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Conserved domains on  [gi|530417932|ref|XP_005260384|]
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eyes absent homolog 2 isoform X3 [Homo sapiens]

Protein Classification

eyes absent family protein( domain architecture ID 11552338)

eyes absent (EYA) family protein functions as a transcriptional coactivator and an aspartyl-based protein tyrosine phosphatase; belongs to the HAD (haloacid dehalogenase) superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_Eya cd02601
protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) ...
 185-456 2.14e-179

protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) and related phosphatase domains; Eyes absent (Eya) is a transcriptional coactivator, and an aspartyl-based protein tyrosine phosphatase. Eya and Six operate as a composite transcription factor, within a conserved network of transcription factors called the retinal determination (RD) network. The RD network interacts with a broad variety of signaling pathways to regulate the development and homeostasis of organs and tissues such as eye, muscle, kidney and ear. To date it is not clear what the physiologically relevant substrates of the Eya protein tyrosine phosphatase are, or whether this phosphatase activity plays a role in transcription. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


:

Pssm-ID: 319789  Cd Length: 271  Bit Score: 502.02  E-value: 2.14e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932 185 IERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQDLS 264
Cdd:cd02601    1 PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDVSSDDNGQDLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932 265 TYNFSADGFHSSAPGANLCLGSGVHGgVDWMRKLAFRYRRVKEMYNTYKNNVGGLIGTPKRETWLQLRAELEALTDLWLT 344
Cdd:cd02601   81 TYNFLTDGFHMRAVAPNLCLPTGVRG-VDWMRKLAFRYRRVKENYNTYKNNVGFLLGEAKREAWLQLRTEIEALTDQWLT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932 345 HSLKALNLINSRPNCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGKESCFERIMQRFGRKAVYVVIGDGVEE 424
Cdd:cd02601  160 LALKALDLISSRENCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKIGKESCFERIQQRFGRKCVYVCIGDGVEE 239

                        250       260       270
                 ....*....|....*....|....*....|..
gi 530417932 425 EQGAKKHNMPFWRISCHADLEALRHALELEYL 456
Cdd:cd02601  240 EQAAKKHNVPFWRISTHSDLLALHHALELEYL 271
 
Name Accession Description Interval E-value
HAD_Eya cd02601
protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) ...
 185-456 2.14e-179

protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) and related phosphatase domains; Eyes absent (Eya) is a transcriptional coactivator, and an aspartyl-based protein tyrosine phosphatase. Eya and Six operate as a composite transcription factor, within a conserved network of transcription factors called the retinal determination (RD) network. The RD network interacts with a broad variety of signaling pathways to regulate the development and homeostasis of organs and tissues such as eye, muscle, kidney and ear. To date it is not clear what the physiologically relevant substrates of the Eya protein tyrosine phosphatase are, or whether this phosphatase activity plays a role in transcription. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319789  Cd Length: 271  Bit Score: 502.02  E-value: 2.14e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932 185 IERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQDLS 264
Cdd:cd02601    1 PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDVSSDDNGQDLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932 265 TYNFSADGFHSSAPGANLCLGSGVHGgVDWMRKLAFRYRRVKEMYNTYKNNVGGLIGTPKRETWLQLRAELEALTDLWLT 344
Cdd:cd02601   81 TYNFLTDGFHMRAVAPNLCLPTGVRG-VDWMRKLAFRYRRVKENYNTYKNNVGFLLGEAKREAWLQLRTEIEALTDQWLT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932 345 HSLKALNLINSRPNCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGKESCFERIMQRFGRKAVYVVIGDGVEE 424
Cdd:cd02601  160 LALKALDLISSRENCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKIGKESCFERIQQRFGRKCVYVCIGDGVEE 239

                        250       260       270
                 ....*....|....*....|....*....|..
gi 530417932 425 EQGAKKHNMPFWRISCHADLEALRHALELEYL 456
Cdd:cd02601  240 EQAAKKHNVPFWRISTHSDLLALHHALELEYL 271
EYA-cons_domain TIGR01658
eyes absent protein conserved domain; This domain is common to all eyes absent (EYA) homologs. ...
 185-456 4.84e-125

eyes absent protein conserved domain; This domain is common to all eyes absent (EYA) homologs. Metazoan EYA's also contain a variable N-terminal domain consisting largely of low-complexity sequences.


