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Conserved domains on  [gi|71424396|ref|XP_812787|]
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tyrosine phosphatase, putative [Trypanosoma cruzi]

Protein Classification

phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase PTEN family protein( domain architecture ID 12998259)

phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase PTEN family protein similar to Arabidopsis thaliana PTEN2B which is a protein tyrosine phosphatase that also has a weak lipid phosphatase activity towards PtdIns(3)P

EC:  3.1.3.48|3.1.3.67
Gene Ontology:  GO:0016791|GO:0016314|GO:0004725
PubMed:  27514797

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 32-196 5.63e-85

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


:

Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 253.28  E-value: 5.63e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396  32 DLVQIHRRIVCMGFPALGIESFYRNRYKDVLRYLDHMYGTDYMVYNLCAEpkYRYDLTFFHGRVREFPFPDHWACPLIMI 111
Cdd:cd14509   1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLCSE--RSYDPSKFNGRVAEYPFDDHNPPPLELI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396 112 PRFVEDAVRYITSADhaqEAVVVVHCKAGKGRTGLLTCCLLMEIEPSigGLAKNAISYYGIQRTFDGRGLTLPSQLRYVE 191
Cdd:cd14509  79 KPFCEDVDEWLKEDE---KNVAAVHCKAGKGRTGVMICCYLLYLGKF--PSAKEALDFYGAKRTKNKKGVTIPSQRRYVY 153


                ....*
gi 71424396 192 YYERL 196
Cdd:cd14509 154 YYSRL 158
 
Name Accession Description Interval E-value
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 32-196 5.63e-85

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 253.28  E-value: 5.63e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396  32 DLVQIHRRIVCMGFPALGIESFYRNRYKDVLRYLDHMYGTDYMVYNLCAEpkYRYDLTFFHGRVREFPFPDHWACPLIMI 111
Cdd:cd14509   1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLCSE--RSYDPSKFNGRVAEYPFDDHNPPPLELI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396 112 PRFVEDAVRYITSADhaqEAVVVVHCKAGKGRTGLLTCCLLMEIEPSigGLAKNAISYYGIQRTFDGRGLTLPSQLRYVE 191
Cdd:cd14509  79 KPFCEDVDEWLKEDE---KNVAAVHCKAGKGRTGVMICCYLLYLGKF--PSAKEALDFYGAKRTKNKKGVTIPSQRRYVY 153


                ....*
gi 71424396 192 YYERL 196
Cdd:cd14509 154 YYSRL 158
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
75-197 1.17e-11

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 61.53  E-value: 1.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396  75 VYNLCAEPKYRYDLTFFHG-RVREFPFPDHWACPLIMIprfvEDAVRYITSADHAQEaVVVVHCKAGKGRTGLLTCCLLM 153
Cdd:COG2453  29 VVSLTEEEELLLGLLEEAGlEYLHLPIPDFGAPDDEQL----QEAVDFIDEALREGK-KVLVHCRGGIGRTGTVAAAYLV 103

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71424396 154 EiepsiGGL-AKNAISYygIQRTFDGRGLTlPSQLRYVEYYERLR 197
Cdd:COG2453 104 L-----LGLsAEEALAR--VRAARPGAVET-PAQRAFLERFAKRL 140
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
103-153 5.14e-04

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 38.88  E-value: 5.14e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 71424396    103 HWACPLIMIPRFVEDAVRYITSADHAQE-----AVVVVHCKAGKGRTGLLtCCLLM 153
Cdd:smart00404   7 YTGWPDHGVPESPDSILELLRAVKKNLNqsessGPVVVHCSAGVGRTGTF-VAIDI 61
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 111-153 5.00e-03

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: 36.47  E-value: 5.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 71424396   111 IPRFVEDAVRYITSADHAQEAVVVvHCKAGKGRTGLLTCCLLM 153
Cdd:pfam00782  51 ISKYLEEAVEFIDDARQKGGKVLV-HCQAGISRSATLIIAYLM 92
 
Name Accession Description Interval E-value
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 32-196 5.63e-85

