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Conserved domains on  [gi|1983851324|gb|KAG3244708|]
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hypothetical protein PI124_g10530 [Phytophthora idaei]

Protein Classification

protein-tyrosine phosphatase family protein( domain architecture ID 13026123)

protein-tyrosine phosphatase family protein, similar to Saccharomyces cerevisiae OCA6 that is required for replication of Brome mosaic virus, but may be inactive as a protein-tyrosine phosphatase as it lacks the CxxxxxR catalytic motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PFA-DSP_Oca6 cd17663
atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 6; ...
 9-172 2.63e-96

atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 6; Oxidant-induced cell-cycle arrest protein 6 (Oca6) is an atypical dual specificity phosphatase of unknown function. It belongs to a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds called plant and fungi atypical dual-specificity phosphatases (PFA-DSPs). Oca6 may be an inactive DSP-like protein as it lacks the CxxxxxR catalytic motif.


:

Pssm-ID: 350501 [Multi-domain]  Cd Length: 162  Bit Score: 279.57  E-value: 2.63e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324   9 IPPFRFSTVQQGLYRGAYPTLKNFRFLRRLGLKTLVSVIPEPPTSDLADFCANEKITLLHFYAEKFTSDNVTVSPATAAQ 88
Cdd:cd17663     1 IPPFRFATVEPGLYRGAYPRLKNFRFLRRLKLKTIVSLTPEPPTEDLANFCEAENITLIHISAEKFKKGKVPLSYSTVIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324  89 IVEILVQKKNLPLYIHCLDGSNVTGIVVMILRKLQNWTKLATVSEFCRFTRDhgIEKDESEYLAAFSEEIVVTADAPQWL 168
Cdd:cd17663    81 ILQLLIDKDNLPVYIHCLDGRHVTGLVVACLRKLQFWSSIAIFAEFLRFART--ISSEERAFIENFKGEIEVPANKPKWL 158


                  ....
gi 1983851324 169 WNGV 172
Cdd:cd17663   159 WGGV 162
 
Name Accession Description Interval E-value
PFA-DSP_Oca6 cd17663
atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 6; ...
 9-172 2.63e-96

atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 6; Oxidant-induced cell-cycle arrest protein 6 (Oca6) is an atypical dual specificity phosphatase of unknown function. It belongs to a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds called plant and fungi atypical dual-specificity phosphatases (PFA-DSPs). Oca6 may be an inactive DSP-like protein as it lacks the CxxxxxR catalytic motif.


Pssm-ID: 350501 [Multi-domain]  Cd Length: 162  Bit Score: 279.57  E-value: 2.63e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324   9 IPPFRFSTVQQGLYRGAYPTLKNFRFLRRLGLKTLVSVIPEPPTSDLADFCANEKITLLHFYAEKFTSDNVTVSPATAAQ 88
Cdd:cd17663     1 IPPFRFATVEPGLYRGAYPRLKNFRFLRRLKLKTIVSLTPEPPTEDLANFCEAENITLIHISAEKFKKGKVPLSYSTVIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324  89 IVEILVQKKNLPLYIHCLDGSNVTGIVVMILRKLQNWTKLATVSEFCRFTRDhgIEKDESEYLAAFSEEIVVTADAPQWL 168
Cdd:cd17663    81 ILQLLIDKDNLPVYIHCLDGRHVTGLVVACLRKLQFWSSIAIFAEFLRFART--ISSEERAFIENFKGEIEVPANKPKWL 158


                  ....
gi 1983851324 169 WNGV 172
Cdd:cd17663   159 WGGV 162
Y_phosphatase2 pfam03162
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 8-158 4.42e-42

Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 families.


