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Conserved domains on  [gi|122114545|ref|NP_033990|]
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M-phase inducer phosphatase 3 [Mus musculus]

Protein Classification

M-phase inducer phosphatase( domain architecture ID 10107435)

M-phase inducer phosphatase is a tyrosine protein phosphatase which may function as a dosage-dependent inducer in mitotic control

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 275-394 1.07e-61

Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. Cdc25A phosphatase functions to regulate S phase entry and Cdc25B is required for G2/M phase transition of the cell cycle. The Cdc25 domain binds oxyanions at the catalytic site and has the signature motif (H/YCxxxxxR).


:

Pssm-ID: 238788 [Multi-domain]  Cd Length: 121  Bit Score: 195.90  E-value: 1.07e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122114545 275 LKYISPDTVAALLSGKFQSVIERFYIIDCRYPYEYLGGHILGALNLHSQKELHEFFLRKPVVPlDIQKRVIIVFLCEFSS 354
Cdd:cd01530    1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVA-SKKKRRVLIFHCEFSS 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 122114545 355 ERGPRMCRSLREKDRALN--QYPALYYPELYILKGGYRDFFP 394
Cdd:cd01530   80 KRGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
 
Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 275-394 1.07e-61

Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. Cdc25A phosphatase functions to regulate S phase entry and Cdc25B is required for G2/M phase transition of the cell cycle. The Cdc25 domain binds oxyanions at the catalytic site and has the signature motif (H/YCxxxxxR).


Pssm-ID: 238788 [Multi-domain]  Cd Length: 121  Bit Score: 195.90  E-value: 1.07e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122114545 275 LKYISPDTVAALLSGKFQSVIERFYIIDCRYPYEYLGGHILGALNLHSQKELHEFFLRKPVVPlDIQKRVIIVFLCEFSS 354
Cdd:cd01530    1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVA-SKKKRRVLIFHCEFSS 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 122114545 355 ERGPRMCRSLREKDRALN--QYPALYYPELYILKGGYRDFFP 394
Cdd:cd01530   80 KRGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
258-413 7.34e-46

Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 164.44  E-value: 7.34e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122114545 258 DFSKVCVLP---TVPGKHPDLKYISPDTVAALLSGKFQSVIERFYIIDCRYPYEYLGGHILGALNLHSQKELHEFFLRKP 334
Cdd:COG5105  221 SFSNGEVFPlptLGPGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLFRHKP 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122114545 335 vvpldIQKRVIIVFLCEFSSERGPRMCRSLREKDRALNQ--YPALYYPELYILKGGYRDFFPEYMELCDPQSYCPMLHQD 412
Cdd:COG5105  301 -----LTHPRALIFHCEFSSHRAPRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTMNNAE 375


                 .
gi 122114545 413 H 413
Cdd:COG5105  376 L 376
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 296-396 1.46e-18

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: 80.58  E-value: 1.46e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122114545   296 ERFYIIDCRYPYEYLGGHILGALNLHSQKELHEFF------LRKPVVPLDIQKRVIIVFLCeFSSERGPRMCRSLREKDr 369
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGeldileFEELLKRLGLDKDKPVVVYC-RSGNRSAKAAWLLRELG- 80

                           90       100
                   ....*....|....*....|....*..
gi 122114545   370 alnqypalyYPELYILKGGYRDFFPEY 396
Cdd:smart00450  81 ---------FKNVYLLDGGYKEWSAAG 98
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 300-392 2.27e-09

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: 54.41  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122114545  300 IIDCRYPYEYLGGHILGALNLHSQKELHEF--FLRKPVVPLDIQKRVIIVFLCEfSSERGPRMCRSLREKDralnqypal 377
Cdd:pfam00581   8 LIDVRPPEEYAKGHIPGAVNVPLSSLSLPPlpLLELLEKLLELLKDKPIVVYCN-SGNRAAAAAALLKALG--------- 77

                          90
                  ....*....|....*
gi 122114545  378 yYPELYILKGGYRDF 392
Cdd:pfam00581  78 -YKNVYVLDGGFEAW 91
 
Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 275-394 1.07e-61

Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. Cdc25A phosphatase functions to regulate S phase entry and Cdc25B is required for G2/M phase transition of the cell cycle. The Cdc25 domain binds oxyanions at the catalytic site and has the signature motif (H/YCxxxxxR).


Pssm-ID: 238788 [Multi-domain]  Cd Length: 121  Bit Score: 195.90  E-value: 1.07e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122114545 275 LKYISPDTVAALLSGKFQSVIERFYIIDCRYPYEYLGGHILGALNLHSQKELHEFFLRKPVVPlDIQKRVIIVFLCEFSS 354
Cdd:cd01530    1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVA-SKKKRRVLIFHCEFSS 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 122114545 355 ERGPRMCRSLREKDRALN--QYPALYYPELYILKGGYRDFFP 394
Cdd:cd01530   80 KRGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
258-413 7.34e-46

Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 164.44  E-value: 7.34e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122114545 258 DFSKVCVLP---TVPGKHPDLKYISPDTVAALLSGKFQSVIERFYIIDCRYPYEYLGGHILGALNLHSQKELHEFFLRKP 334
Cdd:COG5105  221 SFSNGEVFPlptLGPGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLFRHKP 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122114545 335 vvpldIQKRVIIVFLCEFSSERGPRMCRSLREKDRALNQ--YPALYYPELYILKGGYRDFFPEYMELCDPQSYCPMLHQD 412
Cdd:COG5105  301 -----LTHPRALIFHCEFSSHRAPRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTMNNAE 375


                 .
gi 122114545 413 H 413
Cdd:COG5105  376 L 376
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 275-394 7.70e-27

Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included in this CD are eukaryotic arsenate resistance proteins such as Saccharomyces cerevisiae Acr2p and similar proteins. Cdc25 phosphatases activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. The Cdc25 and Acr2p RHOD domains have the signature motif (H/YCxxxxxR).


