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Conserved domains on  [gi|1002297294|ref|XP_015612074|]
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probable tyrosine-protein phosphatase DSP4 isoform X2 [Oryza sativa Japonica Group]

Protein Classification

protein-tyrosine phosphatase Siw14 family protein( domain architecture ID 12998404)

protein-tyrosine phosphatase Siw14 family protein that contains a protein-tyrosine phosphatase (PTP) domain similar to the atypical dual specificity phosphatase (DSP) Saccharomyces serevisiae Siw14 that functions as an inositol pyrophosphate phosphatase, hydrolyzing the beta-phosphate from 5-diphosphoinositol pentakisphosphate

CATH:  3.90.190.10
EC:  3.1.3.48
Gene Ontology:  GO:0004721|GO:0004725|GO:0006470
PubMed:  27514797|17057753
SCOP:  3000304

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PFA-DSP_Siw14 cd14528
atypical dual specificity phosphatases similar to yeast Siw14; This subfamily contains ...
 62-209 3.77e-99

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: 284.23  E-value: 3.77e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  62 LLVPPLNFAMVDHGVYRSGFPDISNLPFVESLRLRSVLCLCPEPYPEANQEFLRAHGIRLFQFGIDGSKEPFVNIPEDRI 141
Cdd:cd14528     1 LLIPPLNFSMVDKGVYRSGYPNKKNFPFLRTLGLRSILYLCPEDYPESNLEFLKENGIKLFQFGIEGNKEPFVDIPEELI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002297294 142 REALKVVLDVANHPVLIHCKRGKHRTGCVVGCLRKLQRWCLTSIFDEYQRFAAAKARVSDLRFMELFD 209
Cdd:cd14528    81 RDALKVLLDPRNHPVLIHCNKGKHRTGCLVGCLRKLQNWSLTSIFDEYRRFAGPKARMLDQQFIELFD 148
 
Name Accession Description Interval E-value
PFA-DSP_Siw14 cd14528
atypical dual specificity phosphatases similar to yeast Siw14; This subfamily contains ...
 62-209 3.77e-99

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: 284.23  E-value: 3.77e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  62 LLVPPLNFAMVDHGVYRSGFPDISNLPFVESLRLRSVLCLCPEPYPEANQEFLRAHGIRLFQFGIDGSKEPFVNIPEDRI 141
Cdd:cd14528     1 LLIPPLNFSMVDKGVYRSGYPNKKNFPFLRTLGLRSILYLCPEDYPESNLEFLKENGIKLFQFGIEGNKEPFVDIPEELI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002297294 142 REALKVVLDVANHPVLIHCKRGKHRTGCVVGCLRKLQRWCLTSIFDEYQRFAAAKARVSDLRFMELFD 209
Cdd:cd14528    81 RDALKVLLDPRNHPVLIHCNKGKHRTGCLVGCLRKLQNWSLTSIFDEYRRFAGPKARMLDQQFIELFD 148
Y_phosphatase2 pfam03162
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 63-212 1.33e-73

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


Pssm-ID: 397328 [Multi-domain]  Cd Length: 150  Bit Score: 219.93  E-value: 1.33e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  63 LVPPLNFAMVDHGVYRSGFPDISNLPFVESLRLRSVLCLCPEPYPEANQEFLRAHGIRLFQFGIDGSKEPFVNIPEDRIR 142
Cdd:pfam03162   1 LVPPLNFSPVEPGLYRSSYPRANNFSFLRSLRLKTIISLSPEPYPQDNLQFLESEHIKLYHIHMEGNKDPFVNIPSHLLR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294 143 EALKVVLDVANHPVLIHCKRGKHRTGCVVGCLRKLQRWCLTSIFDEYQRFAAAKARVSDLRFMELFDISS 212
Cdd:pfam03162  81 RALKLLLNKDNYPVLIHCNRGKHRTGLVIGCLRKLQKWSLASILNEYRRFSGSKARIVDEEFIEIFDSEL 150
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
84-174 1.30e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 49.20  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  84 ISNLPFVESLRLRS-----VLCLCPEPypEANQEFLRAHGIRLFQFGIdgskEPFVNIPEDRIREALKVVLD--VANHPV 156
Cdd:COG2453    10 GGPLPGGGEADLKRegidaVVSLTEEE--ELLLGLLEEAGLEYLHLPI----PDFGAPDDEQLQEAVDFIDEalREGKKV 83

