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Conserved domains on  [gi|530410557|ref|XP_005256813|]
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nucleoredoxin isoform X1 [Homo sapiens]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 274-367 2.33e-69

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd03071:

Pssm-ID: 469754  Cd Length: 116  Bit Score: 213.37  E-value: 2.33e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557 274 DSEDDGESEAAKQLIQPIAEKIIAKYKAKEEEAPLLFFVAGEDDMTDSLRDYTNLPEAAPLLTILDMSARAKYVMDVEEI 353
Cdd:cd03071   23 DSEDEGESEAAKQLIQPIAEKIIAKYKAKEEEAPLLFFVAGEDDMTDSLRDYTNLPEAAPLLTILDMSARAKYVMDVEEI 102

                         90
                 ....*....|....
gi 530410557 354 TPAIVEAFVNDFLA 367
Cdd:cd03071  103 TPAIVEAFVSDFLA 116
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 176-273 1.62e-54

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd03009:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 131  Bit Score: 175.94  E-value: 1.62e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557 176 GPLLRNNGQSLESSSLEGSHVGVYFSAHWCPPCRSLTRVLVESYRKIKEAGQNFEIIFVSADRSEESFKQYFSEMPWLAV 255
Cdd:cd03009    1 DFLLRNDGGKVPVSSLEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKESGKNFEIVFISWDRDEESFNDYFSKMPWLAV 80

                         90
                 ....*....|....*...
gi 530410557 256 PYTDEARRSRLNRLYGIQ 273
Cdd:cd03009   81 PFSDRERRSRLNRTFKIE 98
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 11-165 1.74e-25

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd03009:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 131  Bit Score: 99.67  E-value: 1.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557  11 EKLVTGGGEEVDVHSLGArgiSLLGLYFGCSLSAPCAQLSASLAAFYGRLRgdaaagpgpgagagaaaepEPRRRLEIVF 90
Cdd:cd03009    1 DFLLRNDGGKVPVSSLEG---KTVGLYFSASWCPPCRAFTPKLVEFYEKLK-------------------ESGKNFEIVF 58

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530410557  91 VSSDQDQRQWQDFVRDMPWLALPYKEKHRKLKLWNKYRISNIPSLIFLDAtTGKVVCRNGLLVIRdDPEGLEFPW 165
Cdd:cd03009   59 ISWDRDEESFNDYFSKMPWLAVPFSDRERRSRLNRTFKIEGIPTLIILDA-DGEVVTTDARELVL-EYGADAFPF 131
 
Name Accession Description Interval E-value
PDI_b'_NRX cd03071
PDIb' family, NRX subgroup, redox inactive TRX-like domain b'; composed of vertebrate ...
 274-367 2.33e-69

PDIb' family, NRX subgroup, redox inactive TRX-like domain b'; composed of vertebrate nucleoredoxins (NRX). NRX is a 400-amino acid nuclear protein with one redox active TRX domain followed by one redox inactive TRX-like domain homologous to the b' domain of PDI. In vitro studies show that NRX has thiol oxidoreductase activity and that it may be involved in the redox regulation of transcription, in a manner different from that of TRX or glutaredoxin. NRX enhances the activation of NF-kB by TNFalpha, as well as PMA-1 induced AP-1 and FK-induced CREB activation. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. The mouse NRX gene is implicated in streptozotocin-induced diabetes. Similar to PDI, the b' domain of NRX is likely involved in substrate recognition.


Pssm-ID: 239369  Cd Length: 116  Bit Score: 213.37  E-value: 2.33e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557 274 DSEDDGESEAAKQLIQPIAEKIIAKYKAKEEEAPLLFFVAGEDDMTDSLRDYTNLPEAAPLLTILDMSARAKYVMDVEEI 353
Cdd:cd03071   23 DSEDEGESEAAKQLIQPIAEKIIAKYKAKEEEAPLLFFVAGEDDMTDSLRDYTNLPEAAPLLTILDMSARAKYVMDVEEI 102

                         90
                 ....*....|....
gi 530410557 354 TPAIVEAFVNDFLA 367
Cdd:cd03071  103 TPAIVEAFVSDFLA 116
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 176-273 1.62e-54

Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 175.94  E-value: 1.62e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557 176 GPLLRNNGQSLESSSLEGSHVGVYFSAHWCPPCRSLTRVLVESYRKIKEAGQNFEIIFVSADRSEESFKQYFSEMPWLAV 255
Cdd:cd03009    1 DFLLRNDGGKVPVSSLEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKESGKNFEIVFISWDRDEESFNDYFSKMPWLAV 80

