NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|392891422|ref|NP_496197|]
View 

M-phase inducer phosphatase [Caenorhabditis elegans]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 58-176 2.56e-56

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: 177.03  E-value: 2.56e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891422  58 FRSISATVFASLLRDR--SRCLQLIIFDCRYPFEYFGGHIKGAVNIYSLDELGKYLYDEYGVKSTLGGLIPIFYCEYSQV 135
Cdd:cd01530    1 LKRISPETLARLLQGKydNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLIFHCEFSSK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 392891422 136 RGPAMARRLRKIDTHRNNHRAAALDFPEIYLLDKGYVNFWS 176
Cdd:cd01530   81 RGPRMARHLRNLDRELNSNRYPLLYYPEIYILEGGYKNFFE 121
 
Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 58-176 2.56e-56

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: 177.03  E-value: 2.56e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891422  58 FRSISATVFASLLRDR--SRCLQLIIFDCRYPFEYFGGHIKGAVNIYSLDELGKYLYDEYGVKSTLGGLIPIFYCEYSQV 135
Cdd:cd01530    1 LKRISPETLARLLQGKydNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLIFHCEFSSK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 392891422 136 RGPAMARRLRKIDTHRNNHRAAALDFPEIYLLDKGYVNFWS 176
Cdd:cd01530   81 RGPRMARHLRNLDRELNSNRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
55-192 2.91e-25

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 103.58  E-value: 2.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891422  55 SSSFRSISATVFASLLRDRSR--CLQLIIFDCRYPFEYFGGHIKGAVNIYSLDELGkylyDEYGVKSTLGGLIPIFYCEY 132
Cdd:COG5105  238 SDSIQRISVETLKQVLEGMYNidFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLG----LLFRHKPLTHPRALIFHCEF 313

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891422 133 SQVRGPAMARRLRKIDTHRNNHRAAALDFPEIYLLDKGYVNFWSDvsLRDLCEPRYYISM 192
Cdd:COG5105  314 SSHRAPRLAQHLRNMDRMKNPDHYPLLTYPEVYILEGGYKKFYSN--YPDLCDPKGYVTM 371
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 78-178 1.23e-13

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: 65.56  E-value: 1.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891422    78 QLIIFDCRYPFEYFGGHIKGAVNIYSLDELGKYLY-------DEYGVKSTLGGLIPIFYCeYSQVRGPAMARRLRKidth 150
Cdd:smart00450   4 KVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGEldilefeELLKRLGLDKDKPVVVYC-RSGNRSAKAAWLLRE---- 78

                           90       100
                   ....*....|....*....|....*...
gi 392891422   151 rnnhraaaLDFPEIYLLDKGYVNFWSDV 178
Cdd:smart00450  79 --------LGFKNVYLLDGGYKEWSAAG 98
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 78-174 3.37e-10

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: 55.57  E-value: 3.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891422   78 QLIIFDCRYPFEYFGGHIKGAVNIySLDELGKYLYDEYGVKSTLGGLIP----IFYCEYSQvRGPAMARRLRKidthrnn 153
Cdd:pfam00581   5 KVVLIDVRPPEEYAKGHIPGAVNV-PLSSLSLPPLPLLELLEKLLELLKdkpiVVYCNSGN-RAAAAAALLKA------- 75

                          90       100
                  ....*....|....*....|.
gi 392891422  154 hraaaLDFPEIYLLDKGYVNF 174
Cdd:pfam00581  76 -----LGYKNVYVLDGGFEAW 91
 
Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 58-176 2.56e-56

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: 177.03  E-value: 2.56e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891422  58 FRSISATVFASLLRDR--SRCLQLIIFDCRYPFEYFGGHIKGAVNIYSLDELGKYLYDEYGVKSTLGGLIPIFYCEYSQV 135
Cdd:cd01530    1 LKRISPETLARLLQGKydNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLIFHCEFSSK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 392891422 136 RGPAMARRLRKIDTHRNNHRAAALDFPEIYLLDKGYVNFWS 176
Cdd:cd01530   81 RGPRMARHLRNLDRELNSNRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
55-192 2.91e-25

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 103.58  E-value: 2.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891422  55 SSSFRSISATVFASLLRDRSR--CLQLIIFDCRYPFEYFGGHIKGAVNIYSLDELGkylyDEYGVKSTLGGLIPIFYCEY 132
Cdd:COG5105  238 SDSIQRISVETLKQVLEGMYNidFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLG----LLFRHKPLTHPRALIFHCEF 313

