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Conserved domains on  [gi|1720353667|ref|XP_030103330|]
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eyes absent homolog 1 isoform X1 [Mus musculus]

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) ...
 321-566 1.69e-158

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: 455.03  E-value: 1.69e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 321 LERVFIWDLDETIIVFHSLLTGSYANRYGRDPPTSVSLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLS 400
Cdd:cd02601     1 PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDVSSDDNGQDLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 401 TYNFGTDGFPAAATSANLCLATGVRGgVDWMRKLAFRYRRVKEIYNTYKNNVGGLLGPAKREAWLQLRAEIEALTDSWLT 480
Cdd:cd02601    81 TYNFLTDGFHMRAVAPNLCLPTGVRG-VDWMRKLAFRYRRVKENYNTYKNNVGFLLGEAKREAWLQLRTEIEALTDQWLT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 481 LALKALSLIHSRTNCVNILVTTTQLIPALAKVLLYGLGIVFPIENIYSATKIGKESCFERIIQRFGRKVVYVVIGDGVEE 560
Cdd:cd02601   160 LALKALDLISSRENCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKIGKESCFERIQQRFGRKCVYVCIGDGVEE 239


                  ....*.
gi 1720353667 561 EQGAKK 566
Cdd:cd02601   240 EQAAKK 245
 
Name Accession Description Interval E-value
HAD_Eya cd02601
protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) ...
 321-566 1.69e-158

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: 455.03  E-value: 1.69e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 321 LERVFIWDLDETIIVFHSLLTGSYANRYGRDPPTSVSLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLS 400
Cdd:cd02601     1 PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDVSSDDNGQDLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 401 TYNFGTDGFPAAATSANLCLATGVRGgVDWMRKLAFRYRRVKEIYNTYKNNVGGLLGPAKREAWLQLRAEIEALTDSWLT 480
Cdd:cd02601    81 TYNFLTDGFHMRAVAPNLCLPTGVRG-VDWMRKLAFRYRRVKENYNTYKNNVGFLLGEAKREAWLQLRTEIEALTDQWLT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 481 LALKALSLIHSRTNCVNILVTTTQLIPALAKVLLYGLGIVFPIENIYSATKIGKESCFERIIQRFGRKVVYVVIGDGVEE 560
Cdd:cd02601   160 LALKALDLISSRENCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKIGKESCFERIQQRFGRKCVYVCIGDGVEE 239


                  ....*.
gi 1720353667 561 EQGAKK 566
Cdd:cd02601   240 EQAAKK 245
EYA-cons_domain TIGR01658
eyes absent protein conserved domain; This domain is common to all eyes absent (EYA) homologs. ...
 321-565 4.79e-118

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: 351.85  E-value: 4.79e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 321 LERVFIWDLDETIIVFHSLLTGSYANRYG--RDPPTSVSLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQD 398
Cdd:TIGR01658   1 PENVYVWDMDETLILLHSLLNGSYAESFNgsKDHKRGVEIGRRWEEMILEICDTHFFYEEIEECNEPFLDDVRSYDDGKD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 399 LSTYNFGTDGFPAAatSANLCLatgvrggvdwmRKLAFRYRRVKEIYNTYknnVGGLLGPAKREAWLQLRAEIEALTDSW 478
Cdd:TIGR01658  81 LSRYEFKTDGFSTP--TDDLNK-----------RKLAYRHRAVAEIYEKG---LGPLLDPESMEALDELYSETDVYTDRW 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 479 LTLALK---------------ALSLIHSRTNCVNILVTTTQLIPALAKVLLYGLGIVFPIENIYSATKIGKESCFERIIQ 543
Cdd:TIGR01658 145 LSSALKfleqcscveessdgtSLIEISSRDNCINVLVTSGQLIPSLAKCLLFRLDTIFRIENVYSSIKVGKLQCFKWIKE 224

                         250       260
                  ....*....|....*....|...
gi 1720353667 544 RFGR-KVVYVVIGDGVEEEQGAK 565
Cdd:TIGR01658 225 RFGHpKVRFCAIGDGWEECTAAQ 247
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 323-567 2.25e-07

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: 51.43  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 323 RVFIWDLDETIIVFHSLLTGSYANrygrdpptsvslglrmeemifNLADTHLFFNDLEECDQVHIDdvsSDDNGQDLsty 402
Cdd:pfam00702   2 KAVVFDLDGTLTDGEPVVTEAIAE---------------------LASEHPLAKAIVAAAEDLPIP---VEDFTARL--- 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 403 nfgtdgfpaaatsanlclatgVRGGVDWMRKLafryrrvkeiyNTYKNNVGGLLGPAKREAWLQLRAEIEALTDSWLTL- 481
Cdd:pfam00702  55 ---------------------LLGKRDWLEEL-----------DILRGLVETLEAEGLTVVLVELLGVIALADELKLYPg 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 482 ALKALSLIHSRTNCVnILVTTTQLIPALAKVLLYGLGIVFPIENIYSATKIGK--ESCFERIIQRFGRKV-VYVVIGDGV 558
Cdd:pfam00702 103 AAEALKALKERGIKV-AILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKpkPEIYLAALERLGVKPeEVLMVGDGV 181


