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Conserved domains on  [gi|2462502517|ref|XP_054189978|]
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dual specificity protein phosphatase 10 isoform X2 [Homo sapiens]

Protein Classification

DSP_MapKP domain-containing protein( domain architecture ID 10106634)

DSP_MapKP domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 149-271 4.42e-41

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: 138.57  E-value: 4.42e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502517 149 IIYPNDLAKKMTKCSKshlpsqGPVIIDCRPFMEYNKSHIQGAVHINCAdKISRRRLQQGKITVLDLISCREGKDSFKRI 228
Cdd:cd01446     1 TIDCAWLAALLREGGE------RLLLLDCRPFLEYSSSHIRGAVNVCCP-TILRRRLQGGKILLQQLLSCPEDRDRLRRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462502517 229 FSKEIIVYDENTNEPSRVMPSQPLHIVLESLKR---EGKEPLVLKG 271
Cdd:cd01446    74 ESLAVVVYDESSSDRERLREDSTAESVLGKLLRklqEGCSVYLLKG 119
 
Name Accession Description Interval E-value
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 149-271 4.42e-41

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: 138.57  E-value: 4.42e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502517 149 IIYPNDLAKKMTKCSKshlpsqGPVIIDCRPFMEYNKSHIQGAVHINCAdKISRRRLQQGKITVLDLISCREGKDSFKRI 228
Cdd:cd01446     1 TIDCAWLAALLREGGE------RLLLLDCRPFLEYSSSHIRGAVNVCCP-TILRRRLQGGKILLQQLLSCPEDRDRLRRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462502517 229 FSKEIIVYDENTNEPSRVMPSQPLHIVLESLKR---EGKEPLVLKG 271
Cdd:cd01446    74 ESLAVVVYDESSSDRERLREDSTAESVLGKLLRklqEGCSVYLLKG 119
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 170-238 2.51e-09

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: 53.62  E-value: 2.51e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462502517  170 QGPVIIDCRPFMEYNKSHIQGAVHINCADKISRRRLQQGKITVLDLISCREGKDsfkrifsKEIIVYDE 238
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLGLDKD-------KPVVVYCR 64
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 169-271 4.34e-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: 52.87  E-value: 4.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502517 169 SQGPVIIDCRPFMEYNKSHIQGAVHINCADkisrrrLQQGKITVLDLIscregKDSFKRIFSKEIIVYDENTNEPSRvmp 248
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSS------LSLPPLPLLELL-----EKLLELLKDKPIVVYCNSGNRAAA--- 68

                          90       100
                  ....*....|....*....|....
gi 2462502517 249 sqplhiVLESLKREG-KEPLVLKG 271
Cdd:pfam00581  69 ------AAALLKALGyKNVYVLDG 86
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 145-194 3.65e-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: 44.96  E-value: 3.65e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462502517 145 ASIKIIYPNDLAKKMTkcskshlpSQGPVIIDCRPFMEYNKSHIQGAVHI 194
Cdd:COG0607     1 ASVKEISPAELAELLE--------SEDAVLLDVREPEEFAAGHIPGAINI 42
 
Name Accession Description Interval E-value
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 149-271 4.42e-41

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: 138.57  E-value: 4.42e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502517 149 IIYPNDLAKKMTKCSKshlpsqGPVIIDCRPFMEYNKSHIQGAVHINCAdKISRRRLQQGKITVLDLISCREGKDSFKRI 228
Cdd:cd01446     1 TIDCAWLAALLREGGE------RLLLLDCRPFLEYSSSHIRGAVNVCCP-TILRRRLQGGKILLQQLLSCPEDRDRLRRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462502517 229 FSKEIIVYDENTNEPSRVMPSQPLHIVLESLKR---EGKEPLVLKG 271
Cdd:cd01446    74 ESLAVVVYDESSSDRERLREDSTAESVLGKLLRklqEGCSVYLLKG 119
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 170-238 2.51e-09

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: 53.62  E-value: 2.51e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462502517  170 QGPVIIDCRPFMEYNKSHIQGAVHINCADKISRRRLQQGKITVLDLISCREGKDsfkrifsKEIIVYDE 238
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLGLDKD-------KPVVVYCR 64
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 169-271 4.34e-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: 52.87  E-value: 4.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502517 169 SQGPVIIDCRPFMEYNKSHIQGAVHINCADkisrrrLQQGKITVLDLIscregKDSFKRIFSKEIIVYDENTNEPSRvmp 248
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSS------LSLPPLPLLELL-----EKLLELLKDKPIVVYCNSGNRAAA--- 68

                          90       100
                  ....*....|....*....|....
gi 2462502517 249 sqplhiVLESLKREG-KEPLVLKG 271
Cdd:pfam00581  69 ------AAALLKALGyKNVYVLDG 86
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 145-194 3.65e-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: 44.96  E-value: 3.65e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462502517 145 ASIKIIYPNDLAKKMTkcskshlpSQGPVIIDCRPFMEYNKSHIQGAVHI 194
Cdd:COG0607     1 ASVKEISPAELAELLE--------SEDAVLLDVREPEEFAAGHIPGAINI 42
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 164-224 5.95e-05

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: 40.75  E-value: 5.95e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462502517 164 KSHLPSQGPVIIDCRPFMEYNKSHIQGAVHI---NCADKISRRRLQQGKITVLdliSCREGKDS 224
Cdd:cd00158     3 KELLDDEDAVLLDVREPEEYAAGHIPGAINIplsELEERAALLELDKDKPIVV---YCRSGNRS 63
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 164-241 1.81e-04

3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 42.08  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502517 164 KSHLPSQGPVIIDCRPFM-----EYNKSHIQGAVHINCADKISRRRlQQGKITVLDliscregKDSFKRIFSK------- 231
Cdd:COG2897     2 AAHLDDPDVVILDVRWDLpdgraAYEAGHIPGAVFLDLDTDLSDPR-SPGRHPLPS-------PEAFAALLGAlgisndt 73

                          90
                  ....*....|
gi 2462502517 232 EIIVYDENTN 241
Cdd:COG2897    74 TVVVYDDGGG 83
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 149-241 4.13e-04

Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the 1st repeat, which does not contain the catalytically active Cys residue. The role of the 1st repeat is uncertain, but it is believed to be involved in protein interaction.


Pssm-ID: 238725 [Multi-domain]  Cd Length: 122  Bit Score: 39.14  E-value: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502517 149 IIYPNDLAKkmtkcsksHLPSQGPVIIDCRPFM-------EYNKSHIQGAVHINCADKISRRRLQQGkitvlDLISCreg 221
Cdd:cd01448     1 LVSPDWLAE--------HLDDPDVRILDARWYLpdrdgrkEYLEGHIPGAVFFDLDEDLDDKSPGPH-----MLPSP--- 64

                          90       100
                  ....*....|....*....|....*..
gi 2462502517 222 kDSFKRIFSK-------EIIVYDENTN 241
Cdd:cd01448    65 -EEFAELLGSlgisnddTVVVYDDGGG 90
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 173-207 1.39e-03

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: 37.97  E-value: 1.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2462502517 173 VIIDCR-PFmEYNKSHIQGAVHINCADKISRRRLQQ 207
Cdd:cd01530    25 IIIDCRfPY-EYNGGHIKGAVNLSTKDELEEFFLDK 59
 
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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