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Conserved domains on  [gi|2573424328|ref|WP_308424622|]
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MULTISPECIES: tyrosine-protein phosphatase [Bacteria]

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 ...
 12-160 9.81e-40

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 cd14505:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 163  Bit Score: 132.00  E-value: 9.81e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  12 TLDNGARLIFTPCPGTQSA----NLTDSVATLKQAGTDMLLTLMFDQEMAENNASDLAKVCAEQDIQWLQLPIADDAAPN 87
Cdd:cd14505     8 MLGNAGSLGLTPCPGCKFKdhrrDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPIPDGGVPS 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2573424328  88 SvfETQWQLHQATILAVLEQQGTVAVHCRGGSGRTGLVIGLILLAYGWPAP--KVIQQVQQIRPKALKHPVQLNY 160
Cdd:cd14505    88 D--IAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLLLELGDTLDpeQAIAAVRALRPGAIQTPKQENF 160
 
Name Accession Description Interval E-value
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 12-160 9.81e-40

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: 132.00  E-value: 9.81e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  12 TLDNGARLIFTPCPGTQSA----NLTDSVATLKQAGTDMLLTLMFDQEMAENNASDLAKVCAEQDIQWLQLPIADDAAPN 87
Cdd:cd14505     8 MLGNAGSLGLTPCPGCKFKdhrrDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPIPDGGVPS 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2573424328  88 SvfETQWQLHQATILAVLEQQGTVAVHCRGGSGRTGLVIGLILLAYGWPAP--KVIQQVQQIRPKALKHPVQLNY 160
Cdd:cd14505    88 D--IAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLLLELGDTLDpeQAIAAVRALRPGAIQTPKQENF 160
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
15-160 2.43e-28

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 101.97  E-value: 2.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  15 NGARLIFTPCPGTqsanltdSVATLKQAGTDMLLTLMFDQEmaennasDLAKVCAEQDIQWLQLPIADDAAPnsvfeTQW 94
Cdd:COG2453     4 IPGLLAGGPLPGG-------GEADLKREGIDAVVSLTEEEE-------LLLGLLEEAGLEYLHLPIPDFGAP-----DDE 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2573424328  95 QLHQA--TILAVLEQQGTVAVHCRGGSGRTGLVIGLILLAYGWPAPKVIQQVQQIRPKALKHPVQLNY 160
Cdd:COG2453    65 QLQEAvdFIDEALREGKKVLVHCRGGIGRTGTVAAAYLVLLGLSAEEALARVRAARPGAVETPAQRAF 132
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 55-150 3.01e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 44.63  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  55 EMAENNASDLAKVCA---------EQDIQWLQLPIADDAAPNSVFETQW-QLHQATILAVLEQQGTVAVHCRGGSGRTGL 124
Cdd:PTZ00242   35 ELQRYNVTHLVRVCGptydaelleKNGIEVHDWPFDDGAPPPKAVIDNWlRLLDQEFAKQSTPPETIAVHCVAGLGRAPI 114

                          90       100
                  ....*....|....*....|....*.
gi 2573424328 125 VIGLILLAYGWPAPkvIQQVQQIRPK 150
Cdd:PTZ00242  115 LVALALVEYGGMEP--LDAVGFVREK 138
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
57-150 3.97e-06

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 44.20  E-value: 3.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328   57 AENNASDLAKVCAEQDIQWLQLPIADdaapNSVFETQWQLHQAT--ILAVLEQQGTVAVHCRGGSGRTG-LVIGLILLAY 133
Cdd:smart00195  29 HVINVTNEVPNYNGSDFTYLGVPIDD----NTETKISPYFPEAVefIEDAESKGGKVLVHCQAGVSRSAtLIIAYLMKTR 104

                           90
                   ....*....|....*..
gi 2573424328  134 GWPAPKVIQQVQQIRPK 150
Cdd:smart00195 105 NMSLNDAYDFVKDRRPI 121
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 72-149 1.89e-04