Pssm-ID: 238720 [Multi-domain]  Cd Length: 113  Bit Score: 104.03  E-value: 7.70e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122114545 275 LKYISPDTVAALLSGKFQSVIERFYIIDCRYPyEYLGGHILGALNLHSQkELHEFFLRKPVVpLDIQKRVIIVFLCEFSS 354
Cdd:cd01443    1 LKYISPEELVALLENSDSNAGKDFVVVDLRRD-DYEGGHIKGSINLPAQ-SCYQTLPQVYAL-FSLAGVKLAIFYCGSSQ 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 122114545 355 ERGPRMCRSLREKDRAlnqyPALYYPELYILKGGYRDFFP 394
Cdd:cd01443   78 GRGPRAARWFADYLRK----VGESLPKSYILTGGIKAWYH 113
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 296-396 1.46e-18

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: 80.58  E-value: 1.46e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122114545   296 ERFYIIDCRYPYEYLGGHILGALNLHSQKELHEFF------LRKPVVPLDIQKRVIIVFLCeFSSERGPRMCRSLREKDr 369
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGeldileFEELLKRLGLDKDKPVVVYC-RSGNRSAKAAWLLRELG- 80

                           90       100
                   ....*....|....*....|....*..
gi 122114545   370 alnqypalyYPELYILKGGYRDFFPEY 396
Cdd:smart00450  81 ---------FKNVYLLDGGYKEWSAAG 98
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 275-389 3.42e-12

Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain superfamily. Included in this CD is the Saccharomyces cerevisiae arsenate reductase protein, Acr2p, and other yeast and plant homologs.


Pssm-ID: 238789 [Multi-domain]  Cd Length: 113  Bit Score: 62.82  E-value: 3.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122114545 275 LKYISPDTvaalLSGKFQSVIERFYIIDCRyPYEYLGGHILGALNLHSQKELHEF-FLRKPVVPLDIQKrviIVFLCEFS 353
Cdd:cd01531    1 VSYISPAQ----LKGWIRNGRPPFQVVDVR-DEDYAGGHIKGSWHYPSTRFKAQLnQLVQLLSGSKKDT---VVFHCALS 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 122114545 354 SERGP----RMCRSLREKDRALNQypalyyPELYILKGGY 389
Cdd:cd01531   73 QVRGPsaarKFLRYLDEEDLETSK------FEVYVLHGGF 106
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 296-390 1.66e-10

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. 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 certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 57.31  E-value: 1.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122114545 296 ERFYIIDCRYPYEYLGGHILGALNLhsqkELHEFFLRKPVVPLDIQKRVIIVflCEfSSERGPRMCRSLREkdralnqyp 375
Cdd:cd00158    9 EDAVLLDVREPEEYAAGHIPGAINI----PLSELEERAALLELDKDKPIVVY--CR-SGNRSARAAKLLRK--------- 72

                         90
                 ....*....|....*
gi 122114545 376 aLYYPELYILKGGYR 390
Cdd:cd00158   73 -AGGTNVYNLEGGML 86
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 274-391 2.06e-09

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 54.59  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122114545 274 DLKYISPDTVAALLSGkfqsviERFYIIDCRYPYEYLGGHILGALNLhsqkELHEffLRKPVVPLDIQKRVIIVflCEfS 353
Cdd:COG0607    2 SVKEISPAELAELLES------EDAVLLDVREPEEFAAGHIPGAINI----PLGE--LAERLDELPKDKPIVVY--CA-S 66

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 122114545 354 SERGPRMCRSLRekdralnqypALYYPELYILKGGYRD 391
Cdd:COG0607   67 GGRSAQAAALLR----------RAGYTNVYNLAGGIEA 94
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 300-392 2.27e-09

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: 54.41  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122114545  300 IIDCRYPYEYLGGHILGALNLHSQKELHEF--FLRKPVVPLDIQKRVIIVFLCEfSSERGPRMCRSLREKDralnqypal 377
Cdd:pfam00581   8 LIDVRPPEEYAKGHIPGAVNVPLSSLSLPPlpLLELLEKLLELLKDKPIVVYCN-SGNRAAAAAALLKALG--------- 77

                          90
                  ....*....|....*
gi 122114545  378 yYPELYILKGGYRDF 392
Cdd:pfam00581  78 -YKNVYVLDGGFEAW 91
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 278-400 3.55e-04

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: 40.34  E-value: 3.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122114545 278 ISPDTVAALLsgkfQSVIERFYIIDCRYPYEYLGGHILGALNLH------------SQKELHEFFLRKPVVPLDIQKRVI 345
Cdd:cd01446    2 IDCAWLAALL----REGGERLLLLDCRPFLEYSSSHIRGAVNVCcptilrrrlqggKILLQQLLSCPEDRDRLRRGESLA 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 122114545 346 IVFLCEFSSERGPRM----CRSLREKDRALNQYPalyyPELYILKGGYRDFFPEYMELC 400
Cdd:cd01446   78 VVVYDESSSDRERLRedstAESVLGKLLRKLQEG----CSVYLLKGGFEQFSSEFPELC 132
 
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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