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Conserved domains on  [gi|254911007|ref|NP_742108|]
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eyes absent homolog 2 isoform c [Homo sapiens]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
267-459 3.29e-111

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member cd02601:

Pssm-ID: 473868  Cd Length: 271  Bit Score: 329.07  E-value: 3.29e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911007 267 IERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQDLS 346
Cdd:cd02601    1 PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDVSSDDNGQDLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911007 347 TYNFSADGFHSSAPGANLCLGSGVHgGVDWMRKLAFRYRRVKEMYNTYKNNVG--------------------------- 399
Cdd:cd02601   81 TYNFLTDGFHMRAVAPNLCLPTGVR-GVDWMRKLAFRYRRVKENYNTYKNNVGfllgeakreawlqlrteiealtdqwlt 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911007 400 ----------------------------------------------------GKESCFERIMQRFGRKAVYVVIGDGVEE 427
Cdd:cd02601  160 lalkaldlissrencvnvlvtttqlipalakvllyglgsvfpieniysatkiGKESCFERIQQRFGRKCVYVCIGDGVEE 239
                        250       260       270
                 ....*....|....*....|....*....|..
gi 254911007 428 EQGAKKHNMPFWRISCHADLEALRHALELEYL 459
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) ...
267-459 3.29e-111

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: 329.07  E-value: 3.29e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911007 267 IERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQDLS 346
Cdd:cd02601    1 PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDVSSDDNGQDLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911007 347 TYNFSADGFHSSAPGANLCLGSGVHgGVDWMRKLAFRYRRVKEMYNTYKNNVG--------------------------- 399
Cdd:cd02601   81 TYNFLTDGFHMRAVAPNLCLPTGVR-GVDWMRKLAFRYRRVKENYNTYKNNVGfllgeakreawlqlrteiealtdqwlt 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911007 400 ----------------------------------------------------GKESCFERIMQRFGRKAVYVVIGDGVEE 427
Cdd:cd02601  160 lalkaldlissrencvnvlvtttqlipalakvllyglgsvfpieniysatkiGKESCFERIQQRFGRKCVYVCIGDGVEE 239
                        250       260       270
                 ....*....|....*....|....*....|..
gi 254911007 428 EQGAKKHNMPFWRISCHADLEALRHALELEYL 459
Cdd:cd02601  240 EQAAKKHNVPFWRISTHSDLLALHHALELEYL 271
EYA-cons_domain TIGR01658
eyes absent protein conserved domain; This domain is common to all eyes absent (EYA) homologs. ...
267-459 3.04e-71

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: 226.66  E-value: 3.04e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911007  267 IERVFVWDLDETIIIFHSLLTGTFASRYG--KDTTTSVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQD 344
Cdd:TIGR01658   1 PENVYVWDMDETLILLHSLLNGSYAESFNgsKDHKRGVEIGRRWEEMILEICDTHFFYEEIEECNEPFLDDVRSYDDGKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911007  345 LSTYNFSADGFHSSAPgaNLCLgsgvhggvdwmRKLAFRYRRVKEMYNTY------------------------------ 394
Cdd:TIGR01658  81 LSRYEFKTDGFSTPTD--DLNK-----------RKLAYRHRAVAEIYEKGlgplldpesmealdelysetdvytdrwlss 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911007  395 --------------------------KNNVG-----------------------------------GKESCFERIMQRFG 413
Cdd:TIGR01658 148 alkfleqcscveessdgtslieissrDNCINvlvtsgqlipslakcllfrldtifrienvyssikvGKLQCFKWIKERFG 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 254911007  414 R-KAVYVVIGDGVEEEQGAKKHNMPFWRISCHADLEALRHALELEYL 459
Cdd:TIGR01658 228 HpKVRFCAIGDGWEECTAAQAMNWPFVKIDLHPDSSHRFPGLTLKTL 274
 
Name Accession Description Interval E-value
HAD_Eya cd02601
protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) ...
267-459 3.29e-111

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: 329.07  E-value: 3.29e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911007 267 IERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQDLS 346
Cdd:cd02601    1 PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDVSSDDNGQDLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911007 347 TYNFSADGFHSSAPGANLCLGSGVHgGVDWMRKLAFRYRRVKEMYNTYKNNVG--------------------------- 399
Cdd:cd02601   81 TYNFLTDGFHMRAVAPNLCLPTGVR-GVDWMRKLAFRYRRVKENYNTYKNNVGfllgeakreawlqlrteiealtdqwlt 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911007 400 ----------------------------------------------------GKESCFERIMQRFGRKAVYVVIGDGVEE 427
Cdd:cd02601  160 lalkaldlissrencvnvlvtttqlipalakvllyglgsvfpieniysatkiGKESCFERIQQRFGRKCVYVCIGDGVEE 239
                        250       260       270
                 ....*....|....*....|....*....|..
gi 254911007 428 EQGAKKHNMPFWRISCHADLEALRHALELEYL 459
Cdd:cd02601  240 EQAAKKHNVPFWRISTHSDLLALHHALELEYL 271
EYA-cons_domain TIGR01658
eyes absent protein conserved domain; This domain is common to all eyes absent (EYA) homologs. ...
267-459 3.04e-71

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: 226.66  E-value: 3.04e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911007  267 IERVFVWDLDETIIIFHSLLTGTFASRYG--KDTTTSVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQD 344
Cdd:TIGR01658   1 PENVYVWDMDETLILLHSLLNGSYAESFNgsKDHKRGVEIGRRWEEMILEICDTHFFYEEIEECNEPFLDDVRSYDDGKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911007  345 LSTYNFSADGFHSSAPgaNLCLgsgvhggvdwmRKLAFRYRRVKEMYNTY------------------------------ 394
Cdd:TIGR01658  81 LSRYEFKTDGFSTPTD--DLNK-----------RKLAYRHRAVAEIYEKGlgplldpesmealdelysetdvytdrwlss 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911007  395 --------------------------KNNVG-----------------------------------GKESCFERIMQRFG 413
Cdd:TIGR01658 148 alkfleqcscveessdgtslieissrDNCINvlvtsgqlipslakcllfrldtifrienvyssikvGKLQCFKWIKERFG 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 254911007  414 R-KAVYVVIGDGVEEEQGAKKHNMPFWRISCHADLEALRHALELEYL 459
Cdd:TIGR01658 228 HpKVRFCAIGDGWEECTAAQAMNWPFVKIDLHPDSSHRFPGLTLKTL 274
 
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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