NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1167750697|gb|ARB02560|]
View 

PTENbeta [Homo sapiens]

Protein Classification

phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN( domain architecture ID 12998284)

phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 170-327 2.24e-113

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: 333.40  E-value: 2.24e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 170 DLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKP 249
Cdd:cd14509     1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLCSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1167750697 250 FCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYL 327
Cdd:cd14509    81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTKNKKGVTIPSQRRYVYYYSRL 158
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 334-495 3.94e-42

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


:

Pssm-ID: 463081  Cd Length: 133  Bit Score: 147.42  E-value: 3.94e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 334 YRPVALLFHKMMFETIPMF-SGGTCNPQFVVCQLKVKI---YSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNK 409
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFkSGGGCRPYIRIYQNKKKVfstSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 410 MLKKDKMFHFWVNTFFIPgpeetsekvengslcdqeidsicsieradndkeYLVLTLTKNDLDKANKDKANRYFSPNFKV 489
Cdd:pfam10409  81 LLSEEKMFRFWFNTSFIE---------------------------------DNTLTLPKNELDKADKDKKDKRFPKDFKV 127


                  ....*.
gi 1167750697 490 KLYFTK 495
Cdd:pfam10409 128 ELLFSE 133
 
Name Accession Description Interval E-value
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 170-327 2.24e-113

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: 333.40  E-value: 2.24e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 170 DLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKP 249
Cdd:cd14509     1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLCSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1167750697 250 FCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYL 327
Cdd:cd14509    81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTKNKKGVTIPSQRRYVYYYSRL 158
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 334-495 3.94e-42

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


Pssm-ID: 463081  Cd Length: 133  Bit Score: 147.42  E-value: 3.94e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 334 YRPVALLFHKMMFETIPMF-SGGTCNPQFVVCQLKVKI---YSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNK 409
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFkSGGGCRPYIRIYQNKKKVfstSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 410 MLKKDKMFHFWVNTFFIPgpeetsekvengslcdqeidsicsieradndkeYLVLTLTKNDLDKANKDKANRYFSPNFKV 489
Cdd:pfam10409  81 LLSEEKMFRFWFNTSFIE---------------------------------DNTLTLPKNELDKADKDKKDKRFPKDFKV 127


                  ....*.
gi 1167750697 490 KLYFTK 495
Cdd:pfam10409 128 ELLFSE 133
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
176-324 5.01e-17

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 77.70  E-value: 5.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 176 PNIIA-MGFPAERLEGVYRNNIDDVVrfldskhknhykiyNLCAERHYD---TAKFNCRVAQYPFEDHNPPQLELIKPFC 251
Cdd:COG2453     5 PGLLAgGPLPGGGEADLKREGIDAVV--------------SLTEEEELLlglLEEAGLEYLHLPIPDFGAPDDEQLQEAV 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167750697 252 EDLDQWLSEDdnHVAAIHCKAGKGRTGVMICAYLLHRGkfLKAQEALDFygeVRTRDKKGVTIPSQRRYVYYY 324
Cdd:COG2453    71 DFIDEALREG--KKVLVHCRGGIGRTGTVAAAYLVLLG--LSAEEALAR---VRAARPGAVETPAQRAFLERF 136
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
238-329 1.03e-10

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 58.52  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697  238 DHN-PPQLELIKPFCEDLDQWLS-EDDNHVAAIHCKAGKGRTGVMICAYLLHRgKFLKAQEALDFYGEVRT-RDKKGVTI 314
Cdd:smart00404  12 DHGvPESPDSILELLRAVKKNLNqSESSGPVVVHCSAGVGRTGTFVAIDILLQ-QLEAEAGEVDIFDTVKElRSQRPGMV 90

                           90
                   ....*....|....*
gi 1167750697  315 PSQRRYVYYYSYLLK 329
Cdd:smart00404  91 QTEEQYLFLYRALLE 105
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 193-309 3.72e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 47.32  E-value: 3.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 193 RNNIDDVVRfldskhknhykiynlCAERHYDTAKF---NCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSED--DNHVAA 267
Cdd:PTZ00242   38 RYNVTHLVR---------------VCGPTYDAELLeknGIEVHDWPFDDGAPPPKAVIDNWLRLLDQEFAKQstPPETIA 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1167750697 268 IHCKAGKGRTGVMICAYLLHRGKFlkaqEALDFYGEVRTRDK 309
Cdd:PTZ00242  103 VHCVAGLGRAPILVALALVEYGGM----EPLDAVGFVREKRK 140
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 242-305 2.05e-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: 41.48  E-value: 2.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167750697 242 PQLELIKPFCEDLDQwlsedDNHVAAIHCKAGKGRTGVMICAYLLHRGKfLKAQEALDFYGEVR 305
Cdd:pfam00782  53 KYLEEAVEFIDDARQ-----KGGKVLVHCQAGISRSATLIIAYLMKTRN-LSLNEAYSFVKERR 110
 
