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Conserved domains on  [gi|1720360381|ref|XP_030100738|]
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eyes absent homolog 4 isoform X7 [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) ...
306-577 8.04e-170

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: 482.38  E-value: 8.04e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381 306 LERVFVWDLDETIIVFHSLLTGSYAQKYGKDPPMAVTLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLS 385
Cdd:cd02601     1 PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDVSSDDNGQDLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381 386 TYSFATDGFHAAASSANLCLPTGVRGgVDWMRKLAFRYRRVKELYNTYKNNVGGLLGPAKRDAWLQLRAEIEGLTDSWLT 465
Cdd:cd02601    81 TYNFLTDGFHMRAVAPNLCLPTGVRG-VDWMRKLAFRYRRVKENYNTYKNNVGFLLGEAKREAWLQLRTEIEALTDQWLT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381 466 NALKSLSIISTRSNCVNVLVTTTQLIPALAKVLLYSLGGAFPIENIYSATKIGKESCFERIVSRFGTNITYVVIGDGRDE 545
Cdd:cd02601   160 LALKALDLISSRENCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKIGKESCFERIQQRFGRKCVYVCIGDGVEE 239
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720360381 546 EHAANQHNMPFWRISSHSDLLALHQALELEYL 577
Cdd:cd02601   240 EQAAKKHNVPFWRISTHSDLLALHHALELEYL 271
PTZ00395 super family cl33180
Sec24-related protein; Provisional
100-279 7.32e-04

Sec24-related protein; Provisional


The actual alignment was detected with superfamily member PTZ00395:

Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 42.75  E-value: 7.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381  100 AYAGQTQYSGMQQPAVYT--AYSQTGQ--------PYSLPAYdlgvmlpaiktesglsqTQSPLQSGCLSYSPgFSTPQP 169
Cdd:PTZ00395   378 AWAGGPHSNASYNCAAYSnaAQSNAAQsnagfsnaGYSNPGN-----------------SNPGYNNAPNSNTP-YNNPPN 439
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381  170 GQTPYS---YQMPGSSFAP-SSTIYANNSVSNSTnfSSSQQDYPS-YTAFGQNQYAQYYSASTYGAYMTSNNTADGTSSS 244
Cdd:PTZ00395   440 SNTPYSnppNSNPPYSNLPySNTPYSNAPLSNAP--PSSAKDHHSaYHAAYQHRAANQPAANLPTANQPAANNFHGAAGN 517
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1720360381  245 TSTYQLQESLQGLTSQPGEFDTVQSPSTPIKDLDD 279
Cdd:PTZ00395   518 SVGNPFASRPFGSAPYGGNAATTADPNGIAKREDH 552
 
Name Accession Description Interval E-value
HAD_Eya cd02601
protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) ...
306-577 8.04e-170

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: 482.38  E-value: 8.04e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381 306 LERVFVWDLDETIIVFHSLLTGSYAQKYGKDPPMAVTLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLS 385
Cdd:cd02601     1 PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDVSSDDNGQDLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381 386 TYSFATDGFHAAASSANLCLPTGVRGgVDWMRKLAFRYRRVKELYNTYKNNVGGLLGPAKRDAWLQLRAEIEGLTDSWLT 465
Cdd:cd02601    81 TYNFLTDGFHMRAVAPNLCLPTGVRG-VDWMRKLAFRYRRVKENYNTYKNNVGFLLGEAKREAWLQLRTEIEALTDQWLT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381 466 NALKSLSIISTRSNCVNVLVTTTQLIPALAKVLLYSLGGAFPIENIYSATKIGKESCFERIVSRFGTNITYVVIGDGRDE 545
Cdd:cd02601   160 LALKALDLISSRENCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKIGKESCFERIQQRFGRKCVYVCIGDGVEE 239
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720360381 546 EHAANQHNMPFWRISSHSDLLALHQALELEYL 577
Cdd:cd02601   240 EQAAKKHNVPFWRISTHSDLLALHHALELEYL 271
EYA-cons_domain TIGR01658
eyes absent protein conserved domain; This domain is common to all eyes absent (EYA) homologs. ...
306-577 1.92e-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: 394.99  E-value: 1.92e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381 306 LERVFVWDLDETIIVFHSLLTGSYAQKYG--KDPPMAVTLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQD 383
Cdd:TIGR01658   1 PENVYVWDMDETLILLHSLLNGSYAESFNgsKDHKRGVEIGRRWEEMILEICDTHFFYEEIEECNEPFLDDVRSYDDGKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381 384 LSTYSFATDGFHAAasSANLCLptgvrggvdwmRKLAFRYRRVKELYNTYknnVGGLLGPAKRDAWLQLRAEIEGLTDSW 463
Cdd:TIGR01658  81 LSRYEFKTDGFSTP--TDDLNK-----------RKLAYRHRAVAEIYEKG---LGPLLDPESMEALDELYSETDVYTDRW 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381 464 LTNALK---------------SLSIISTRSNCVNVLVTTTQLIPALAKVLLYSLGGAFPIENIYSATKIGKESCFERIVS 528
Cdd:TIGR01658 145 LSSALKfleqcscveessdgtSLIEISSRDNCINVLVTSGQLIPSLAKCLLFRLDTIFRIENVYSSIKVGKLQCFKWIKE 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720360381 529 RFG-TNITYVVIGDGRDEEHAANQHNMPFWRISSHSDLLALHQALELEYL 577
Cdd:TIGR01658 225 RFGhPKVRFCAIGDGWEECTAAQAMNWPFVKIDLHPDSSHRFPGLTLKTL 274
PTZ00395 PTZ00395
Sec24-related protein; Provisional
100-279 7.32e-04

