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Conserved domains on  [gi|1958743172|ref|XP_038952801|]
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M-phase inducer phosphatase 3 isoform X5 [Rattus norvegicus]

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 ...
 89-208 1.11e-60

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: 187.43  E-value: 1.11e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743172  89 LKYISPDTVAALLSGKFQSVIERFYIIDCRYPYEYLGGHILGALNLYSQKELYEFFLKKPVVPeDTQKRVIIVFLCEFSS 168
Cdd:cd01530     1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVA-SKKKRRVLIFHCEFSS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958743172 169 ERGPRMCRSLREKDRALN--QYPALYYPELYILRGGYRDFFP 208
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 ...
 89-208 1.11e-60

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: 187.43  E-value: 1.11e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743172  89 LKYISPDTVAALLSGKFQSVIERFYIIDCRYPYEYLGGHILGALNLYSQKELYEFFLKKPVVPeDTQKRVIIVFLCEFSS 168
Cdd:cd01530     1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVA-SKKKRRVLIFHCEFSS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958743172 169 ERGPRMCRSLREKDRALN--QYPALYYPELYILRGGYRDFFP 208
Cdd:cd01530    80 KRGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
72-227 7.12e-49

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 166.75  E-value: 7.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743172  72 DFSKACVLP---TVPGKHQDLKYISPDTVAALLSGKFQSVIERFYIIDCRYPYEYLGGHILGALNLYSQKELYEFFLKKP 148
Cdd:COG5105   221 SFSNGEVFPlptLGPGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLFRHKP 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743172 149 VVpedtqKRVIIVFLCEFSSERGPRMCRSLREKDRALNQ--YPALYYPELYILRGGYRDFFPEYMELCEPQGYCPMLHQD 226
Cdd:COG5105   301 LT-----HPRALIFHCEFSSHRAPRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTMNNAE 375


                  .
gi 1958743172 227 H 227
Cdd:COG5105   376 L 376
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 110-210 3.76e-17

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: 74.42  E-value: 3.76e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743172  110 ERFYIIDCRYPYEYLGGHILGALNLYSQKELYEFFLKKPVVPEDTQKR------VIIVFLCeFSSERGPRMCRSLREKDr 183
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRlgldkdKPVVVYC-RSGNRSAKAAWLLRELG- 80

                           90       100
                   ....*....|....*....|....*..
gi 1958743172  184 alnqypalyYPELYILRGGYRDFFPEY 210
Cdd:smart00450  81 ---------FKNVYLLDGGYKEWSAAG 98
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 114-206 2.77e-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: 52.87  E-value: 2.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743172 114 IIDCRYPYEYLGGHILGALNL-YSQKELYEF-FLKKPVVPEDTQKRVIIVFLCEfSSERGPRMCRSLREKDralnqypal 191
Cdd:pfam00581   8 LIDVRPPEEYAKGHIPGAVNVpLSSLSLPPLpLLELLEKLLELLKDKPIVVYCN-SGNRAAAAAALLKALG--------- 77

                          90
                  ....*....|....*
gi 1958743172 192 yYPELYILRGGYRDF 206
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 ...
 89-208 1.11e-60

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: 187.43  E-value: 1.11e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743172  89 LKYISPDTVAALLSGKFQSVIERFYIIDCRYPYEYLGGHILGALNLYSQKELYEFFLKKPVVPeDTQKRVIIVFLCEFSS 168
Cdd:cd01530     1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVA-SKKKRRVLIFHCEFSS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958743172 169 ERGPRMCRSLREKDRALN--QYPALYYPELYILRGGYRDFFP 208
Cdd:cd01530    80 KRGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
72-227 7.12e-49

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 166.75  E-value: 7.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743172  72 DFSKACVLP---TVPGKHQDLKYISPDTVAALLSGKFQSVIERFYIIDCRYPYEYLGGHILGALNLYSQKELYEFFLKKP 148
Cdd:COG5105   221 SFSNGEVFPlptLGPGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLFRHKP 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743172 149 VVpedtqKRVIIVFLCEFSSERGPRMCRSLREKDRALNQ--YPALYYPELYILRGGYRDFFPEYMELCEPQGYCPMLHQD 226
Cdd:COG5105   301 LT-----HPRALIFHCEFSSHRAPRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTMNNAE 375