                          90
                  ....*....|....*...
gi 1002297294 157 LIHCKRGKHRTGCVVGCL 174
Cdd:COG2453    84 LVHCRGGIGRTGTVAAAY 101
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
75-173 1.49e-05

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 43.43  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294   75 GVYRSGFPDISNLPFVESLRLRSVLCLCPEPYPEANQEFLRahgirlfqFGIDGSKEPFVNIPEDrIREALKVVLDVAN- 153
Cdd:smart00195   7 HLYLGSYSDALNLALLKKLGITHVINVTNEVPNYNGSDFTY--------LGVPIDDNTETKISPY-FPEAVEFIEDAESk 77

                           90       100
                   ....*....|....*....|.
gi 1002297294  154 -HPVLIHCKRGKHRTGCVVGC 173
Cdd:smart00195  78 gGKVLVHCQAGVSRSATLIIA 98
 
Name Accession Description Interval E-value
PFA-DSP_Siw14 cd14528
atypical dual specificity phosphatases similar to yeast Siw14; This subfamily contains ...
 62-209 3.77e-99

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: 284.23  E-value: 3.77e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  62 LLVPPLNFAMVDHGVYRSGFPDISNLPFVESLRLRSVLCLCPEPYPEANQEFLRAHGIRLFQFGIDGSKEPFVNIPEDRI 141
Cdd:cd14528     1 LLIPPLNFSMVDKGVYRSGYPNKKNFPFLRTLGLRSILYLCPEDYPESNLEFLKENGIKLFQFGIEGNKEPFVDIPEELI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002297294 142 REALKVVLDVANHPVLIHCKRGKHRTGCVVGCLRKLQRWCLTSIFDEYQRFAAAKARVSDLRFMELFD 209
Cdd:cd14528    81 RDALKVLLDPRNHPVLIHCNKGKHRTGCLVGCLRKLQNWSLTSIFDEYRRFAGPKARMLDQQFIELFD 148
Y_phosphatase2 pfam03162
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 63-212 1.33e-73

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


Pssm-ID: 397328 [Multi-domain]  Cd Length: 150  Bit Score: 219.93  E-value: 1.33e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  63 LVPPLNFAMVDHGVYRSGFPDISNLPFVESLRLRSVLCLCPEPYPEANQEFLRAHGIRLFQFGIDGSKEPFVNIPEDRIR 142
Cdd:pfam03162   1 LVPPLNFSPVEPGLYRSSYPRANNFSFLRSLRLKTIISLSPEPYPQDNLQFLESEHIKLYHIHMEGNKDPFVNIPSHLLR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294 143 EALKVVLDVANHPVLIHCKRGKHRTGCVVGCLRKLQRWCLTSIFDEYQRFAAAKARVSDLRFMELFDISS 212
Cdd:pfam03162  81 RALKLLLNKDNYPVLIHCNRGKHRTGLVIGCLRKLQKWSLASILNEYRRFSGSKARIVDEEFIEIFDSEL 150
PFA-DSP cd14501
plant and fungi atypical dual-specificity phosphatase; Plant and fungi atypical ...
 64-208 1.51e-67

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: 204.45  E-value: 1.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  64 VPPLNFAMVDHGVYRSGFPDISNLPFVESLRLRSVLCLCPEPYPEANQEFLRAHGIRLFQFGIDGSKEPF----VNIPED 139
Cdd:cd14501     1 VPPLNFSIVEPGLYRSAYPTPANFPFLKTLGLKTIILLSPEPPPKPVLSFLTENGIKLIHLGMLSSKRADsvpwDPLAYE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002297294 140 RIREALKVVLDVANHPVLIHCKRGKHRTGCVVGCLRKLQRWCLTSIFDEYQRFAAAKARVSDLRFMELF 208
Cdd:cd14501    81 LVKRALEILLDKTNYPVLVHCSLGEHRTGVVVGCLRKLQGWSLASILDEYRLFAGSKERYVDEQFIELF 149
PFA-DSP_unk cd18538
unknown subfamily of atypical dual-specificity phosphatases from fungi; This uncharacterized ...
 65-208 4.22e-63

