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Conserved domains on  [gi|966915800|ref|XP_014987903|]
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eyes absent homolog 3 isoform X5 [Macaca mulatta]

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) ...
258-519 6.95e-127

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: 371.82  E-value: 6.95e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915800 258 LERVFLWDLDETIIIFHSLLTGSYAQKYGKDPTVVIGSGLTMEEMIFEVADTHLFFNDLEECDQVHVEDVASDDNGQDLS 337
Cdd:cd02601    1 PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDVSSDDNGQDLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915800 338 NYSFSTDGFSGSGGSGSHGSSVGVqGGVDWMRKLAFRYRKVREIYDKHKSNVGGLLSPQRKEALQRLRAEIEVLTDSWLG 417
Cdd:cd02601   81 TYNFLTDGFHMRAVAPNLCLPTGV-RGVDWMRKLAFRYRRVKENYNTYKNNVGFLLGEAKREAWLQLRTEIEALTDQWLT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915800 418 TALKSLLLIQSRKNCVNVLITTTQLVPALAKVLLYGLGEIFPIENIYSATKIGKESCFERIVSRFGKKVTYVVIGDGRDE 497
Cdd:cd02601  160 LALKALDLISSRENCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKIGKESCFERIQQRFGRKCVYVCIGDGVEE 239
                        250       260
                 ....*....|....*....|....*....
gi 966915800 498 EIAAKQ-QLYFL------DLEALGCQLEP 519
Cdd:cd02601  240 EQAAKKhNVPFWristhsDLLALHHALEL 268
 
Name Accession Description Interval E-value
HAD_Eya cd02601
protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) ...
258-519 6.95e-127

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: 371.82  E-value: 6.95e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915800 258 LERVFLWDLDETIIIFHSLLTGSYAQKYGKDPTVVIGSGLTMEEMIFEVADTHLFFNDLEECDQVHVEDVASDDNGQDLS 337
Cdd:cd02601    1 PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDVSSDDNGQDLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915800 338 NYSFSTDGFSGSGGSGSHGSSVGVqGGVDWMRKLAFRYRKVREIYDKHKSNVGGLLSPQRKEALQRLRAEIEVLTDSWLG 417
Cdd:cd02601   81 TYNFLTDGFHMRAVAPNLCLPTGV-RGVDWMRKLAFRYRRVKENYNTYKNNVGFLLGEAKREAWLQLRTEIEALTDQWLT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915800 418 TALKSLLLIQSRKNCVNVLITTTQLVPALAKVLLYGLGEIFPIENIYSATKIGKESCFERIVSRFGKKVTYVVIGDGRDE 497
Cdd:cd02601  160 LALKALDLISSRENCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKIGKESCFERIQQRFGRKCVYVCIGDGVEE 239
                        250       260
                 ....*....|....*....|....*....
gi 966915800 498 EIAAKQ-QLYFL------DLEALGCQLEP 519
Cdd:cd02601  240 EQAAKKhNVPFWristhsDLLALHHALEL 268
EYA-cons_domain TIGR01658
eyes absent protein conserved domain; This domain is common to all eyes absent (EYA) homologs. ...
258-503 6.55e-124