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 39.17  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  72 DIQWLQLPIADdaapNSVFETQWQLHQAT--ILAVLEQQGTVAVHCRGGSGRTGLVIGLILLAY-GWPAPKVIQQVQQIR 148
Cdd:pfam00782  35 GILYLRIPVED----NHETNISKYLEEAVefIDDARQKGGKVLVHCQAGISRSATLIIAYLMKTrNLSLNEAYSFVKERR 110


                  .
gi 2573424328 149 P 149
Cdd:pfam00782 111 P 111
 
Name Accession Description Interval E-value
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 12-160 9.81e-40

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: 132.00  E-value: 9.81e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  12 TLDNGARLIFTPCPGTQSA----NLTDSVATLKQAGTDMLLTLMFDQEMAENNASDLAKVCAEQDIQWLQLPIADDAAPN 87
Cdd:cd14505     8 MLGNAGSLGLTPCPGCKFKdhrrDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPIPDGGVPS 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2573424328  88 SvfETQWQLHQATILAVLEQQGTVAVHCRGGSGRTGLVIGLILLAYGWPAP--KVIQQVQQIRPKALKHPVQLNY 160
Cdd:cd14505    88 D--IAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLLLELGDTLDpeQAIAAVRALRPGAIQTPKQENF 160
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
15-160 2.43e-28

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 101.97  E-value: 2.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  15 NGARLIFTPCPGTqsanltdSVATLKQAGTDMLLTLMFDQEmaennasDLAKVCAEQDIQWLQLPIADDAAPnsvfeTQW 94
Cdd:COG2453     4 IPGLLAGGPLPGG-------GEADLKREGIDAVVSLTEEEE-------LLLGLLEEAGLEYLHLPIPDFGAP-----DDE 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2573424328  95 QLHQA--TILAVLEQQGTVAVHCRGGSGRTGLVIGLILLAYGWPAPKVIQQVQQIRPKALKHPVQLNY 160
Cdd:COG2453    65 QLQEAvdFIDEALREGKKVLVHCRGGIGRTGTVAAAYLVLLGLSAEEALARVRAARPGAVETPAQRAF 132
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 19-149 2.47e-10

dual specificity phosphatase domain of laforin and similar domains; This family is composed of glucan phosphatases including vertebrate dual specificity protein phosphatase laforin, also called lafora PTPase (LAFPTPase), and plant starch excess4 (SEX4). Laforin is a glycogen phosphatase; its gene is mutated in Lafora progressive myoclonus epilepsy or Lafora disease (LD), a fatal autosomal recessive neurodegenerative disorder characterized by the presence of progressive neurological deterioration, myoclonus, and epilepsy. One characteristic of LD is the accumulation of insoluble glucans. Laforin prevents LD by at least two mechanisms: by preventing hyperphosphorylation of glycogen by dephosphorylating it, allowing proper glycogen formation, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with malin. Laforin contains an N-terminal CBM20 (carbohydrate-binding module, family 20) domain and a C-terminal catalytic dual specificity phosphatase (DSP) domain. Plant SEX4 regulate starch metabolism by selectively dephosphorylating glucose moieties within starch glucan chains. It contains an N-terminal catalytic DSP domain and a C-terminal Early (E) set domain.


Pssm-ID: 350375 [Multi-domain]  Cd Length: 146  Bit Score: 55.67  E-value: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  19 LIFTPCPgtQSANltdSVATLKQAGTDMLLTLMFDQEMA--ENNASDLAKVCAEQDIQWLQLPIADdaapNSVFETQWQL 96
Cdd:cd14526    10 LIVGSCP--QNPE---DVDRLKKEGVTAVLNLQTDSDMEywGVDIDSIRKACKESGIRYVRLPIRD----FDTEDLRQKL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2573424328  97 HQA--TILAVLEQQGTVAVHCRGGSGR-TGLVIGLILLAYGWPAPKVIQQVQQIRP 149
Cdd:cd14526    81 PQAvaLLYRLLKNGGTVYVHCTAGLGRaPATVIAYLYWVLGYSLDEAYYLLTSKRP 136
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 72-150 5.03e-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: 51.89  E-value: 5.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  72 DIQWLQLPIADDAAPnsvfeTQWQLHQAtiLAVLEQQGT----VAVHCRGGSGRTGLVIGLILLAYGW-PAPKVIQQVQQ 146
Cdd:cd14504    49 GLRYHHIPIEDYTPP-----TLEQIDEF--LDIVEEANAkneaVLVHCLAGKGRTGTMLACYLVKTGKiSAVDAINEIRR 121