Pssm-ID: 397328 [Multi-domain]  Cd Length: 150  Bit Score: 140.96  E-value: 4.42e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324   8 LIPPFRFSTVQQGLYRGAYPTLKNFRFLRRLGLKTLVSVIPEPPTSDLADFCANEKITLLHFYAEKFTSDNVTVSPATAA 87
Cdd:pfam03162   1 LVPPLNFSPVEPGLYRSSYPRANNFSFLRSLRLKTIISLSPEPYPQDNLQFLESEHIKLYHIHMEGNKDPFVNIPSHLLR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1983851324  88 QIVEILVQKKNLPLYIHCLDGSNVTGIVVMILRKLQNWTKLATVSEFCRFTRDHGIEKDEsEYLAAFSEEI 158
Cdd:pfam03162  81 RALKLLLNKDNYPVLIHCNRGKHRTGLVIGCLRKLQKWSLASILNEYRRFSGSKARIVDE-EFIEIFDSEL 150
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
21-158 4.51e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 39.57  E-value: 4.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324  21 LYRGAYPTLKNFRfLRRLGLKTLVSVIPEPPtsDLADFCANEKITLLHFYaekfTSDNVTVSPATAAQIVEILVQ--KKN 98
Cdd:COG2453     8 LAGGPLPGGGEAD-LKREGIDAVVSLTEEEE--LLLGLLEEAGLEYLHLP----IPDFGAPDDEQLQEAVDFIDEalREG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1983851324  99 LPLYIHCLDGSNVTGIVV---MILRKLQNWTKLATVSEfcrfTRDHGIEKDE-SEYLAAFSEEI 158
Cdd:COG2453    81 KKVLVHCRGGIGRTGTVAaayLVLLGLSAEEALARVRA----ARPGAVETPAqRAFLERFAKRL 140
 
Name Accession Description Interval E-value
PFA-DSP_Oca6 cd17663
atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 6; ...
 9-172 2.63e-96

atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 6; Oxidant-induced cell-cycle arrest protein 6 (Oca6) is an atypical dual specificity phosphatase of unknown function. It belongs to a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds called plant and fungi atypical dual-specificity phosphatases (PFA-DSPs). Oca6 may be an inactive DSP-like protein as it lacks the CxxxxxR catalytic motif.


Pssm-ID: 350501 [Multi-domain]  Cd Length: 162  Bit Score: 279.57  E-value: 2.63e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324   9 IPPFRFSTVQQGLYRGAYPTLKNFRFLRRLGLKTLVSVIPEPPTSDLADFCANEKITLLHFYAEKFTSDNVTVSPATAAQ 88
Cdd:cd17663     1 IPPFRFATVEPGLYRGAYPRLKNFRFLRRLKLKTIVSLTPEPPTEDLANFCEAENITLIHISAEKFKKGKVPLSYSTVIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324  89 IVEILVQKKNLPLYIHCLDGSNVTGIVVMILRKLQNWTKLATVSEFCRFTRDhgIEKDESEYLAAFSEEIVVTADAPQWL 168
Cdd:cd17663    81 ILQLLIDKDNLPVYIHCLDGRHVTGLVVACLRKLQFWSSIAIFAEFLRFART--ISSEERAFIENFKGEIEVPANKPKWL 158


                  ....
gi 1983851324 169 WNGV 172
Cdd:cd17663   159 WGGV 162
Y_phosphatase2 pfam03162
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 8-158 4.42e-42

Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 families.


Pssm-ID: 397328 [Multi-domain]  Cd Length: 150  Bit Score: 140.96  E-value: 4.42e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324   8 LIPPFRFSTVQQGLYRGAYPTLKNFRFLRRLGLKTLVSVIPEPPTSDLADFCANEKITLLHFYAEKFTSDNVTVSPATAA 87
Cdd:pfam03162   1 LVPPLNFSPVEPGLYRSSYPRANNFSFLRSLRLKTIISLSPEPYPQDNLQFLESEHIKLYHIHMEGNKDPFVNIPSHLLR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1983851324  88 QIVEILVQKKNLPLYIHCLDGSNVTGIVVMILRKLQNWTKLATVSEFCRFTRDHGIEKDEsEYLAAFSEEI 158
Cdd:pfam03162  81 RALKLLLNKDNYPVLIHCNRGKHRTGLVIGCLRKLQKWSLASILNEYRRFSGSKARIVDE-EFIEIFDSEL 150
PFA-DSP_Siw14 cd14528
atypical dual specificity phosphatases similar to yeast Siw14; This subfamily contains ...
 8-138 9.11e-35

atypical dual specificity phosphatases similar to yeast Siw14; This subfamily contains Saccharomyces Siw14 and a novel phosphatase from the Arabidopsis thaliana gene locus At1g05000. Siw14, also known as Oca3, plays a role in actin filament organization and endocytosis. Siw14 has been shown to be an inositol pyrophosphate phosphatase, hydrolyzing the beta-phosphate from 5-diphosphoinositol pentakisphosphate (5PP-IP5or IP7). The At1g05000 protein, also called AtPFA-DSP1, has been shown to have highest activity toward olyphosphate (poly-P(12-13)) and deoxyribo- and ribonucleoside triphosphates, and less activity toward phosphoenolpyruvate, phosphotyrosine, phosphotyrosine-containing peptides, and phosphatidylinositols. This subfamily belongs to a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds called plant and fungi atypical dual-specificity phosphatases (PFA-DSPs).


