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Conserved domains on  [gi|442621662|ref|NP_001263066|]
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string, isoform B [Drosophila melanogaster]

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 ...
 297-425 2.26e-61

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: 195.90  E-value: 2.26e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442621662 297 LKSISSETVARLLKGEFSDKVASYRIIDCRYPYEFEGGHIEGAKNLYTTEQILDEFLTVQQTELQQqqnaesghKRNIII 376
Cdd:cd01530    1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKK--------KRRVLI 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 442621662 377 FHCEFSSERGPKMSRFLRNLDRERNTNAYPALHYPEIYLLHNGYKEFFE 425
Cdd:cd01530   73 FHCEFSSKRGPRMARHLRNLDRELNSNRYPLLYYPEIYILEGGYKNFFE 121
 
Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 297-425 2.26e-61

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: 195.90  E-value: 2.26e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442621662 297 LKSISSETVARLLKGEFSDKVASYRIIDCRYPYEFEGGHIEGAKNLYTTEQILDEFLTVQQTELQQqqnaesghKRNIII 376
Cdd:cd01530    1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKK--------KRRVLI 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 442621662 377 FHCEFSSERGPKMSRFLRNLDRERNTNAYPALHYPEIYLLHNGYKEFFE 425
Cdd:cd01530   73 FHCEFSSKRGPRMARHLRNLDRELNSNRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
269-439 2.48e-37

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 141.72  E-value: 2.48e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442621662 269 SENRNEPELIGDFSKAYALPLM---EGRHRDLKSISSETVARLLKGEFSDKVASYRIIDCRYPYEFEGGHIEGAKNLYTT 345
Cdd:COG5105  210 AENSHLIDFFKSFSNGEVFPLPtlgPGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISST 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442621662 346 EQILDEFLTvqqtelqqqqnaESGHKRNIIIFHCEFSSERGPKMSRFLRNLDRERNTNAYPALHYPEIYLLHNGYKEFFE 425
Cdd:COG5105  290 KKLGLLFRH------------KPLTHPRALIFHCEFSSHRAPRLAQHLRNMDRMKNPDHYPLLTYPEVYILEGGYKKFYS 357

                        170
                 ....*....|....
gi 442621662 426 SHVELCEPHAYRTM 439
Cdd:COG5105  358 NYPDLCDPKGYVTM 371
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 318-429 4.29e-20

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: 84.82  E-value: 4.29e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442621662   318 ASYRIIDCRYPYEFEGGHIEGAKNLYtTEQILDEFLTVQQTELQQQQNAESGHKRNIIIFHCeFSSERGPKMSRFLRNLD 397
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIP-LSELLDRRGELDILEFEELLKRLGLDKDKPVVVYC-RSGNRSAKAAWLLRELG 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 442621662   398 rerntnaypalhYPEIYLLHNGYKEFFESHVE 429
Cdd:smart00450  81 ------------FKNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 320-423 3.58e-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: 53.64  E-value: 3.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442621662  320 YRIIDCRYPYEFEGGHIEGAKNLYtteqiLDEFLTVQQTELQQQQNAESGHKRNIIIFHCEfSSERGPKMSRFLRNLDre 399
Cdd:pfam00581   6 VVLIDVRPPEEYAKGHIPGAVNVP-----LSSLSLPPLPLLELLEKLLELLKDKPIVVYCN-SGNRAAAAAALLKALG-- 77

                          90       100
                  ....*....|....*....|....
gi 442621662  400 rntnaypalhYPEIYLLHNGYKEF 423
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 ...
 297-425 2.26e-61

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: 195.90  E-value: 2.26e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442621662 297 LKSISSETVARLLKGEFSDKVASYRIIDCRYPYEFEGGHIEGAKNLYTTEQILDEFLTVQQTELQQqqnaesghKRNIII 376
Cdd:cd01530    1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKK--------KRRVLI 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 442621662 377 FHCEFSSERGPKMSRFLRNLDRERNTNAYPALHYPEIYLLHNGYKEFFE 425
Cdd:cd01530   73 FHCEFSSKRGPRMARHLRNLDRELNSNRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
269-439 2.48e-37

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 141.72  E-value: 2.48e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442621662 269 SENRNEPELIGDFSKAYALPLM---EGRHRDLKSISSETVARLLKGEFSDKVASYRIIDCRYPYEFEGGHIEGAKNLYTT 345
Cdd:COG5105  210 AENSHLIDFFKSFSNGEVFPLPtlgPGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISST 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442621662 346 EQILDEFLTvqqtelqqqqnaESGHKRNIIIFHCEFSSERGPKMSRFLRNLDRERNTNAYPALHYPEIYLLHNGYKEFFE 425
Cdd:COG5105  290 KKLGLLFRH------------KPLTHPRALIFHCEFSSHRAPRLAQHLRNMDRMKNPDHYPLLTYPEVYILEGGYKKFYS 357

                        170
                 ....*....|....
gi 442621662 426 SHVELCEPHAYRTM 439
Cdd:COG5105  358 NYPDLCDPKGYVTM 371
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 297-425 1.46e-23

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: 95.17  E-value: 1.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442621662 297 LKSISSETVARLLKGEFSDKVASYRIIDCRYPyEFEGGHIEGAKNLyTTEQILDEFLTVQqtelqqqqNAESGHKRNIII 376
Cdd:cd01443    1 LKYISPEELVALLENSDSNAGKDFVVVDLRRD-DYEGGHIKGSINL-PAQSCYQTLPQVY--------ALFSLAGVKLAI 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 442621662 377 FHCEFSSERGPKMSRFLRNLDRErntnayPALHYPEIYLLHNGYKEFFE 425
Cdd:cd01443   71 FYCGSSQGRGPRAARWFADYLRK------VGESLPKSYILTGGIKAWYH 113
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 318-429 4.29e-20

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: 84.82  E-value: 4.29e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442621662   318 ASYRIIDCRYPYEFEGGHIEGAKNLYtTEQILDEFLTVQQTELQQQQNAESGHKRNIIIFHCeFSSERGPKMSRFLRNLD 397
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIP-LSELLDRRGELDILEFEELLKRLGLDKDKPVVVYC-RSGNRSAKAAWLLRELG 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 442621662   398 rerntnaypalhYPEIYLLHNGYKEFFESHVE 429
Cdd:smart00450  81 ------------FKNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 320-423 3.58e-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: 53.64  E-value: 3.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442621662  320 YRIIDCRYPYEFEGGHIEGAKNLYtteqiLDEFLTVQQTELQQQQNAESGHKRNIIIFHCEfSSERGPKMSRFLRNLDre 399
Cdd:pfam00581   6 VVLIDVRPPEEYAKGHIPGAVNVP-----LSSLSLPPLPLLELLEKLLELLKDKPIVVYCN-SGNRAAAAAALLKALG-- 77

                          90       100
                  ....*....|....*....|....
gi 442621662  400 rntnaypalhYPEIYLLHNGYKEF 423
Cdd:pfam00581  78 ----------YKNVYVLDGGFEAW 91
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 304-423 4.63e-08

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: 50.38  E-value: 4.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442621662 304 TVARLLKGEfsdkvaSYRIIDCRYPYEFEGGHIEGAKNLYtteqiLDEFLTvqqtelqqQQNAESGHKRNIIIFHCEfSS 383
Cdd:cd00158    1 ELKELLDDE------DAVLLDVREPEEYAAGHIPGAINIP-----LSELEE--------RAALLELDKDKPIVVYCR-SG 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 442621662 384 ERGPKMSRFLRnldrerntnaypALHYPEIYLLHNGYKEF 423
Cdd:cd00158   61 NRSARAAKLLR------------KAGGTNVYNLEGGMLAW 88
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 297-420 1.27e-07

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: 50.10  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442621662 297 LKSISSETVARLLKgEFSDKVAsyrIIDCRyPYEFEGGHIEGAKNL--YTTEQILDEFltvqqtelqqQQNAESGHKRNI 374
Cdd:cd01531    1 VSYISPAQLKGWIR-NGRPPFQ---VVDVR-DEDYAGGHIKGSWHYpsTRFKAQLNQL----------VQLLSGSKKDTV 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 442621662 375 IiFHCEFSSERGP----KMSRFLRNLDRERNTnaypalhyPEIYLLHNGY 420
Cdd:cd01531   66 V-FHCALSQVRGPsaarKFLRYLDEEDLETSK--------FEVYVLHGGF 106
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 296-396 3.10e-06

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: 45.73  E-value: 3.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442621662 296 DLKSISSETVARLLKGEfsdkvaSYRIIDCRYPYEFEGGHIEGAKNLYtteqiLDEFltvqqtelqqQQNAESGHKRNII 375
Cdd:COG0607    2 SVKEISPAELAELLESE------DAVLLDVREPEEFAAGHIPGAINIP-----LGEL----------AERLDELPKDKPI 60

                         90       100
                 ....*....|....*....|.
gi 442621662 376 IFHCEfSSERGPKMSRFLRNL 396
Cdd:COG0607   61 VVYCA-SGGRSAQAAALLRRA 80
 
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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