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891422 133 SQVRGPAMARRLRKIDTHRNNHRAAALDFPEIYLLDKGYVNFWSDvsLRDLCEPRYYISM 192
Cdd:COG5105  314 SSHRAPRLAQHLRNMDRMKNPDHYPLLTYPEVYILEGGYKKFYSN--YPDLCDPKGYVTM 371
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 78-178 1.23e-13

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: 65.56  E-value: 1.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891422    78 QLIIFDCRYPFEYFGGHIKGAVNIYSLDELGKYLY-------DEYGVKSTLGGLIPIFYCeYSQVRGPAMARRLRKidth 150
Cdd:smart00450   4 KVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGEldilefeELLKRLGLDKDKPVVVYC-RSGNRSAKAAWLLRE---- 78

                           90       100
                   ....*....|....*....|....*...
gi 392891422   151 rnnhraaaLDFPEIYLLDKGYVNFWSDV 178
Cdd:smart00450  79 --------LGFKNVYLLDGGYKEWSAAG 98
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 80-171 3.48e-13

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: 64.35  E-value: 3.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891422  80 IIFDCRYPfEYFGGHIKGAVNIYSLDELgKYLYDEYGVKSTLGGLIPIFYCEYSQVRGPAMARRLRKIDthrnnhRAAAL 159
Cdd:cd01443   25 VVVDLRRD-DYEGGHIKGSINLPAQSCY-QTLPQVYALFSLAGVKLAIFYCGSSQGRGPRAARWFADYL------RKVGE 96

                         90
                 ....*....|..
gi 392891422 160 DFPEIYLLDKGY 171
Cdd:cd01443   97 SLPKSYILTGGI 108
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 78-174 3.37e-10

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: 55.57  E-value: 3.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891422   78 QLIIFDCRYPFEYFGGHIKGAVNIySLDELGKYLYDEYGVKSTLGGLIP----IFYCEYSQvRGPAMARRLRKidthrnn 153
Cdd:pfam00581   5 KVVLIDVRPPEEYAKGHIPGAVNV-PLSSLSLPPLPLLELLEKLLELLKdkpiVVYCNSGN-RAAAAAALLKA------- 75

                          90       100
                  ....*....|....*....|.
gi 392891422  154 hraaaLDFPEIYLLDKGYVNF 174
Cdd:pfam00581  76 -----LGYKNVYVLDGGFEAW 91
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 61-175 3.30e-09

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: 53.57  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891422  61 ISATVFASLLRDRSRCLQLIifDCRyPFEYFGGHIKGAVNI------YSLDELGKYLYDeyGVKSTLgglipIFYCEYSQ 134
Cdd:cd01531    4 ISPAQLKGWIRNGRPPFQVV--DVR-DEDYAGGHIKGSWHYpstrfkAQLNQLVQLLSG--SKKDTV-----VFHCALSQ 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 392891422 135 VRGPAMARR----LRKIDTHRNNhraaaldfPEIYLLDKGYvNFW 175
Cdd:cd01531   74 VRGPSAARKflryLDEEDLETSK--------FEVYVLHGGF-NAW 109
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 56-146 1.96e-07

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: 48.43  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891422  56 SSFRSISATVFASLLRDRsrclQLIIFDCRYPFEYFGGHIKGAVNIySLDELGKYLyDEYGVKSTLgglipIFYCeYSQV 135
Cdd:COG0607    1 ASVKEISPAELAELLESE----DAVLLDVREPEEFAAGHIPGAINI-PLGELAERL-DELPKDKPI-----VVYC-ASGG 68

                         90
                 ....*....|.
gi 392891422 136 RGPAMARRLRK 146
Cdd:COG0607   69 RSAQAAALLRR 79
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 66-171 3.78e-06

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: 44.21  E-value: 3.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891422  66 FASLLRDRsrclQLIIFDCRYPFEYFGGHIKGAVNIySLDELGKYLYDEYGVKSTlggliPI-FYCeYSQVRGPAMARRL 144
Cdd:cd00158    2 LKELLDDE----DAVLLDVREPEEYAAGHIPGAINI-PLSELEERAALLELDKDK-----PIvVYC-RSGNRSARAAKLL 70

                         90       100
                 ....*....|....*....|....*..
gi 392891422 145 RKidthrnnhraaaLDFPEIYLLDKGY 171
Cdd:cd00158   71 RK------------AGGTNVYNLEGGM 85
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 60-101 1.49e-03

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: 38.03  E-value: 1.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 392891422  60 SISATVFASLLR-DRSRCLqliIFDCRYPFEYFGGHIKGAVNI 101
Cdd:cd01446    1 TIDCAWLAALLReGGERLL---LLDCRPFLEYSSSHIRGAVNV 40
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH