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Conserved domains on  [gi|17559038|ref|NP_503446|]
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M-phase inducer phosphatase cdc-25.2 [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 ...
 223-341 1.22e-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: 170.86  E-value: 1.22e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559038 223 FRRITAETLRDIFFRLSEkEFDDKYILIDCRYPYEYNRGHIKNAINHFDRVTVSKIFYDENGR--KRCNKIPIFYCEFSQ 300
Cdd:cd01530   1 LKRISPETLARLLQGKYD-NFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVasKKKRRVLIFHCEFSS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17559038 301 ARGPKMAYALRQVDRELNVNHYPKCDYEEMYVLDLGYRNFF 341
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 ...
 223-341 1.22e-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: 170.86  E-value: 1.22e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559038 223 FRRITAETLRDIFFRLSEkEFDDKYILIDCRYPYEYNRGHIKNAINHFDRVTVSKIFYDENGR--KRCNKIPIFYCEFSQ 300
Cdd:cd01530   1 LKRISPETLARLLQGKYD-NFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVasKKKRRVLIFHCEFSS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17559038 301 ARGPKMAYALRQVDRELNVNHYPKCDYEEMYVLDLGYRNFF 341
Cdd:cd01530  80 KRGPRMARHLRNLDRELNSNRYPLLYYPEIYILEGGYKNFF 120
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
212-400 1.53e-26

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 111.28  E-value: 1.53e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559038 212 LKTVAKESSKGFRRITAETLRDIFFRLSEKEFDdKYILIDCRYPYEYNRGHIKNAINHFDRVTVSKIFydengRKRCNKI 291
Cdd:COG5105 230 LPTLGPGKSDSIQRISVETLKQVLEGMYNIDFL-KCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLF-----RHKPLTH 303

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559038 292 P---IFYCEFSQARGPKMAYALRQVDRELNVNHYPKCDYEEMYVLDLGYRNFFfaaneANITNLCQPHAYCEMHDKEHTM 368
Cdd:COG5105 304 PralIFHCEFSSHRAPRLAQHLRNMDRMKNPDHYPLLTYPEVYILEGGYKKFY-----SNYPDLCDPKGYVTMNNAELDY 378

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 17559038 369 E-LKKYN--------FHNKGQSVLRTVSMSRSFKSLPTGSA 400
Cdd:COG5105 379 RcLYKMDkfrrnkkfFATKNNSFGKLALASPDSHDSPTAMA 419
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 243-341 4.92e-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: 4.92e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559038    243 FDDKYILIDCRYPYEYNRGHIKNAIN-------HFDRVTVSKIFYDENGRKRC--NKIPIFYCeFSQARGPKMAYALRqv 313
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNiplsellDRRGELDILEFEELLKRLGLdkDKPVVVYC-RSGNRSAKAAWLLR-- 77

                           90       100
                   ....*....|....*....|....*...
gi 17559038    314 drelnvnhypKCDYEEMYVLDLGYRNFF 341
Cdd:smart00450  78 ----------ELGFKNVYLLDGGYKEWS 95
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 244-340 2.38e-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: 2.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559038   244 DDKYILIDCRYPYEYNRGHIKNAIN--HFDRVTVSKIFYDENGR---KRCNKIPIFYCEFSQaRGPKMAYALRqvdreln 318
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNvpLSSLSLPPLPLLELLEKlleLLKDKPIVVYCNSGN-RAAAAAALLK------- 74

                          90       100
                  ....*....|....*....|..
gi 17559038   319 vnhypKCDYEEMYVLDLGYRNF 340
Cdd:pfam00581  75 -----ALGYKNVYVLDGGFEAW 91
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 243-269 8.44e-03

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 38.27  E-value: 8.44e-03
                         10        20
                 ....*....|....*....|....*..
gi 17559038  243 FDDKYILIDCRYPYEYNRGHIKNAINH 269
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 ...
 223-341 1.22e-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: 170.86  E-value: 1.22e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559038 223 FRRITAETLRDIFFRLSEkEFDDKYILIDCRYPYEYNRGHIKNAINHFDRVTVSKIFYDENGR--KRCNKIPIFYCEFSQ 300
Cdd:cd01530   1 LKRISPETLARLLQGKYD-NFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVasKKKRRVLIFHCEFSS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17559038 301 ARGPKMAYALRQVDRELNVNHYPKCDYEEMYVLDLGYRNFF 341
Cdd:cd01530  80 KRGPRMARHLRNLDRELNSNRYPLLYYPEIYILEGGYKNFF 120
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
212-400 1.53e-26

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 111.28  E-value: 1.53e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559038 212 LKTVAKESSKGFRRITAETLRDIFFRLSEKEFDdKYILIDCRYPYEYNRGHIKNAINHFDRVTVSKIFydengRKRCNKI 291
Cdd:COG5105 230 LPTLGPGKSDSIQRISVETLKQVLEGMYNIDFL-KCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLF-----RHKPLTH 303

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559038 292 P---IFYCEFSQARGPKMAYALRQVDRELNVNHYPKCDYEEMYVLDLGYRNFFfaaneANITNLCQPHAYCEMHDKEHTM 368
Cdd:COG5105 304 PralIFHCEFSSHRAPRLAQHLRNMDRMKNPDHYPLLTYPEVYILEGGYKKFY-----SNYPDLCDPKGYVTMNNAELDY 378

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 17559038 369 E-LKKYN--------FHNKGQSVLRTVSMSRSFKSLPTGSA 400
Cdd:COG5105 379 RcLYKMDkfrrnkkfFATKNNSFGKLALASPDSHDSPTAMA 419
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 243-341 4.92e-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: 4.92e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559038    243 FDDKYILIDCRYPYEYNRGHIKNAIN-------HFDRVTVSKIFYDENGRKRC--NKIPIFYCeFSQARGPKMAYALRqv 313
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNiplsellDRRGELDILEFEELLKRLGLdkDKPVVVYC-RSGNRSAKAAWLLR-- 77

                           90       100
                   ....*....|....*....|....*...
gi 17559038    314 drelnvnhypKCDYEEMYVLDLGYRNFF 341
Cdd:smart00450  78 ----------ELGFKNVYLLDGGYKEWS 95
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 245-341 3.36e-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: 3.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559038 245 DKYILIDCRYPyEYNRGHIKNAIN------HFDRVTVSKIFYdENGRKRCnkipIFYCEFSQARGPKMAYALRQVDREln 318
Cdd:cd01443  22 KDFVVVDLRRD-DYEGGHIKGSINlpaqscYQTLPQVYALFS-LAGVKLA----IFYCGSSQGRGPRAARWFADYLRK-- 93

                        90       100
                ....*....|....*....|...
gi 17559038 319 vnhyPKCDYEEMYVLDLGYRNFF 341
Cdd:cd01443  94 ----VGESLPKSYILTGGIKAWY 112
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 244-340 2.38e-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: 2.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559038   244 DDKYILIDCRYPYEYNRGHIKNAIN--HFDRVTVSKIFYDENGR---KRCNKIPIFYCEFSQaRGPKMAYALRqvdreln 318
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNvpLSSLSLPPLPLLELLEKlleLLKDKPIVVYCNSGN-RAAAAAALLK------- 74

                          90       100
                  ....*....|....*....|..
gi 17559038   319 vnhypKCDYEEMYVLDLGYRNF 340
Cdd:pfam00581  75 -----ALGYKNVYVLDGGFEAW 91
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 223-312 1.38e-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: 1.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559038 223 FRRITAETLRDiffRLSekefDDKYILIDCRYPYEYNRGHIKNAINhfdrVTVSKIfydengRKRCNKIP-----IFYCE 297
Cdd:COG0607   3 VKEISPAELAE---LLE----SEDAVLLDVREPEEFAAGHIPGAIN----IPLGEL------AERLDELPkdkpiVVYCA 65

                        90
                ....*....|....*
gi 17559038 298 fSQARGPKMAYALRQ 312
Cdd:COG0607  66 -SGGRSAQAAALLRR 79
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 238-338 1.95e-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: 1.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559038 238 LSEKEFDDKYILIDCRYPYEYNRGHIKNAINhfdrVTVSKIFYDEN-GRKRCNKIPIFYCEFSQaRGPKMAYALRqvdre 316
Cdd:cd00158   2 LKELLDDEDAVLLDVREPEEYAAGHIPGAIN----IPLSELEERAAlLELDKDKPIVVYCRSGN-RSARAAKLLR----- 71

                        90       100
                ....*....|....*....|..
gi 17559038 317 lnvnhypKCDYEEMYVLDLGYR 338
Cdd:cd00158  72 -------KAGGTNVYNLEGGML 86
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 226-288 8.40e-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: 39.57  E-value: 8.40e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559038 226 ITAETLRDIFfrlseKEFDDKYILIDCRYPYEYNRGHIKNAIN-----------HFDRVTVSKIFYDENGRKRC 288
Cdd:cd01446   2 IDCAWLAALL-----REGGERLLLLDCRPFLEYSSSHIRGAVNvccptilrrrlQGGKILLQQLLSCPEDRDRL 70
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 245-297 1.01e-03

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: 1.01e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17559038 245 DKYILIDCRYPYEYNRGHIKNAINhfdrVTVSKIfydengRKRCNKIP-----IFYCE 297
Cdd:cd01524  12 DGVTLIDVRTPQEFEKGHIKGAIN----IPLDEL------RDRLNELPkdkeiIVYCA 59
RHOD_YbbB cd01520
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ...
 226-268 2.74e-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: 2.74e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 17559038 226 ITAETLRDIFfrlsekefDDKYILIDCRYPYEYNRGHIKNAIN 268
Cdd:cd01520   1 ITAEDLLALR--------KADGPLIDVRSPKEFFEGHLPGAIN 35
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 250-307 5.79e-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: 5.79e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17559038 250 IDCRyPYEYNRGHIKNAINHFDRVTVSKIFYDENGRKRCNKIP-IFYCEFSQARGPKMA 307
Cdd:cd01531  23 VDVR-DEDYAGGHIKGSWHYPSTRFKAQLNQLVQLLSGSKKDTvVFHCALSQVRGPSAA 80
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 243-269 8.44e-03

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 38.27  E-value: 8.44e-03
                         10        20
                 ....*....|....*....|....*..
gi 17559038  243 FDDKYILIDCRYPYEYNRGHIKNAINH 269
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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