Pssm-ID: 350377 [Multi-domain]  Cd Length: 148  Bit Score: 122.06  E-value: 9.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324   8 LIPPFRFSTVQQGLYRGAYPTLKNFRFLRRLGLKTLVSVIPEPPTSDLADFCANEKITLLHFYAEKFTSDNVTVSPATAA 87
Cdd:cd14528     2 LIPPLNFSMVDKGVYRSGYPNKKNFPFLRTLGLRSILYLCPEDYPESNLEFLKENGIKLFQFGIEGNKEPFVDIPEELIR 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1983851324  88 QIVEILVQKKNLPLYIHCLDGSNVTGIVVMILRKLQNWTKLATVSEFCRFT 138
Cdd:cd14528    82 DALKVLLDPRNHPVLIHCNKGKHRTGCLVGCLRKLQNWSLTSIFDEYRRFA 132
PFA-DSP cd14501
plant and fungi atypical dual-specificity phosphatase; Plant and fungi atypical ...
 9-138 2.94e-33

plant and fungi atypical dual-specificity phosphatase; Plant and fungi atypical dual-specificity phosphatases (PFA-DSPs) are a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds. They share structural similarity with atypical- and lipid phosphatase DSPs from mammals. The PFA-DSP group is composed of active as well as inactive phosphatases. The best characterized member is Saccharomyces Siw14, also known as Oca3, which plays a role in actin filament organization and endocytosis. Siw14 has been shown to be an inositol pyrophosphate phosphatase, hydrolyzing the beta-phosphate from 5-diphosphoinositol pentakisphosphate (5PP-IP5or IP7).


Pssm-ID: 350351 [Multi-domain]  Cd Length: 149  Bit Score: 118.17  E-value: 2.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324   9 IPPFRFSTVQQGLYRGAYPTLKNFRFLRRLGLKTLVSVIPEPPTSDLADFCANEKITLLHF----YAEKFTSDNVTVSPA 84
Cdd:cd14501     1 VPPLNFSIVEPGLYRSAYPTPANFPFLKTLGLKTIILLSPEPPPKPVLSFLTENGIKLIHLgmlsSKRADSVPWDPLAYE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1983851324  85 TAAQIVEILVQKKNLPLYIHCLDGSNVTGIVVMILRKLQNWTKLATVSEFCRFT 138
Cdd:cd14501    81 LVKRALEILLDKTNYPVLVHCSLGEHRTGVVVGCLRKLQGWSLASILDEYRLFA 134
PFA-DSP_unk cd18538
unknown subfamily of atypical dual-specificity phosphatases from fungi; This uncharacterized ...
 9-154 2.09e-27

unknown subfamily of atypical dual-specificity phosphatases from fungi; This uncharacterized subfamily belongs to the plant and fungi atypical dual-specificity phosphatases (PFA-DSPs) group of atypical DSPs that present in plants, fungi, kinetoplastids, and slime molds. They share structural similarity with atypical- and lipid phosphatase DSPs from mammals. The PFA-DSP group is composed of active as well as inactive phosphatases. This unknown subgroup contains the conserved the CxxxxxR catalytic motif present in active cysteine phosphatases.