                         90
                 ....*....|....*...
gi 530410557 256 PYTDEARRSRLNRLYGIQ 273
Cdd:cd03009   81 PFSDRERRSRLNRTFKIE 98
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 11-165 1.74e-25

Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 99.67  E-value: 1.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557  11 EKLVTGGGEEVDVHSLGArgiSLLGLYFGCSLSAPCAQLSASLAAFYGRLRgdaaagpgpgagagaaaepEPRRRLEIVF 90
Cdd:cd03009    1 DFLLRNDGGKVPVSSLEG---KTVGLYFSASWCPPCRAFTPKLVEFYEKLK-------------------ESGKNFEIVF 58

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530410557  91 VSSDQDQRQWQDFVRDMPWLALPYKEKHRKLKLWNKYRISNIPSLIFLDAtTGKVVCRNGLLVIRdDPEGLEFPW 165
Cdd:cd03009   59 ISWDRDEESFNDYFSKMPWLAVPFSDRERRSRLNRTFKIEGIPTLIILDA-DGEVVTTDARELVL-EYGADAFPF 131
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 196-273 3.95e-21

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: 86.98  E-value: 3.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557  196 VGVYFSAHWCPPCRSLTRVLVESYRKIKeAGQNFEIIFVSADRSEESFKQYFSEMP--WLAVPYtDEARRSRLNRLYGIQ 273
Cdd:pfam13905   4 VLLYFGASWCKPCRRFTPLLKELYEKLK-KKKNVEIVFVSLDRDLEEFKDYLKKMPkdWLSVPF-DDDERNELKRKYGVN 81
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 33-139 5.26e-19

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: 81.20  E-value: 5.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557   33 LLGLYFGCSLSAPCAQLSASLAAFYGRLRGDaaagpgpgagagaaaepeprRRLEIVFVSSDQDQRQWQDFVRDMP--WL 110
Cdd:pfam13905   3 VVLLYFGASWCKPCRRFTPLLKELYEKLKKK--------------------KNVEIVFVSLDRDLEEFKDYLKKMPkdWL 62

                          90       100
                  ....*....|....*....|....*....
gi 530410557  111 ALPYKEKHRKlKLWNKYRISNIPSLIFLD 139
Cdd:pfam13905  63 SVPFDDDERN-ELKRKYGVNAIPTLVLLD 90
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 226-375 1.84e-10

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 62.00  E-value: 1.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557  226 GQNFEIIFVSADRSEESFKQYFSEMpwlAVPYTDEARRSRLNRLYG--------IQDSEDDGESEAAKQLIQPIAEKiia 297
Cdd:TIGR01130 190 DEKFSKVDGEMDTDVSDLEKFIRAE---SLPLVGEFTQETAAKYFEsgplvvlyYNVDESLDPFEELRNRFLEAAKK--- 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557  298 kYKAKEeeapLLFFVAGEDDMTDSLRDYTNLPEAAPLLTILDMSARAKYVMDVEEITPAIVEAFVNDFLAEKLKP----E 373
Cdd:TIGR01130 264 -FRGKF----VNFAVADEEDFGRELEYFGLKAEKFPAVAIQDLEGNKKYPMDQEEFSSENLEAFVKDFLDGKLKPylksE 338


                  ..
gi 530410557  374 PI 375
Cdd:TIGR01130 339 PI 340
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 198-273 1.41e-07

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 50.07  E-value: 1.41e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530410557 198 VYFSAHWCPPCRSLTRVLVESYRKIKeagqNFEIIFVSADRSEESFKQYFSEMPWLAVPYTDEarRSRLNRLYGIQ 273
Cdd:COG0526   33 VNFWATWCPPCRAEMPVLKELAEEYG----GVVFVGVDVDENPEAVKAFLKELGLPYPVLLDP--DGELAKAYGVR 102
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 36-148 9.01e-05

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 41.98  E-value: 9.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557  36 LYFGCSLSAPCAQLSASLAAFYGRLRGdaaagpgpgagagaaaepeprrrLEIVFVSSDQDQRQWQDFVRDMPWLALPYK 115
Cdd:COG0526   33 VNFWATWCPPCRAEMPVLKELAEEYGG-----------------------VVFVGVDVDENPEAVKAFLKELGLPYPVLL 89

