGELSREyadKGFRMVGI-ISDvsQPEDetALEIVDK 191
Cdd:cd03010     5 AFSLPALPGPDktLTSADLKG-KPYLLNVWASWCAPCREEHPVLMALARQ---GRVPIYGInYKD--NPEN--ALAWLAR 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2105563033 192 TEADYThLVIPDDANmqyRILRNAQV--VPTTIFLDKNG 228
Cdd:cd03010    77 HGNPYA-AVGFDPDG---RVGIDLGVygVPETFLIDGDG 111
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 98-254 1.98e-06

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: 46.69  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033  98 DQQADAENETDKNEifgefktktlDGKDVNQDIFAEADLTMVNIWGTFCGPCIREMPDLGELSREyadkGFRMVGIisDV 177
Cdd:TIGR00385  37 GKPVPAFRLASLDE----------PGQFYTADVLTQGKPVLLNVWASWCPPCRAEHPYLNELAKQ----GLPIVGV--DY 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105563033 178 SQPEDEtALEIVdKTEADYTHLVIpDDANMQYRILRNAQVVPTTIFLDKNGnQVGETYPGAKSKKQWIAVIDKMLEK 254
Cdd:TIGR00385 101 KDDRQN-AIKFL-KELGNPYQLSL-FDPDGMLGLDLGVYGAPETFLVDGNG-VIRYRHAGPLNPEVWTEEFLPLWEK 173
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 146-254 1.99e-05

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 43.35  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 146 CGPCIReM-------PDLgelsREYADKGFRMVGIisDVSQPEDETALEIVDKTEADYTHlvipddanmQYRIlrnaQVV 218
Cdd:COG2143    52 CPYCKK-LhkevfsdPEV----AAYLKENFVVVQL--DAEGDKEVTDFDGETLTEKELAR---------KYGV----RGT 111

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2105563033 219 PTTIFLDKNGNQVGEtYPGAKSKKQWIAVIDKMLEK 254
Cdd:COG2143   112 PTLVFFDAEGKEIAR-IPGYLKPETFLALLKYVAEG 146
PTZ00051 PTZ00051
thioredoxin; Provisional
 130-186 3.39e-04

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 39.09  E-value: 3.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2105563033 130 IFAEADLTMVNIWGTFCGPCIREMPDLGELSREYADKGFRMVGI--ISDVSQPEDETAL 186
Cdd:PTZ00051   14 TLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVdeLSEVAEKENITSM 72
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 128-243 7.48e-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: 37.92  E-value: 7.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 128 QDIFAEADLTMVNIWGTFCGPCIREMPDLGELSREYADKGFRMVgiisDVSQpEDETAleivdkteadythlvipddanM 207
Cdd:cd02947     4 EELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKV----DVDE-NPELA---------------------E 57

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2105563033 208 QYRIlrnaQVVPTTIFLdKNGNQVGETYpGAKSKKQ 243
Cdd:cd02947    58 EYGV----RSIPTFLFF-KNGKEVDRVV-GADPKEE 87
trxA PRK09381
thioredoxin TrxA;
127-166 3.94e-03

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 36.20  E-value: 3.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2105563033 127 NQDIFAEADLTMVNIWGTFCGPCIREMPDLGELSREYADK 166
Cdd:PRK09381   14 DTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGK 53
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 57-135 3.95e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 38.44  E-value: 3.95e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105563033   57 GEDAADKAQTDGQQENKDSAKEDGQKADYQDQQTESQEKSQDQQADAENETDKNEIFGEFKTKTlDGKDVNQDIFAEAD 135
Cdd:TIGR00927  660 GEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEA-EGTEDEGEIETGEE 737
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 137-229 4.57e-03

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: 36.13  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 137 TMVNIWGTFCGPCIREMPDLGELSREYADKGFRMVGiisdVSQPE--DETALEIVDKTEADY--THLVIPDDANMQYRIL 212
Cdd:cd03012    26 VLLDFWTYCCINCLHTLPYLTDLEQKYKDDGLVVIG----VHSPEfaFERDLANVKSAVLRYgiTYPVANDNDYATWRAY 101

                          90
                  ....*....|....*..
gi 2105563033 213 RNaQVVPTTIFLDKNGN 229
Cdd:cd03012   102 GN-QYWPALYLIDPTGN 117
SoxW cd02951
SoxW family; SoxW is a bacterial periplasmic TRX, containing a redox active CXXC motif, ...
 214-254 6.15e-03

SoxW family; SoxW is a bacterial periplasmic TRX, containing a redox active CXXC motif, encoded by a genetic locus (sox operon) involved in thiosulfate oxidation. Sulfur bacteria oxidize sulfur compounds to provide reducing equivalents for carbon dioxide fixation during autotrophic growth and the respiratory electron transport chain. It is unclear what the role of SoxW is, since it has been found to be dispensable in the oxidation of thiosulfate to sulfate. SoxW is specifically kept in the reduced state by SoxV, which is essential in thiosulfate oxidation.


Pssm-ID: 239249 [Multi-domain]  Cd Length: 125  Bit Score: 35.75  E-value: 6.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2105563033 214 NAQVVPTTIFLDKNGNQVGETYPGAKSKKQWIAVIDKMLEK 254
Cdd:cd02951    81 RVRFTPTVIFLDPEGGKEIARLPGYLPPDEFLAYLEYVQEK 121
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 116-229 6.58e-03

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: 35.74  E-value: 6.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105563033 116 FKTKTLDGKDVNQdIFAEADLTMVNIWGTFCGPCIREMPDLGELSREYAdkgfrMVGIISDvSQPEDETAlEIVDKTEAD 195
Cdd:cd03011     3 FTATTLDGEQFDL-ESLSGKPVLVYFWATWCPVCRFTSPTVNQLAADYP-----VVSVALR-SGDDGAVA-RFMQKKGYG 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2105563033 196 YThlVIPDDANMQYRILrNAQVVPTTIFLDKNGN 229
Cdd:cd03011    75 FP--VINDPDGVISARW-GVSVTPAIVIVDPGGI 105
 
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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