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Conserved domains on  [gi|12408658|ref|NP_073720|]
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M-phase inducer phosphatase 3 isoform b [Homo sapiens]

Protein Classification

MIH1 and Cdc25 domain-containing protein( domain architecture ID 11885818)

MIH1 and Cdc25 domain-containing protein

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 ...
 229-348 3.37e-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: 190.89  E-value: 3.37e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658 229 LKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVPLDTQKRIIIvFHCEFSS 308
Cdd:cd01530   1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLI-FHCEFSS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 12408658 309 ERGPRMCRCLREEDRSLN--QYPALYYPELYILKGGYRDFFP 348
Cdd:cd01530  80 KRGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
MIH1 super family cl26959
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
134-374 4.86e-44

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


The actual alignment was detected with superfamily member COG5105:

Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 158.28  E-value: 4.86e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658 134 SRSGLYRSPSMPENLNRPRLKQVEKFKDNTipDKVKKKYFSGQGKLRKglcLKKTVSLCDITITQMLEEDSNQG------ 207
Cdd:COG5105 137 YIKKFYEIPWSSSENIEFEDPGHDPFVDNS--DNSKMNHLRGSGKQPK---CREKIAFAVWTSLQGMRGFSRAGpapaae 211

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658 208 --HLIG---DFSKVCALPTVS---GKHQDLKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEE 279
Cdd:COG5105 212 nsHLIDffkSFSNGEVFPLPTlgpGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKK 291

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658 280 LFNFFLKKPIVpldtqKRIIIVFHCEFSSERGPRMCRCLREEDRSLNQ--YPALYYPELYILKGGYRDFFPEYMELCEPQ 357
Cdd:COG5105 292 LGLLFRHKPLT-----HPRALIFHCEFSSHRAPRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPK 366

                       250
                ....*....|....*..
gi 12408658 358 SYCPMHHQDHkteLLRC 374
Cdd:COG5105 367 GYVTMNNAEL---DYRC 380
 
Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 229-348 3.37e-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: 190.89  E-value: 3.37e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658 229 LKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVPLDTQKRIIIvFHCEFSS 308
Cdd:cd01530   1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLI-FHCEFSS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 12408658 309 ERGPRMCRCLREEDRSLN--QYPALYYPELYILKGGYRDFFP 348
Cdd:cd01530  80 KRGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
134-374 4.86e-44

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 158.28  E-value: 4.86e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658 134 SRSGLYRSPSMPENLNRPRLKQVEKFKDNTipDKVKKKYFSGQGKLRKglcLKKTVSLCDITITQMLEEDSNQG------ 207
Cdd:COG5105 137 YIKKFYEIPWSSSENIEFEDPGHDPFVDNS--DNSKMNHLRGSGKQPK---CREKIAFAVWTSLQGMRGFSRAGpapaae 211

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658 208 --HLIG---DFSKVCALPTVS---GKHQDLKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEE 279
Cdd:COG5105 212 nsHLIDffkSFSNGEVFPLPTlgpGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKK 291

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658 280 LFNFFLKKPIVpldtqKRIIIVFHCEFSSERGPRMCRCLREEDRSLNQ--YPALYYPELYILKGGYRDFFPEYMELCEPQ 357
Cdd:COG5105 292 LGLLFRHKPLT-----HPRALIFHCEFSSHRAPRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPK 366

                       250
                ....*....|....*..
gi 12408658 358 SYCPMHHQDHkteLLRC 374
Cdd:COG5105 367 GYVTMNNAEL---DYRC 380
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 250-350 2.83e-16

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: 73.65  E-value: 2.83e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658    250 EKFYVIDCRYPYEYLGGHIQGALN------LYSQEELFNFFLKKPIVPLDTQKRIIIVFHCeFSSERGPRMCRCLREedr 323
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNiplselLDRRGELDILEFEELLKRLGLDKDKPVVVYC-RSGNRSAKAAWLLRE--- 78

