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Conserved domains on  [gi|666335560|ref|NP_001287941|]
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eyes absent homolog 4 isoform e [Homo sapiens]

Protein Classification

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) ...
 314-585 1.60e-169

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: 481.99  E-value: 1.60e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560 314 LERVFVWDLDETIIVFHSLLTGSYAQKYGKDPPMAVTLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLS 393
Cdd:cd02601    1 PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDVSSDDNGQDLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560 394 TYSFATDGFHAAASSANLCLPTGVRGgVDWMRKLAFRYRRVKELYNTYKNNVGGLLGPAKRDAWLQLRAEIEGLTDSWLT 473
Cdd:cd02601   81 TYNFLTDGFHMRAVAPNLCLPTGVRG-VDWMRKLAFRYRRVKENYNTYKNNVGFLLGEAKREAWLQLRTEIEALTDQWLT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560 474 NALKSLSIISTRSNCINVLVTTTQLIPALAKVLLYSLGGAFPIENIYSATKIGKESCFERIVSRFGTNITYVVIGDGRDE 553
Cdd:cd02601  160 LALKALDLISSRENCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKIGKESCFERIQQRFGRKCVYVCIGDGVEE 239

                        250       260       270
                 ....*....|....*....|....*....|..
gi 666335560 554 EHAANQHNMPFWRISSHSDLLALHQALELEYL 585
Cdd:cd02601  240 EQAAKKHNVPFWRISTHSDLLALHHALELEYL 271
NupH_GANP super family cl25600
Nucleoporin homology of Germinal-centre associated nuclear protein; NupH_GANP is the ...
 18-210 3.33e-03

Nucleoporin homology of Germinal-centre associated nuclear protein; NupH_GANP is the nucleoporin-homology domain at the N-terminus of human GANP or germinal-centre associated nuclear proteins. GANP is part of the TREX-2 complex that links transcription with nuclear messenger RNA export, and it associates with the mRNP particle through the interaction of the NupH_GANP with NXF1, the export factor. This attachment mediates efficient delivery of mRNPs to nuclear pore complexes.


The actual alignment was detected with superfamily member pfam16768:

Pssm-ID: 435572 [Multi-domain]  Cd Length: 292  Bit Score: 39.89  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560   18 ESDVSQSQNSRSMEMQDLASPHtlvGGGDTPGSSKL---EKSNLSSTSVTTNGTGVITSSGysPRSAHQYSPQLYPSKPY 94
Cdd:pfam16768  41 QNNTLSGKNSGFSQVSSFPTTS---GVSHSSSGQTLgftQTSGVGLFSGLEHTPSFVATSG--PSSSSVPSNPGFSFKSP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560   95 PHILSTPAAQTMSAYAGQTQYSGMQQPAvytaysqtgqpYSLPTYDLGVMLPAIKTESGLSQTQSPLQSGCLSYSPGFST 174
Cdd:pfam16768 116 TNLGAFPSTSTFGPESGEVASSGFGKTE-----------FSFKPPENAVFRPIFGAESEPEKTQSQITSGFFTFSHPVSS 184

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 666335560  175 PQPGQTPYSYQMPGSSFAPSSTIYANNSVSNSTNFS 210
Cdd:pfam16768 185 GPGGLAPFSFSQVTSSSATSSNFTFSKPVSSNNSSS 220
 
Name Accession Description Interval E-value
HAD_Eya cd02601
protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) ...
 314-585 1.60e-169

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: 481.99  E-value: 1.60e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560 314 LERVFVWDLDETIIVFHSLLTGSYAQKYGKDPPMAVTLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLS 393
Cdd:cd02601    1 PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDVSSDDNGQDLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560 394 TYSFATDGFHAAASSANLCLPTGVRGgVDWMRKLAFRYRRVKELYNTYKNNVGGLLGPAKRDAWLQLRAEIEGLTDSWLT 473
Cdd:cd02601   81 TYNFLTDGFHMRAVAPNLCLPTGVRG-VDWMRKLAFRYRRVKENYNTYKNNVGFLLGEAKREAWLQLRTEIEALTDQWLT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560 474 NALKSLSIISTRSNCINVLVTTTQLIPALAKVLLYSLGGAFPIENIYSATKIGKESCFERIVSRFGTNITYVVIGDGRDE 553
Cdd:cd02601  160 LALKALDLISSRENCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKIGKESCFERIQQRFGRKCVYVCIGDGVEE 239

                        250       260       270
                 ....*....|....*....|....*....|..
gi 666335560 554 EHAANQHNMPFWRISSHSDLLALHQALELEYL 585
Cdd:cd02601  240 EQAAKKHNVPFWRISTHSDLLALHHALELEYL 271
EYA-cons_domain TIGR01658
eyes absent protein conserved domain; This domain is common to all eyes absent (EYA) homologs. ...
 314-585 2.13e-135

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: 395.37  E-value: 2.13e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560  314 LERVFVWDLDETIIVFHSLLTGSYAQKYG--KDPPMAVTLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQD 391
Cdd:TIGR01658   1 PENVYVWDMDETLILLHSLLNGSYAESFNgsKDHKRGVEIGRRWEEMILEICDTHFFYEEIEECNEPFLDDVRSYDDGKD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560  392 LSTYSFATDGFHAAasSANLCLptgvrggvdwmRKLAFRYRRVKELYNTYknnVGGLLGPAKRDAWLQLRAEIEGLTDSW 471
Cdd:TIGR01658  81 LSRYEFKTDGFSTP--TDDLNK-----------RKLAYRHRAVAEIYEKG---LGPLLDPESMEALDELYSETDVYTDRW 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560  472 LTNALK---------------SLSIISTRSNCINVLVTTTQLIPALAKVLLYSLGGAFPIENIYSATKIGKESCFERIVS 536
Cdd:TIGR01658 145 LSSALKfleqcscveessdgtSLIEISSRDNCINVLVTSGQLIPSLAKCLLFRLDTIFRIENVYSSIKVGKLQCFKWIKE 224

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 666335560  537 RFG-TNITYVVIGDGRDEEHAANQHNMPFWRISSHSDLLALHQALELEYL 585
Cdd:TIGR01658 225 RFGhPKVRFCAIGDGWEECTAAQAMNWPFVKIDLHPDSSHRFPGLTLKTL 274
NupH_GANP pfam16768
Nucleoporin homology of Germinal-centre associated nuclear protein; NupH_GANP is the ...
 18-210 3.33e-03

Nucleoporin homology of Germinal-centre associated nuclear protein; NupH_GANP is the nucleoporin-homology domain at the N-terminus of human GANP or germinal-centre associated nuclear proteins. GANP is part of the TREX-2 complex that links transcription with nuclear messenger RNA export, and it associates with the mRNP particle through the interaction of the NupH_GANP with NXF1, the export factor. This attachment mediates efficient delivery of mRNPs to nuclear pore complexes.


Pssm-ID: 435572 [Multi-domain]  Cd Length: 292  Bit Score: 39.89  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560   18 ESDVSQSQNSRSMEMQDLASPHtlvGGGDTPGSSKL---EKSNLSSTSVTTNGTGVITSSGysPRSAHQYSPQLYPSKPY 94
Cdd:pfam16768  41 QNNTLSGKNSGFSQVSSFPTTS---GVSHSSSGQTLgftQTSGVGLFSGLEHTPSFVATSG--PSSSSVPSNPGFSFKSP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560   95 PHILSTPAAQTMSAYAGQTQYSGMQQPAvytaysqtgqpYSLPTYDLGVMLPAIKTESGLSQTQSPLQSGCLSYSPGFST 174
Cdd:pfam16768 116 TNLGAFPSTSTFGPESGEVASSGFGKTE-----------FSFKPPENAVFRPIFGAESEPEKTQSQITSGFFTFSHPVSS 184

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 666335560  175 PQPGQTPYSYQMPGSSFAPSSTIYANNSVSNSTNFS 210
Cdd:pfam16768 185 GPGGLAPFSFSQVTSSSATSSNFTFSKPVSSNNSSS 220
 
Name Accession Description Interval E-value
HAD_Eya cd02601
protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) ...
 314-585 1.60e-169