Name Accession Description Interval E-value
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 170-327 2.24e-113

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: 333.40  E-value: 2.24e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 170 DLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKP 249
Cdd:cd14509     1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLCSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1167750697 250 FCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYL 327
Cdd:cd14509    81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTKNKKGVTIPSQRRYVYYYSRL 158
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 170-327 1.84e-82

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: 254.04  E-value: 1.84e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 170 DLTYIYPNIIAMGFPAER-LEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIK 248
Cdd:cd14497     1 DLSYITPRIIAMSFPATGyPESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDDDSKFEGRVLHYGFPDHHPPPLGLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 249 PFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKK-GVTIPSQRRYVYYYSYL 327
Cdd:cd14497    81 EIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKRFKEGLpGVTIPSQLRYLQYFERL 160
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 156-327 3.57e-82

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: 253.82  E-value: 3.57e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 156 SRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYP 235
Cdd:cd14510     1 SENKRRYQKDGFDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLCSERGYDPKYFHNRVERVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 236 FEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTR----DK-K 310
Cdd:cd14510    81 IDDHNVPTLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTDksvsSKfQ 160

                         170
                  ....*....|....*..
gi 1167750697 311 GVTIPSQRRYVYYYSYL 327
Cdd:cd14510   161 GVETPSQSRYVGYFEKL 177
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 334-495 3.94e-42

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


Pssm-ID: 463081  Cd Length: 133  Bit Score: 147.42  E-value: 3.94e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 334 YRPVALLFHKMMFETIPMF-SGGTCNPQFVVCQLKVKI---YSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNK 409
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFkSGGGCRPYIRIYQNKKKVfstSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 410 MLKKDKMFHFWVNTFFIPgpeetsekvengslcdqeidsicsieradndkeYLVLTLTKNDLDKANKDKANRYFSPNFKV 489
Cdd:pfam10409  81 LLSEEKMFRFWFNTSFIE---------------------------------DNTLTLPKNELDKADKDKKDKRFPKDFKV 127


                  ....*.
gi 1167750697 490 KLYFTK 495
Cdd:pfam10409 128 ELLFSE 133
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
 168-325 8.22e-41

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: 144.80  E-value: 8.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 168 DLDLTYIYPNIIAMGFPAERLEGVYR-NNIDDVVRFLDSKHKNHYKIYNLcAERHYDTAKFNCRVAQYPFEDHNPPQLEL 246
Cdd:cd14511     8 DLDISYITSRIIVMPFPAEGIESTYRkNNIEDVRAFLDSRHPQKYSVYNL-SPRSYPTLRLPSRVVECSWPYRRAPSLHA 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167750697 247 IKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDkkGVTiPSQRRYVYYYS 325
Cdd:cd14511    87 LYALCRDIYQWLNKDPKNVIVIHCTDGKAASATVVCALLVYCGLFKTPEDALQMFAVKRCPP--GLS-PSELRYLYYFS 162
PTP_tensin cd14508
protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular ...
 170-327 1.22e-40

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: 144.45  E-value: 1.22e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 170 DLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLcAERHYDTAKFNCRVAQYPFEDHNPPQLELIKP 249
Cdd:cd14508     1 DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNL-SERRHDLRSLNPKVLDFGWPELHAPPLEKLCS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 250 FCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKK--GVTIPSQRRYVYYYSYL 327
Cdd:cd14508    80 ICKNMDSWLNADPQNVVVLHCKGGKGRLGVVVSAYMHYSKISATADQALDRFAMKRFYDDKvgPLGQPSQKRYVGYFSGL 159
PTP_tensin-1 cd14560
protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin ...
 170-327 1.93e-35

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: 130.10  E-value: 1.93e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 170 DLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLcAERHYDTAKFNCRVAQYPFEDHNPPQLELIKP 249
Cdd:cd14560     1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNL-SERRHDISKLHPKVLDFGWPDLHAPALEKICS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 250 FCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTI--PSQRRYVYYYSYL 327
Cdd:cd14560    80 ICKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRFYEDKVVPVgqPSQKRYVHYFSGL 159
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 170-327 2.32e-33

