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Conserved domains on  [gi|553905869|gb|AGY75919|]
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phosphatase [Clostridium autoethanogenum DSM 10061]

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 ...
 47-306 1.20e-98

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: 291.59  E-value: 1.20e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553905869  47 QLKIDSKKKNKIPKRFRKTTDDIRVY-GKALNLKGLSSLNASGSAQFTGQNIKMVKEEIGNV---PILVVDLREESHGFI 122
Cdd:cd14495    1 VWRLDAKNKAQLPRNFRTSNDAFKLPlGKVPSRKGLDTLRLSGSAQFSEKQLKAILKKLKEKakgPIYVVDLRQESHGFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553905869 123 NDLAVSWVGEeKNNANKGLTKEQVLKDESEKLKGIKLNEKL------DIEEKEIIPD-----KVQDERKLVEENKMSYVR 191
Cdd:cd14495   81 NGIAVSWYGP-RDWANLGKSQSEVLADERNRLQALLGKKVVsiplgkDKKKSPSQPKtvkveSVRTEEELVKKKGAHYVR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553905869 192 IPVTDTEGPTDEMVDYFISIVKKTPPGTWMHFHCKAGIGRTTTFMTMYDIMKNAKDVSLDDIMERQILLGGKNLL----K 267
Cdd:cd14495  160 IAATDHVWPDDEEIDAFVAFYRSLPADAWLHFHCRAGKGRTTTFMVMYDMLKNPKDVSFDDIIARQYLIGGNYLAyevdK 239

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 553905869 268 PFHKAGSKSSERSEFIKKFYEYAKENKDNFNTSWSEWLK 306
Cdd:cd14495  240 DKNWKRPYYEERAQFLQKFYQYVQENPAGGKTSWSEWLK 278
 
Name Accession Description Interval E-value
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
 47-306 1.20e-98

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: 291.59  E-value: 1.20e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553905869  47 QLKIDSKKKNKIPKRFRKTTDDIRVY-GKALNLKGLSSLNASGSAQFTGQNIKMVKEEIGNV---PILVVDLREESHGFI 122
Cdd:cd14495    1 VWRLDAKNKAQLPRNFRTSNDAFKLPlGKVPSRKGLDTLRLSGSAQFSEKQLKAILKKLKEKakgPIYVVDLRQESHGFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553905869 123 NDLAVSWVGEeKNNANKGLTKEQVLKDESEKLKGIKLNEKL------DIEEKEIIPD-----KVQDERKLVEENKMSYVR 191
Cdd:cd14495   81 NGIAVSWYGP-RDWANLGKSQSEVLADERNRLQALLGKKVVsiplgkDKKKSPSQPKtvkveSVRTEEELVKKKGAHYVR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553905869 192 IPVTDTEGPTDEMVDYFISIVKKTPPGTWMHFHCKAGIGRTTTFMTMYDIMKNAKDVSLDDIMERQILLGGKNLL----K 267
Cdd:cd14495  160 IAATDHVWPDDEEIDAFVAFYRSLPADAWLHFHCRAGKGRTTTFMVMYDMLKNPKDVSFDDIIARQYLIGGNYLAyevdK 239

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 553905869 268 PFHKAGSKSSERSEFIKKFYEYAKENKDNFNTSWSEWLK 306
Cdd:cd14495  240 DKNWKRPYYEERAQFLQKFYQYVQENPAGGKTSWSEWLK 278
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 112-243 1.12e-31

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: 115.87  E-value: 1.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553905869  112 VDLREESHGFINDLAVSWVGEEKNNAN-KGLTK--EQVLKDESEKLK----------------------GIKLNEKLDIE 166
Cdd:pfam14566   1 VNLREEPVVYINGRPYVLREAEDPLNNlKEYPGisAERLERLEARLKedvlaeakknggrvlvhdetedGIGVLTVVDVW 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553905869  167 EKEIIPDKVQDERKLVEENKMSYVRIPVTDTEGPTDEMVDYFISIVKKTPPGTWMHFHCKAGIGRTTTFMTMYDIMK 243
Cdd:pfam14566  81 ESDVQTPEEVYERLKAEGPGVDYRRIPITDEKAPLEEDFDALISIVKDAPEDTALVFNCQMGRGRTTTAMVIADLVR 157
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
176-289 1.86e-12

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 63.45  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553905869 176 QDERKLVEENKMSYVRIPVTDTEGPTDEMVDYFISIVKK-TPPGTWMHFHCKAGIGRTTTFMTMYDImknAKDVSLDDIM 254
Cdd:COG2453   37 ELLLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEaLREGKKVLVHCRGGIGRTGTVAAAYLV---LLGLSAEEAL 113

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 553905869 255 ERQILLGGKNLLKPfhkagskssERSEFIKKFYEY 289
Cdd:COG2453  114 ARVRAARPGAVETP---------AQRAFLERFAKR 139
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
224-256 2.00e-03

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 36.95  E-value: 2.00e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 553905869   224 HCKAGIGRTTTFMTMY----DIMKNAKDVSLDDIMER 256
Cdd:smart00404  45 HCSAGVGRTGTFVAIDillqQLEAEAGEVDIFDTVKE 81
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 180-232 9.33e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 36.15  E-value: 9.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 553905869 180 KLVEENKMSYVRIPVTDTEGPTDEMVDYFISIVKK------TPPGTwMHFHCKAGIGRT 232
Cdd:PTZ00242  55 ELLEKNGIEVHDWPFDDGAPPPKAVIDNWLRLLDQefakqsTPPET-IAVHCVAGLGRA 112
 
Name Accession Description Interval E-value
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
 47-306 1.20e-98

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: 291.59  E-value: 1.20e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553905869  47 QLKIDSKKKNKIPKRFRKTTDDIRVY-GKALNLKGLSSLNASGSAQFTGQNIKMVKEEIGNV---PILVVDLREESHGFI 122
Cdd:cd14495    1 VWRLDAKNKAQLPRNFRTSNDAFKLPlGKVPSRKGLDTLRLSGSAQFSEKQLKAILKKLKEKakgPIYVVDLRQESHGFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553905869 123 NDLAVSWVGEeKNNANKGLTKEQVLKDESEKLKGIKLNEKL------DIEEKEIIPD-----KVQDERKLVEENKMSYVR 191
Cdd:cd14495   81 NGIAVSWYGP-RDWANLGKSQSEVLADERNRLQALLGKKVVsiplgkDKKKSPSQPKtvkveSVRTEEELVKKKGAHYVR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553905869 192 IPVTDTEGPTDEMVDYFISIVKKTPPGTWMHFHCKAGIGRTTTFMTMYDIMKNAKDVSLDDIMERQILLGGKNLL----K 267
Cdd:cd14495  160 IAATDHVWPDDEEIDAFVAFYRSLPADAWLHFHCRAGKGRTTTFMVMYDMLKNPKDVSFDDIIARQYLIGGNYLAyevdK 239

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 553905869 268 PFHKAGSKSSERSEFIKKFYEYAKENKDNFNTSWSEWLK 306
Cdd:cd14495  240 DKNWKRPYYEERAQFLQKFYQYVQENPAGGKTSWSEWLK 278
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 112-243 1.12e-31

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: 115.87  E-value: 1.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553905869  112 VDLREESHGFINDLAVSWVGEEKNNAN-KGLTK--EQVLKDESEKLK----------------------GIKLNEKLDIE 166
Cdd:pfam14566   1 VNLREEPVVYINGRPYVLREAEDPLNNlKEYPGisAERLERLEARLKedvlaeakknggrvlvhdetedGIGVLTVVDVW 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553905869  167 EKEIIPDKVQDERKLVEENKMSYVRIPVTDTEGPTDEMVDYFISIVKKTPPGTWMHFHCKAGIGRTTTFMTMYDIMK 243
Cdd:pfam14566  81 ESDVQTPEEVYERLKAEGPGVDYRRIPITDEKAPLEEDFDALISIVKDAPEDTALVFNCQMGRGRTTTAMVIADLVR 157
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
176-289 1.86e-12

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 63.45  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553905869 176 QDERKLVEENKMSYVRIPVTDTEGPTDEMVDYFISIVKK-TPPGTWMHFHCKAGIGRTTTFMTMYDImknAKDVSLDDIM 254
Cdd:COG2453   37 ELLLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEaLREGKKVLVHCRGGIGRTGTVAAAYLV---LLGLSAEEAL 113

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 553905869 255 ERQILLGGKNLLKPfhkagskssERSEFIKKFYEY 289
Cdd:COG2453  114 ARVRAARPGAVETP---------AQRAFLERFAKR 139
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 176-262 4.39e-10

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: 56.20  E-value: 4.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553905869 176 QDERKLVEENKMSYVRIpvtdtegpTDEMVDYFISIVKKTP-PGTWMHFHCKAGIGRTTTFMTMYDIMKNakDVSLDDIM 254
Cdd:cd14494   21 ADSRFLKQLGVTTIVDL--------TLAMVDRFLEVLDQAEkPGEPVLVHCKAGVGRTGTLVACYLVLLG--GMSAEEAV 90