                  ....
gi 2573424328 147 IRPK 150
Cdd:cd14504   122 IRPG 125
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 104-159 2.59e-08

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 51.20  E-value: 2.59e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2573424328 104 VLEQQGTVAVHCRGGSGRTGLVIGLILL-AYGWPAPKVIQQVQQIRPKALKHPVQLN 159
Cdd:cd14506   105 ALQEGGKVAVHCHAGLGRTGVLIACYLVyALRMSADQAIRLVRSKRPNSIQTRGQVL 161
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 99-161 1.04e-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: 1.04e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2573424328  99 ATILAVLEQQ----GTVAVHCRGGSGRTGLVIGL-ILLAYGWPAPKVIQQVQQIRP-KALKHPVQLNYF 161
Cdd:cd14494    43 DRFLEVLDQAekpgEPVLVHCKAGVGRTGTLVACyLVLLGGMSAEEAVRIVRLIRPgGIPQTIEQLDFL 111
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 59-158 9.15e-07

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: 46.10  E-value: 9.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  59 NNASDLAKvcaeQDIQWLQLPIAD-DAAPNSVfetqwQLHQAT--ILAVLEQQGTVAVHCRGGSGRTGLVIGLILLA-YG 134
Cdd:cd14524    46 NSKEEWKA----LGVEQLRLPTVDfTGVPSLE-----DLEKGVdfILKHREKGKSVYVHCKAGRGRSATIVACYLIQhKG 116

                          90       100
                  ....*....|....*....|....
gi 2573424328 135 WPAPKVIQQVQQIRPKALKHPVQL 158
Cdd:cd14524   117 WSPEEAQEFLRSKRPHILLRLSQR 140
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 109-141 1.06e-06

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: 46.29  E-value: 1.06e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2573424328 109 GTVAVHCRGGSGRTGLVIGLILLA-YGWPAPKVI 141
Cdd:cd14499   110 GAIAVHCKAGLGRTGTLIACYLMKhYGFTAREAI 143
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 55-150 3.01e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 44.63  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  55 EMAENNASDLAKVCA---------EQDIQWLQLPIADDAAPNSVFETQW-QLHQATILAVLEQQGTVAVHCRGGSGRTGL 124
Cdd:PTZ00242   35 ELQRYNVTHLVRVCGptydaelleKNGIEVHDWPFDDGAPPPKAVIDNWlRLLDQEFAKQSTPPETIAVHCVAGLGRAPI 114

                          90       100
                  ....*....|....*....|....*.
gi 2573424328 125 VIGLILLAYGWPAPkvIQQVQQIRPK 150
Cdd:PTZ00242  115 LVALALVEYGGMEP--LDAVGFVREK 138
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
57-150 3.97e-06

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 44.20  E-value: 3.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328   57 AENNASDLAKVCAEQDIQWLQLPIADdaapNSVFETQWQLHQAT--ILAVLEQQGTVAVHCRGGSGRTG-LVIGLILLAY 133
Cdd:smart00195  29 HVINVTNEVPNYNGSDFTYLGVPIDD----NTETKISPYFPEAVefIEDAESKGGKVLVHCQAGVSRSAtLIIAYLMKTR 104

                           90
                   ....*....|....*..
gi 2573424328  134 GWPAPKVIQQVQQIRPK 150
Cdd:smart00195 105 NMSLNDAYDFVKDRRPI 121
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 22-146 6.93e-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: 43.52  E-value: 6.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  22 TPCPGT--QSANLT--DSVATLKQAGTDMLLTLMFDQEMAENNAsdlaKVCAEQDIQWLQLPIADDAAPNSvfetqwQLH 97
Cdd:cd14529     8 DVTPYVlyRSAQLSpdEDRALLKKLGIKTVIDLRGADERAASEE----AAAKIDGVKYVNLPLSATRPTES------DVQ 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2573424328  98 QATILAV-LEQQGTVAVHCRGGSGRTGLVIGLILLAYGWPAPKVIQQVQQ 146
Cdd:cd14529    78 SFLLIMDlKLAPGPVLIHCKHGKDRTGLVSALYRIVYGGSKEEANEDYRL 127
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 52-150 1.33e-05

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: 42.98  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  52 FDQEMAENNASDLAKVC---------AEQDIQWLQLPIADDAAPNSVFETQW-QLHQATILAVLEQQGTVAVHCRGGSGR 121
Cdd:cd14500    29 YIKELKKYNVTDLVRVCeptydkeplEKAGIKVHDWPFDDGSPPPDDVVDDWlDLLKTRFKEEGKPGACIAVHCVAGLGR 108

                          90       100
                  ....*....|....*....|....*....
gi 2573424328 122 TGLVIGLILLAYGWpapKVIQQVQQIRPK 150
Cdd:cd14500   109 APVLVAIALIELGM---KPEDAVEFIRKK 134
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 105-160 2.61e-05

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: 42.18  E-value: 2.61e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2573424328 105 LEQQGTVAVHCRGGSGRTGLVIGLILLAYGW--PAPKVIQQVQQIRPKALKHPV----QLNY 160
Cdd:cd14497    92 EDPNNVAVVHCKAGKGRTGTVICAYLLYYGQysTADEALEYFAKKRFKEGLPGVtipsQLRY 153
PRK12361 PRK12361
hypothetical protein; Provisional
 70-162 4.11e-05

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 42.69  E-value: 4.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  70 EQDIQWLQLPIADDAAPnsvfeTQWQLHQAtiLAVLEQQ----GTVAVHCRGGSGRTGLVIGLILLAygwPAPK-----V 140
Cdd:PRK12361  140 EEDIDYLNIPILDHSVP-----TLAQLNQA--INWIHRQvranKSVVVHCALGRGRSVLVLAAYLLC---KDPDltveeV 209

                          90       100
                  ....*....|....*....|..
gi 2573424328 141 IQQVQQIRPKALKHPVQLNYFN 162
Cdd:PRK12361  210 LQQIKQIRKTARLNKRQLRALE 231
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 67-157 5.67e-05

unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily is composed of uncharacterized bacterial and plant dual-specificity protein phosphatases. DUSPs function as a protein-serine/threonine phosphatases (EC 3.1.3.16) and a protein-tyrosine-phosphatases (EC 3.1.3.48).


Pssm-ID: 350376 [Multi-domain]  Cd Length: 136  Bit Score: 40.72  E-value: 5.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  67 VCAE-----QDIQWLQLPIADDAAPnsvfeTQWQLHQA--TILAVLEQQGTVAVHCRGGSGRTGLVIGLILLAYGwPAPK 139
Cdd:cd14527    33 LTAElprprKRQAYRCVPLLDLVAP-----TPEQLERAvaWIEELRAQGGPVLVHCALGYGRSATVVAAWLLAYG-RAKS 106

                          90       100
                  ....*....|....*....|.
gi 2573424328 140 V---IQQVQQIRPKALKHPVQ 157
Cdd:cd14527   107 VaeaEALIRAARPQVVLNPAQ 127
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
99-142 6.98e-05

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


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 41.48  E-value: 6.98e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2573424328  99 ATILAVL--EQQGTVAVHCRGGSGRTGLVIGLILLAYGWPAPKVIQ 142
Cdd:COG2365   122 RAAFRALadAENGPVLFHCTAGKDRTGVAAALLLLALGVPRETIMA 167
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
86-148 8.82e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 39.65  E-value: 8.82e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2573424328   86 PNSVFETQWQLHQAtiLAVLEQQGTVAVHCRGGSGRTGLVIGLILLA----YGWPAPKVIQQVQQIR 148
Cdd:smart00404  19 PDSILELLRAVKKN--LNQSESSGPVVVHCSAGVGRTGTFVAIDILLqqleAEAGEVDIFDTVKELR 83
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 86-148 8.82e-05

