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Conserved domains on  [gi|7298278|gb|AAF53508|]
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twine, isoform A [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 ...
 243-363 6.69e-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: 193.20  E-value: 6.69e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7298278  243 LKTISSDTLARLIQGEFDEQLGSqggYEIIDCRYPYEFLGGHIRGAKNLYTRGQIQEAF--PTLTSNQENRRIYVFHCEF 320
Cdd:cd01530   1 LKRISPETLARLLQGKYDNFFDK---YIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFldKPGVASKKKRRVLIFHCEF 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 7298278  321 SSERGPKLLRYLRSNDRSQHTHNYPALDYPELYILHNGYKEFF 363
Cdd:cd01530  78 SSKRGPRMARHLRNLDRELNSNRYPLLYYPEIYILEGGYKNFF 120
 
Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 243-363 6.69e-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: 193.20  E-value: 6.69e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7298278  243 LKTISSDTLARLIQGEFDEQLGSqggYEIIDCRYPYEFLGGHIRGAKNLYTRGQIQEAF--PTLTSNQENRRIYVFHCEF 320
Cdd:cd01530   1 LKRISPETLARLLQGKYDNFFDK---YIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFldKPGVASKKKRRVLIFHCEF 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 7298278  321 SSERGPKLLRYLRSNDRSQHTHNYPALDYPELYILHNGYKEFF 363
Cdd:cd01530  78 SSKRGPRMARHLRNLDRELNSNRYPLLYYPEIYILEGGYKNFF 120
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
224-397 1.10e-36

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 139.02  E-value: 1.10e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7298278  224 DLSKPCTLPCLATGIRHRD-LKTISSDTLARLIQGEFDEqlgSQGGYEIIDCRYPYEFLGGHIRGAKNLYTRGQIQEAFp 302
Cdd:COG5105 221 SFSNGEVFPLPTLGPGKSDsIQRISVETLKQVLEGMYNI---DFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLF- 296

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7298278  303 tLTSNQENRRIYVFHCEFSSERGPKLLRYLRSNDRSQHTHNYPALDYPELYILHNGYKEFFGLYSQLCQPSQYVPMLAPA 382
Cdd:COG5105 297 -RHKPLTHPRALIFHCEFSSHRAPRLAQHLRNMDRMKNPDHYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTMNNAE 375

                       170       180
                ....*....|....*....|....*.
gi 7298278  383 HN-------DEFR----YFRAKTKSW 397
Cdd:COG5105 376 LDyrclykmDKFRrnkkFFATKNNSF 401
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 265-363 4.76e-15

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: 70.57  E-value: 4.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7298278     265 SQGGYEIIDCRYPYEFLGGHIRGAKNL----------YTRGQIQEAFPTLTSNQENRRIyVFHCeFSSERGPKLLRYLRS 334
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIplselldrrgELDILEFEELLKRLGLDKDKPV-VVYC-RSGNRSAKAAWLLRE 78

                           90       100
                   ....*....|....*....|....*....
gi 7298278     335 ndrsqhthnypaLDYPELYILHNGYKEFF 363
Cdd:smart00450  79 ------------LGFKNVYLLDGGYKEWS 95
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 266-362 9.66e-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: 55.18  E-value: 9.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7298278    266 QGGYEIIDCRYPYEFLGGHIRGAKNL------YTRGQIQEAFPTLTSNQENRRIyVFHCEfSSERGPKLLRYLRsndrsq 339
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVplsslsLPPLPLLELLEKLLELLKDKPI-VVYCN-SGNRAAAAAALLK------ 74

                          90       100
                  ....*....|....*....|...
gi 7298278    340 hthnypALDYPELYILHNGYKEF 362
Cdd:pfam00581  75 ------ALGYKNVYVLDGGFEAW 91
 
Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 243-363 6.69e-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: 193.20  E-value: 6.69e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7298278  243 LKTISSDTLARLIQGEFDEQLGSqggYEIIDCRYPYEFLGGHIRGAKNLYTRGQIQEAF--PTLTSNQENRRIYVFHCEF 320
Cdd:cd01530   1 LKRISPETLARLLQGKYDNFFDK---YIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFldKPGVASKKKRRVLIFHCEF 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 7298278  321 SSERGPKLLRYLRSNDRSQHTHNYPALDYPELYILHNGYKEFF 363
Cdd:cd01530  78 SSKRGPRMARHLRNLDRELNSNRYPLLYYPEIYILEGGYKNFF 120
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
224-397 1.10e-36

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 139.02  E-value: 1.10e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7298278  224 DLSKPCTLPCLATGIRHRD-LKTISSDTLARLIQGEFDEqlgSQGGYEIIDCRYPYEFLGGHIRGAKNLYTRGQIQEAFp 302
Cdd:COG5105 221 SFSNGEVFPLPTLGPGKSDsIQRISVETLKQVLEGMYNI---DFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLF- 296

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7298278  303 tLTSNQENRRIYVFHCEFSSERGPKLLRYLRSNDRSQHTHNYPALDYPELYILHNGYKEFFGLYSQLCQPSQYVPMLAPA 382
Cdd:COG5105 297 -RHKPLTHPRALIFHCEFSSHRAPRLAQHLRNMDRMKNPDHYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTMNNAE 375

                       170       180
                ....*....|....*....|....*.
gi 7298278  383 HN-------DEFR----YFRAKTKSW 397
Cdd:COG5105 376 LDyrclykmDKFRrnkkFFATKNNSF 401
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 243-363 1.04e-16

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: 75.52  E-value: 1.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7298278  243 LKTISSDTLARLIQGEFDEQLGSqggYEIIDCRYPyEFLGGHIRGAKNL------YTRGQIQEAFptltsNQENRRIYVF 316
Cdd:cd01443   1 LKYISPEELVALLENSDSNAGKD---FVVVDLRRD-DYEGGHIKGSINLpaqscyQTLPQVYALF-----SLAGVKLAIF 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 7298278  317 HCEFSSERGPKLLRYLRSNDRSqhthnyPALDYPELYILHNGYKEFF 363
Cdd:cd01443  72 YCGSSQGRGPRAARWFADYLRK------VGESLPKSYILTGGIKAWY 112
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 265-363 4.76e-15

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: 70.57  E-value: 4.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7298278     265 SQGGYEIIDCRYPYEFLGGHIRGAKNL----------YTRGQIQEAFPTLTSNQENRRIyVFHCeFSSERGPKLLRYLRS 334
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIplselldrrgELDILEFEELLKRLGLDKDKPV-VVYC-RSGNRSAKAAWLLRE 78

                           90       100
                   ....*....|....*....|....*....
gi 7298278     335 ndrsqhthnypaLDYPELYILHNGYKEFF 363
Cdd:smart00450  79 ------------LGFKNVYLLDGGYKEWS 95
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 266-362 9.66e-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: 55.18  E-value: 9.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7298278    266 QGGYEIIDCRYPYEFLGGHIRGAKNL------YTRGQIQEAFPTLTSNQENRRIyVFHCEfSSERGPKLLRYLRsndrsq 339
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVplsslsLPPLPLLELLEKLLELLKDKPI-VVYCN-SGNRAAAAAALLK------ 74

                          90       100
                  ....*....|....*....|...
gi 7298278    340 hthnypALDYPELYILHNGYKEF 362
Cdd:pfam00581  75 ------ALGYKNVYVLDGGFEAW 91
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 243-359 1.58e-09

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: 55.11  E-value: 1.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7298278  243 LKTISSDTLARLIQGefdeqlgSQGGYEIIDCRyPYEFLGGHIRGAKNlYTRGQIQEAFPTLTSNQENRRI--YVFHCEF 320
Cdd:cd01531   1 VSYISPAQLKGWIRN-------GRPPFQVVDVR-DEDYAGGHIKGSWH-YPSTRFKAQLNQLVQLLSGSKKdtVVFHCAL 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 7298278  321 SSERGP----KLLRYLRSNDRSQhthnypalDYPELYILHNGY 359
Cdd:cd01531  72 SQVRGPsaarKFLRYLDEEDLET--------SKFEVYVLHGGF 106
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 242-361 1.81e-08

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: 51.89  E-value: 1.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7298278  242 DLKTISSDTLARLIQgefdeqlgsQGGYEIIDCRYPYEFLGGHIRGAKNLyTRGQIQEAFPTLTSNQEnrriYVFHCEfS 321
Cdd:COG0607   2 SVKEISPAELAELLE---------SEDAVLLDVREPEEFAAGHIPGAINI-PLGELAERLDELPKDKP----IVVYCA-S 66

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 7298278  322 SERGPKLLRYLRsndrsqhthnypALDYPELYILHNGYKE 361
Cdd:COG0607  67 GGRSAQAAALLR------------RAGYTNVYNLAGGIEA 94
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 262-362 5.98e-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: 47.29  E-value: 5.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7298278  262 QLGSQGGYEIIDCRYPYEFLGGHIRGAKNLyTRGQIQEAFPTLTSNQEnrRIYVFHCEfSSERGPKLLRYLRsndrsqht 341
Cdd:cd00158   4 ELLDDEDAVLLDVREPEEYAAGHIPGAINI-PLSELEERAALLELDKD--KPIVVYCR-SGNRSARAAKLLR-------- 71

                        90       100
                ....*....|....*....|.
gi 7298278  342 hnypALDYPELYILHNGYKEF 362
Cdd:cd00158  72 ----KAGGTNVYNLEGGMLAW 88
 
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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