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Conserved domains on  [gi|23477616|gb|AAN34781|]
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thioredoxin-like protein p19 [Homo sapiens]

Protein Classification

ERp19 domain-containing protein( domain architecture ID 10121655)

ERp19 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ERp19 cd02959
Endoplasmic reticulum protein 19 (ERp19) family; ERp19 is also known as ERp18, a protein ...
 36-152 3.70e-75

Endoplasmic reticulum protein 19 (ERp19) family; ERp19 is also known as ERp18, a protein located in the ER containing one redox active TRX domain. Denaturation studies indicate that the reduced form is more stable than the oxidized form, suggesting that the protein is involved in disulfide bond formation. In vitro, ERp19 has been shown to possess thiol-disulfide oxidase activity which is dependent on the presence of both active site cysteines. Although described as protein disulfide isomerase (PDI)-like, the protein does not complement for PDI activity. ERp19 shows a wide tissue distribution but is most abundant in liver, testis, heart and kidney.


:

Pssm-ID: 239257 [Multi-domain]  Cd Length: 117  Bit Score: 220.46  E-value: 3.70e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23477616  36 DHIHWRTLEDGKKEAAASGLPLMVIIHKSWCGACKALKPKFAESTEISELSHNFVMVNLEDEEEPKDEDFSPDGGYIPRI 115
Cdd:cd02959   1 DHIHWVTLEDGIKEAKDSGKPLMLLIHKTWCGACKALKPKFAESKEISELSHNFVMVNLEDDEEPKDEEFSPDGGYIPRI 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 23477616 116 LFLDPSGKVHPEIINENGNPSYKYFYVSAEQVVQGMK 152
Cdd:cd02959  81 LFLDPSGDVHPEIINKKGNPNYKYFYSSAAQVTESMK 117
 
Name Accession Description Interval E-value
ERp19 cd02959
Endoplasmic reticulum protein 19 (ERp19) family; ERp19 is also known as ERp18, a protein ...
 36-152 3.70e-75

Endoplasmic reticulum protein 19 (ERp19) family; ERp19 is also known as ERp18, a protein located in the ER containing one redox active TRX domain. Denaturation studies indicate that the reduced form is more stable than the oxidized form, suggesting that the protein is involved in disulfide bond formation. In vitro, ERp19 has been shown to possess thiol-disulfide oxidase activity which is dependent on the presence of both active site cysteines. Although described as protein disulfide isomerase (PDI)-like, the protein does not complement for PDI activity. ERp19 shows a wide tissue distribution but is most abundant in liver, testis, heart and kidney.


Pssm-ID: 239257 [Multi-domain]  Cd Length: 117  Bit Score: 220.46  E-value: 3.70e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23477616  36 DHIHWRTLEDGKKEAAASGLPLMVIIHKSWCGACKALKPKFAESTEISELSHNFVMVNLEDEEEPKDEDFSPDGGYIPRI 115
Cdd:cd02959   1 DHIHWVTLEDGIKEAKDSGKPLMLLIHKTWCGACKALKPKFAESKEISELSHNFVMVNLEDDEEPKDEEFSPDGGYIPRI 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 23477616 116 LFLDPSGKVHPEIINENGNPSYKYFYVSAEQVVQGMK 152
Cdd:cd02959  81 LFLDPSGDVHPEIINKKGNPNYKYFYSSAAQVTESMK 117
Thioredoxin_7 pfam13899
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 42-120 6.91e-16

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 433567 [Multi-domain]  Cd Length: 84  Bit Score: 68.54  E-value: 6.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23477616    42 TLEDGKKEAAASGLPLMVIIHKSWCGACKALKPKFAESTEISE-LSHNFVMVNLEDEEEPKDEDFSPDGGYIPRILFLDP 120
Cdd:pfam13899   5 DLEEALAAAAERGKPVLVDFGADWCFTCQVLERDFLSHEEVKAaLAKNFVLLRLDWTSRDANITRAFDGQGVPHIAFLDP 84
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 12-124 1.98e-07

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 47.98  E-value: 1.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23477616  12 LLGFSFLLLVISsdghnglGKGFGDHIHW-RTLEDGKKEAAASGLPLMVIIHKSWCGACKALKPKFAESTEISE-LSHNF 89
Cdd:COG2143   4 LLLLLLLLLLLA-------AAAAAQEISFlLDLEEDLALAKAEGKPILLFFESDWCPYCKKLHKEVFSDPEVAAyLKENF 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 23477616  90 VMVNLEDEEEPKDEDFspDGG--------------YIPRILFLDPSGKV 124
Cdd:COG2143  77 VVVQLDAEGDKEVTDF--DGEtltekelarkygvrGTPTLVFFDAEGKE 123
 
