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Conserved domains on  [gi|922581018|ref|NP_001300079|]
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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

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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 ...
 201-319 1.74e-51

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: 169.71  E-value: 1.74e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581018 201 FRRITAETLRDIFFRLSEkEFDDKYILIDCRYPYEYNRGHIKNAINHFDRVTVSKIFYDENGR--KRCNKIPIFYCEFSQ 278
Cdd:cd01530    1 LKRISPETLARLLQGKYD-NFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVasKKKRRVLIFHCEFSS 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 922581018 279 ARGPKMAYALRQVDRELNVNHYPKCDYEEMYVLDLGYRNFF 319
Cdd:cd01530   80 KRGPRMARHLRNLDRELNSNRYPLLYYPEIYILEGGYKNFF 120
 
Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 201-319 1.74e-51

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: 169.71  E-value: 1.74e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581018 201 FRRITAETLRDIFFRLSEkEFDDKYILIDCRYPYEYNRGHIKNAINHFDRVTVSKIFYDENGR--KRCNKIPIFYCEFSQ 278
Cdd:cd01530    1 LKRISPETLARLLQGKYD-NFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVasKKKRRVLIFHCEFSS 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 922581018 279 ARGPKMAYALRQVDRELNVNHYPKCDYEEMYVLDLGYRNFF 319
Cdd:cd01530   80 KRGPRMARHLRNLDRELNSNRYPLLYYPEIYILEGGYKNFF 120
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
190-378 8.94e-27

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 111.67  E-value: 8.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581018 190 LKTVAKESSKGFRRITAETLRDIFFRLSEKEFDdKYILIDCRYPYEYNRGHIKNAINHFDRVTVSKIFydengRKRCNKI 269
Cdd:COG5105  230 LPTLGPGKSDSIQRISVETLKQVLEGMYNIDFL-KCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLF-----RHKPLTH 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581018 270 P---IFYCEFSQARGPKMAYALRQVDRELNVNHYPKCDYEEMYVLDLGYRNFFfaaneANITNLCQPHAYCEMHDKEHTM 346
Cdd:COG5105  304 PralIFHCEFSSHRAPRLAQHLRNMDRMKNPDHYPLLTYPEVYILEGGYKKFY-----SNYPDLCDPKGYVTMNNAELDY 378

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 922581018 347 E-LKKYN--------FHNKGQSVLRTVSMSRSFKSLPTGSA 378
Cdd:COG5105  379 RcLYKMDkfrrnkkfFATKNNSFGKLALASPDSHDSPTAMA 419
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 221-319 4.59e-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: 76.34  E-value: 4.59e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581018   221 FDDKYILIDCRYPYEYNRGHIKNAIN-------HFDRVTVSKIFYDENGRKRC--NKIPIFYCeFSQARGPKMAYALRqv 291
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNiplsellDRRGELDILEFEELLKRLGLdkDKPVVVYC-RSGNRSAKAAWLLR-- 77

                           90       100
                   ....*....|....*....|....*...
gi 922581018   292 drelnvnhypKCDYEEMYVLDLGYRNFF 319
Cdd:smart00450  78 ----------ELGFKNVYLLDGGYKEWS 95
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 222-318 2.26e-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: 57.11  E-value: 2.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581018  222 DDKYILIDCRYPYEYNRGHIKNAIN--HFDRVTVSKIFYDENGR---KRCNKIPIFYCEFSQaRGPKMAYALRqvdreln 296
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNvpLSSLSLPPLPLLELLEKlleLLKDKPIVVYCNSGN-RAAAAAALLK------- 74

                          90       100
                  ....*....|....*....|..
gi 922581018  297 vnhypKCDYEEMYVLDLGYRNF 318
Cdd:pfam00581  75 -----ALGYKNVYVLDGGFEAW 91
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 221-247 7.91e-03

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 38.27  E-value: 7.91e-03
                         10        20
                 ....*....|....*....|....*..
gi 922581018 221 FDDKYILIDCRYPYEYNRGHIKNAINH 247
Cdd:PRK11784  12 FLNDTPLIDVRSPIEFAEGHIPGAINL 38
 
Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 201-319 1.74e-51

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: 169.71  E-value: 1.74e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581018 201 FRRITAETLRDIFFRLSEkEFDDKYILIDCRYPYEYNRGHIKNAINHFDRVTVSKIFYDENGR--KRCNKIPIFYCEFSQ 278
Cdd:cd01530    1 LKRISPETLARLLQGKYD-NFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVasKKKRRVLIFHCEFSS 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 922581018 279 ARGPKMAYALRQVDRELNVNHYPKCDYEEMYVLDLGYRNFF 319
Cdd:cd01530   80 KRGPRMARHLRNLDRELNSNRYPLLYYPEIYILEGGYKNFF 120
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
190-378 8.94e-27

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 111.67  E-value: 8.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581018 190 LKTVAKESSKGFRRITAETLRDIFFRLSEKEFDdKYILIDCRYPYEYNRGHIKNAINHFDRVTVSKIFydengRKRCNKI 269
Cdd:COG5105  230 LPTLGPGKSDSIQRISVETLKQVLEGMYNIDFL-KCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLF-----RHKPLTH 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581018 270 P---IFYCEFSQARGPKMAYALRQVDRELNVNHYPKCDYEEMYVLDLGYRNFFfaaneANITNLCQPHAYCEMHDKEHTM 346
Cdd:COG5105  304 PralIFHCEFSSHRAPRLAQHLRNMDRMKNPDHYPLLTYPEVYILEGGYKKFY-----SNYPDLCDPKGYVTMNNAELDY 378