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: 192.97  E-value: 4.22e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  65 PPLNFAMVDHGVYRSGFPDISNLPFVESLRLRSVLCLCPEPYPEANQEFLRAHGIRLFQFGIDGSKEPFVNIPEDRIREA 144
Cdd:cd18538     2 LPPNFGVVVPGVYRSSFPKPENFGFLKSLGLRTILTLVQEEYSPEFLNFLRENGIQHFHIAMLGNKDPKVSIPDHTMNRI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002297294 145 LKVVLDVANHPVLIHCKRGKHRTGCVVGCLRKLQRWCLTSIFDEYQRFAAAKARVSDLRFMELF 208
Cdd:cd18538    82 LRIILDKENHPILVHCNKGKHRTGCVIACFRKLQGWDVENVLEEYLSYAHPKSRDLDEEYIENF 145
PFA-DSP_Oca1 cd14531
atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 1; ...
 63-209 4.66e-53

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: 167.47  E-value: 4.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  63 LVPPLNFAMVDHGVYRSGFPDISNLPFVESLRLRSVLCLCPEPYPEANQEFLRAHGIRLFQFGIDGSKEPFVN-IPEDRI 141
Cdd:cd14531     2 FIPPLNFGMVEEDLYRSGQPTPINFPFLERLKLKTIIYLAPDEPSDQFLEFCEDQNINLVHLGGDDSTESRQNpLSEELV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002297294 142 REALKVVLDVANHPVLIHCKRGKHRTGCVVGCLRKLQRWCLTSIFDEYQRFAAAKARVSDLRFMELFD 209
Cdd:cd14531    82 LAALHIILDPDNYPLLVMCNLGRHRTGTVVGCLRKLQRWNLSSIFEEYRRFAGSKVRLLNEQFIELFD 149
PFA-DSP_Oca2 cd17661
atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 2; ...
 64-208 5.61e-48

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: 154.48  E-value: 5.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  64 VPPLNFAMVDHGVYRSGFPDISNLPFVESLRLRSVLCLC-PEPYPEANQEFLRAHGIRLFQFGIDGSKEPFVNIPEDRIR 142
Cdd:cd17661     1 VPPLNFSLVADGIYRSGHPMPINYPFLKQLNLKTIIYLGdKDPYRQDYLDFLQSQGIELYYFDFSSSSEPFTEEDQERME 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002297294 143 EALKVVLDVANHPVLIHCKRGKHRTGCVVGCLRK-LQRWCLTSIFDEYQRFAAAKARVsDLRFMELF 208
Cdd:cd17661    81 QALKLLLDKRNYPILVHSNKGKHRVGVLVGIMRKlLQGWCLAGIFDEYGRFAGGKGET-DLEFIETF 146
PFA-DSP_Oca6 cd17663
atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 6; ...
 64-193 1.20e-36

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: 126.26  E-value: 1.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  64 VPPLNFAMVDHGVYRSGFPDISNLPFVESLRLRSVLCLCPEPYPEANQEFLRAHGIRLFQFGIDGSKEPFVNIPEDRIRE 143
Cdd:cd17663     1 IPPFRFATVEPGLYRGAYPRLKNFRFLRRLKLKTIVSLTPEPPTEDLANFCEAENITLIHISAEKFKKGKVPLSYSTVIQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002297294 144 ALKVVLDVANHPVLIHCKRGKHRTGCVVGCLRKLQRWCLTSIFDEYQRFA 193
Cdd:cd17663    81 ILQLLIDKDNLPVYIHCLDGRHVTGLVVACLRKLQFWSSIAIFAEFLRFA 130
PFA-DSP_Oca4 cd17662
atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 4; ...
 63-209 1.76e-25

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: 97.65  E-value: 1.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  63 LVPPLNFAMVDHGVYRSGFPDISNLPFVESLRLRSVLCLCPEPYPEANQEFLRAHGIRLFQFGI---------------- 126
Cdd:cd17662     1 LVPPANFGIVEPGIYRCSKLSTLNFSFLETLNLKTIVFVGGQEPSKFFKEFFERNNIELIVLRDadfsnhhhpgknsssg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294 127 --DGSKEPFVNIPE------------DRIREALKVVLDVANHPVLIHCKRGKHRTGCVVGCLRKLQRWCLTSIFDEYQRF 192
Cdd:cd17662    81 klQGNTDVNDLEPIntnyhlwkndldMLIKSTLLQRIFEKNLPVLNHNKLLVDKTSTVIGCLRRIQKWNFSSIINEYRRF 160