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: 39.65  E-value: 8.82e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2573424328   86 PNSVFETQWQLHQAtiLAVLEQQGTVAVHCRGGSGRTGLVIGLILLA----YGWPAPKVIQQVQQIR 148
Cdd:smart00012  19 PDSILELLRAVKKN--LNQSESSGPVVVHCSAGVGRTGTFVAIDILLqqleAEAGEVDIFDTVKELR 83
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 52-165 9.27e-05

protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), also known as protein-tyrosine phosphatase of regenerating liver 2 (PRL-2), stimulates progression from G1 into S phase during mitosis and promotes tumors. It regulates tumor cell migration and invasion through an ERK-dependent signaling pathway. Its overexpression correlates with breast tumor formation and progression. PRL-2 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: 350512 [Multi-domain]  Cd Length: 155  Bit Score: 40.37  E-value: 9.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  52 FDQEMAENNASDLAKVC---------AEQDIQWLQLPIADDAAPNSVFETQWQLHQATILAvlEQQGT-VAVHCRGGSGR 121
Cdd:cd18536    30 FTEELKKYGVTTLVRVCdatydkapvEKEGIQVLDWPFDDGAPPPNQIVDDWLNLLKTKFR--EEPGCcVAVHCVAGLGR 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2573424328 122 TGLVIGLILLAYGWPAPKVIQQVQQIRPKALKHPvQLNYFNSQR 165
Cdd:cd18536   108 APVLVALALIECGMKYEDAVQFIRQKRRGAFNSK-QLLYLEKYR 150
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 72-149 1.89e-04

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 39.17  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  72 DIQWLQLPIADdaapNSVFETQWQLHQAT--ILAVLEQQGTVAVHCRGGSGRTGLVIGLILLAY-GWPAPKVIQQVQQIR 148
Cdd:pfam00782  35 GILYLRIPVED----NHETNISKYLEEAVefIDDARQKGGKVLVHCQAGISRSATLIIAYLMKTrNLSLNEAYSFVKERR 110


                  .
gi 2573424328 149 P 149
Cdd:pfam00782 111 P 111
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 52-165 4.32e-04

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: 38.90  E-value: 4.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  52 FDQEMAENNASDLAKVCA---------EQDIQWLQLPIADDAAPNSVFETQWqLHQATILAVLEQQGTVAVHCRGGSGRT 122
Cdd:cd18537    33 FIEELKKYGVTTVVRVCEatydttlveKEGIQVLDWPFDDGAPPSNQIVDDW-LNLLKVKFREEPGCCIAVHCVAGLGRA 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2573424328 123 GLVIGLILLAYGWPAPKVIQQVQQIRPKALKHPvQLNYFNSQR 165
Cdd:cd18537   112 PVLVALALIECGMKYEDAVQFIRQKRRGAFNSK-QLLYLEKYR 153
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 42-134 5.92e-04

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 38.76  E-value: 5.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  42 AGTDMLLTLmFDQEMAENNASDLAKVC---------AEQDIQWLQLPIADDAAPNSVFETQWqlhqATIL-AVLEQQGTV 111
Cdd:PTZ00393   99 APTNDLLPL-YIKEMKNYNVTDLVRTCertyndgeiTSAGINVHELIFPDGDAPTVDIVSNW----LTIVnNVIKNNRAV 173

                          90       100
                  ....*....|....*....|...
gi 2573424328 112 AVHCRGGSGRTGLVIGLILLAYG 134
Cdd:PTZ00393  174 AVHCVAGLGRAPVLASIVLIEFG 196
PFA-DSP_unk cd18538
unknown subfamily of atypical dual-specificity phosphatases from fungi; This uncharacterized ...
 111-161 1.20e-03

