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Conserved domains on  [gi|42569581|ref|NP_180855|]
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Phosphotyrosine protein phosphatases superfamily protein [Arabidopsis thaliana]

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 ...
 61-241 3.85e-90

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: 263.04  E-value: 3.85e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581  61 LIPPLNFSMVDNGIFRSGFPDSANFSFIKTLGLRSIISLCPEPYPENNMQFLKSNGISLFQFGIEGSKskclpglenevw 140
Cdd:cd14528   2 LIPPLNFSMVDKGVYRSGYPNKKNFPFLRTLGLRSILYLCPEDYPESNLEFLKENGIKLFQFGIEGNK------------ 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581 141 lhiwsskhqkedfytngnsktsEPFVDILDQKIREALKVLLDEKNHPLLIHCKRGKHRTGCLVGCMRKLQKWCITSILDE 220
Cdd:cd14528  70 ----------------------EPFVDIPEELIRDALKVLLDPRNHPVLIHCNKGKHRTGCLVGCLRKLQNWSLTSIFDE 127

                       170       180
                ....*....|....*....|.
gi 42569581 221 YKRFAAAKARVSDQRFLESFD 241
Cdd:cd14528 128 YRRFAGPKARMLDQQFIELFD 148
 
Name Accession Description Interval E-value
PFA-DSP_Siw14 cd14528
atypical dual specificity phosphatases similar to yeast Siw14; This subfamily contains ...
 61-241 3.85e-90

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: 263.04  E-value: 3.85e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581  61 LIPPLNFSMVDNGIFRSGFPDSANFSFIKTLGLRSIISLCPEPYPENNMQFLKSNGISLFQFGIEGSKskclpglenevw 140
Cdd:cd14528   2 LIPPLNFSMVDKGVYRSGYPNKKNFPFLRTLGLRSILYLCPEDYPESNLEFLKENGIKLFQFGIEGNK------------ 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581 141 lhiwsskhqkedfytngnsktsEPFVDILDQKIREALKVLLDEKNHPLLIHCKRGKHRTGCLVGCMRKLQKWCITSILDE 220
Cdd:cd14528  70 ----------------------EPFVDIPEELIRDALKVLLDPRNHPVLIHCNKGKHRTGCLVGCLRKLQNWSLTSIFDE 127

                       170       180
                ....*....|....*....|.
gi 42569581 221 YKRFAAAKARVSDQRFLESFD 241
Cdd:cd14528 128 YRRFAGPKARMLDQQFIELFD 148
Y_phosphatase2 pfam03162
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 61-243 1.32e-70

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


Pssm-ID: 397328 [Multi-domain]  Cd Length: 150  Bit Score: 213.38  E-value: 1.32e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581    61 LIPPLNFSMVDNGIFRSGFPDSANFSFIKTLGLRSIISLCPEPYPENNMQFLKSNGISLFQFGIEGSKskclpglenevw 140
Cdd:pfam03162   1 LVPPLNFSPVEPGLYRSSYPRANNFSFLRSLRLKTIISLSPEPYPQDNLQFLESEHIKLYHIHMEGNK------------ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581   141 lhiwsskhqkedfytngnsktsEPFVDILDQKIREALKVLLDEKNHPLLIHCKRGKHRTGCLVGCMRKLQKWCITSILDE 220
Cdd:pfam03162  69 ----------------------DPFVNIPSHLLRRALKLLLNKDNYPVLIHCNRGKHRTGLVIGCLRKLQKWSLASILNE 126

                         170       180
                  ....*....|....*....|...
gi 42569581   221 YKRFAAAKARVSDQRFLESFDVS 243
Cdd:pfam03162 127 YRRFSGSKARIVDEEFIEIFDSE 149
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
74-206 4.03e-05

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


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 43.79  E-value: 4.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581  74 IFRSG---FPDSANFSFIKTLGLRSII--------SLCPEPYPEnnmqflksnGISLFQFGIegskskcLPGLENEVWLH 142
Cdd:COG2365  27 LYRSGalsRLTDADLARLADLGIRTVIdlrspaevARAPDRLPP---------GVRYVHLPV-------LPDDAEALLEE 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42569581 143 IWSSKHQKEDFYtNGNSKTSEPFVDILDQK-IREALKVLLDEKNHPLLIHCKRGKHRTGclVGCM 206
Cdd:COG2365  91 LRDGDLTPGDAE-EFMLELYRAFVDPDAADaYRAAFRALADAENGPVLFHCTAGKDRTG--VAAA 152
 
Name Accession Description Interval E-value
PFA-DSP_Siw14 cd14528
atypical dual specificity phosphatases similar to yeast Siw14; This subfamily contains ...
 61-241 3.85e-90

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: 263.04  E-value: 3.85e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581  61 LIPPLNFSMVDNGIFRSGFPDSANFSFIKTLGLRSIISLCPEPYPENNMQFLKSNGISLFQFGIEGSKskclpglenevw 140
Cdd:cd14528   2 LIPPLNFSMVDKGVYRSGYPNKKNFPFLRTLGLRSILYLCPEDYPESNLEFLKENGIKLFQFGIEGNK------------ 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581 141 lhiwsskhqkedfytngnsktsEPFVDILDQKIREALKVLLDEKNHPLLIHCKRGKHRTGCLVGCMRKLQKWCITSILDE 220
Cdd:cd14528  70 ----------------------EPFVDIPEELIRDALKVLLDPRNHPVLIHCNKGKHRTGCLVGCLRKLQNWSLTSIFDE 127

                       170       180
                ....*....|....*....|.
gi 42569581 221 YKRFAAAKARVSDQRFLESFD 241
Cdd:cd14528 128 YRRFAGPKARMLDQQFIELFD 148
Y_phosphatase2 pfam03162
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 61-243 1.32e-70

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


Pssm-ID: 397328 [Multi-domain]  Cd Length: 150  Bit Score: 213.38  E-value: 1.32e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581    61 LIPPLNFSMVDNGIFRSGFPDSANFSFIKTLGLRSIISLCPEPYPENNMQFLKSNGISLFQFGIEGSKskclpglenevw 140
Cdd:pfam03162   1 LVPPLNFSPVEPGLYRSSYPRANNFSFLRSLRLKTIISLSPEPYPQDNLQFLESEHIKLYHIHMEGNK------------ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581   141 lhiwsskhqkedfytngnsktsEPFVDILDQKIREALKVLLDEKNHPLLIHCKRGKHRTGCLVGCMRKLQKWCITSILDE 220
Cdd:pfam03162  69 ----------------------DPFVNIPSHLLRRALKLLLNKDNYPVLIHCNRGKHRTGLVIGCLRKLQKWSLASILNE 126

                         170       180
                  ....*....|....*....|...
gi 42569581   221 YKRFAAAKARVSDQRFLESFDVS 243
Cdd:pfam03162 127 YRRFSGSKARIVDEEFIEIFDSE 149
PFA-DSP cd14501
plant and fungi atypical dual-specificity phosphatase; Plant and fungi atypical ...
 62-240 1.27e-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: 206.00  E-value: 1.27e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581  62 IPPLNFSMVDNGIFRSGFPDSANFSFIKTLGLRSIISLCPEPYPENNMQFLKSNGISLFQFGIegskskclpglenevwl 141
Cdd:cd14501   1 VPPLNFSIVEPGLYRSAYPTPANFPFLKTLGLKTIILLSPEPPPKPVLSFLTENGIKLIHLGM----------------- 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581 142 hiWSSKHQKedfytngnsktSEPFVDILDQKIREALKVLLDEKNHPLLIHCKRGKHRTGCLVGCMRKLQKWCITSILDEY 221
Cdd:cd14501  64 --LSSKRAD-----------SVPWDPLAYELVKRALEILLDKTNYPVLVHCSLGEHRTGVVVGCLRKLQGWSLASILDEY 130

                       170
                ....*....|....*....
gi 42569581 222 KRFAAAKARVSDQRFLESF 240
Cdd:cd14501 131 RLFAGSKERYVDEQFIELF 149
PFA-DSP_unk cd18538
unknown subfamily of atypical dual-specificity phosphatases from fungi; This uncharacterized ...
 62-240 4.22e-57

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: 179.10  E-value: 4.22e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581  62 IPPLNFSMVDNGIFRSGFPDSANFSFIKTLGLRSIISLCPEPYPENNMQFLKSNGISLFQFGIEGSKskclpglenevwl 141
Cdd:cd18538   1 GLPPNFGVVVPGVYRSSFPKPENFGFLKSLGLRTILTLVQEEYSPEFLNFLRENGIQHFHIAMLGNK------------- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581 142 hiwsskhqkedfytngnsktsEPFVDILDQKIREALKVLLDEKNHPLLIHCKRGKHRTGCLVGCMRKLQKWCITSILDEY 221
Cdd:cd18538  68 ---------------------DPKVSIPDHTMNRILRIILDKENHPILVHCNKGKHRTGCVIACFRKLQGWDVENVLEEY 126

                       170
                ....*....|....*....
gi 42569581 222 KRFAAAKARVSDQRFLESF 240
Cdd:cd18538 127 LSYAHPKSRDLDEEYIENF 145
PFA-DSP_Oca1 cd14531
atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 1; ...
 61-241 1.55e-43