                           90       100
                   ....*....|....*....|....*..
gi 12408658    324 slnqypaLYYPELYILKGGYRDFFPEY 350
Cdd:smart00450  79 -------LGFKNVYLLDGGYKEWSAAG 98
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 228-345 1.17e-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: 55.36  E-value: 1.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658 228 DLKYVNPETVAALLSGkfqgliEKFYVIDCRYPYEYLGGHIQGALNLYSQEelfnffLKKPIVPLDTQKRiiIVFHCEfS 307
Cdd:COG0607   2 SVKEISPAELAELLES------EDAVLLDVREPEEFAAGHIPGAINIPLGE------LAERLDELPKDKP--IVVYCA-S 66

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 12408658 308 SERGPRMCRCLReedrslnqypALYYPELYILKGGYRD 345
Cdd:COG0607  67 GGRSAQAAALLR----------RAGYTNVYNLAGGIEA 94
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 254-346 2.90e-08

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: 50.95  E-value: 2.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658   254 VIDCRYPYEYLGGHIQGALNLYSQEELFNF--FLKKPIVPLDTQKRIIIVFHCEfSSERGPRMCRCLReedrslnqypAL 331
Cdd:pfam00581   8 LIDVRPPEEYAKGHIPGAVNVPLSSLSLPPlpLLELLEKLLELLKDKPIVVYCN-SGNRAAAAAALLK----------AL 76

                          90
                  ....*....|....*
gi 12408658   332 YYPELYILKGGYRDF 346
Cdd:pfam00581  77 GYKNVYVLDGGFEAW 91
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 137-196 5.17e-06

M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer phosphatases (EC:3.1.3.48), which also contain the pfam00581 domain. These proteins are involved in the control of mitosis.


Pssm-ID: 461962  Cd Length: 269  Bit Score: 47.44  E-value: 5.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12408658   137 GLYRSPSMPENLNRPRLKQVEKFKDNTIPDKVK-KKYFSG-------QGKLRKGLCLKKTVSLCDITI 196
Cdd:pfam06617 200 RLFRSPSMPSPVIRPALKRPERPQDEDTPVKVKrRRSVAGtqveaeeQEPESPRSLLQRSKSLCHQEI 267
 
Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 229-348 3.37e-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: 190.89  E-value: 3.37e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658 229 LKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVPLDTQKRIIIvFHCEFSS 308
Cdd:cd01530   1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLI-FHCEFSS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 12408658 309 ERGPRMCRCLREEDRSLN--QYPALYYPELYILKGGYRDFFP 348
Cdd:cd01530  80 KRGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
134-374 4.86e-44

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 158.28  E-value: 4.86e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658 134 SRSGLYRSPSMPENLNRPRLKQVEKFKDNTipDKVKKKYFSGQGKLRKglcLKKTVSLCDITITQMLEEDSNQG------ 207
Cdd:COG5105 137 YIKKFYEIPWSSSENIEFEDPGHDPFVDNS--DNSKMNHLRGSGKQPK---CREKIAFAVWTSLQGMRGFSRAGpapaae 211

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658 208 --HLIG---DFSKVCALPTVS---GKHQDLKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEE 279
Cdd:COG5105 212 nsHLIDffkSFSNGEVFPLPTlgpGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKK 291

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658 280 LFNFFLKKPIVpldtqKRIIIVFHCEFSSERGPRMCRCLREEDRSLNQ--YPALYYPELYILKGGYRDFFPEYMELCEPQ 357
Cdd:COG5105 292 LGLLFRHKPLT-----HPRALIFHCEFSSHRAPRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPK 366

                       250
                ....*....|....*..
gi 12408658 358 SYCPMHHQDHkteLLRC 374
Cdd:COG5105 367 GYVTMNNAEL---DYRC 380
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 229-348 2.35e-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: 104.80  E-value: 2.35e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658 229 LKYVNPETVAALLSGKFQGLIEKFYVIDCRYPyEYLGGHIQGALNLYSQEelFNFFLKKPIVPLDTQKRIIIVFHCEFSS 308
Cdd:cd01443   1 LKYISPEELVALLENSDSNAGKDFVVVDLRRD-DYEGGHIKGSINLPAQS--CYQTLPQVYALFSLAGVKLAIFYCGSSQ 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 12408658 309 ERGPRMCRCLREEDRSlnqyPALYYPELYILKGGYRDFFP 348
Cdd:cd01443  78 GRGPRAARWFADYLRK----VGESLPKSYILTGGIKAWYH 113
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 250-350 2.83e-16