Pssm-ID: 350514 [Multi-domain]  Cd Length: 145  Bit Score: 103.22  E-value: 2.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324   9 IPPFRFSTVQQGLYRGAYPTLKNFRFLRRLGLKTLVSVIPEPPTSDLADFCANEKITllHFYAEKFTSDNVTVS--PATA 86
Cdd:cd18538     1 GLPPNFGVVVPGVYRSSFPKPENFGFLKSLGLRTILTLVQEEYSPEFLNFLRENGIQ--HFHIAMLGNKDPKVSipDHTM 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1983851324  87 AQIVEILVQKKNLPLYIHCLDGSNVTGIVVMILRKLQNWTKLATVSEFCRFTRDHGIEKDEsEYLAAF 154
Cdd:cd18538    79 NRILRIILDKENHPILVHCNKGKHRTGCVIACFRKLQGWDVENVLEEYLSYAHPKSRDLDE-EYIENF 145
PFA-DSP_Oca1 cd14531
atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 1; ...
 8-138 3.48e-27

atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 1; Oxidant-induced cell-cycle arrest protein 1 (Oca1) is an atypical dual specificity phosphatase whose gene is required for G1 arrest in response to the lipid oxidation product linoleic acid hydroperoxide. It may function in linking growth, stress responses, and the cell cycle. Oca1 belongs to a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds called plant and fungi atypical dual-specificity phosphatases (PFA-DSPs).


Pssm-ID: 350379 [Multi-domain]  Cd Length: 149  Bit Score: 102.76  E-value: 3.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324   8 LIPPFRFSTVQQGLYRGAYPTLKNFRFLRRLGLKTLVSVIPEPPTSDLADFCANEKITlLHFYAEKFT--SDNVTVSPAT 85
Cdd:cd14531     2 FIPPLNFGMVEEDLYRSGQPTPINFPFLERLKLKTIIYLAPDEPSDQFLEFCEDQNIN-LVHLGGDDSteSRQNPLSEEL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1983851324  86 AAQIVEILVQKKNLPLYIHCLDGSNVTGIVVMILRKLQNWTkLATVS-EFCRFT 138
Cdd:cd14531    81 VLAALHIILDPDNYPLLVMCNLGRHRTGTVVGCLRKLQRWN-LSSIFeEYRRFA 133
PFA-DSP_Oca2 cd17661
atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 2; ...
 9-154 5.03e-22

atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 2; Oxidant-induced cell-cycle arrest protein 2 (Oca2) is an atypical dual specificity phosphatase of unknown function. It has been identified as a putative negative regulator acting on cell wall integrity and mating MAPK pathways in yeast. It belongs to a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds called plant and fungi atypical dual-specificity phosphatases (PFA-DSPs). Oca2 may be an inactive DSP-like protein as it lacks the CxxxxxR catalytic motif.


Pssm-ID: 350499 [Multi-domain]  Cd Length: 146  Bit Score: 89.00  E-value: 5.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324   9 IPPFRFSTVQQGLYRGAYPTLKNFRFLRRLGLKTLVSV-IPEPPTSDLADFCANEKITLLHFYAEKFTSDNVTVSPATAA 87
Cdd:cd17661     1 VPPLNFSLVADGIYRSGHPMPINYPFLKQLNLKTIIYLgDKDPYRQDYLDFLQSQGIELYYFDFSSSSEPFTEEDQERME 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1983851324  88 QIVEILVQKKNLPLYIHCLDGSNVTGIVVMILRKLQNWTKLATV-SEFCRFTRDHGiEKDeSEYLAAF 154
Cdd:cd17661    81 QALKLLLDKRNYPILVHSNKGKHRVGVLVGIMRKLLQGWCLAGIfDEYGRFAGGKG-ETD-LEFIETF 146
PFA-DSP_Oca4 cd17662
atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 4; ...
 8-138 1.10e-13

atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 4; Oxidant-induced cell-cycle arrest protein 4 (Oca4) is an atypical dual specificity phosphatase of unknown function. It belongs to a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds called plant and fungi atypical dual-specificity phosphatases (PFA-DSPs). Oca4 may be an inactive DSP-like protein as it lacks the CxxxxxR catalytic motif.