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 253.28  E-value: 5.63e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396  32 DLVQIHRRIVCMGFPALGIESFYRNRYKDVLRYLDHMYGTDYMVYNLCAEpkYRYDLTFFHGRVREFPFPDHWACPLIMI 111
Cdd:cd14509   1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLCSE--RSYDPSKFNGRVAEYPFDDHNPPPLELI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396 112 PRFVEDAVRYITSADhaqEAVVVVHCKAGKGRTGLLTCCLLMEIEPSigGLAKNAISYYGIQRTFDGRGLTLPSQLRYVE 191
Cdd:cd14509  79 KPFCEDVDEWLKEDE---KNVAAVHCKAGKGRTGVMICCYLLYLGKF--PSAKEALDFYGAKRTKNKKGVTIPSQRRYVY 153


                ....*
gi 71424396 192 YYERL 196
Cdd:cd14509 154 YYSRL 158
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 32-196 6.61e-47

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: 155.82  E-value: 6.61e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396  32 DLVQIHRRIVCMGFPALGI-ESFYRNRYKDVLRYLDHMYGTDYMVYNLCAEpKYRYDlTFFHGRVREFPFPDHWACPLIM 110
Cdd:cd14497   1 DLSYITPRIIAMSFPATGYpESLYRNSIDDVANFLNTHHPDHYMIFNLSEE-EYDDD-SKFEGRVLHYGFPDHHPPPLGL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396 111 IPRFVEDAVRYItSADhaQEAVVVVHCKAGKGRTGLLTCCLLMEIepSIGGLAKNAISYYGIQRT-FDGRGLTLPSQLRY 189
Cdd:cd14497  79 LLEIVDDIDSWL-SED--PNNVAVVHCKAGKGRTGTVICAYLLYY--GQYSTADEALEYFAKKRFkEGLPGVTIPSQLRY 153


                ....*..
gi 71424396 190 VEYYERL 196
Cdd:cd14497 154 LQYFERL 160
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 29-196 3.61e-44

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: 149.44  E-value: 3.61e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396  29 VDLDLVQIHRRIVCMGFPALGIESFYRNRYKDVLRYLDHMYGTDYMVYNLCAEPKyrYDLTFFHGRVREFPFPDHWACPL 108
Cdd:cd14510  12 FDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLCSERG--YDPKYFHNRVERVPIDDHNVPTL 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396 109 IMIPRFVEDAVRYItSADhaQEAVVVVHCKAGKGRTGLLTCCLLMEIE--PSigglAKNAISYYGIQRTFDG-----RGL 181
Cdd:cd14510  90 DEMLSFTAEVREWM-AAD--PKNVVAIHCKGGKGRTGTMVCAWLIYSGqfES----AKEALEYFGERRTDKSvsskfQGV 162

                       170
                ....*....|....*
gi 71424396 182 TLPSQLRYVEYYERL 196
Cdd:cd14510 163 ETPSQSRYVGYFEKL 177
PTP_tensin cd14508
protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular ...
 32-196 1.90e-23

protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular proteins (tensin-1, -2, -3 and -4) act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Dysregulation of tensin expression has been implicated in human cancer. Tensin-1, -2, and -3 contain an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. In addition, tensin-2 contains a zinc finger N-terminal to its PTP domain. Tensin-4 is not included in this model as it does not contain a PTP-like domain.


Pssm-ID: 350358 [Multi-domain]  Cd Length: 159  Bit Score: 94.38  E-value: 1.90e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396  32 DLVQIHRRIVCMGFPALGIESFYRNRYKDVLRYLDHMYGTDYMVYNLcAEPkyRYDLTFFHGRVREFPFPDHWACPLIMI 111
Cdd:cd14508   1 DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNL-SER--RHDLRSLNPKVLDFGWPELHAPPLEKL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396 112 PRFVEDAVRYITSADHaqeAVVVVHCKAGKGRTGLLTCClLMEIEpSIGGLAKNAISYYGIQRTFDGR--GLTLPSQLRY 189
Cdd:cd14508  78 CSICKNMDSWLNADPQ---NVVVLHCKGGKGRLGVVVSA-YMHYS-KISATADQALDRFAMKRFYDDKvgPLGQPSQKRY 152


                ....*..
gi 71424396 190 VEYYERL 196
Cdd:cd14508 153 VGYFSGL 159
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
 30-192 6.76e-23

protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily contains proteins similar to auxilin, characterized by also containing a J domain. It includes auxilin, also called auxilin-1, and cyclin-G-associated kinase (GAK), also called auxilin-2. Auxilin-1 and -2 facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, while auxilin-1 which is nerve-specific. Both proteins contain a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with clathrin-binding and J domains. In addition, GAK contains an N-terminal protein kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2.