                         170
                  ....*....|....*..
gi 1002297294 193 AAAKARVSDLRFMELFD 209
Cdd:cd17662   161 AGKSSNYFAETFLELFD 177
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 99-204 2.91e-11

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 58.52  E-value: 2.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  99 LCLCPEPYPEANQEFLRAHGIRLFqfgidgskepfVNIPEDRIREALKVVLDV--ANHPVLIHCKRGKHRTGCVVGCLR- 175
Cdd:cd14494    11 AGALPLSPLEADSRFLKQLGVTTI-----------VDLTLAMVDRFLEVLDQAekPGEPVLVHCKAGVGRTGTLVACYLv 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1002297294 176 KLQRWCLTSIFDEYQRF--AAAKARVSDLRF 204
Cdd:cd14494    80 LLGGMSAEEAVRIVRLIrpGGIPQTIEQLDF 110
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 68-175 1.46e-08

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: 51.99  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  68 NFAMV-DHGVYRSGFPDI-SNLPFVESLRLRSVLCLcPEPYPEANQEFLRAH--GIRLFQFGIDGskepfVNIPEDRIRE 143
Cdd:cd14529     5 NFRDVtPYVLYRSAQLSPdEDRALLKKLGIKTVIDL-RGADERAASEEAAAKidGVKYVNLPLSA-----TRPTESDVQS 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1002297294 144 ALKVVLDVANH-PVLIHCKRGKHRTGCVVGCLR 175
Cdd:cd14529    79 FLLIMDLKLAPgPVLIHCKHGKDRTGLVSALYR 111
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
84-174 1.30e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 49.20  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  84 ISNLPFVESLRLRS-----VLCLCPEPypEANQEFLRAHGIRLFQFGIdgskEPFVNIPEDRIREALKVVLD--VANHPV 156
Cdd:COG2453    10 GGPLPGGGEADLKRegidaVVSLTEEE--ELLLGLLEEAGLEYLHLPI----PDFGAPDDEQLQEAVDFIDEalREGKKV 83

                          90
                  ....*....|....*...
gi 1002297294 157 LIHCKRGKHRTGCVVGCL 174
Cdd:COG2453    84 LVHCRGGIGRTGTVAAAY 101
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 72-182 1.38e-06

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: 46.00  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  72 VDHGVYRSGFPDISNLPFVESLRLRSVLCLCPEPYPEANQEFLRAHGIRLFqfgiDGSKEP-FVNIPE--DRIREALKvv 148
Cdd:cd14498     4 ILPGLYLGSLDAAQDKELLKKLGITHILNVAGEPPPNKFPDGIKYLRIPIE----DSPDEDiLSHFEEaiEFIEEALK-- 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1002297294 149 ldvANHPVLIHCKRGKHRTGCVV-GCLRKLQRWCL 182
Cdd:cd14498    78 ---KGGKVLVHCQAGVSRSATIViAYLMKKYGWSL 109
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
75-173 1.49e-05

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 43.43  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294   75 GVYRSGFPDISNLPFVESLRLRSVLCLCPEPYPEANQEFLRahgirlfqFGIDGSKEPFVNIPEDrIREALKVVLDVAN- 153
Cdd:smart00195   7 HLYLGSYSDALNLALLKKLGITHVINVTNEVPNYNGSDFTY--------LGVPIDDNTETKISPY-FPEAVEFIEDAESk 77

                           90       100
                   ....*....|....*....|.
gi 1002297294  154 -HPVLIHCKRGKHRTGCVVGC 173
Cdd:smart00195  78 gGKVLVHCQAGVSRSATLIIA 98
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 79-173 1.63e-05

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: 43.42  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  79 SGFP-DISNLPFVESLRLRSVLCLCPEPYPEANQEFlraHGIRLFQFGIDGSKEPfvNIPEdrIREALKVVLDV--ANHP 155
Cdd:cd14504    12 MAFPrLPEHYAYLNENGIRHVVTLTEEPPPEHSDTC---PGLRYHHIPIEDYTPP--TLEQ--IDEFLDIVEEAnaKNEA 84

                          90
                  ....*....|....*...
gi 1002297294 156 VLIHCKRGKHRTGCVVGC 173
Cdd:cd14504    85 VLVHCLAGKGRTGTMLAC 102
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 87-196 6.79e-05

protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or PTP localized to the mitochondrion 1 (PTPMT1), also called phosphoinositide lipid phosphatase (PLIP), phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1, or PTEN-like phosphatase, is a lipid phosphatase or phosphatidylglycerophosphatase (EC 3.1.3.27) which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). It is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. It is essential for the biosynthesis of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. PTPMT1 also plays a crucial role in hematopoietic stem cell (HSC) function, and has been shown to display activity toward phosphoprotein substrates.