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 922581018 347 E-LKKYN--------FHNKGQSVLRTVSMSRSFKSLPTGSA 378
Cdd:COG5105  379 RcLYKMDkfrrnkkfFATKNNSFGKLALASPDSHDSPTAMA 419
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 221-319 4.59e-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: 76.34  E-value: 4.59e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581018   221 FDDKYILIDCRYPYEYNRGHIKNAIN-------HFDRVTVSKIFYDENGRKRC--NKIPIFYCeFSQARGPKMAYALRqv 291
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNiplsellDRRGELDILEFEELLKRLGLdkDKPVVVYC-RSGNRSAKAAWLLR-- 77

                           90       100
                   ....*....|....*....|....*...
gi 922581018   292 drelnvnhypKCDYEEMYVLDLGYRNFF 319
Cdd:smart00450  78 ----------ELGFKNVYLLDGGYKEWS 95
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 223-319 3.18e-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: 65.89  E-value: 3.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581018 223 DKYILIDCRYPyEYNRGHIKNAIN------HFDRVTVSKIFYdENGRKRCnkipIFYCEFSQARGPKMAYALRQVDREln 296
Cdd:cd01443   22 KDFVVVDLRRD-DYEGGHIKGSINlpaqscYQTLPQVYALFS-LAGVKLA----IFYCGSSQGRGPRAARWFADYLRK-- 93

                         90       100
                 ....*....|....*....|...
gi 922581018 297 vnhyPKCDYEEMYVLDLGYRNFF 319
Cdd:cd01443   94 ----VGESLPKSYILTGGIKAWY 112
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 222-318 2.26e-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: 57.11  E-value: 2.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581018  222 DDKYILIDCRYPYEYNRGHIKNAIN--HFDRVTVSKIFYDENGR---KRCNKIPIFYCEFSQaRGPKMAYALRqvdreln 296
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNvpLSSLSLPPLPLLELLEKlleLLKDKPIVVYCNSGN-RAAAAAALLK------- 74

                          90       100
                  ....*....|....*....|..
gi 922581018  297 vnhypKCDYEEMYVLDLGYRNF 318
Cdd:pfam00581  75 -----ALGYKNVYVLDGGFEAW 91
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 201-290 1.31e-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: 49.58  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581018 201 FRRITAETLRDiffRLSekefDDKYILIDCRYPYEYNRGHIKNAINhfdrVTVSKIfydengRKRCNKIP-----IFYCE 275
Cdd:COG0607    3 VKEISPAELAE---LLE----SEDAVLLDVREPEEFAAGHIPGAIN----IPLGEL------AERLDELPkdkpiVVYCA 65

                         90
                 ....*....|....*
gi 922581018 276 fSQARGPKMAYALRQ 290
Cdd:COG0607   66 -SGGRSAQAAALLRR 79
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 216-316 1.85e-07

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: 48.84  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581018 216 LSEKEFDDKYILIDCRYPYEYNRGHIKNAINhfdrVTVSKIFYDEN-GRKRCNKIPIFYCEFSQaRGPKMAYALRqvdre 294
Cdd:cd00158    2 LKELLDDEDAVLLDVREPEEYAAGHIPGAIN----IPLSELEERAAlLELDKDKPIVVYCRSGN-RSARAAKLLR----- 71

                         90       100
                 ....*....|....*....|..
gi 922581018 295 lnvnhypKCDYEEMYVLDLGYR 316
Cdd:cd00158   72 -------KAGGTNVYNLEGGML 86
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 204-266 9.10e-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: 39.19  E-value: 9.10e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922581018 204 ITAETLRDIFfrlseKEFDDKYILIDCRYPYEYNRGHIKNAIN-----------HFDRVTVSKIFYDENGRKRC 266
Cdd:cd01446    2 IDCAWLAALL-----REGGERLLLLDCRPFLEYSSSHIRGAVNvccptilrrrlQGGKILLQQLLSCPEDRDRL 70
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 223-275 9.64e-04

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.


Pssm-ID: 238782 [Multi-domain]  Cd Length: 90  Bit Score: 38.02  E-value: 9.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 922581018 223 DKYILIDCRYPYEYNRGHIKNAINhfdrVTVSKIfydengRKRCNKIP-----IFYCE 275
Cdd:cd01524   12 DGVTLIDVRTPQEFEKGHIKGAIN----IPLDEL------RDRLNELPkdkeiIVYCA 59
RHOD_YbbB cd01520
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ...
 204-246 2.59e-03

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP /GTP binding proteins including E. coli YbbB.


Pssm-ID: 238778 [Multi-domain]  Cd Length: 128  Bit Score: 38.04  E-value: 2.59e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 922581018 204 ITAETLRDIFfrlsekefDDKYILIDCRYPYEYNRGHIKNAIN 246
Cdd:cd01520    1 ITAEDLLALR--------KADGPLIDVRSPKEFFEGHLPGAIN 35
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 228-285 5.49e-03

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: 36.62  E-value: 5.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 922581018 228 IDCRyPYEYNRGHIKNAINHFDRVTVSKIFYDENGRKRCNKIP-IFYCEFSQARGPKMA 285
Cdd:cd01531   23 VDVR-DEDYAGGHIKGSWHYPSTRFKAQLNQLVQLLSGSKKDTvVFHCALSQVRGPSAA 80
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 221-247 7.91e-03

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 38.27  E-value: 7.91e-03
                         10        20
                 ....*....|....*....|....*..
gi 922581018 221 FDDKYILIDCRYPYEYNRGHIKNAINH 247
Cdd:PRK11784  12 FLNDTPLIDVRSPIEFAEGHIPGAINL 38
 
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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