                         90       100       110
                 ....*....|....*....|....*....|...
gi 530410557 116 EkhRKLKLWNKYRISNIPSLIFLDAtTGKVVCR 148
Cdd:COG0526   90 D--PDGELAKAYGVRGIPTTVLIDK-DGKIVAR 119
 
Name Accession Description Interval E-value
PDI_b'_NRX cd03071
PDIb' family, NRX subgroup, redox inactive TRX-like domain b'; composed of vertebrate ...
 274-367 2.33e-69

PDIb' family, NRX subgroup, redox inactive TRX-like domain b'; composed of vertebrate nucleoredoxins (NRX). NRX is a 400-amino acid nuclear protein with one redox active TRX domain followed by one redox inactive TRX-like domain homologous to the b' domain of PDI. In vitro studies show that NRX has thiol oxidoreductase activity and that it may be involved in the redox regulation of transcription, in a manner different from that of TRX or glutaredoxin. NRX enhances the activation of NF-kB by TNFalpha, as well as PMA-1 induced AP-1 and FK-induced CREB activation. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. The mouse NRX gene is implicated in streptozotocin-induced diabetes. Similar to PDI, the b' domain of NRX is likely involved in substrate recognition.


Pssm-ID: 239369  Cd Length: 116  Bit Score: 213.37  E-value: 2.33e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557 274 DSEDDGESEAAKQLIQPIAEKIIAKYKAKEEEAPLLFFVAGEDDMTDSLRDYTNLPEAAPLLTILDMSARAKYVMDVEEI 353
Cdd:cd03071   23 DSEDEGESEAAKQLIQPIAEKIIAKYKAKEEEAPLLFFVAGEDDMTDSLRDYTNLPEAAPLLTILDMSARAKYVMDVEEI 102

                         90
                 ....*....|....
gi 530410557 354 TPAIVEAFVNDFLA 367
Cdd:cd03071  103 TPAIVEAFVSDFLA 116
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 176-273 1.62e-54

Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 175.94  E-value: 1.62e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557 176 GPLLRNNGQSLESSSLEGSHVGVYFSAHWCPPCRSLTRVLVESYRKIKEAGQNFEIIFVSADRSEESFKQYFSEMPWLAV 255
Cdd:cd03009    1 DFLLRNDGGKVPVSSLEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKESGKNFEIVFISWDRDEESFNDYFSKMPWLAV 80

                         90
                 ....*....|....*...
gi 530410557 256 PYTDEARRSRLNRLYGIQ 273
Cdd:cd03009   81 PFSDRERRSRLNRTFKIE 98
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 195-273 2.05e-43

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: 146.99  E-value: 2.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557 195 HVGVYFSAHWCPPCRSLTRVLVESYRKIKEAGQNFEIIFVSADRSEESFKQYFSEM-PWLAVPYTDEARRSRLNRLYGIQ 273
Cdd:cd02964   19 TVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGKNFEIVFVSRDRSEESFNEYFSEMpPWLAVPFEDEELRELLEKQFKVE 98
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 11-165 1.74e-25

Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 99.67  E-value: 1.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557  11 EKLVTGGGEEVDVHSLGArgiSLLGLYFGCSLSAPCAQLSASLAAFYGRLRgdaaagpgpgagagaaaepEPRRRLEIVF 90
Cdd:cd03009    1 DFLLRNDGGKVPVSSLEG---KTVGLYFSASWCPPCRAFTPKLVEFYEKLK-------------------ESGKNFEIVF 58

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530410557  91 VSSDQDQRQWQDFVRDMPWLALPYKEKHRKLKLWNKYRISNIPSLIFLDAtTGKVVCRNGLLVIRdDPEGLEFPW 165
Cdd:cd03009   59 ISWDRDEESFNDYFSKMPWLAVPFSDRERRSRLNRTFKIEGIPTLIILDA-DGEVVTTDARELVL-EYGADAFPF 131
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 17-165 1.71e-23

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: 94.60  E-value: 1.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557  17 GGEEVDVHSLGARgisLLGLYFGCSLSAPCAQLSASLAAFYGRLRgdaaagpgpgagagaaaepEPRRRLEIVFVSSDQD 96
Cdd:cd02964    6 GEGVVPVSALEGK---TVGLYFSASWCPPCRAFTPKLVEFYEKLK-------------------EEGKNFEIVFVSRDRS 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557  97 QRQWQDFVRDM-PWLALPYKEKHRKLKLWNKYRISNIPSLIFLDAtTGKVVCRNGLLVIRDDPEGLEFPW 165
Cdd:cd02964   64 EESFNEYFSEMpPWLAVPFEDEELRELLEKQFKVEGIPTLVVLKP-DGDVVTTNARDEVEEDPGACAFPW 132
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 196-273 3.95e-21