                 ....*...
gi 553905869 255 ERQILLGG 262
Cdd:cd14494   91 RIVRLIRP 98
PTP_paladin cd14496
protein tyrosine phosphatase-like domains of paladin; Paladin is a putative phosphatase, which ...
 41-237 3.64e-09

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: 55.32  E-value: 3.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553905869  41 IQNRNVQLKIDSKKknkipkRFRKTTDDIRVYGkALNLKGLSSLNASGSAQFTGQNIKMVKEEIG-----NVPILVVDLR 115
Cdd:cd14496    5 VLGAGTILKSDHFP------GCQSLTLPERVEG-APNFRRVPGLPVYGVAQPTIDGIRRVLSRLGaapdgRGRVVWVNLR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553905869 116 EESHGFINDlavswvgeeknnankgltKEQVLKDESEKLKgiklnekldieekeiipdkvqderklveenkmsYVRIPVT 195
Cdd:cd14496   78 EEPVVYING------------------RPFVLREVERRVD---------------------------------YHRIPIT 106

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 553905869 196 DTEGPTDEMVDYFISIVKKTPPGTWMH-FHCKAGIGRTTTFMT 237
Cdd:cd14496  107 DEKAPEPGDFDALLEVILSTDDPTTAFvFNCQMGRGRTTTGMV 149
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 169-289 5.73e-09

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: 53.82  E-value: 5.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553905869 169 EIIPDKVQDERKlveenKMSYVRIPVTDTEGPTDEMVDYFISIVKK--TPPGTWMhFHCKAGIGRTTTFMTMYdIMKNAK 246
Cdd:cd14504   37 EEPPPEHSDTCP-----GLRYHHIPIEDYTPPTLEQIDEFLDIVEEanAKNEAVL-VHCLAGKGRTGTMLACY-LVKTGK 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 553905869 247 DVSLDDIMERQILLGGknllkpfhkaGSKSSERSEFIKKFYEY 289
Cdd:cd14504  110 ISAVDAINEIRRIRPG----------SIETSEQEKFVIQFAKT 142
PTP_paladin_2 cd17660
protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative ...
 187-236 1.63e-07

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: 50.94  E-value: 1.63e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 553905869 187 MSYVRIPVTDTEGPTDEMVDYFISIVKKTP---PGTWMHFHCKAGIGRTTTFM 236
Cdd:cd17660  103 LTYRRIPIPDFCAPREEDFDRLLEAMKSALaedSGTAFVFNCLDGKGRTTTAM 155
PTP-bact cd14503
bacterial tyrosine-protein phosphataseS similar to Neisseria NMA1982; This subfamily is ...
 172-239 2.82e-06

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: 46.09  E-value: 2.82e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553905869 172 PDKVQDERKLVEENKMSYVRIPVtDTEGPTDEMVDYFISIVKKTPPGTwMHFHCKAGiGRTTTFMTMY 239
Cdd:cd14503   40 ENALPNEAAAVTAAGMEYVHIPV-DWDNPTPEDVERFFEVMDAAQGKP-VLVHCASN-MRASAFWYLY 104
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 200-244 1.72e-05

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: 44.37  E-value: 1.72e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 553905869 200 PTDEMVDYFISIVKKTPpGTwMHFHCKAGIGRTTTFMTMYdIMKN 244
Cdd:cd14499   93 PSDDIVKKFLDICENEK-GA-IAVHCKAGLGRTGTLIACY-LMKH 134
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 186-252 1.17e-03

dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is composed of dual specificity protein phosphatase 14 (DUSP14, also known as MKP-6), 18 (DUSP18), 21 (DUSP21), 28 (DUSP28), and similar proteins. They function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48), and are atypical DUSPs. They contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP14 directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses. DUSP18 has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane. DUSP28 has been implicated in hepatocellular carcinoma progression and in migratory activity and drug resistance of pancreatic cancer cells.