Pssm-ID: 350361 [Multi-domain]  Cd Length: 164  Bit Score: 93.18  E-value: 6.76e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396  30 DLDLVQIHRRIVCMGFPALGIESFYR-NRYKDVLRYLDHMYGTDYMVYNLcaEPKyRYDLTFFHGRVREFPFPDHWACPL 108
Cdd:cd14511   8 DLDISYITSRIIVMPFPAEGIESTYRkNNIEDVRAFLDSRHPQKYSVYNL--SPR-SYPTLRLPSRVVECSWPYRRAPSL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396 109 IMIPRFVEDAVRYItSADHAQeaVVVVHCKAGKGRTGLLTCCLLMeiepsIGGLAKN---AISYYGIQRTfdGRGLTlPS 185
Cdd:cd14511  85 HALYALCRDIYQWL-NKDPKN--VIVIHCTDGKAASATVVCALLV-----YCGLFKTpedALQMFAVKRC--PPGLS-PS 153


                ....*..
gi 71424396 186 QLRYVEY 192
Cdd:cd14511 154 ELRYLYY 160
PTP_tensin-1 cd14560
protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin ...
 32-196 1.05e-18

protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. It plays an essential role in TGF-beta-induced myofibroblast differentiation and myofibroblast-mediated formation of extracellular fibronectin and collagen matrix. It also positively regulates RhoA activity through its interaction with DLC1, a RhoGAP-containing tumor suppressor; the tensin-1-DLC1-RhoA signaling axis is critical in regulating cellular functions that lead to angiogenesis. Tensin-1 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350408 [Multi-domain]  Cd Length: 159  Bit Score: 81.56  E-value: 1.05e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396  32 DLVQIHRRIVCMGFPALGIESFYRNRYKDVLRYLDHMYGTDYMVYNLCAEpkyRYDLTFFHGRVREFPFPDHWACPLIMI 111
Cdd:cd14560   1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSER---RHDISKLHPKVLDFGWPDLHAPALEKI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396 112 PRFVEDAVRYITSADHaqeAVVVVHCKAGKGRTGLLTCCLLMeiEPSIGGLAKNAISYYGIQRTFDGRGLTL--PSQLRY 189
Cdd:cd14560  78 CSICKAMDTWLNADPH---NVVVIHNKGNRGRTGVVIAAYMH--YSNISASADQALDRFAMKRFYEDKVVPVgqPSQKRY 152


                ....*..
gi 71424396 190 VEYYERL 196
Cdd:cd14560 153 VHYFSGL 159
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 32-196 2.13e-17

protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called tensin-like SH2 domain-containing protein 1 (TENS1) or tumor endothelial marker (TEM6). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-3 contributes to cell migration, anchorage-independent growth, tumorigenesis, and metastasis of cancer cells. It cooperates with Dock5, an exchange factor for the small GTPase Rac, for osteoclast activity to ensure the correct organization of podosomes. Tensin-3 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350409 [Multi-domain]  Cd Length: 159  Bit Score: 78.06  E-value: 2.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396  32 DLVQIHRRIVCMGFPALGIESFYRNRYKDVLRYLDHMYGTDYMVYNLCAEpkyRYDLTFFHGRVREFPFPDHWACPLIMI 111
Cdd:cd14561   1 DLTYITERIIAVSFPADCSEETYLHNLQDVTRMLKSKHGDNYLVLNLSEK---RYELTKLNPKIMDVGWPDLHAPPLDKM 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396 112 PRFVEDAVRYITSadhAQEAVVVVHCKAGKGRTGLLTCCLLMEIepSIGGLAKNAISYYGIQRTFDGR--GLTLPSQLRY 189
Cdd:cd14561  78 CTICKAMESWLNS---DPLHVVVIHCRGGKGRIGVVISSYMHFT--NVSASADQALDRFAMKKFYDDKvsALMQPSQKRY 152