                  ....*....
gi 1720353667 559 EEEQGAKKA 567
Cdd:pfam00702 182 NDIPAAKAA 190
 
Name Accession Description Interval E-value
HAD_Eya cd02601
protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) ...
 321-566 1.69e-158

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: 455.03  E-value: 1.69e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 321 LERVFIWDLDETIIVFHSLLTGSYANRYGRDPPTSVSLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLS 400
Cdd:cd02601     1 PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDVSSDDNGQDLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 401 TYNFGTDGFPAAATSANLCLATGVRGgVDWMRKLAFRYRRVKEIYNTYKNNVGGLLGPAKREAWLQLRAEIEALTDSWLT 480
Cdd:cd02601    81 TYNFLTDGFHMRAVAPNLCLPTGVRG-VDWMRKLAFRYRRVKENYNTYKNNVGFLLGEAKREAWLQLRTEIEALTDQWLT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 481 LALKALSLIHSRTNCVNILVTTTQLIPALAKVLLYGLGIVFPIENIYSATKIGKESCFERIIQRFGRKVVYVVIGDGVEE 560
Cdd:cd02601   160 LALKALDLISSRENCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKIGKESCFERIQQRFGRKCVYVCIGDGVEE 239


                  ....*.
gi 1720353667 561 EQGAKK 566
Cdd:cd02601   240 EQAAKK 245
EYA-cons_domain TIGR01658
eyes absent protein conserved domain; This domain is common to all eyes absent (EYA) homologs. ...
 321-565 4.79e-118

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: 351.85  E-value: 4.79e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 321 LERVFIWDLDETIIVFHSLLTGSYANRYG--RDPPTSVSLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQD 398
Cdd:TIGR01658   1 PENVYVWDMDETLILLHSLLNGSYAESFNgsKDHKRGVEIGRRWEEMILEICDTHFFYEEIEECNEPFLDDVRSYDDGKD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 399 LSTYNFGTDGFPAAatSANLCLatgvrggvdwmRKLAFRYRRVKEIYNTYknnVGGLLGPAKREAWLQLRAEIEALTDSW 478
Cdd:TIGR01658  81 LSRYEFKTDGFSTP--TDDLNK-----------RKLAYRHRAVAEIYEKG---LGPLLDPESMEALDELYSETDVYTDRW 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 479 LTLALK---------------ALSLIHSRTNCVNILVTTTQLIPALAKVLLYGLGIVFPIENIYSATKIGKESCFERIIQ 543
Cdd:TIGR01658 145 LSSALKfleqcscveessdgtSLIEISSRDNCINVLVTSGQLIPSLAKCLLFRLDTIFRIENVYSSIKVGKLQCFKWIKE 224

                         250       260
                  ....*....|....*....|...
gi 1720353667 544 RFGR-KVVYVVIGDGVEEEQGAK 565
Cdd:TIGR01658 225 RFGHpKVRFCAIGDGWEECTAAQ 247
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 323-567 2.25e-07

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: 51.43  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 323 RVFIWDLDETIIVFHSLLTGSYANrygrdpptsvslglrmeemifNLADTHLFFNDLEECDQVHIDdvsSDDNGQDLsty 402
Cdd:pfam00702   2 KAVVFDLDGTLTDGEPVVTEAIAE---------------------LASEHPLAKAIVAAAEDLPIP---VEDFTARL--- 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 403 nfgtdgfpaaatsanlclatgVRGGVDWMRKLafryrrvkeiyNTYKNNVGGLLGPAKREAWLQLRAEIEALTDSWLTL- 481
Cdd:pfam00702  55 ---------------------LLGKRDWLEEL-----------DILRGLVETLEAEGLTVVLVELLGVIALADELKLYPg 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353667 482 ALKALSLIHSRTNCVnILVTTTQLIPALAKVLLYGLGIVFPIENIYSATKIGK--ESCFERIIQRFGRKV-VYVVIGDGV 558
Cdd:pfam00702 103 AAEALKALKERGIKV-AILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKpkPEIYLAALERLGVKPeEVLMVGDGV 181


                  ....*....
gi 1720353667 559 EEEQGAKKA 567
Cdd:pfam00702 182 NDIPAAKAA 190
 
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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