Pssm-ID: 273739  Cd Length: 274  Bit Score: 364.17  E-value: 4.84e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932  185 IERVFVWDLDETIIIFHSLLTGTFASRYG--KDTTTSVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQD 262
Cdd:TIGR01658   1 PENVYVWDMDETLILLHSLLNGSYAESFNgsKDHKRGVEIGRRWEEMILEICDTHFFYEEIEECNEPFLDDVRSYDDGKD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932  263 LSTYNFSADGFHSSAPgaNLCLgsgvhggvdwmRKLAFRYRRVKEMYNTYknnVGGLIGTPKRETWLQLRAELEALTDLW 342
Cdd:TIGR01658  81 LSRYEFKTDGFSTPTD--DLNK-----------RKLAYRHRAVAEIYEKG---LGPLLDPESMEALDELYSETDVYTDRW 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932  343 LTHSLK---------------ALNLINSRPNCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGKESCFERIMQ 407
Cdd:TIGR01658 145 LSSALKfleqcscveessdgtSLIEISSRDNCINVLVTSGQLIPSLAKCLLFRLDTIFRIENVYSSIKVGKLQCFKWIKE 224

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 530417932  408 RFGR-KAVYVVIGDGVEEEQGAKKHNMPFWRISCHADLEALRHALELEYL 456
Cdd:TIGR01658 225 RFGHpKVRFCAIGDGWEECTAAQAMNWPFVKIDLHPDSSHRFPGLTLKTL 274
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 187-432 3.56e-05

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 44.50  E-value: 3.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932  187 RVFVWDLDETIIIFHSLLTGTFASrygkdtttsvriglmmeemifNLADTHLFFNDLEDCDQIHVDdvsSDDNGQDLsty 266
Cdd:pfam00702   2 KAVVFDLDGTLTDGEPVVTEAIAE---------------------LASEHPLAKAIVAAAEDLPIP---VEDFTARL--- 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932  267 nfsadgfhssapganlclgsgVHGGVDWMRKLafryrrvkemyNTYKNNVGGLIGTPKRETWLQLRAELEALTDLWLT-H 345
Cdd:pfam00702  55 ---------------------LLGKRDWLEEL-----------DILRGLVETLEAEGLTVVLVELLGVIALADELKLYpG 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932  346 SLKALNLINSRpNCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGK--ESCFERIMQRFG-RKAVYVVIGDGV 422
Cdd:pfam00702 103 AAEALKALKER-GIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKpkPEIYLAALERLGvKPEEVLMVGDGV 181

                         250
                  ....*....|
gi 530417932  423 EEEQGAKKHN 432
Cdd:pfam00702 182 NDIPAAKAAG 191
 
Name Accession Description Interval E-value
HAD_Eya cd02601
protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) ...
 185-456 2.14e-179

protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) and related phosphatase domains; Eyes absent (Eya) is a transcriptional coactivator, and an aspartyl-based protein tyrosine phosphatase. Eya and Six operate as a composite transcription factor, within a conserved network of transcription factors called the retinal determination (RD) network. The RD network interacts with a broad variety of signaling pathways to regulate the development and homeostasis of organs and tissues such as eye, muscle, kidney and ear. To date it is not clear what the physiologically relevant substrates of the Eya protein tyrosine phosphatase are, or whether this phosphatase activity plays a role in transcription. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319789  Cd Length: 271  Bit Score: 502.02  E-value: 2.14e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932 185 IERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQDLS 264
Cdd:cd02601    1 PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDVSSDDNGQDLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932 265 TYNFSADGFHSSAPGANLCLGSGVHGgVDWMRKLAFRYRRVKEMYNTYKNNVGGLIGTPKRETWLQLRAELEALTDLWLT 344
Cdd:cd02601   81 TYNFLTDGFHMRAVAPNLCLPTGVRG-VDWMRKLAFRYRRVKENYNTYKNNVGFLLGEAKREAWLQLRTEIEALTDQWLT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932 345 HSLKALNLINSRPNCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGKESCFERIMQRFGRKAVYVVIGDGVEE 424
Cdd:cd02601  160 LALKALDLISSRENCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKIGKESCFERIQQRFGRKCVYVCIGDGVEE 239

