NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|50732569|ref|XP_418698|]
View 

anterior gradient protein 2 homolog [Gallus gallus]

Protein Classification

glutathione S-transferase; glutathione S-transferase omega family protein( domain architecture ID 10121657)

glutathione S-transferase catalyzes the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress| glutathione S-transferase (GST) omega family protein such as class-omega GSTs, which catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins than GSTs

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AGR cd02960
Anterior Gradient (AGR) family; members of this family are similar to secreted proteins ...
 44-172 1.32e-92

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: 265.13  E-value: 1.32e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50732569  44 GWGDQLIWTQTYEEALFRSKNSNKPLMIIHHLDDCPHSQALKKVFAEHKEIQKLA-EKFILLNLVYETTDKNLAPDGQYV 122
Cdd:cd02960   1 GWGDDIIWVQTYEEGLYKAKKSNKPLMVIHHLEDCPHSQALKKAFAEHKEIQKLAqEDFIMLNLVHETTDKNLSPDGQYV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 50732569 123 PRILFIDPSLTVRADITGRYSNRLYAYEPSDISLLYSNMQKALKLLKTEL 172
Cdd:cd02960  81 PRIMFVDPSLTVRADITGRYSNRLYTYEPADIPLLIENMKKALKLLKTEL 130
 
Name Accession Description Interval E-value
AGR cd02960
Anterior Gradient (AGR) family; members of this family are similar to secreted proteins ...
 44-172 1.32e-92

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: 265.13  E-value: 1.32e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50732569  44 GWGDQLIWTQTYEEALFRSKNSNKPLMIIHHLDDCPHSQALKKVFAEHKEIQKLA-EKFILLNLVYETTDKNLAPDGQYV 122
Cdd:cd02960   1 GWGDDIIWVQTYEEGLYKAKKSNKPLMVIHHLEDCPHSQALKKAFAEHKEIQKLAqEDFIMLNLVHETTDKNLSPDGQYV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 50732569 123 PRILFIDPSLTVRADITGRYSNRLYAYEPSDISLLYSNMQKALKLLKTEL 172
Cdd:cd02960  81 PRIMFVDPSLTVRADITGRYSNRLYTYEPADIPLLIENMKKALKLLKTEL 130
Thioredoxin_7 pfam13899
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 51-130 1.36e-27

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: 98.59  E-value: 1.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50732569    51 WTQTYEEALFRSKNSNKPLMIIHHLDDCPHSQALKKVFAEHKEIQK-LAEKFILLNLVYETTDKNL--APDGQYVPRILF 127
Cdd:pfam13899   2 WLSDLEEALAAAAERGKPVLVDFGADWCFTCQVLERDFLSHEEVKAaLAKNFVLLRLDWTSRDANItrAFDGQGVPHIAF 81


                  ...
gi 50732569   128 IDP 130
Cdd:pfam13899  82 LDP 84
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 51-140 7.08e-08

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 49.13  E-value: 7.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50732569  51 WTQTYEEALFRSKNSNKPLMIIHHLDDCPHSQALKKVFAEHKEIQKLAEK-FILLNLVYETTDKNLAPDGQ--------- 120
Cdd:COG2143  25 FLLDLEEDLALAKAEGKPILLFFESDWCPYCKKLHKEVFSDPEVAAYLKEnFVVVQLDAEGDKEVTDFDGEtltekelar 104

                        90       100
                ....*....|....*....|....*
gi 50732569 121 -----YVPRILFIDPSLTVRADITG 140
Cdd:COG2143 105 kygvrGTPTLVFFDAEGKEIARIPG 129
 
Name Accession Description Interval E-value
AGR cd02960
Anterior Gradient (AGR) family; members of this family are similar to secreted proteins ...
 44-172 1.32e-92

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: 265.13  E-value: 1.32e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50732569  44 GWGDQLIWTQTYEEALFRSKNSNKPLMIIHHLDDCPHSQALKKVFAEHKEIQKLA-EKFILLNLVYETTDKNLAPDGQYV 122
Cdd:cd02960   1 GWGDDIIWVQTYEEGLYKAKKSNKPLMVIHHLEDCPHSQALKKAFAEHKEIQKLAqEDFIMLNLVHETTDKNLSPDGQYV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 50732569 123 PRILFIDPSLTVRADITGRYSNRLYAYEPSDISLLYSNMQKALKLLKTEL 172
Cdd:cd02960  81 PRIMFVDPSLTVRADITGRYSNRLYTYEPADIPLLIENMKKALKLLKTEL 130
Thioredoxin_7 pfam13899
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 51-130 1.36e-27

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: 98.59  E-value: 1.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50732569    51 WTQTYEEALFRSKNSNKPLMIIHHLDDCPHSQALKKVFAEHKEIQK-LAEKFILLNLVYETTDKNL--APDGQYVPRILF 127
Cdd:pfam13899   2 WLSDLEEALAAAAERGKPVLVDFGADWCFTCQVLERDFLSHEEVKAaLAKNFVLLRLDWTSRDANItrAFDGQGVPHIAF 81


                  ...
gi 50732569   128 IDP 130
Cdd:pfam13899  82 LDP 84
ERp19 cd02959
Endoplasmic reticulum protein 19 (ERp19) family; ERp19 is also known as ERp18, a protein ...
 47-149 3.38e-22

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: 86.03  E-value: 3.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50732569  47 DQLIWtQTYEEALFRSKNSNKPLMIIHHLDDCPHSQALKKVFAEHKEIQKLAEKFILLNLV--YETTDKNLAPDGQYVPR 124
Cdd:cd02959   1 DHIHW-VTLEDGIKEAKDSGKPLMLLIHKTWCGACKALKPKFAESKEISELSHNFVMVNLEddEEPKDEEFSPDGGYIPR 79

                        90       100
                ....*....|....*....|....*
gi 50732569 125 ILFIDPSLTVRADITGRYSNRLYAY 149
Cdd:cd02959  80 ILFLDPSGDVHPEIINKKGNPNYKY 104
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 51-140 7.08e-08

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 49.13  E-value: 7.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50732569  51 WTQTYEEALFRSKNSNKPLMIIHHLDDCPHSQALKKVFAEHKEIQKLAEK-FILLNLVYETTDKNLAPDGQ--------- 120
Cdd:COG2143  25 FLLDLEEDLALAKAEGKPILLFFESDWCPYCKKLHKEVFSDPEVAAYLKEnFVVVQLDAEGDKEVTDFDGEtltekelar 104

                        90       100
                ....*....|....*....|....*
gi 50732569 121 -----YVPRILFIDPSLTVRADITG 140
Cdd:COG2143 105 kygvrGTPTLVFFDAEGKEIARIPG 129
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
63-130 4.73e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 35.09  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50732569    63 KNSNKPLMIIHHLDDCPHSQALKKVFAEHKEIQKL---AEKFILLNlVYETTDKNLAPDG-------------QYVPRIL 126
Cdd:pfam13098   1 KGNGKPVLVVFTDPDCPYCKKLKKELLEDPDVTVYlgpNFVFIAVN-IWCAKEVAKAFTDilenkelgrkygvRGTPTIV 79


                  ....
gi 50732569   127 FIDP 130
Cdd:pfam13098  80 FFDG 83
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 70-135 9.18e-03

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: 33.44  E-value: 9.18e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50732569  70 MIIHHLDDCPHSQALKKVFAEHKEIQKlaekfillNLVYETTDKNLAPD---------GQYVPRILFIDPSLTVR 135
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELALLNK--------GVKFEAVDVDEDPAlekelkrygVGGVPTLVVFGPGIGVK 67
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH