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Conserved domains on  [gi|963702547|ref|WP_058387481|]
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tyrosine protein phosphatase [Legionella cherrii]

Protein Classification

protein-tyrosine phosphatase family protein( domain architecture ID 1000023)

cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 37-312 7.64e-109

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.


The actual alignment was detected with superfamily member cd14495:

Pssm-ID: 475123  Cd Length: 278  Bit Score: 317.78  E-value: 7.64e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963702547  37 CIVEDSEFSFSPLKWFRDASMIAAAYQG---NTLGIRDLAISGSEEPSEKGWKDISEYIARQGRTKVLVLDLRQESHGYI 113
Cdd:cd14495    1 VWRLDAKNKAQLPRNFRTSNDAFKLPLGkvpSRKGLDTLRLSGSAQFSEKQLKAILKKLKEKAKGPIYVVDLRQESHGFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963702547 114 NGRAITLVSEYDWINRGKSNAQSLTDQEDWLKSLRAQKKINGVLSSQQfaAKEYSSGKTIPVKVVKNEADLVSRLGFDYR 193
Cdd:cd14495   81 NGIAVSWYGPRDWANLGKSQSEVLADERNRLQALLGKKVVSIPLGKDK--KKSPSQPKTVKVESVRTEEELVKKKGAHYV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963702547 194 RLYVTDHAAPSDSEVDTFVEIIKNASKDTWFHLHCRGGKGRTSTFFVMFDMLKNADKVSFEEIIARHASIPPYYNLSEVH 273
Cdd:cd14495  159 RIAATDHVWPDDEEIDAFVAFYRSLPADAWLHFHCRAGKGRTTTFMVMYDMLKNPKDVSFDDIIARQYLIGGNYLAYEVD 238

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 963702547 274 RGDPFLTPYYEQRITFLSRFYQFAQQFLKGYQGTWSQWN 312
Cdd:cd14495  239 KDKNWKRPYYEERAQFLQKFYQYVQENPAGGKTSWSEWL 277
 
Name Accession Description Interval E-value
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
 37-312 7.64e-109

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates.


Pssm-ID: 350345  Cd Length: 278  Bit Score: 317.78  E-value: 7.64e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963702547  37 CIVEDSEFSFSPLKWFRDASMIAAAYQG---NTLGIRDLAISGSEEPSEKGWKDISEYIARQGRTKVLVLDLRQESHGYI 113
Cdd:cd14495    1 VWRLDAKNKAQLPRNFRTSNDAFKLPLGkvpSRKGLDTLRLSGSAQFSEKQLKAILKKLKEKAKGPIYVVDLRQESHGFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963702547 114 NGRAITLVSEYDWINRGKSNAQSLTDQEDWLKSLRAQKKINGVLSSQQfaAKEYSSGKTIPVKVVKNEADLVSRLGFDYR 193
Cdd:cd14495   81 NGIAVSWYGPRDWANLGKSQSEVLADERNRLQALLGKKVVSIPLGKDK--KKSPSQPKTVKVESVRTEEELVKKKGAHYV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963702547 194 RLYVTDHAAPSDSEVDTFVEIIKNASKDTWFHLHCRGGKGRTSTFFVMFDMLKNADKVSFEEIIARHASIPPYYNLSEVH 273
Cdd:cd14495  159 RIAATDHVWPDDEEIDAFVAFYRSLPADAWLHFHCRAGKGRTTTFMVMYDMLKNPKDVSFDDIIARQYLIGGNYLAYEVD 238

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 963702547 274 RGDPFLTPYYEQRITFLSRFYQFAQQFLKGYQGTWSQWN 312
Cdd:cd14495  239 KDKNWKRPYYEERAQFLQKFYQYVQENPAGGKTSWSEWL 277
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 103-246 2.87e-38

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 133.21  E-value: 2.87e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963702547  103 LDLRQESHGYINGRAITLVSEYDWINRGKSNAQSLTDQ-EDWLKSLR------AQKKINGVLSSQQFAAKEYSS------ 169
Cdd:pfam14566   1 VNLREEPVVYINGRPYVLREAEDPLNNLKEYPGISAERlERLEARLKedvlaeAKKNGGRVLVHDETEDGIGVLtvvdvw 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963702547  170 GKTIPVKVVKNEADLVSRLGFDYRRLYVTDHAAPSDSEVDTFVEIIKNASKDTWFHLHCRGGKGRTSTFFVMFDMLK 246
Cdd:pfam14566  81 ESDVQTPEEVYERLKAEGPGVDYRRIPITDEKAPLEEDFDALISIVKDAPEDTALVFNCQMGRGRTTTAMVIADLVR 157
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
182-286 9.11e-13

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 64.61  E-value: 9.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963702547 182 ADLVSRLGFDYRRLYVTDHAAPSDSEVDTFVEIIKNA-SKDTWFHLHCRGGKGRTSTFFVMFDMLKNadkVSFEEIIARH 260
Cdd:COG2453   40 LGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEAlREGKKVLVHCRGGIGRTGTVAAAYLVLLG---LSAEEALARV 116

                         90       100
                 ....*....|....*....|....*.
gi 963702547 261 ASIPPYYNLSEVHRGdpFLTPYYEQR 286
Cdd:COG2453  117 RAARPGAVETPAQRA--FLERFAKRL 140
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
199-257 5.51e-03

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 35.80  E-value: 5.51e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 963702547   199 DHAAPSDSE-VDTFVEIIKNASKDTWFH----LHCRGGKGRTSTfFVMFDML-----KNADKVSFEEII 257
Cdd:smart00404  12 DHGVPESPDsILELLRAVKKNLNQSESSgpvvVHCSAGVGRTGT-FVAIDILlqqleAEAGEVDIFDTV 79
 
Name Accession Description Interval E-value
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
 37-312 7.64e-109

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates.