                ....*..
gi 71424396 190 VEYYERL 196
Cdd:cd14561 153 VQFLSGL 159
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
 32-196 1.42e-14

protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called tensin-like C1 domain-containing phosphatase (TENC1) or C1 domain-containing phosphatase and tensin homolog (C1-TEN). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-2 is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It also modulates cell contractility and remodeling of collagen fibers through the DLC1, a RhoGAP that binds to tensins in focal adhesions. Tensin-2 may have phosphatase activity; it reduces AKT1 phosphorylation. It contains an N-terminal region with a zinc finger, a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350410 [Multi-domain]  Cd Length: 159  Bit Score: 70.36  E-value: 1.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396  32 DLVQIHRRIVCMGFPALGIESFYRNRYKDVLRYLDHMYGTDYMVYNLCAEpkyRYDLTFFHGRVREFPFPDHWACPLIMI 111
Cdd:cd14562   1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNLSEK---RHDITRLNPKVQDFGWPDLHAPPLDKI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396 112 PRFVEDAVRYITSadhAQEAVVVVHCKAGKGRTGLLTCCLLMEIEPSIGglAKNAISYYGIqRTF--DGRGLTL-PSQLR 188
Cdd:cd14562  78 CSICKAMETWLNA---DPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAG--ADQALSTLAM-RKFceDKVATSLqPSQRR 151


                ....*...
gi 71424396 189 YVEYYERL 196
Cdd:cd14562 152 YISYFGGL 159
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 30-192 6.34e-14

protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated kinase (GAK), also called auxilin-2, contains an N-terminal protein kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with clathrin-binding and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor.


Pssm-ID: 350412 [Multi-domain]  Cd Length: 163  Bit Score: 68.78  E-value: 6.34e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396  30 DLDLVQIHRRIVCMGFPALGIESFYRNRYKDVLRYLDHMYGTDYMVYNLCaepKYRYDLTFFHGRVREFPFPDHWACPLI 109
Cdd:cd14564   8 DLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLS---QRTYRPSRFHNRVSECGWPARRAPNLQ 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396 110 MIPRFVEDAVRYITsadHAQEAVVVVHCKAGKGRTGLLTCCLLMEIEpsIGGLAKNAISYYGIQRTFDGRGltlPSQLRY 189
Cdd:cd14564  85 NLYSICKNMHLWLK---QDQKNICIVHCLDGRAASAVVVCSFLCFCR--LFTTAEAAVYMFSMKRCPPGIW---PSHKRY 156


                ...
gi 71424396 190 VEY 192
Cdd:cd14564 157 IEY 159
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
75-197 1.17e-11

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 61.53  E-value: 1.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396  75 VYNLCAEPKYRYDLTFFHG-RVREFPFPDHWACPLIMIprfvEDAVRYITSADHAQEaVVVVHCKAGKGRTGLLTCCLLM 153
Cdd:COG2453  29 VVSLTEEEELLLGLLEEAGlEYLHLPIPDFGAPDDEQL----QEAVDFIDEALREGK-KVLVHCRGGIGRTGTVAAAYLV 103

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71424396 154 EiepsiGGL-AKNAISYygIQRTFDGRGLTlPSQLRYVEYYERLR 197
Cdd:COG2453 104 L-----LGLsAEEALAR--VRAARPGAVET-PAQRAFLERFAKRL 140
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 30-152 1.05e-09

N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 or DnaJ homolog subfamily C member 6 (DNAJC6), is a J-domain containing protein that recruits the ATP-dependent chaperone Hsc70 to newly budded clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles, driving the clathrin assembly#disassembly cycle. Mutations in the DNAJC6 gene, encoding auxilin, are associated with early-onset Parkinson's disease. Auxilin contains an N-terminal protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN, a phosphoinositide 3-phosphatase, and a C-terminal region with clathrin-binding and J domains.


Pssm-ID: 350411 [Multi-domain]  Cd Length: 163  Bit Score: 56.81  E-value: 1.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396  30 DLDLVQIHRRIVCMGFPALGIESFYRNRYKDVLRYLDHMYGTDYMVYNLcaEPKYrYDLTFFHGRVREFPFPDHWACPLI 109
Cdd:cd14563   8 ELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNL--SQKS-YRSAKFHNRVSECSWPVRQAPSLH 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 71424396 110 MIPRFVEDAVRYITsadHAQEAVVVVHCKAGKGRTGLLTCCLL 152
Cdd:cd14563  85 NLFAVCKNMHNWLQ---QNPKNVCVIHCMDGRAASAVLVSAMF 124
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 133-190 2.47e-07

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: 49.57  E-value: 2.47e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71424396 133 VVVHCKAGKGRTGLLTCCLLMEIEPSIGglAKNAISyygIQRTFDGRGLTLPSQLRYV 190
Cdd:cd14505 109 VLIHCKGGLGRTGLIAACLLLELGDTLD--PEQAIA---AVRALRPGAIQTPKQENFL 161
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 115-192 1.36e-06

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: 46.57  E-value: 1.36e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71424396 115 VEDAVRYITSAdHAQEAVVVVHCKAGKGRTGLLTCCLLMEiepsIGGL-AKNAISYYGIQRTfdGRGLTLPSQLRYVEY 192
Cdd:cd14494  42 VDRFLEVLDQA-EKPGEPVLVHCKAGVGRTGTLVACYLVL----LGGMsAEEAVRIVRLIRP--GGIPQTIEQLDFLIK 113
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 95-153 5.19e-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: 5.19e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71424396  95 VREFPFPDHW-ACP-----LIMIPRF-------VEDAVRYITSADHAQEAVVVvHCKAGKGRTGLLTCCLLM 153
Cdd:cd14504  35 LTEEPPPEHSdTCPglryhHIPIEDYtpptleqIDEFLDIVEEANAKNEAVLV-HCLAGKGRTGTMLACYLV 105
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 132-153 1.17e-04

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: 42.05  E-value: 1.17e-04
                        10        20
                ....*....|....*....|..
gi 71424396 132 VVVVHCKAGKGRTGLLTCCLLM 153
Cdd:cd14499 111 AIAVHCKAGLGRTGTLIACYLM 132
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 94-153 1.58e-04

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: 42.34  E-value: 1.58e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71424396  94 RVREFPFPDHWACPLimipRFVEDAVRYITSAdhAQEAV-VVVHCKAGKGRTGLLTCCLLM 153
Cdd:cd14506  78 YFYNFGWKDYGVPSL----TTILDIVKVMAFA--LQEGGkVAVHCHAGLGRTGVLIACYLV 132
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 101-149 4.49e-04

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 40.82  E-value: 4.49e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71424396 101 PDHWAcplimiPRFVEDAVRYITSADH-AQEAVVVVHCKAGKGRTGLLTC 149
Cdd:cd14538 116 PDHGT------PQSADPLLRFIRYMRRiHNSGPIVVHCSAGIGRTGVLIT 159
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
103-153 5.14e-04

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 38.88  E-value: 5.14e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 71424396    103 HWACPLIMIPRFVEDAVRYITSADHAQE-----AVVVVHCKAGKGRTGLLtCCLLM 153
Cdd:smart00404   7 YTGWPDHGVPESPDSILELLRAVKKNLNqsessGPVVVHCSAGVGRTGTF-VAIDI 61
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 103-153 5.14e-04

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: 38.88  E-value: 5.14e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 71424396    103 HWACPLIMIPRFVEDAVRYITSADHAQE-----AVVVVHCKAGKGRTGLLtCCLLM 153
Cdd:smart00012   7 YTGWPDHGVPESPDSILELLRAVKKNLNqsessGPVVVHCSAGVGRTGTF-VAIDI 61
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 133-193 1.29e-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: 38.89  E-value: 1.29e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71424396 133 VVVHCKAGKGRTGLLTCCLLMEIEPSIGGLAKNA-ISYYGIqrTFDGRGLTLPSQLRYVEYY 193
Cdd:cd14529  92 VLIHCKHGKDRTGLVSALYRIVYGGSKEEANEDYrLSNRHL--EGLRSGIALDSKGGVKGRY 151
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 75-154 1.89e-03

