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Conserved domains on  [gi|567316256|ref|NP_001274512|]
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M-phase inducer phosphatase 3 isoform c [Homo sapiens]

Protein Classification

M-phase inducer phosphatase; rhodanese domain-containing protein( domain architecture ID 11885818)

M-phase inducer phosphatase is a tyrosine protein phosphatase which may function as a dosage-dependent inducer in mitotic control| rhodanese domain-containing protein may function as a sulfurtransferase

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 ...
 380-499 3.21e-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: 194.75  E-value: 3.21e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256 380 LKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVPLDTQKRIIIvFHCEFSS 459
Cdd:cd01530    1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLI-FHCEFSS 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 567316256 460 ERGPRMCRCLREEDRSLN--QYPALYYPELYILKGGYRDFFP 499
Cdd:cd01530   80 KRGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
MIH1 super family cl26959
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
285-525 1.83e-43

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: 160.20  E-value: 1.83e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256 285 SRSGLYRSPSMPENLNRPRLKQVEKFKDNTipDKVKKKYFSGQGKLRKglcLKKTVSLCDITITQMLEEDSNQG------ 358
Cdd:COG5105  137 YIKKFYEIPWSSSENIEFEDPGHDPFVDNS--DNSKMNHLRGSGKQPK---CREKIAFAVWTSLQGMRGFSRAGpapaae 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256 359 --HLIG---DFSKVCALPTVS---GKHQDLKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEE 430
Cdd:COG5105  212 nsHLIDffkSFSNGEVFPLPTlgpGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKK 291

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256 431 LFNFFLKKPIVpldtqKRIIIVFHCEFSSERGPRMCRCLREEDRSLNQ--YPALYYPELYILKGGYRDFFPEYMELCEPQ 508
Cdd:COG5105  292 LGLLFRHKPLT-----HPRALIFHCEFSSHRAPRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPK 366

                        250
                 ....*....|....*..
gi 567316256 509 SYCPMHHQDHkteLLRC 525
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 ...
 380-499 3.21e-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: 194.75  E-value: 3.21e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256 380 LKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVPLDTQKRIIIvFHCEFSS 459
Cdd:cd01530    1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLI-FHCEFSS 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 567316256 460 ERGPRMCRCLREEDRSLN--QYPALYYPELYILKGGYRDFFP 499
Cdd:cd01530   80 KRGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
285-525 1.83e-43

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 160.20  E-value: 1.83e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256 285 SRSGLYRSPSMPENLNRPRLKQVEKFKDNTipDKVKKKYFSGQGKLRKglcLKKTVSLCDITITQMLEEDSNQG------ 358
Cdd:COG5105  137 YIKKFYEIPWSSSENIEFEDPGHDPFVDNS--DNSKMNHLRGSGKQPK---CREKIAFAVWTSLQGMRGFSRAGpapaae 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256 359 --HLIG---DFSKVCALPTVS---GKHQDLKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEE 430
Cdd:COG5105  212 nsHLIDffkSFSNGEVFPLPTlgpGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKK 291

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256 431 LFNFFLKKPIVpldtqKRIIIVFHCEFSSERGPRMCRCLREEDRSLNQ--YPALYYPELYILKGGYRDFFPEYMELCEPQ 508
Cdd:COG5105  292 LGLLFRHKPLT-----HPRALIFHCEFSSHRAPRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPK 366

                        250
                 ....*....|....*..
gi 567316256 509 SYCPMHHQDHkteLLRC 525
Cdd:COG5105  367 GYVTMNNAEL---DYRC 380
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 401-501 4.51e-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: 4.51e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256   401 EKFYVIDCRYPYEYLGGHIQGALN------LYSQEELFNFFLKKPIVPLDTQKRIIIVFHCeFSSERGPRMCRCLREedr 474
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNiplselLDRRGELDILEFEELLKRLGLDKDKPVVVYC-RSGNRSAKAAWLLRE--- 78

                           90       100
                   ....*....|....*....|....*..
gi 567316256   475 slnqypaLYYPELYILKGGYRDFFPEY 501
Cdd:smart00450  79 -------LGFKNVYLLDGGYKEWSAAG 98
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 379-496 1.68e-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: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256 379 DLKYVNPETVAALLSGkfqgliEKFYVIDCRYPYEYLGGHIQGALNLYSQEelfnffLKKPIVPLDTQKRiiIVFHCEfS 458
Cdd:COG0607    2 SVKEISPAELAELLES------EDAVLLDVREPEEFAAGHIPGAINIPLGE------LAERLDELPKDKP--IVVYCA-S 66

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 567316256 459 SERGPRMCRCLReedrslnqypALYYPELYILKGGYRD 496
Cdd:COG0607   67 GGRSAQAAALLR----------RAGYTNVYNLAGGIEA 94
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 405-497 4.12e-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: 4.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256  405 VIDCRYPYEYLGGHIQGALNLYSQEELFNF--FLKKPIVPLDTQKRIIIVFHCEfSSERGPRMCRCLReedrslnqypAL 482
Cdd:pfam00581   8 LIDVRPPEEYAKGHIPGAVNVPLSSLSLPPlpLLELLEKLLELLKDKPIVVYCN-SGNRAAAAAALLK----------AL 76

                          90
                  ....*....|....*
gi 567316256  483 YYPELYILKGGYRDF 497
Cdd:pfam00581  77 GYKNVYVLDGGFEAW 91
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 288-347 8.55e-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: 8.55e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567316256  288 GLYRSPSMPENLNRPRLKQVEKFKDNTIPDKVK-KKYFSG-------QGKLRKGLCLKKTVSLCDITI 347
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 ...
 380-499 3.21e-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: 194.75  E-value: 3.21e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256 380 LKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVPLDTQKRIIIvFHCEFSS 459
Cdd:cd01530    1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLI-FHCEFSS 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 567316256 460 ERGPRMCRCLREEDRSLN--QYPALYYPELYILKGGYRDFFP 499
Cdd:cd01530   80 KRGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
285-525 1.83e-43