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: 144.36  E-value: 1.55e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581  61 LIPPLNFSMVDNGIFRSGFPDSANFSFIKTLGLRSIISLCPEPYPENNMQFLKSNGISLFQFGIEGSKskclpglenevw 140
Cdd:cd14531   2 FIPPLNFGMVEEDLYRSGQPTPINFPFLERLKLKTIIYLAPDEPSDQFLEFCEDQNINLVHLGGDDST------------ 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581 141 lhiwsskhqkedfyTNGNSKTSEPFVdildqkiREALKVLLDEKNHPLLIHCKRGKHRTGCLVGCMRKLQKWCITSILDE 220
Cdd:cd14531  70 --------------ESRQNPLSEELV-------LAALHIILDPDNYPLLVMCNLGRHRTGTVVGCLRKLQRWNLSSIFEE 128

                       170       180
                ....*....|....*....|.
gi 42569581 221 YKRFAAAKARVSDQRFLESFD 241
Cdd:cd14531 129 YRRFAGSKVRLLNEQFIELFD 149
PFA-DSP_Oca2 cd17661
atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 2; ...
 62-240 2.31e-41

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: 138.69  E-value: 2.31e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581  62 IPPLNFSMVDNGIFRSGFPDSANFSFIKTLGLRSIISLC-PEPYPENNMQFLKSNGISLFQFGIEGSKskclpglenevw 140
Cdd:cd17661   1 VPPLNFSLVADGIYRSGHPMPINYPFLKQLNLKTIIYLGdKDPYRQDYLDFLQSQGIELYYFDFSSSS------------ 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581 141 lhiwsskhqkedfytngnsktsEPFVDILDQKIREALKVLLDEKNHPLLIHCKRGKHRTGCLVGCMRK-LQKWCITSILD 219
Cdd:cd17661  69 ----------------------EPFTEEDQERMEQALKLLLDKRNYPILVHSNKGKHRVGVLVGIMRKlLQGWCLAGIFD 126

                       170       180
                ....*....|....*....|.
gi 42569581 220 EYKRFAAAKARVsDQRFLESF 240
Cdd:cd17661 127 EYGRFAGGKGET-DLEFIETF 146
PFA-DSP_Oca6 cd17663
atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 6; ...
 62-240 4.22e-35

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: 123.18  E-value: 4.22e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581  62 IPPLNFSMVDNGIFRSGFPDSANFSFIKTLGLRSIISLCPEPYPENNMQFLKSNGISLfqfgiegskskclpglenevwL 141
Cdd:cd17663   1 IPPFRFATVEPGLYRGAYPRLKNFRFLRRLKLKTIVSLTPEPPTEDLANFCEAENITL---------------------I 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581 142 HIWSSKHQKEDfytngnsktsepfVDILDQKIREALKVLLDEKNHPLLIHCKRGKHRTGCLVGCMRKLQKWCITSILDEY 221
Cdd:cd17663  60 HISAEKFKKGK-------------VPLSYSTVIQILQLLIDKDNLPVYIHCLDGRHVTGLVVACLRKLQFWSSIAIFAEF 126

                       170
                ....*....|....*....
gi 42569581 222 KRFAAAKARvSDQRFLESF 240
Cdd:cd17663 127 LRFARTISS-EERAFIENF 144
PFA-DSP_Oca4 cd17662
atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 4; ...
 61-241 4.56e-30

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: 110.74  E-value: 4.56e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581  61 LIPPLNFSMVDNGIFRSGFPDSANFSFIKTLGLRSIISLCPEPYPENNMQFLKSNGISLFQFGIEGSKSKCLPGlENEVW 140
Cdd:cd17662   1 LVPPANFGIVEPGIYRCSKLSTLNFSFLETLNLKTIVFVGGQEPSKFFKEFFERNNIELIVLRDADFSNHHHPG-KNSSS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581 141 LHIWSSKHQKEDFYTNGNSKTSEPfvdILDQKIREALKVLLDEKNHPLLIHCKRGKHRTGCLVGCMRKLQKWCITSILDE 220
Cdd:cd17662  80 GKLQGNTDVNDLEPINTNYHLWKN---DLDMLIKSTLLQRIFEKNLPVLNHNKLLVDKTSTVIGCLRRIQKWNFSSIINE 156

                       170       180
                ....*....|....*....|.
gi 42569581 221 YKRFAAAKARVSDQRFLESFD 241
Cdd:cd17662 157 YRRFAGKSSNYFAETFLELFD 177
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 165-238 2.09e-12