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: 38.01  E-value: 1.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71424396  75 VYNLCAEpkyrYDLTFFHGRVRE----------FPFPDHWACPLIMIprfVEDAVRYITsaDHAQEAV-VVVHCKAGKGR 143
Cdd:cd14524  32 VITMNEE----YETRFFCNSKEEwkalgveqlrLPTVDFTGVPSLED---LEKGVDFIL--KHREKGKsVYVHCKAGRGR 102

                        90
                ....*....|.
gi 71424396 144 TGLLTCCLLME 154
Cdd:cd14524 103 SATIVACYLIQ 113
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
111-153 2.15e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 37.65  E-value: 2.15e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 71424396    111 IPRFVEDAVRYITSAdHAQEAVVVVHCKAGKGRTGLLTCCLLM 153
Cdd:smart00195  60 ISPYFPEAVEFIEDA-ESKGGKVLVHCQAGVSRSATLIIAYLM 101
DSP_DUSP9 cd14644
dual specificity phosphatase domain of dual specificity protein phosphatase 9; Dual ...
 91-154 4.54e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 9; Dual specificity protein phosphatase 9 (DUSP9), also called mitogen-activated protein kinase (MAPK) phosphatase 4 (MKP-4), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class II subfamily and is an ERK-selective cytoplasmic MKP. DUSP9 is a mediator of bone morphogenetic protein (BMP) signaling to control the appropriate ERK activity critical for the determination of embryonic stem cell fate. Down-regulation of DUSP9 expression has been linked to severe pre-eclamptic placenta as well as cancers such as hepatocellular carcinoma. DUSP9 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350492 [Multi-domain]  Cd Length: 145  Bit Score: 36.90  E-value: 4.54e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71424396  91 FHgrVREFPFPDHWACPLimiPRFVEDAVRYITSAdHAQEAVVVVHCKAGKGRTGLLTCCLLME 154
Cdd:cd14644  49 FH--YKQIPISDHWSQNL---SQFFPEAIEFIDEA-LSQNCGVLVHCLAGISRSVTVTVAYLMQ 106
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 111-153 5.00e-03

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: 36.47  E-value: 5.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 71424396   111 IPRFVEDAVRYITSADHAQEAVVVvHCKAGKGRTGLLTCCLLM 153
Cdd:pfam00782  51 ISKYLEEAVEFIDDARQKGGKVLV-HCQAGISRSATLIIAYLM 92
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
134-154 7.90e-03

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 37.38  E-value: 7.90e-03
                        10        20
                ....*....|....*....|.
gi 71424396 134 VVHCKAGKGRTGLLTCCLLME 154
Cdd:COG5599 210 VVHCRAGVGRTGTLIACLALS 230
DSP_DUSP7 cd14643
dual specificity phosphatase domain of dual specificity protein phosphatase 7; Dual ...
 94-154 8.16e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 7; Dual specificity protein phosphatase 7 (DUSP7), also called mitogen-activated protein kinase (MAPK) phosphatase X (MKP-X) or dual specificity protein phosphatase PYST2, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class II subfamily and is an ERK-selective cytoplasmic MKP. DUSP7 has been shown as an essential regulator of multiple steps in oocyte meiosis. Due to alternative promoter usage, the PYST2 gene gives rise to two isoforms, PYST2-S and PYST2-L. PYST2-L is over-expressed in leukocytes derived from AML and ALL patients as well as in some solid tumors and lymphoblastoid cell lines; it plays a role in cell-crowding. It contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350491 [Multi-domain]  Cd Length: 149  Bit Score: 36.54  E-value: 8.16e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71424396  94 RVREFPFPDHWACPLimiPRFVEDAVRYITSAdHAQEAVVVVHCKAGKGRTGLLTCCLLME 154
Cdd:cd14643  53 KYKQIPISDHWSQNL---SQFFPEAISFIDEA-RSKKCGILVHCLAGISRSVTVTVAYLMQ 109
 
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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