Pssm-ID: 350364 [Multi-domain]  Cd Length: 133  Bit Score: 38.30  E-value: 1.17e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553905869 186 KMSYVRIPVTDTegPTDEMVDYFISIVKKtppgtwMH----------FHCKAGIGRTTTFMTMYdIMKNAKdVSLDD 252
Cdd:cd14514   43 GIEYLRVPVEDS--PHADLSPHFDEVADK------IHqvkrrggrtlVHCVAGVSRSATLCLAY-LMKYEG-MTLRE 109
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 189-252 1.72e-03

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: 38.51  E-value: 1.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553905869 189 YVRIPvTDTEGPTDEMVDYFISIV-KKTPPGTWMhFHCKAGIGRTTTFMTMY-DIMKNAKDVSLDD 252
Cdd:cd14529   61 YVNLP-LSATRPTESDVQSFLLIMdLKLAPGPVL-IHCKHGKDRTGLVSALYrIVYGGSKEEANED 124
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 181-238 1.93e-03

protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), also known as protein-tyrosine phosphatase of regenerating liver 1 (PRL-1), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It may play a role in the development and maintenance of differentiating epithelial tissues. PRL-1 promotes cell growth and migration by activating both the ERK1/2 and RhoA pathways. It is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350513 [Multi-domain]  Cd Length: 167  Bit Score: 38.52  E-value: 1.93e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553905869 181 LVEENKMSYVRIPVTDTEGPTDEMVDYFISIVK---KTPPGTWMHFHCKAGIGRTTTFMTM 238
Cdd:cd18537   57 LVEKEGIQVLDWPFDDGAPPSNQIVDDWLNLLKvkfREEPGCCIAVHCVAGLGRAPVLVAL 117
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
224-256 2.00e-03

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 36.95  E-value: 2.00e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 553905869   224 HCKAGIGRTTTFMTMY----DIMKNAKDVSLDDIMER 256
Cdd:smart00404  45 HCSAGVGRTGTFVAIDillqQLEAEAGEVDIFDTVKE 81
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 224-256 2.00e-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: 36.95  E-value: 2.00e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 553905869   224 HCKAGIGRTTTFMTMY----DIMKNAKDVSLDDIMER 256
Cdd:smart00012  45 HCSAGVGRTGTFVAIDillqQLEAEAGEVDIFDTVKE 81
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 213-255 2.68e-03

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 38.88  E-value: 2.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 553905869 213 KKTPPGTWMHFHCKAGIGRTTTFMTMyDI-MKNAKDVSLDDIME 255
Cdd:cd14543  205 KGHPPGPPIVVHCSAGIGRTGTFCTL-DIcLSQLEDVGTLNVMQ 247
PTP_paladin_1 cd17659
protein tyrosine phosphatase-like domain of paladin, repeat 1; Paladin is a putative ...
 187-243 3.19e-03

protein tyrosine phosphatase-like domain of paladin, repeat 1; 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 1.


Pssm-ID: 350497  Cd Length: 220  Bit Score: 38.30  E-value: 3.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553905869 187 MSYVRIPVTDTEGPTDEMVDYFISIVKKTPPGTWMHFH-------CKAGIGRTTTFMTMYDIMK 243
Cdd:cd17659   95 YRYHRLPLPEDGAPLEIQFDAFVNVLRENPSLSDAIGLlpallfsCQPGVGRTNLAMVLGTLVL 158
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 224-255 3.28e-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: 38.15  E-value: 3.28e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 553905869 224 HCKAGIGRTTTFMTMYDIMKNAKDVSLDDIME 255
Cdd:cd14559  174 HCRAGVGRTGQLAAAMELNKSPNNLSVEDIVS 205
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 179-232 7.72e-03

protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), also known as protein-tyrosine phosphatases of regenerating liver (PRLs) constitute a family of small, prenylated phosphatases that are the most oncogenic of all PTPs. They stimulate progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. They associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation. Vertebrates contain three members: PRL-1, PRL-2, and PRL-3.


Pssm-ID: 350350 [Multi-domain]  Cd Length: 156  Bit Score: 36.43  E-value: 7.72e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 553905869 179 RKLVEENKMSYVRIPVTDTEGPTDEMVDYFISIVKKT-----PPGTWMHFHCKAGIGRT 232
Cdd:cd14500   51 KEPLEKAGIKVHDWPFDDGSPPPDDVVDDWLDLLKTRfkeegKPGACIAVHCVAGLGRA 109
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 180-232 9.33e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 36.15  E-value: 9.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 553905869 180 KLVEENKMSYVRIPVTDTEGPTDEMVDYFISIVKK------TPPGTwMHFHCKAGIGRT 232
Cdd:PTZ00242  55 ELLEKNGIEVHDWPFDDGAPPPKAVIDNWLRLLDQefakqsTPPET-IAVHCVAGLGRA 112
 
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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