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: 481.99  E-value: 1.60e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560 314 LERVFVWDLDETIIVFHSLLTGSYAQKYGKDPPMAVTLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLS 393
Cdd:cd02601    1 PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDVSSDDNGQDLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560 394 TYSFATDGFHAAASSANLCLPTGVRGgVDWMRKLAFRYRRVKELYNTYKNNVGGLLGPAKRDAWLQLRAEIEGLTDSWLT 473
Cdd:cd02601   81 TYNFLTDGFHMRAVAPNLCLPTGVRG-VDWMRKLAFRYRRVKENYNTYKNNVGFLLGEAKREAWLQLRTEIEALTDQWLT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560 474 NALKSLSIISTRSNCINVLVTTTQLIPALAKVLLYSLGGAFPIENIYSATKIGKESCFERIVSRFGTNITYVVIGDGRDE 553
Cdd:cd02601  160 LALKALDLISSRENCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKIGKESCFERIQQRFGRKCVYVCIGDGVEE 239

                        250       260       270
                 ....*....|....*....|....*....|..
gi 666335560 554 EHAANQHNMPFWRISSHSDLLALHQALELEYL 585
Cdd:cd02601  240 EQAAKKHNVPFWRISTHSDLLALHHALELEYL 271
EYA-cons_domain TIGR01658
eyes absent protein conserved domain; This domain is common to all eyes absent (EYA) homologs. ...
 314-585 2.13e-135

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: 395.37  E-value: 2.13e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560  314 LERVFVWDLDETIIVFHSLLTGSYAQKYG--KDPPMAVTLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQD 391
Cdd:TIGR01658   1 PENVYVWDMDETLILLHSLLNGSYAESFNgsKDHKRGVEIGRRWEEMILEICDTHFFYEEIEECNEPFLDDVRSYDDGKD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560  392 LSTYSFATDGFHAAasSANLCLptgvrggvdwmRKLAFRYRRVKELYNTYknnVGGLLGPAKRDAWLQLRAEIEGLTDSW 471
Cdd:TIGR01658  81 LSRYEFKTDGFSTP--TDDLNK-----------RKLAYRHRAVAEIYEKG---LGPLLDPESMEALDELYSETDVYTDRW 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560  472 LTNALK---------------SLSIISTRSNCINVLVTTTQLIPALAKVLLYSLGGAFPIENIYSATKIGKESCFERIVS 536
Cdd:TIGR01658 145 LSSALKfleqcscveessdgtSLIEISSRDNCINVLVTSGQLIPSLAKCLLFRLDTIFRIENVYSSIKVGKLQCFKWIKE 224

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 666335560  537 RFG-TNITYVVIGDGRDEEHAANQHNMPFWRISSHSDLLALHQALELEYL 585
Cdd:TIGR01658 225 RFGhPKVRFCAIGDGWEECTAAQAMNWPFVKIDLHPDSSHRFPGLTLKTL 274
NupH_GANP pfam16768
Nucleoporin homology of Germinal-centre associated nuclear protein; NupH_GANP is the ...
 18-210 3.33e-03

Nucleoporin homology of Germinal-centre associated nuclear protein; NupH_GANP is the nucleoporin-homology domain at the N-terminus of human GANP or germinal-centre associated nuclear proteins. GANP is part of the TREX-2 complex that links transcription with nuclear messenger RNA export, and it associates with the mRNP particle through the interaction of the NupH_GANP with NXF1, the export factor. This attachment mediates efficient delivery of mRNPs to nuclear pore complexes.


Pssm-ID: 435572 [Multi-domain]  Cd Length: 292  Bit Score: 39.89  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560   18 ESDVSQSQNSRSMEMQDLASPHtlvGGGDTPGSSKL---EKSNLSSTSVTTNGTGVITSSGysPRSAHQYSPQLYPSKPY 94
Cdd:pfam16768  41 QNNTLSGKNSGFSQVSSFPTTS---GVSHSSSGQTLgftQTSGVGLFSGLEHTPSFVATSG--PSSSSVPSNPGFSFKSP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335560   95 PHILSTPAAQTMSAYAGQTQYSGMQQPAvytaysqtgqpYSLPTYDLGVMLPAIKTESGLSQTQSPLQSGCLSYSPGFST 174
Cdd:pfam16768 116 TNLGAFPSTSTFGPESGEVASSGFGKTE-----------FSFKPPENAVFRPIFGAESEPEKTQSQITSGFFTFSHPVSS 184

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 666335560  175 PQPGQTPYSYQMPGSSFAPSSTIYANNSVSNSTNFS 210
Cdd:pfam16768 185 GPGGLAPFSFSQVTSSSATSSNFTFSKPVSSNNSSS 220
 
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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