Pssm-ID: 350374 [Multi-domain]  Cd Length: 149  Bit Score: 41.48  E-value: 6.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  87 LPF-------VESLRLRSVLCLCPE---PYPEANQEFLRAHGIRLFQFG-IDgskepFVNIPE-DRIREALKVVLDVANH 154
Cdd:cd14524    14 LPFrsmtvalVAKENVRGVITMNEEyetRFFCNSKEEWKALGVEQLRLPtVD-----FTGVPSlEDLEKGVDFILKHREK 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1002297294 155 --PVLIHCKRGKHRTGCVVGC-LRKLQRWCltsiFDEYQRFAAAK 196
Cdd:cd14524    89 gkSVYVHCKAGRGRSATIVACyLIQHKGWS----PEEAQEFLRSK 129
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
139-168 9.19e-05

Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 42.25  E-value: 9.19e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1002297294 139 DRIREALKVVLDVANHPVLIHCKRGKHRTG 168
Cdd:COG2365   119 DAYRAAFRALADAENGPVLFHCTAGKDRTG 148
COG3453 COG3453
Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family ...
 96-171 3.38e-04

Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family [General function prediction only];


Pssm-ID: 442676 [Multi-domain]  Cd Length: 125  Bit Score: 39.05  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294  96 RSVLCLCP------EPYPEANQEFLRAHGIRLFQFGIDGSkepfvNIPEDRIrEALKVVLDVANHPVLIHCKRGKhRTGC 169
Cdd:COG3453    28 KTVINLRPdgeepdQPAAADEAAAAEAAGLEYVHIPVTGG-----AITDEDV-EAFAAALAAAPGPVLAHCRSGT-RSSA 100


                  ..
gi 1002297294 170 VV 171
Cdd:COG3453   101 LW 102
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 111-203 1.20e-03

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 38.40  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002297294 111 QEFLRAHGIRLFQFGI-DGSkepfvnIPEDR-----IREALKVVLDvANHPVLIHCKRGKHRTGCVVGCLRKLQRWCLTS 184
Cdd:cd14505    65 LEQYQQAGITWHHLPIpDGG------VPSDIaqwqeLLEELLSALE-NGKKVLIHCKGGLGRTGLIAACLLLELGDTLDP 137

                          90
                  ....*....|....*....
gi 1002297294 185 ifdeyqrfAAAKARVSDLR 203
Cdd:cd14505   138 --------EQAIAAVRALR 148
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 139-168 2.22e-03

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


Pssm-ID: 463853 [Multi-domain]  Cd Length: 243  Bit Score: 37.99  E-value: 2.22e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1002297294 139 DRIREALKVVLDvANHPVLIHCKRGKHRTG 168
Cdd:pfam13350 116 AAYRALFEALAD-NDGPVLFHCTAGKDRTG 144
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 153-208 7.51e-03

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 36.02  E-value: 7.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002297294 153 NHPVLIHCKRGKHRTGCVVGC--LRKLQRWCLTSIFDEY--QRFAAAKARV---SDLRFMELF 208
Cdd:cd14497    95 NNVAVVHCKAGKGRTGTVICAylLYYGQYSTADEALEYFakKRFKEGLPGVtipSQLRYLQYF 157
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 117-173 8.10e-03

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 35.89  E-value: 8.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002297294 117 HGIR---LFqFgIDGSkepfvnIPEDRI-REALKVVlDVANHPVLIHCKRGKHRTGCVVGC 173
Cdd:cd14499    78 AGIRhydLY-F-PDGS------TPSDDIvKKFLDIC-ENEKGAIAVHCKAGLGRTGTLIAC 129
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
119-187 8.60e-03

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 36.07  E-value: 8.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002297294 119 IRLFQF------GIDGSKEPFVNIpedrIREALKVVLDVANHPVLIHCKRGKHRTGCVVG---CLRKLQRWCLTSIFD 187
Cdd:pfam00102 133 VKHFHYtgwpdhGVPESPNSLLDL----LRKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAidiALQQLEAEGEVDIFQ 206
 
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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