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 160.20  E-value: 1.83e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256 285 SRSGLYRSPSMPENLNRPRLKQVEKFKDNTipDKVKKKYFSGQGKLRKglcLKKTVSLCDITITQMLEEDSNQG------ 358
Cdd:COG5105  137 YIKKFYEIPWSSSENIEFEDPGHDPFVDNS--DNSKMNHLRGSGKQPK---CREKIAFAVWTSLQGMRGFSRAGpapaae 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256 359 --HLIG---DFSKVCALPTVS---GKHQDLKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEE 430
Cdd:COG5105  212 nsHLIDffkSFSNGEVFPLPTlgpGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKK 291

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256 431 LFNFFLKKPIVpldtqKRIIIVFHCEFSSERGPRMCRCLREEDRSLNQ--YPALYYPELYILKGGYRDFFPEYMELCEPQ 508
Cdd:COG5105  292 LGLLFRHKPLT-----HPRALIFHCEFSSHRAPRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPK 366

                        250
                 ....*....|....*..
gi 567316256 509 SYCPMHHQDHkteLLRC 525
Cdd:COG5105  367 GYVTMNNAEL---DYRC 380
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 380-499 4.68e-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: 105.57  E-value: 4.68e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256 380 LKYVNPETVAALLSGKFQGLIEKFYVIDCRYPyEYLGGHIQGALNLYSQEelFNFFLKKPIVPLDTQKRIIIVFHCEFSS 459
Cdd:cd01443    1 LKYISPEELVALLENSDSNAGKDFVVVDLRRD-DYEGGHIKGSINLPAQS--CYQTLPQVYALFSLAGVKLAIFYCGSSQ 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 567316256 460 ERGPRMCRCLREEDRSlnqyPALYYPELYILKGGYRDFFP 499
Cdd:cd01443   78 GRGPRAARWFADYLRK----VGESLPKSYILTGGIKAWYH 113
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 401-501 4.51e-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: 4.51e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256   401 EKFYVIDCRYPYEYLGGHIQGALN------LYSQEELFNFFLKKPIVPLDTQKRIIIVFHCeFSSERGPRMCRCLREedr 474
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNiplselLDRRGELDILEFEELLKRLGLDKDKPVVVYC-RSGNRSAKAAWLLRE--- 78

                           90       100
                   ....*....|....*....|....*..
gi 567316256   475 slnqypaLYYPELYILKGGYRDFFPEY 501
Cdd:smart00450  79 -------LGFKNVYLLDGGYKEWSAAG 98
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 380-494 2.73e-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: 2.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256 380 LKYVNPETvaalLSGKFQGLIEKFYVIDCRyPYEYLGGHIQGALNLYSQEelfnfFLKKP---IVPLDTQKRIIIVFHCE 456
Cdd:cd01531    1 VSYISPAQ----LKGWIRNGRPPFQVVDVR-DEDYAGGHIKGSWHYPSTR-----FKAQLnqlVQLLSGSKKDTVVFHCA 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 567316256 457 FSSERGP----RMCRCLREEDRSLNQypalyyPELYILKGGY 494
Cdd:cd01531   71 LSQVRGPsaarKFLRYLDEEDLETSK------FEVYVLHGGF 106
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 379-496 1.68e-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: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256 379 DLKYVNPETVAALLSGkfqgliEKFYVIDCRYPYEYLGGHIQGALNLYSQEelfnffLKKPIVPLDTQKRiiIVFHCEfS 458
Cdd:COG0607    2 SVKEISPAELAELLES------EDAVLLDVREPEEFAAGHIPGAINIPLGE------LAERLDELPKDKP--IVVYCA-S 66

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 567316256 459 SERGPRMCRCLReedrslnqypALYYPELYILKGGYRD 496
Cdd:COG0607   67 GGRSAQAAALLR----------RAGYTNVYNLAGGIEA 94
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 401-495 2.44e-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: 2.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256 401 EKFYVIDCRYPYEYLGGHIQGALNLysqeELFNFFLKKPIVPLDTQKRiiIVFHCEfSSERGPRMCRCLREedrslnqyp 480
Cdd:cd00158    9 EDAVLLDVREPEEYAAGHIPGAINI----PLSELEERAALLELDKDKP--IVVYCR-SGNRSARAAKLLRK--------- 72

                         90
                 ....*....|....*
gi 567316256 481 aLYYPELYILKGGYR 495
Cdd:cd00158   73 -AGGTNVYNLEGGML 86
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 405-497 4.12e-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: 4.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316256  405 VIDCRYPYEYLGGHIQGALNLYSQEELFNF--FLKKPIVPLDTQKRIIIVFHCEfSSERGPRMCRCLReedrslnqypAL 482
Cdd:pfam00581   8 LIDVRPPEEYAKGHIPGAVNVPLSSLSLPPlpLLELLEKLLELLKDKPIVVYCN-SGNRAAAAAALLK----------AL 76

                          90
                  ....*....|....*
gi 567316256  483 YYPELYILKGGYRDF 497
Cdd:pfam00581  77 GYKNVYVLDGGFEAW 91
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 288-347 8.55e-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: 8.55e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567316256  288 GLYRSPSMPENLNRPRLKQVEKFKDNTIPDKVK-KKYFSG-------QGKLRKGLCLKKTVSLCDITI 347
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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