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: 86.98  E-value: 3.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557  196 VGVYFSAHWCPPCRSLTRVLVESYRKIKeAGQNFEIIFVSADRSEESFKQYFSEMP--WLAVPYtDEARRSRLNRLYGIQ 273
Cdd:pfam13905   4 VLLYFGASWCKPCRRFTPLLKELYEKLK-KKKNVEIVFVSLDRDLEEFKDYLKKMPkdWLSVPF-DDDERNELKRKYGVN 81
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 33-139 5.26e-19

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: 81.20  E-value: 5.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557   33 LLGLYFGCSLSAPCAQLSASLAAFYGRLRGDaaagpgpgagagaaaepeprRRLEIVFVSSDQDQRQWQDFVRDMP--WL 110
Cdd:pfam13905   3 VVLLYFGASWCKPCRRFTPLLKELYEKLKKK--------------------KNVEIVFVSLDRDLEEFKDYLKKMPkdWL 62

                          90       100
                  ....*....|....*....|....*....
gi 530410557  111 ALPYKEKHRKlKLWNKYRISNIPSLIFLD 139
Cdd:pfam13905  63 SVPFDDDERN-ELKRKYGVNAIPTLVLLD 90
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 275-366 9.96e-13

Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI, calsequestrin and other PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5 and PDIR. PDI, ERp57, ERp72, P5 and PDIR are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive domains are implicated in substrate recognition with the b' domain serving as the primary substrate binding site. Only the b' domain is necessary for the binding of small peptide substrates. In addition to the b' domain, other domains are required for the binding of larger polypeptide substrates. The b' domain is also implicated in chaperone activity.


Pssm-ID: 239280 [Multi-domain]  Cd Length: 103  Bit Score: 63.83  E-value: 9.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557 275 SEDDGESEAAKQLIQPIAEKIIAKykakeeeapLLFFVAGEDDMtDSLRDYTNLPEA-APLLTILDMSARAKYVMDVEEI 353
Cdd:cd02982   21 NKDDSESEELRERFKEVAKKFKGK---------LLFVVVDADDF-GRHLEYFGLKEEdLPVIAIINLSDGKKYLMPEEEL 90

                         90
                 ....*....|...
gi 530410557 354 TPAIVEAFVNDFL 366
Cdd:cd02982   91 TAESLEEFVEDFL 103
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 226-375 1.84e-10

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 62.00  E-value: 1.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557  226 GQNFEIIFVSADRSEESFKQYFSEMpwlAVPYTDEARRSRLNRLYG--------IQDSEDDGESEAAKQLIQPIAEKiia 297
Cdd:TIGR01130 190 DEKFSKVDGEMDTDVSDLEKFIRAE---SLPLVGEFTQETAAKYFEsgplvvlyYNVDESLDPFEELRNRFLEAAKK--- 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557  298 kYKAKEeeapLLFFVAGEDDMTDSLRDYTNLPEAAPLLTILDMSARAKYVMDVEEITPAIVEAFVNDFLAEKLKP----E 373
Cdd:TIGR01130 264 -FRGKF----VNFAVADEEDFGRELEYFGLKAEKFPAVAIQDLEGNKKYPMDQEEFSSENLEAFVKDFLDGKLKPylksE 338


                  ..
gi 530410557  374 PI 375
Cdd:TIGR01130 339 PI 340
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 198-273 1.41e-07

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 50.07  E-value: 1.41e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530410557 198 VYFSAHWCPPCRSLTRVLVESYRKIKeagqNFEIIFVSADRSEESFKQYFSEMPWLAVPYTDEarRSRLNRLYGIQ 273
Cdd:COG0526   33 VNFWATWCPPCRAEMPVLKELAEEYG----GVVFVGVDVDENPEAVKAFLKELGLPYPVLLDP--DGELAKAYGVR 102
TryX_like_RdCVF cd03008
Tryparedoxin (TryX)-like family, Rod-derived cone viability factor (RdCVF) subfamily; RdCVF is ...
 33-150 2.32e-07

Tryparedoxin (TryX)-like family, Rod-derived cone viability factor (RdCVF) subfamily; RdCVF is a thioredoxin (TRX)-like protein specifically expressed in photoreceptors. RdCVF was isolated and identified as a factor that supports cone survival in retinal cultures. Cone photoreceptor loss is responsible for the visual handicap resulting from the inherited disease, retinitis pigmentosa. RdCVF shows 33% similarity to TRX but does not exhibit any detectable thiol oxidoreductase activity.