Name Accession Description Interval E-value
ERp19 cd02959
Endoplasmic reticulum protein 19 (ERp19) family; ERp19 is also known as ERp18, a protein ...
 36-152 3.70e-75

Endoplasmic reticulum protein 19 (ERp19) family; ERp19 is also known as ERp18, a protein located in the ER containing one redox active TRX domain. Denaturation studies indicate that the reduced form is more stable than the oxidized form, suggesting that the protein is involved in disulfide bond formation. In vitro, ERp19 has been shown to possess thiol-disulfide oxidase activity which is dependent on the presence of both active site cysteines. Although described as protein disulfide isomerase (PDI)-like, the protein does not complement for PDI activity. ERp19 shows a wide tissue distribution but is most abundant in liver, testis, heart and kidney.


Pssm-ID: 239257 [Multi-domain]  Cd Length: 117  Bit Score: 220.46  E-value: 3.70e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23477616  36 DHIHWRTLEDGKKEAAASGLPLMVIIHKSWCGACKALKPKFAESTEISELSHNFVMVNLEDEEEPKDEDFSPDGGYIPRI 115
Cdd:cd02959   1 DHIHWVTLEDGIKEAKDSGKPLMLLIHKTWCGACKALKPKFAESKEISELSHNFVMVNLEDDEEPKDEEFSPDGGYIPRI 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 23477616 116 LFLDPSGKVHPEIINENGNPSYKYFYVSAEQVVQGMK 152
Cdd:cd02959  81 LFLDPSGDVHPEIINKKGNPNYKYFYSSAAQVTESMK 117
AGR cd02960
Anterior Gradient (AGR) family; members of this family are similar to secreted proteins ...
 33-154 2.99e-24

Anterior Gradient (AGR) family; members of this family are similar to secreted proteins encoded by the cement gland-specific genes XAG-1 and XAG-2, expressed in the anterior region of dorsal ectoderm of Xenopus. They are implicated in the formation of the cement gland and the induction of forebrain fate. The human homologs, hAG-2 and hAG-3, are secreted proteins associated with estrogen-positive breast tumors. Yeast two-hybrid studies identified the metastasis-associated C4.4a protein and dystroglycan as binding partners, indicating possible roles in the development and progression of breast cancer. hAG-2 has also been implicated in prostate cancer. Its gene was cloned as an androgen-inducible gene and it was shown to be overexpressed in prostate cancer cells at the mRNA and protein levels. AGR proteins contain one conserved cysteine corresponding to the first cysteine in the CXXC motif of TRX. They show high sequence similarity to ERp19.


Pssm-ID: 239258 [Multi-domain]  Cd Length: 130  Bit Score: 91.41  E-value: 2.99e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23477616  33 GFGDHIHW-RTLEDGKKEAAASGLPLMVIIHKSWCGACKALKPKFAESTEISELSH-NFVMVNLEDEEEPKDedFSPDGG 110
Cdd:cd02960   1 GWGDDIIWvQTYEEGLYKAKKSNKPLMVIHHLEDCPHSQALKKAFAEHKEIQKLAQeDFIMLNLVHETTDKN--LSPDGQ 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 23477616 111 YIPRILFLDPSGKVHPEIINENGNPSYKYFYVSAEQVVQGMKEA 154
Cdd:cd02960  79 YVPRIMFVDPSLTVRADITGRYSNRLYTYEPADIPLLIENMKKA 122
Thioredoxin_7 pfam13899
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 42-120 6.91e-16

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 433567 [Multi-domain]  Cd Length: 84  Bit Score: 68.54  E-value: 6.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23477616    42 TLEDGKKEAAASGLPLMVIIHKSWCGACKALKPKFAESTEISE-LSHNFVMVNLEDEEEPKDEDFSPDGGYIPRILFLDP 120
Cdd:pfam13899   5 DLEEALAAAAERGKPVLVDFGADWCFTCQVLERDFLSHEEVKAaLAKNFVLLRLDWTSRDANITRAFDGQGVPHIAFLDP 84
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 12-124 1.98e-07

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 47.98  E-value: 1.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23477616  12 LLGFSFLLLVISsdghnglGKGFGDHIHW-RTLEDGKKEAAASGLPLMVIIHKSWCGACKALKPKFAESTEISE-LSHNF 89
Cdd:COG2143   4 LLLLLLLLLLLA-------AAAAAQEISFlLDLEEDLALAKAEGKPILLFFESDWCPYCKKLHKEVFSDPEVAAyLKENF 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 23477616  90 VMVNLEDEEEPKDEDFspDGG--------------YIPRILFLDPSGKV 124
Cdd:COG2143  77 VVVQLDAEGDKEVTDF--DGEtltekelarkygvrGTPTLVFFDAEGKE 123
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 4-156 2.03e-05

Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 43.64  E-value: 2.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23477616   4 RPRLGATCLLGFSFLLLVISSDGHNGL--------GKGFGDHIHWRT-LEDGKKEAAASGLPLMVIIHKSWCGACKALKp 74
Cdd:COG4232 261 VRKGLGLLLLLAGLALLLGALSGADPLqplaagaaAAAAAAGLAWQAdLEAALAEARAEGKPVFVDFTADWCVTCKENE- 339

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23477616  75 KFAESTE--ISELSHNFVMV-----NLEDEEEPKDEDFSPDGgyIPRILFLDPSGKVHPEIinengnpsykYFYVSAEQV 147
Cdd:COG4232 340 RTVFSDPevQAALADDVVLLkadvtDNDPEITALLKRFGRFG--VPTYVFYDPDGEELPRL----------GFMLTADEF 407


                ....*....
gi 23477616 148 VQGMKEAQE 156
Cdd:COG4232 408 LAALEKAKG 416
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 49-123 7.81e-05

TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport.


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 40.78  E-value: 7.81e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23477616  49 EAAASGLPLMVIIHKSWCGACKALKPKFAESTEISELSHNFVMVNLEDEE-EPKDEDFSPDGgyIPRILFLDPSGK 123
Cdd:cd02950  15 VALSNGKPTLVEFYADWCTVCQEMAPDVAKLKQKYGDQVNFVMLNVDNPKwLPEIDRYRVDG--IPHFVFLDREGN 88
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 48-93 3.72e-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: 3.72e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 23477616  48 KEAAASGLPLMVIIHKSWCGACKALKPKFAE-STEISELshNFVMVN 93
Cdd:cd02947   4 EELIKSAKPVVVDFWAPWCGPCKAIAPVLEElAEEYPKV--KFVKVD 48
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 58-125 4.43e-04

Thioredoxin (TRX) superfamily; 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 TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 37.29  E-value: 4.43e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23477616  58 MVIIHKSWCGACKALKPKFAESTEISELSHnFVMVNLEDEEEPKDEDFSPDGGYIPRILFLDPSGKVH 125
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELALLNKGVK-FEAVDVDEDPALEKELKRYGVGGVPTLVVFGPGIGVK 67
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 47-78 6.92e-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: 37.49  E-value: 6.92e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 23477616  47 KKEAAASGLPLMVIIHKSWCGACKALKPKFAE 78
Cdd:COG3118  11 EEEVLESDKPVLVDFWAPWCGPCKMLAPVLEE 42
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 47-93 4.54e-03

PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces cerevisiae MPD1 protein, which contains a single redox active TRX domain located at the N-terminus, and an ER retention signal at the C-terminus indicative of an ER-resident protein. MPD1 has been shown to suppress the maturation defect of carboxypeptidase Y caused by deletion of the yeast PDI1 gene. Other characterized members of this subfamily include the Aspergillus niger prpA protein and Giardia PDI-1. PrpA is non-essential to strain viability, however, its transcript level is induced by heterologous protein expression suggesting a possible role in oxidative protein folding during high protein production. Giardia PDI-1 has the ability to refold scrambled RNase and exhibits transglutaminase activity.


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 35.03  E-value: 4.54e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 23477616  47 KKEAAASGLPLMVIIHKSWCGACKALKPKFAESTEISELSHNFVMVN 93
Cdd:cd03002  11 DKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVD 57
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 64-94 7.80e-03

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 34.52  E-value: 7.80e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 23477616    64 SWCGACKALKPKFAESTEisELSHNFVMVNL 94
Cdd:pfam00085  28 PWCGPCKMLAPEYEELAQ--EYKGNVVFAKV 56
 
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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