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Conserved domains on  [gi|505625|gb|AAA85136|]
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PAC-1 [Mus musculus domesticus]

Protein Classification

DSP_MapKP domain-containing protein( domain architecture ID 10106634)

DSP_MapKP domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 13-147 6.02e-45

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


:

Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 144.73  E-value: 6.02e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505625    13 LECAALGVLLREPreAERTLLLDCRPFLAFCRSHVRAARPVPWNALLRRRAPGTpAAALACLLPDRALRARLGRGELARA 92
Cdd:cd01446   2 IDCAWLAALLREG--GERLLLLDCRPFLEYSSSHIRGAVNVCCPTILRRRLQGG-KILLQQLLSCPEDRDRLRRGESLAV 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 505625    93 VVLDESSASVTELPPDGPAHLLLAALQHEMRGGPtTVCFLRGGFKSFQTYCPDLC 147
Cdd:cd01446  79 VVYDESSSDRERLREDSTAESVLGKLLRKLQEGC-SVYLLKGGFEQFSSEFPELC 132
 
Name Accession Description Interval E-value
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 13-147 6.02e-45

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 144.73  E-value: 6.02e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505625    13 LECAALGVLLREPreAERTLLLDCRPFLAFCRSHVRAARPVPWNALLRRRAPGTpAAALACLLPDRALRARLGRGELARA 92
Cdd:cd01446   2 IDCAWLAALLREG--GERLLLLDCRPFLEYSSSHIRGAVNVCCPTILRRRLQGG-KILLQQLLSCPEDRDRLRRGESLAV 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 505625    93 VVLDESSASVTELPPDGPAHLLLAALQHEMRGGPtTVCFLRGGFKSFQTYCPDLC 147
Cdd:cd01446  79 VVYDESSSDRERLREDSTAESVLGKLLRKLQEGC-SVYLLKGGFEQFSSEFPELC 132
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 27-145 1.51e-12

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 60.55  E-value: 1.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505625       27 EAERTLLLDCRPFLAFCRSHVRAARPVPWNALLRRRAPGTPaaalaclLPDRALRARLGRGELARAVVLDESSASVTELp 106
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDI-------LEFEELLKRLGLDKDKPVVVYCRSGNRSAKA- 72

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 505625      107 pdgpAHLLLAAlqhemrgGPTTVCFLRGGFKSFQTYCPD 145
Cdd:smart00450  73 ----AWLLREL-------GFKNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 27-140 2.81e-07

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 46.32  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505625      27 EAERTLLLDCRPFLAFCRSHVRAARPVPWNALLRRRAPGTP-AAALACLLPDRalrarlgrgelaRAVVLDESsasvtel 105
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLElLEKLLELLKDK------------PIVVYCNS------- 62

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 505625     106 ppdGPAHLLLAALQHEMrgGPTTVCFLRGGFKSFQ 140
Cdd:pfam00581  63 ---GNRAAAAAALLKAL--GYKNVYVLDGGFEAWK 92
 
Name Accession Description Interval E-value
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 13-147 6.02e-45

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 144.73  E-value: 6.02e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505625    13 LECAALGVLLREPreAERTLLLDCRPFLAFCRSHVRAARPVPWNALLRRRAPGTpAAALACLLPDRALRARLGRGELARA 92
Cdd:cd01446   2 IDCAWLAALLREG--GERLLLLDCRPFLEYSSSHIRGAVNVCCPTILRRRLQGG-KILLQQLLSCPEDRDRLRRGESLAV 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 505625    93 VVLDESSASVTELPPDGPAHLLLAALQHEMRGGPtTVCFLRGGFKSFQTYCPDLC 147
Cdd:cd01446  79 VVYDESSSDRERLREDSTAESVLGKLLRKLQEGC-SVYLLKGGFEQFSSEFPELC 132
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 27-145 1.51e-12

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 60.55  E-value: 1.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505625       27 EAERTLLLDCRPFLAFCRSHVRAARPVPWNALLRRRAPGTPaaalaclLPDRALRARLGRGELARAVVLDESSASVTELp 106
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDI-------LEFEELLKRLGLDKDKPVVVYCRSGNRSAKA- 72

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 505625      107 pdgpAHLLLAAlqhemrgGPTTVCFLRGGFKSFQTYCPD 145
Cdd:smart00450  73 ----AWLLREL-------GFKNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 27-140 2.81e-07

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 46.32  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505625      27 EAERTLLLDCRPFLAFCRSHVRAARPVPWNALLRRRAPGTP-AAALACLLPDRalrarlgrgelaRAVVLDESsasvtel 105
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLElLEKLLELLKDK------------PIVVYCNS------- 62

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 505625     106 ppdGPAHLLLAALQHEMrgGPTTVCFLRGGFKSFQ 140
Cdd:pfam00581  63 ---GNRAAAAAALLKAL--GYKNVYVLDGGFEAWK 92
 
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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