Pssm-ID: 350345  Cd Length: 278  Bit Score: 317.78  E-value: 7.64e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963702547  37 CIVEDSEFSFSPLKWFRDASMIAAAYQG---NTLGIRDLAISGSEEPSEKGWKDISEYIARQGRTKVLVLDLRQESHGYI 113
Cdd:cd14495    1 VWRLDAKNKAQLPRNFRTSNDAFKLPLGkvpSRKGLDTLRLSGSAQFSEKQLKAILKKLKEKAKGPIYVVDLRQESHGFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963702547 114 NGRAITLVSEYDWINRGKSNAQSLTDQEDWLKSLRAQKKINGVLSSQQfaAKEYSSGKTIPVKVVKNEADLVSRLGFDYR 193
Cdd:cd14495   81 NGIAVSWYGPRDWANLGKSQSEVLADERNRLQALLGKKVVSIPLGKDK--KKSPSQPKTVKVESVRTEEELVKKKGAHYV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963702547 194 RLYVTDHAAPSDSEVDTFVEIIKNASKDTWFHLHCRGGKGRTSTFFVMFDMLKNADKVSFEEIIARHASIPPYYNLSEVH 273
Cdd:cd14495  159 RIAATDHVWPDDEEIDAFVAFYRSLPADAWLHFHCRAGKGRTTTFMVMYDMLKNPKDVSFDDIIARQYLIGGNYLAYEVD 238

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 963702547 274 RGDPFLTPYYEQRITFLSRFYQFAQQFLKGYQGTWSQWN 312
Cdd:cd14495  239 KDKNWKRPYYEERAQFLQKFYQYVQENPAGGKTSWSEWL 277
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 103-246 2.87e-38

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 133.21  E-value: 2.87e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963702547  103 LDLRQESHGYINGRAITLVSEYDWINRGKSNAQSLTDQ-EDWLKSLR------AQKKINGVLSSQQFAAKEYSS------ 169
Cdd:pfam14566   1 VNLREEPVVYINGRPYVLREAEDPLNNLKEYPGISAERlERLEARLKedvlaeAKKNGGRVLVHDETEDGIGVLtvvdvw 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963702547  170 GKTIPVKVVKNEADLVSRLGFDYRRLYVTDHAAPSDSEVDTFVEIIKNASKDTWFHLHCRGGKGRTSTFFVMFDMLK 246
Cdd:pfam14566  81 ESDVQTPEEVYERLKAEGPGVDYRRIPITDEKAPLEEDFDALISIVKDAPEDTALVFNCQMGRGRTTTAMVIADLVR 157
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
182-286 9.11e-13

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 64.61  E-value: 9.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963702547 182 ADLVSRLGFDYRRLYVTDHAAPSDSEVDTFVEIIKNA-SKDTWFHLHCRGGKGRTSTFFVMFDMLKNadkVSFEEIIARH 260
Cdd:COG2453   40 LGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEAlREGKKVLVHCRGGIGRTGTVAAAYLVLLG---LSAEEALARV 116

                         90       100
                 ....*....|....*....|....*.
gi 963702547 261 ASIPPYYNLSEVHRGdpFLTPYYEQR 286
Cdd:COG2453  117 RAARPGAVETPAQRA--FLERFAKRL 140
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 205-259 4.56e-07

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: 47.73  E-value: 4.56e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 963702547 205 DSEVDTFVEIIKNA-SKDTWFHLHCRGGKGRTSTFFVMFDMLKNadKVSFEEIIAR 259
Cdd:cd14494   39 LAMVDRFLEVLDQAeKPGEPVLVHCKAGVGRTGTLVACYLVLLG--GMSAEEAVRI 92
PTP_paladin cd14496
protein tyrosine phosphatase-like domains of paladin; Paladin is a putative phosphatase, which ...
 174-237 2.31e-06

protein tyrosine phosphatase-like domains of paladin; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two protein tyrosine phosphatase (PTP)-like domains. This model represents both repeats.


Pssm-ID: 350346 [Multi-domain]  Cd Length: 185  Bit Score: 47.23  E-value: 2.31e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963702547 174 PVKVVKNEADLVSRLGF--DYRRLYVTDHAAPSDSEVDTFVEIIKNA-SKDTWFHLHCRGGKGRTST 237
Cdd:cd14496   80 PVVYINGRPFVLREVERrvDYHRIPITDEKAPEPGDFDALLEVILSTdDPTTAFVFNCQMGRGRTTT 146
PTP_paladin_2 cd17660
protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative ...
 187-241 3.45e-05

protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 2.