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: 73.65  E-value: 2.83e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658    250 EKFYVIDCRYPYEYLGGHIQGALN------LYSQEELFNFFLKKPIVPLDTQKRIIIVFHCeFSSERGPRMCRCLREedr 323
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNiplselLDRRGELDILEFEELLKRLGLDKDKPVVVYC-RSGNRSAKAAWLLRE--- 78

                           90       100
                   ....*....|....*....|....*..
gi 12408658    324 slnqypaLYYPELYILKGGYRDFFPEY 350
Cdd:smart00450  79 -------LGFKNVYLLDGGYKEWSAAG 98
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 229-343 1.87e-11

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: 60.51  E-value: 1.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658 229 LKYVNPETvaalLSGKFQGLIEKFYVIDCRyPYEYLGGHIQGALNLYSQEelfnfFLKKP---IVPLDTQKRIIIVFHCE 305
Cdd:cd01531   1 VSYISPAQ----LKGWIRNGRPPFQVVDVR-DEDYAGGHIKGSWHYPSTR-----FKAQLnqlVQLLSGSKKDTVVFHCA 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 12408658 306 FSSERGP----RMCRCLREEDRSLNQypalyyPELYILKGGY 343
Cdd:cd01531  71 LSQVRGPsaarKFLRYLDEEDLETSK------FEVYVLHGGF 106
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 228-345 1.17e-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: 55.36  E-value: 1.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658 228 DLKYVNPETVAALLSGkfqgliEKFYVIDCRYPYEYLGGHIQGALNLYSQEelfnffLKKPIVPLDTQKRiiIVFHCEfS 307
Cdd:COG0607   2 SVKEISPAELAELLES------EDAVLLDVREPEEFAAGHIPGAINIPLGE------LAERLDELPKDKP--IVVYCA-S 66

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 12408658 308 SERGPRMCRCLReedrslnqypALYYPELYILKGGYRD 345
Cdd:COG0607  67 GGRSAQAAALLR----------RAGYTNVYNLAGGIEA 94
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 250-344 1.72e-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: 54.23  E-value: 1.72e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658 250 EKFYVIDCRYPYEYLGGHIQGALNLysqeELFNFFLKKPIVPLDTQKRiiIVFHCEfSSERGPRMCRCLREedrslnqyp 329
Cdd:cd00158   9 EDAVLLDVREPEEYAAGHIPGAINI----PLSELEERAALLELDKDKP--IVVYCR-SGNRSARAAKLLRK--------- 72

                        90
                ....*....|....*
gi 12408658 330 aLYYPELYILKGGYR 344
Cdd:cd00158  73 -AGGTNVYNLEGGML 86
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 254-346 2.90e-08

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: 50.95  E-value: 2.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408658   254 VIDCRYPYEYLGGHIQGALNLYSQEELFNF--FLKKPIVPLDTQKRIIIVFHCEfSSERGPRMCRCLReedrslnqypAL 331
Cdd:pfam00581   8 LIDVRPPEEYAKGHIPGAVNVPLSSLSLPPlpLLELLEKLLELLKDKPIVVYCN-SGNRAAAAAALLK----------AL 76

                          90
                  ....*....|....*
gi 12408658   332 YYPELYILKGGYRDF 346
Cdd:pfam00581  77 GYKNVYVLDGGFEAW 91
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 137-196 5.17e-06

M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer phosphatases (EC:3.1.3.48), which also contain the pfam00581 domain. These proteins are involved in the control of mitosis.


Pssm-ID: 461962  Cd Length: 269  Bit Score: 47.44  E-value: 5.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12408658   137 GLYRSPSMPENLNRPRLKQVEKFKDNTIPDKVK-KKYFSG-------QGKLRKGLCLKKTVSLCDITI 196
Cdd:pfam06617 200 RLFRSPSMPSPVIRPALKRPERPQDEDTPVKVKrRRSVAGtqveaeeQEPESPRSLLQRSKSLCHQEI 267
 
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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