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: 6.55e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915800  258 LERVFLWDLDETIIIFHSLLTGSYAQKYG--KDPTVVIGSGLTMEEMIFEVADTHLFFNDLEECDQVHVEDVASDDNGQD 335
Cdd:TIGR01658   1 PENVYVWDMDETLILLHSLLNGSYAESFNgsKDHKRGVEIGRRWEEMILEICDTHFFYEEIEECNEPFLDDVRSYDDGKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915800  336 LSNYSFSTDGFSGSGGSGSHgssvgvqggvdwmRKLAFRYRKVREIYDKHksnVGGLLSPQRKEALQRLRAEIEVLTDSW 415
Cdd:TIGR01658  81 LSRYEFKTDGFSTPTDDLNK-------------RKLAYRHRAVAEIYEKG---LGPLLDPESMEALDELYSETDVYTDRW 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915800  416 LGTALK---------------SLLLIQSRKNCVNVLITTTQLVPALAKVLLYGLGEIFPIENIYSATKIGKESCFERIVS 480
Cdd:TIGR01658 145 LSSALKfleqcscveessdgtSLIEISSRDNCINVLVTSGQLIPSLAKCLLFRLDTIFRIENVYSSIKVGKLQCFKWIKE 224
                         250       260
                  ....*....|....*....|....
gi 966915800  481 RFGK-KVTYVVIGDGRDEEIAAKQ 503
Cdd:TIGR01658 225 RFGHpKVRFCAIGDGWEECTAAQA 248
 
Name Accession Description Interval E-value
HAD_Eya cd02601
protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) ...
258-519 6.95e-127

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: 371.82  E-value: 6.95e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915800 258 LERVFLWDLDETIIIFHSLLTGSYAQKYGKDPTVVIGSGLTMEEMIFEVADTHLFFNDLEECDQVHVEDVASDDNGQDLS 337
Cdd:cd02601    1 PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDVSSDDNGQDLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915800 338 NYSFSTDGFSGSGGSGSHGSSVGVqGGVDWMRKLAFRYRKVREIYDKHKSNVGGLLSPQRKEALQRLRAEIEVLTDSWLG 417
Cdd:cd02601   81 TYNFLTDGFHMRAVAPNLCLPTGV-RGVDWMRKLAFRYRRVKENYNTYKNNVGFLLGEAKREAWLQLRTEIEALTDQWLT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915800 418 TALKSLLLIQSRKNCVNVLITTTQLVPALAKVLLYGLGEIFPIENIYSATKIGKESCFERIVSRFGKKVTYVVIGDGRDE 497
Cdd:cd02601  160 LALKALDLISSRENCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKIGKESCFERIQQRFGRKCVYVCIGDGVEE 239
                        250       260
                 ....*....|....*....|....*....
gi 966915800 498 EIAAKQ-QLYFL------DLEALGCQLEP 519
Cdd:cd02601  240 EQAAKKhNVPFWristhsDLLALHHALEL 268
EYA-cons_domain TIGR01658
eyes absent protein conserved domain; This domain is common to all eyes absent (EYA) homologs. ...
258-503 6.55e-124

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: 6.55e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915800  258 LERVFLWDLDETIIIFHSLLTGSYAQKYG--KDPTVVIGSGLTMEEMIFEVADTHLFFNDLEECDQVHVEDVASDDNGQD 335
Cdd:TIGR01658   1 PENVYVWDMDETLILLHSLLNGSYAESFNgsKDHKRGVEIGRRWEEMILEICDTHFFYEEIEECNEPFLDDVRSYDDGKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915800  336 LSNYSFSTDGFSGSGGSGSHgssvgvqggvdwmRKLAFRYRKVREIYDKHksnVGGLLSPQRKEALQRLRAEIEVLTDSW 415
Cdd:TIGR01658  81 LSRYEFKTDGFSTPTDDLNK-------------RKLAYRHRAVAEIYEKG---LGPLLDPESMEALDELYSETDVYTDRW 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915800  416 LGTALK---------------SLLLIQSRKNCVNVLITTTQLVPALAKVLLYGLGEIFPIENIYSATKIGKESCFERIVS 480
Cdd:TIGR01658 145 LSSALKfleqcscveessdgtSLIEISSRDNCINVLVTSGQLIPSLAKCLLFRLDTIFRIENVYSSIKVGKLQCFKWIKE 224
                         250       260
                  ....*....|....*....|....
gi 966915800  481 RFGK-KVTYVVIGDGRDEEIAAKQ 503
Cdd:TIGR01658 225 RFGHpKVRFCAIGDGWEECTAAQA 248
 
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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