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 42.75  E-value: 7.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381  100 AYAGQTQYSGMQQPAVYT--AYSQTGQ--------PYSLPAYdlgvmlpaiktesglsqTQSPLQSGCLSYSPgFSTPQP 169
Cdd:PTZ00395   378 AWAGGPHSNASYNCAAYSnaAQSNAAQsnagfsnaGYSNPGN-----------------SNPGYNNAPNSNTP-YNNPPN 439
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381  170 GQTPYS---YQMPGSSFAP-SSTIYANNSVSNSTnfSSSQQDYPS-YTAFGQNQYAQYYSASTYGAYMTSNNTADGTSSS 244
Cdd:PTZ00395   440 SNTPYSnppNSNPPYSNLPySNTPYSNAPLSNAP--PSSAKDHHSaYHAAYQHRAANQPAANLPTANQPAANNFHGAAGN 517
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1720360381  245 TSTYQLQESLQGLTSQPGEFDTVQSPSTPIKDLDD 279
Cdd:PTZ00395   518 SVGNPFASRPFGSAPYGGNAATTADPNGIAKREDH 552
NupH_GANP pfam16768
Nucleoporin homology of Germinal-centre associated nuclear protein; NupH_GANP is the ...
48-203 2.23e-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: 40.28  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381  48 SGLSSTSVTTNGTGVITSSGysPRSAQQYSPQLYPSKPYPHILSTPAAQTMSAYAGQTQYSGMQQPAvytaysqtgqpYS 127
Cdd:pfam16768  79 SGVGLFSGLEHTPSFVATSG--PSSSSVPSNPGFSFKSPTNLGAFPSTSTFGPESGEVASSGFGKTE-----------FS 145
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360381 128 LPAYDLGVMLPAIKTESGLSQTQSPLQSGCLSYSPGFSTPQPGQTPYSYQMPGSSFAPSSTIYANNSVSNSTNFSS 203
Cdd:pfam16768 146 FKPPENAVFRPIFGAESEPEKTQSQITSGFFTFSHPVSSGPGGLAPFSFSQVTSSSATSSNFTFSKPVSSNNSSSA 221
 
Name Accession Description Interval E-value
HAD_Eya cd02601
protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) ...
306-577 8.04e-170