Pssm-ID: 350498  Cd Length: 216  Bit Score: 44.00  E-value: 3.45e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 963702547 187 RLGFDYRRLYVTDHAAPSDSEVDTFVEIIKNASKD---TWFHLHCRGGKGRTSTFFVM 241
Cdd:cd17660  100 PVGLTYRRIPIPDFCAPREEDFDRLLEAMKSALAEdsgTAFVFNCLDGKGRTTTAMVI 157
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 189-238 5.06e-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: 42.65  E-value: 5.06e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 963702547 189 GFDYRRLYVTDHAAPSDSEVDTFVEIIK--NASKDTWFhLHCRGGKGRTSTF 238
Cdd:cd14504   49 GLRYHHIPIEDYTPPTLEQIDEFLDIVEeaNAKNEAVL-VHCLAGKGRTGTM 99
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 147-285 9.92e-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: 41.86  E-value: 9.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963702547 147 LRAQKKINGVLSSQQfaakEYSSgktipvKVVKNEADLVSRLGFDYRRLYVTDH-AAPSDSEVDTFVEII-KNASKDTWF 224
Cdd:cd14524   23 LVAKENVRGVITMNE----EYET------RFFCNSKEEWKALGVEQLRLPTVDFtGVPSLEDLEKGVDFIlKHREKGKSV 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 963702547 225 HLHCRGGKGRTSTFFVMFDMLKNadKVSFEEIIARHASIPPYYNLSEVHRgdPFLTPYYEQ 285
Cdd:cd14524   93 YVHCKAGRGRSATIVACYLIQHK--GWSPEEAQEFLRSKRPHILLRLSQR--EVLEEFYRK 149
PTP-bact cd14503
bacterial tyrosine-protein phosphataseS similar to Neisseria NMA1982; This subfamily is ...
 180-263 2.88e-04

bacterial tyrosine-protein phosphataseS similar to Neisseria NMA1982; This subfamily is composed of bacterial tyrosine-protein phosphatases similar to Neisseria meningitidis NMA1982, which displays phosphatase activity but whose biological function is still unknown.


Pssm-ID: 350353 [Multi-domain]  Cd Length: 136  Bit Score: 40.31  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963702547 180 NEADLVSRLGFDYRRLYVtDHAAPSDSEVDTFVEIIKNASKDTWFhLHCRGGKgRTSTFFVMFDMLKNAdkVSFEEIIAR 259
Cdd:cd14503   45 NEAAAVTAAGMEYVHIPV-DWDNPTPEDVERFFEVMDAAQGKPVL-VHCASNM-RASAFWYLYRALDGG--VSEEEAIQL 119


                 ....
gi 963702547 260 HASI 263
Cdd:cd14503  120 MRSA 123
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
159-259 1.50e-03

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 39.69  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963702547 159 SQQFAAKEY------SSGKTIPVKV--VKNEADlvsrlgfdyrrlyvtdHAAPSDSEVDTFVEIIKNASKDTWFH----- 225
Cdd:COG5599  147 RDGIEARTYvltikgTGQKKIEIPVlhVKNWPD----------------HGAISAEALKNLADLIDKKEKIKDPDkllpv 210

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 963702547 226 LHCRGGKGRTSTFFV---MFDMLKNAD--KVSFEEIIAR 259
Cdd:COG5599  211 VHCRAGVGRTGTLIAclaLSKSINALVqiTLSVEEIVID 249
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 170-258 3.07e-03

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 38.53  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963702547 170 GKTIPVKVVKNEADLVSRLGFDYRRLYVTDHAAPSDSEvDTFVEIIknaskdtwfhlHCRGGKGRTSTFFVMFDMLKNAD 249
Cdd:cd14559  129 HTAISSEGLKELADLVNKSAEEKRNFYKSKGSSAINDK-NKLLPVI-----------HCRAGVGRTGQLAAAMELNKSPN 196


                 ....*....
gi 963702547 250 KVSFEEIIA 258
Cdd:cd14559  197 NLSVEDIVS 205
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
199-257 5.51e-03

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 35.80  E-value: 5.51e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 963702547   199 DHAAPSDSE-VDTFVEIIKNASKDTWFH----LHCRGGKGRTSTfFVMFDML-----KNADKVSFEEII 257
Cdd:smart00404  12 DHGVPESPDsILELLRAVKKNLNQSESSgpvvVHCSAGVGRTGT-FVAIDILlqqleAEAGEVDIFDTV 79
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 199-257 5.51e-03

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 35.80  E-value: 5.51e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 963702547   199 DHAAPSDSE-VDTFVEIIKNASKDTWFH----LHCRGGKGRTSTfFVMFDML-----KNADKVSFEEII 257
Cdd:smart00012  12 DHGVPESPDsILELLRAVKKNLNQSESSgpvvVHCSAGVGRTGT-FVAIDILlqqleAEAGEVDIFDTV 79
 
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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