                        250       260       270
                 ....*....|....*....|....*....|..
gi 530417932 425 EQGAKKHNMPFWRISCHADLEALRHALELEYL 456
Cdd:cd02601  240 EQAAKKHNVPFWRISTHSDLLALHHALELEYL 271
EYA-cons_domain TIGR01658
eyes absent protein conserved domain; This domain is common to all eyes absent (EYA) homologs. ...
 185-456 4.84e-125

eyes absent protein conserved domain; This domain is common to all eyes absent (EYA) homologs. Metazoan EYA's also contain a variable N-terminal domain consisting largely of low-complexity sequences.


Pssm-ID: 273739  Cd Length: 274  Bit Score: 364.17  E-value: 4.84e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932  185 IERVFVWDLDETIIIFHSLLTGTFASRYG--KDTTTSVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQD 262
Cdd:TIGR01658   1 PENVYVWDMDETLILLHSLLNGSYAESFNgsKDHKRGVEIGRRWEEMILEICDTHFFYEEIEECNEPFLDDVRSYDDGKD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932  263 LSTYNFSADGFHSSAPgaNLCLgsgvhggvdwmRKLAFRYRRVKEMYNTYknnVGGLIGTPKRETWLQLRAELEALTDLW 342
Cdd:TIGR01658  81 LSRYEFKTDGFSTPTD--DLNK-----------RKLAYRHRAVAEIYEKG---LGPLLDPESMEALDELYSETDVYTDRW 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932  343 LTHSLK---------------ALNLINSRPNCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGKESCFERIMQ 407
Cdd:TIGR01658 145 LSSALKfleqcscveessdgtSLIEISSRDNCINVLVTSGQLIPSLAKCLLFRLDTIFRIENVYSSIKVGKLQCFKWIKE 224

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 530417932  408 RFGR-KAVYVVIGDGVEEEQGAKKHNMPFWRISCHADLEALRHALELEYL 456
Cdd:TIGR01658 225 RFGHpKVRFCAIGDGWEECTAAQAMNWPFVKIDLHPDSSHRFPGLTLKTL 274
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 187-432 3.56e-05

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 44.50  E-value: 3.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932  187 RVFVWDLDETIIIFHSLLTGTFASrygkdtttsvriglmmeemifNLADTHLFFNDLEDCDQIHVDdvsSDDNGQDLsty 266
Cdd:pfam00702   2 KAVVFDLDGTLTDGEPVVTEAIAE---------------------LASEHPLAKAIVAAAEDLPIP---VEDFTARL--- 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932  267 nfsadgfhssapganlclgsgVHGGVDWMRKLafryrrvkemyNTYKNNVGGLIGTPKRETWLQLRAELEALTDLWLT-H 345
Cdd:pfam00702  55 ---------------------LLGKRDWLEEL-----------DILRGLVETLEAEGLTVVLVELLGVIALADELKLYpG 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417932  346 SLKALNLINSRpNCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGK--ESCFERIMQRFG-RKAVYVVIGDGV 422
Cdd:pfam00702 103 AAEALKALKER-GIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKpkPEIYLAALERLGvKPEEVLMVGDGV 181

                         250
                  ....*....|
gi 530417932  423 EEEQGAKKHN 432
Cdd:pfam00702 182 NDIPAAKAAG 191
 
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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