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: 482.38  E-value: 8.04e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381 306 LERVFVWDLDETIIVFHSLLTGSYAQKYGKDPPMAVTLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLS 385
Cdd:cd02601     1 PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDVSSDDNGQDLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381 386 TYSFATDGFHAAASSANLCLPTGVRGgVDWMRKLAFRYRRVKELYNTYKNNVGGLLGPAKRDAWLQLRAEIEGLTDSWLT 465
Cdd:cd02601    81 TYNFLTDGFHMRAVAPNLCLPTGVRG-VDWMRKLAFRYRRVKENYNTYKNNVGFLLGEAKREAWLQLRTEIEALTDQWLT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381 466 NALKSLSIISTRSNCVNVLVTTTQLIPALAKVLLYSLGGAFPIENIYSATKIGKESCFERIVSRFGTNITYVVIGDGRDE 545
Cdd:cd02601   160 LALKALDLISSRENCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKIGKESCFERIQQRFGRKCVYVCIGDGVEE 239
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720360381 546 EHAANQHNMPFWRISSHSDLLALHQALELEYL 577
Cdd:cd02601   240 EQAAKKHNVPFWRISTHSDLLALHHALELEYL 271
EYA-cons_domain TIGR01658
eyes absent protein conserved domain; This domain is common to all eyes absent (EYA) homologs. ...
306-577 1.92e-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: 394.99  E-value: 1.92e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381 306 LERVFVWDLDETIIVFHSLLTGSYAQKYG--KDPPMAVTLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQD 383
Cdd:TIGR01658   1 PENVYVWDMDETLILLHSLLNGSYAESFNgsKDHKRGVEIGRRWEEMILEICDTHFFYEEIEECNEPFLDDVRSYDDGKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381 384 LSTYSFATDGFHAAasSANLCLptgvrggvdwmRKLAFRYRRVKELYNTYknnVGGLLGPAKRDAWLQLRAEIEGLTDSW 463
Cdd:TIGR01658  81 LSRYEFKTDGFSTP--TDDLNK-----------RKLAYRHRAVAEIYEKG---LGPLLDPESMEALDELYSETDVYTDRW 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381 464 LTNALK---------------SLSIISTRSNCVNVLVTTTQLIPALAKVLLYSLGGAFPIENIYSATKIGKESCFERIVS 528
Cdd:TIGR01658 145 LSSALKfleqcscveessdgtSLIEISSRDNCINVLVTSGQLIPSLAKCLLFRLDTIFRIENVYSSIKVGKLQCFKWIKE 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720360381 529 RFG-TNITYVVIGDGRDEEHAANQHNMPFWRISSHSDLLALHQALELEYL 577
Cdd:TIGR01658 225 RFGhPKVRFCAIGDGWEECTAAQAMNWPFVKIDLHPDSSHRFPGLTLKTL 274
PTZ00395 PTZ00395
Sec24-related protein; Provisional
100-279 7.32e-04

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 42.75  E-value: 7.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381  100 AYAGQTQYSGMQQPAVYT--AYSQTGQ--------PYSLPAYdlgvmlpaiktesglsqTQSPLQSGCLSYSPgFSTPQP 169
Cdd:PTZ00395   378 AWAGGPHSNASYNCAAYSnaAQSNAAQsnagfsnaGYSNPGN-----------------SNPGYNNAPNSNTP-YNNPPN 439
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381  170 GQTPYS---YQMPGSSFAP-SSTIYANNSVSNSTnfSSSQQDYPS-YTAFGQNQYAQYYSASTYGAYMTSNNTADGTSSS 244
Cdd:PTZ00395   440 SNTPYSnppNSNPPYSNLPySNTPYSNAPLSNAP--PSSAKDHHSaYHAAYQHRAANQPAANLPTANQPAANNFHGAAGN 517
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1720360381  245 TSTYQLQESLQGLTSQPGEFDTVQSPSTPIKDLDD 279
Cdd:PTZ00395   518 SVGNPFASRPFGSAPYGGNAATTADPNGIAKREDH 552
NupH_GANP pfam16768
Nucleoporin homology of Germinal-centre associated nuclear protein; NupH_GANP is the ...
48-203 2.23e-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: 40.28  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360381  48 SGLSSTSVTTNGTGVITSSGysPRSAQQYSPQLYPSKPYPHILSTPAAQTMSAYAGQTQYSGMQQPAvytaysqtgqpYS 127
Cdd:pfam16768  79 SGVGLFSGLEHTPSFVATSG--PSSSSVPSNPGFSFKSPTNLGAFPSTSTFGPESGEVASSGFGKTE-----------FS 145
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360381 128 LPAYDLGVMLPAIKTESGLSQTQSPLQSGCLSYSPGFSTPQPGQTPYSYQMPGSSFAPSSTIYANNSVSNSTNFSS 203
Cdd:pfam16768 146 FKPPENAVFRPIFGAESEPEKTQSQITSGFFTFSHPVSSGPGGLAPFSFSQVTSSSATSSNFTFSKPVSSNNSSSA 221
 
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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