                  .
gi 1958743172 227 H 227
Cdd:COG5105   376 L 376
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 89-208 3.61e-29

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: 106.34  E-value: 3.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743172  89 LKYISPDTVAALLSGKFQSVIERFYIIDCRYPyEYLGGHILGALNLYSQkELYEFFLKKP-VVPEDtqKRVIIVFLCEFS 167
Cdd:cd01443     1 LKYISPEELVALLENSDSNAGKDFVVVDLRRD-DYEGGHIKGSINLPAQ-SCYQTLPQVYaLFSLA--GVKLAIFYCGSS 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958743172 168 SERGPRMCRSLREKDRAlnqyPALYYPELYILRGGYRDFFP 208
Cdd:cd01443    77 QGRGPRAARWFADYLRK----VGESLPKSYILTGGIKAWYH 113
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 110-210 3.76e-17

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: 74.42  E-value: 3.76e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743172  110 ERFYIIDCRYPYEYLGGHILGALNLYSQKELYEFFLKKPVVPEDTQKR------VIIVFLCeFSSERGPRMCRSLREKDr 183
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRlgldkdKPVVVYC-RSGNRSAKAAWLLRELG- 80

                           90       100
                   ....*....|....*....|....*..
gi 1958743172  184 alnqypalyYPELYILRGGYRDFFPEY 210
Cdd:smart00450  81 ---------FKNVYLLDGGYKEWSAAG 98
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 89-203 4.28e-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: 61.28  E-value: 4.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743172  89 LKYISPDTvaalLSGKFQSVIERFYIIDCRyPYEYLGGHILGALNLYSQKELYEF-FLKKPVVPEDTQKrviIVFLCEFS 167
Cdd:cd01531     1 VSYISPAQ----LKGWIRNGRPPFQVVDVR-DEDYAGGHIKGSWHYPSTRFKAQLnQLVQLLSGSKKDT---VVFHCALS 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958743172 168 SERGP----RMCRSLREKDRALNQypalyyPELYILRGGY 203
Cdd:cd01531    73 QVRGPsaarKFLRYLDEEDLETSK------FEVYVLHGGF 106
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 88-205 4.50e-10

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: 55.74  E-value: 4.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743172  88 DLKYISPDTVAALLSGkfqsviERFYIIDCRYPYEYLGGHILGALNLysqkELYEFFLKKPVVPEDTQkrviIVFLCEfS 167
Cdd:COG0607     2 SVKEISPAELAELLES------EDAVLLDVREPEEFAAGHIPGAINI----PLGELAERLDELPKDKP----IVVYCA-S 66

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958743172 168 SERGPRMCRSLRekdralnqypALYYPELYILRGGYRD 205
Cdd:COG0607    67 GGRSAQAAALLR----------RAGYTNVYNLAGGIEA 94
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 110-204 1.26e-09

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: 53.84  E-value: 1.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743172 110 ERFYIIDCRYPYEYLGGHILGALNLysqkELYEFFLKKPVVPEDTQKRVIIVflCEfSSERGPRMCRSLREkdralnqyp 189
Cdd:cd00158     9 EDAVLLDVREPEEYAAGHIPGAINI----PLSELEERAALLELDKDKPIVVY--CR-SGNRSARAAKLLRK--------- 72

                          90
                  ....*....|....*
gi 1958743172 190 aLYYPELYILRGGYR 204
Cdd:cd00158    73 -AGGTNVYNLEGGML 86
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 114-206 2.77e-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: 52.87  E-value: 2.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743172 114 IIDCRYPYEYLGGHILGALNL-YSQKELYEF-FLKKPVVPEDTQKRVIIVFLCEfSSERGPRMCRSLREKDralnqypal 191
Cdd:pfam00581   8 LIDVRPPEEYAKGHIPGAVNVpLSSLSLPPLpLLELLEKLLELLKDKPIVVYCN-SGNRAAAAAALLKALG--------- 77

                          90
                  ....*....|....*
gi 1958743172 192 yYPELYILRGGYRDF 206
Cdd:pfam00581  78 -YKNVYVLDGGFEAW 91
 
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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