Pssm-ID: 350500 [Multi-domain]  Cd Length: 177  Bit Score: 67.60  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324   8 LIPPFRFSTVQQGLYRGAYPTLKNFRFLRRLGLKTLVSVIPEPPTSDLADFCANEKITLLHFYAEKFTSDNVTVSPATAA 87
Cdd:cd17662     1 LVPPANFGIVEPGIYRCSKLSTLNFSFLETLNLKTIVFVGGQEPSKFFKEFFERNNIELIVLRDADFSNHHHPGKNSSSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324  88 QI------------------------------VEILVQKKNLPLYIHCLDGSNVTGIVVMILRKLQNWTKLATVSEFCRF 137
Cdd:cd17662    81 KLqgntdvndlepintnyhlwkndldmlikstLLQRIFEKNLPVLNHNKLLVDKTSTVIGCLRRIQKWNFSSIINEYRRF 160


                  .
gi 1983851324 138 T 138
Cdd:cd17662   161 A 161
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 20-156 1.16e-07

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 50.07  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324  20 GLYRGAYPTLK-NFRFLRRLGLKTLVSVI-PEPPTSDLADFCANEKITLLHFyaeKFTSDNVTVSpatAAQIVEILVQKK 97
Cdd:cd14529    13 VLYRSAQLSPDeDRALLKKLGIKTVIDLRgADERAASEEAAAKIDGVKYVNL---PLSATRPTES---DVQSFLLIMDLK 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1983851324  98 N--LPLYIHCLDGSNVTGIVVMILRKLQNWTKLATVSEFCRFTR----------DHGIEKDESEYLAAFSE 156
Cdd:cd14529    87 LapGPVLIHCKHGKDRTGLVSALYRIVYGGSKEEANEDYRLSNRhleglrsgiaLDSKGGVKGRYLAAYFE 157
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
21-158 4.51e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 39.57  E-value: 4.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324  21 LYRGAYPTLKNFRfLRRLGLKTLVSVIPEPPtsDLADFCANEKITLLHFYaekfTSDNVTVSPATAAQIVEILVQ--KKN 98
Cdd:COG2453     8 LAGGPLPGGGEAD-LKREGIDAVVSLTEEEE--LLLGLLEEAGLEYLHLP----IPDFGAPDDEQLQEAVDFIDEalREG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1983851324  99 LPLYIHCLDGSNVTGIVV---MILRKLQNWTKLATVSEfcrfTRDHGIEKDE-SEYLAAFSEEI 158
Cdd:COG2453    81 KKVLVHCRGGIGRTGTVAaayLVLLGLSAEEALARVRA----ARPGAVETPAqRAFLERFAKRL 140
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 14-113 2.15e-03

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 37.64  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324  14 FSTVQQGLYRG-AYPTL-KNFRFLRRLGLKTLVSVIPEPPTSDLaDFCANekITLLHFYAEKFTsdnvtvsPATAAQIVE 91
Cdd:cd14504     1 FSWVIPGKLAGmAFPRLpEHYAYLNENGIRHVVTLTEEPPPEHS-DTCPG--LRYHHIPIEDYT-------PPTLEQIDE 70

                          90       100
                  ....*....|....*....|....*..
gi 1983851324  92 IL-----VQKKNLPLYIHCLDGSNVTG 113
Cdd:cd14504    71 FLdiveeANAKNEAVLVHCLAGKGRTG 97
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 15-126 6.25e-03

dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in typical and atypical dual-specificity phosphatases (DUSPs), which function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Typical DUSPs, also called mitogen-activated protein kinase (MAPK) phosphatases (MKPs), deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Atypical DUSPs contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Also included in this family are dual specificity phosphatase-like domains of catalytically inactive members such as serine/threonine/tyrosine-interacting protein (STYX) and serine/threonine/tyrosine interacting like 1 (STYXL1), as well as active phosphatases with substrates that are not phosphoproteins such as PTP localized to the mitochondrion 1 (PTPMT1), which is a lipid phosphatase, and laforin, which is a glycogen phosphatase.


Pssm-ID: 350348 [Multi-domain]  Cd Length: 135  Bit Score: 35.98  E-value: 6.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983851324  15 STVQQGLYRGAYPTLKNFRFLRRLGLKTLVSVIPEPPTSDladfcANEKITLLHFYAEKFTSDNVTVS-PATAAQIVEIL 93
Cdd:cd14498     2 SEILPGLYLGSLDAAQDKELLKKLGITHILNVAGEPPPNK-----FPDGIKYLRIPIEDSPDEDILSHfEEAIEFIEEAL 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1983851324  94 VQKKNlpLYIHCLDG---SnVTgIVVMILRKLQNWT 126
Cdd:cd14498    77 KKGGK--VLVHCQAGvsrS-AT-IVIAYLMKKYGWS 108
 
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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