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: 61.98  E-value: 2.09e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42569581 165 FVDILDQKIREALKVLLD--EKNHPLLIHCKRGKHRTGCLVGCMR-KLQKWCITSILDEYKRF--AAAKARVSDQRFLE 238
Cdd:cd14494  34 IVDLTLAMVDRFLEVLDQaeKPGEPVLVHCKAGVGRTGTLVACYLvLLGGMSAEEAVRIVRLIrpGGIPQTIEQLDFLI 112
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 66-200 2.67e-06

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: 46.21  E-value: 2.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581  66 NF-SMVDNGIFRSGFPDS-ANFSFIKTLGLRSIISL-CPEPYPENNMQFLKSNGISLFQFGIEGskskclpglenevwlh 142
Cdd:cd14529   5 NFrDVTPYVLYRSAQLSPdEDRALLKKLGIKTVIDLrGADERAASEEAAAKIDGVKYVNLPLSA---------------- 68

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42569581 143 iWSSKHQKEDFYTNgnsktsepFVDILDQkirealkvlldekNHPLLIHCKRGKHRTG 200
Cdd:cd14529  69 -TRPTESDVQSFLL--------IMDLKLA-------------PGPVLIHCKHGKDRTG 104
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
74-206 4.03e-05

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


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 43.79  E-value: 4.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581  74 IFRSG---FPDSANFSFIKTLGLRSII--------SLCPEPYPEnnmqflksnGISLFQFGIegskskcLPGLENEVWLH 142
Cdd:COG2365  27 LYRSGalsRLTDADLARLADLGIRTVIdlrspaevARAPDRLPP---------GVRYVHLPV-------LPDDAEALLEE 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42569581 143 IWSSKHQKEDFYtNGNSKTSEPFVDILDQK-IREALKVLLDEKNHPLLIHCKRGKHRTGclVGCM 206
Cdd:COG2365  91 LRDGDLTPGDAE-EFMLELYRAFVDPDAADaYRAAFRALADAENGPVLFHCTAGKDRTG--VAAA 152
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 142-240 4.23e-04

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: 39.87  E-value: 4.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581 142 HIWSSKHQKEDFYTNGNSKTSE-PFVD------ILDQKIREALKVLLDE-KNHPLLIHCKRGKHRTGCLVGCMRKLQKWC 213
Cdd:cd14497  44 MIFNLSEEEYDDDSKFEGRVLHyGFPDhhppplGLLLEIVDDIDSWLSEdPNNVAVVHCKAGKGRTGTVICAYLLYYGQY 123

                        90       100       110
                ....*....|....*....|....*....|....
gi 42569581 214 IT--SILDEY--KRFAAAKARV---SDQRFLESF 240
Cdd:cd14497 124 STadEALEYFakKRFKEGLPGVtipSQLRYLQYF 157
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
69-205 8.52e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 38.41  E-value: 8.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581  69 MVDNGIFRSGFPDSANFSfIKTLGLRSIISLCPEPypENNMQFLKSNGIslfqfgiegskskclpgleneVWLHIWSskh 148
Cdd:COG2453   3 IIPGLLAGGPLPGGGEAD-LKREGIDAVVSLTEEE--ELLLGLLEEAGL---------------------EYLHLPI--- 55

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42569581 149 qkEDFYTNgnskTSEPFVDILDQkIREALKvlldeKNHPLLIHCKRGKHRTGCLVGC 205
Cdd:COG2453  56 --PDFGAP----DDEQLQEAVDF-IDEALR-----EGKKVLVHCRGGIGRTGTVAAA 100
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 173-206 2.24e-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: 38.38  E-value: 2.24e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 42569581   173 IREALKVLLDEkNHPLLIHCKRGKHRTGclVGCM 206
Cdd:pfam13350 118 YRALFEALADN-DGPVLFHCTAGKDRTG--VAAA 148
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 77-205 4.76e-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: 36.49  E-value: 4.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569581  77 SGFPDS-ANFSFIKTLGLRSIISLCPEPYPEnnmqflksngISLFQFGIegskskclpgleneVWLHIwsskhqkedfyt 155
Cdd:cd14504  12 MAFPRLpEHYAYLNENGIRHVVTLTEEPPPE----------HSDTCPGL--------------RYHHI------------ 55

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42569581 156 ngnsktsePFVDI----LDQkIREALKVLLDE--KNHPLLIHCKRGKHRTGCLVGC 205
Cdd:cd14504  56 --------PIEDYtpptLEQ-IDEFLDIVEEAnaKNEAVLVHCLAGKGRTGTMLAC 102
 
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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