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: 37.35  E-value: 1.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2573424328 111 VAVHCRGGSGRTGLVIGLILLAYGWPAPKVIQQVQQI-RPKAlkHPVQLNYF 161
Cdd:cd18538    93 ILVHCNKGKHRTGCVIACFRKLQGWDVENVLEEYLSYaHPKS--RDLDEEYI 142
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 52-165 1.28e-03

protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), also known as protein-tyrosine phosphatase of regenerating liver 3 (PRL-3), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It exerts its oncogenic functions through activation of PI3K/Akt, which is a key regulator of the rapamycin-sensitive mTOR complex 1. PRL-3 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: 350511 [Multi-domain]  Cd Length: 154  Bit Score: 37.31  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  52 FDQEMAENNASDLAKVCA--------EQD-IQWLQLPIADDAAPNSVFETQW-QLHQATILavlEQQGT-VAVHCRGGSG 120
Cdd:cd18535    29 FIEDLKKYGATTVVRVCEvtydktplEKDgITVVDWPFDDGAPPPGKVVEDWlSLLKTKFC---EDPGCcVAVHCVAGLG 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2573424328 121 RTGLVIGLILLAYGWPAPKVIQQVQQIRPKALKHPvQLNYFNSQR 165
Cdd:cd18535   106 RAPVLVALALIESGMKYEDAIQFIRQKRRGAINSK-QLTYLEKYR 149
DSP_slingshot_3 cd14571
dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein ...
 54-155 1.87e-03

dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein phosphatase slingshot homolog 3 (SSH3), also called SSH-like protein 3, is part of the slingshot (SSH) family, whose members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. The Xenopus homolog (xSSH) is involved in the gastrulation movement. Mouse SSH3 dephosphorylates actin-depolymerizing factor (ADF) and cofilin but is dispensable for development. There are at least two human SSH3 isoforms reported: hSSH-3L (long) and hSSH-3. As SSH family phosphatases, they contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. In addition, hSSH-3L contains a C-terminal tail while hSSH-3 does not.


Pssm-ID: 350419 [Multi-domain]  Cd Length: 144  Bit Score: 36.77  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  54 QEMAENNASDLAKVCAEQD------IQWLQLPIADDAAPNSVfeTQWQLHQATILAVLEQQGTVAVHCRGGSGRTG-LVI 126
Cdd:cd14571    23 EELQRNRVSHILNVTREIDnffperFTYMNIRVYDEEATQLL--PHWKETHRFIEAARAQGTRVLVHCKMGVSRSAsTVI 100

                          90       100
                  ....*....|....*....|....*....
gi 2573424328 127 GLILLAYGWPAPKVIQQVQQIRPKALKHP 155
Cdd:cd14571   101 AYAMKQYGWTLEQALRHVRERRPIVQPNP 129
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 103-134 2.42e-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: 37.22  E-value: 2.42e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2573424328 103 AVLEQQGTVAVHCRGGSGRTGLVIGLILLAYG 134
Cdd:pfam13350 124 ALADNDGPVLFHCTAGKDRTGVAAALLLSLLG 155
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 70-149 2.55e-03

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


Pssm-ID: 350348 [Multi-domain]  Cd Length: 135  Bit Score: 35.98  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573424328  70 EQDIQWLQLPIADDaapnSVFETQWQLHQAT--ILAVLEQQGTVAVHCRGGSGR--TgLVIGLILLAYGWPAPKVIQQVQ 145
Cdd:cd14498    43 PDGIKYLRIPIEDS----PDEDILSHFEEAIefIEEALKKGGKVLVHCQAGVSRsaT-IVIAYLMKKYGWSLEEALELVK 117


                  ....
gi 2573424328 146 QIRP 149
Cdd:cd14498   118 SRRP 121
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 111-134 3.28e-03

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 36.19  E-value: 3.28e-03
                          10        20
                  ....*....|....*....|....
gi 2573424328 111 VAVHCRGGSGRTGLVIGLILLAYG 134
Cdd:cd14510   111 VAIHCKGGKGRTGTMVCAWLIYSG 134
 
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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