Pssm-ID: 239306  Cd Length: 146  Bit Score: 49.82  E-value: 2.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557  33 LLGLYFGCSLSAPCAQLSASLAAFYGRLRGDAAAGPGPgagagaaaepeprrRLEIVFVSSDQDQRQWQDFVRDMP--WL 110
Cdd:cd03008   27 VLLLFFGAVVSPQCQLFAPKLKDFFVRLTDEFYVDRSA--------------QLALVYVSMDQSEQQQESFLKDMPkkWL 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 530410557 111 ALPYKEKHRKlKLWNKYRISNIPSLIFLDAtTGKVVCRNG 150
Cdd:cd03008   93 FLPFEDEFRR-ELEAQFSVEELPTVVVLKP-DGDVLAANA 130
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
198-241 1.23e-05

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 44.47  E-value: 1.23e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 530410557 198 VYFSAHWCPPCRSLTRVLVESYRKIKEAGqnFEIIFVSADRSEE 241
Cdd:COG1225   26 LYFYATWCPGCTAELPELRDLYEEFKDKG--VEVLGVSSDSDEA 67
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 198-246 6.37e-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: 6.37e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530410557 198 VYFSAHWCPPCRSLTRVLVEsyrkIKEAGQNFEIIFVSADRSEESFKQY 246
Cdd:cd02947   15 VDFWAPWCGPCKAIAPVLEE----LAEEYPKVKFVKVDVDENPELAEEY 59
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 36-148 9.01e-05

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 41.98  E-value: 9.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410557  36 LYFGCSLSAPCAQLSASLAAFYGRLRGdaaagpgpgagagaaaepeprrrLEIVFVSSDQDQRQWQDFVRDMPWLALPYK 115
Cdd:COG0526   33 VNFWATWCPPCRAEMPVLKELAEEYGG-----------------------VVFVGVDVDENPEAVKAFLKELGLPYPVLL 89

                         90       100       110
                 ....*....|....*....|....*....|...
gi 530410557 116 EkhRKLKLWNKYRISNIPSLIFLDAtTGKVVCR 148
Cdd:COG0526   90 D--PDGELAKAYGVRGIPTTVLIDK-DGKIVAR 119
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 198-273 9.97e-05

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: 41.45  E-value: 9.97e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530410557 198 VYFSAHWCPPCRSLTRVLVESYRKIKeaGQNFEIIFVSADRSEES-FKQYFSEMPWLAVPYTDEarRSRLNRLYGIQ 273
Cdd:cd02966   24 VNFWASWCPPCRAEMPELEALAKEYK--DDGVEVVGVNVDDDDPAaVKAFLKKYGITFPVLLDP--DGELAKAYGVR 96
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 198-246 7.98e-04

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: 38.65  E-value: 7.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530410557 198 VYFSAHWCPPCRSLTRVLVESyrkIKEAGQNFEIIFVSADRSEESFKQY 246
Cdd:COG3118   23 VDFWAPWCGPCKMLAPVLEEL---AAEYGGKVKFVKVDVDENPELAAQF 68
TryX_like_RdCVF cd03008
Tryparedoxin (TryX)-like family, Rod-derived cone viability factor (RdCVF) subfamily; RdCVF is ...
 198-263 9.09e-04

Tryparedoxin (TryX)-like family, Rod-derived cone viability factor (RdCVF) subfamily; RdCVF is a thioredoxin (TRX)-like protein specifically expressed in photoreceptors. RdCVF was isolated and identified as a factor that supports cone survival in retinal cultures. Cone photoreceptor loss is responsible for the visual handicap resulting from the inherited disease, retinitis pigmentosa. RdCVF shows 33% similarity to TRX but does not exhibit any detectable thiol oxidoreductase activity.


Pssm-ID: 239306  Cd Length: 146  Bit Score: 39.42  E-value: 9.09e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530410557 198 VYFSAHWCPPCRSLTRVLVESYRKIK-----EAGQNFEIIFVSADRSEESFKQYFSEMP--WLAVPYTDEARR 263
Cdd:cd03008   30 LFFGAVVSPQCQLFAPKLKDFFVRLTdefyvDRSAQLALVYVSMDQSEQQQESFLKDMPkkWLFLPFEDEFRR 102
 
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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