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: 124.67  E-value: 2.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 170 DLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLcAERHYDTAKFNCRVAQYPFEDHNPPQLELIKP 249
Cdd:cd14561     1 DLTYITERIIAVSFPADCSEETYLHNLQDVTRMLKSKHGDNYLVLNL-SEKRYELTKLNPKIMDVGWPDLHAPPLDKMCT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 250 FCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKK--GVTIPSQRRYVYYYSYL 327
Cdd:cd14561    80 ICKAMESWLNSDPLHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMKKFYDDKvsALMQPSQKRYVQFLSGL 159
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
 170-327 2.10e-31

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: 119.28  E-value: 2.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 170 DLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHyDTAKFNCRVAQYPFEDHNPPQLELIKP 249
Cdd:cd14562     1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNLSEKRH-DITRLNPKVQDFGWPDLHAPPLDKICS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 250 FCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVR-TRDKKGVTI-PSQRRYVYYYSYL 327
Cdd:cd14562    80 ICKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALSTLAMRKfCEDKVATSLqPSQRRYISYFGGL 159
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 168-323 1.32e-30

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: 116.93  E-value: 1.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 168 DLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCaERHYDTAKFNCRVAQYPFEDHNPPQLELI 247
Cdd:cd14564     8 DLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLS-QRTYRPSRFHNRVSECGWPARRAPNLQNL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167750697 248 KPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALdfYGEVRTRDKKGVTiPSQRRYVYY 323
Cdd:cd14564    87 YSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAV--YMFSMKRCPPGIW-PSHKRYIEY 159
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 168-323 2.54e-27

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: 108.04  E-value: 2.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 168 DLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLcAERHYDTAKFNCRVAQYPFEDHNPPQLELI 247
Cdd:cd14563     8 ELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNL-SQKSYRSAKFHNRVSECSWPVRQAPSLHNL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167750697 248 KPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFygeVRTRDKKGVTIPSQRRYVYY 323
Cdd:cd14563    87 FAVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQL---LNAKRPGIGLWPSHRRYIGY 159
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 171-323 9.00e-18

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: 78.93  E-value: 9.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 171 LTYIYP-NIIAMGFPAERLEgvyrnnidDVVRFLDSKHknHYKIYNLCaerhydtakfncrvaqypfedhnppqLELIKP 249
Cdd:cd14494     1 FNWIDPlRLIAGALPLSPLE--------ADSRFLKQLG--VTTIVDLT--------------------------LAMVDR 44

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167750697 250 FCEDLDQWLSedDNHVAAIHCKAGKGRTGVMICAYLLHRGKFlKAQEALDFYGEVRTRDKKgvTIPSQRRYVYY 323
Cdd:cd14494    45 FLEVLDQAEK--PGEPVLVHCKAGVGRTGTLVACYLVLLGGM-SAEEAVRIVRLIRPGGIP--QTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
176-324 5.01e-17

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 77.70  E-value: 5.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 176 PNIIA-MGFPAERLEGVYRNNIDDVVrfldskhknhykiyNLCAERHYD---TAKFNCRVAQYPFEDHNPPQLELIKPFC 251
Cdd:COG2453     5 PGLLAgGPLPGGGEADLKREGIDAVV--------------SLTEEEELLlglLEEAGLEYLHLPIPDFGAPDDEQLQEAV 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167750697 252 EDLDQWLSEDdnHVAAIHCKAGKGRTGVMICAYLLHRGkfLKAQEALDFygeVRTRDKKGVTIPSQRRYVYYY 324
Cdd:COG2453    71 DFIDEALREG--KKVLVHCRGGIGRTGTVAAAYLVLLG--LSAEEALAR---VRAARPGAVETPAQRAFLERF 136
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 193-297 7.12e-11

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: 60.93  E-value: 7.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 193 RNNIDDVVRfLDSKhknhykIYNlcAER-------HYDtakfncrvaqYPFEDHNPPQLELIKPFCEdldqwLSEDDNHV 265
Cdd:cd14499    56 KLGVTTVVR-LNKK------LYD--AKRftdagirHYD----------LYFPDGSTPSDDIVKKFLD-----ICENEKGA 111

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1167750697 266 AAIHCKAGKGRTGVMICAYLLHRGKFlKAQEA 297
Cdd:cd14499   112 IAVHCKAGLGRTGTLIACYLMKHYGF-TAREA 142
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
238-329 1.03e-10

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 58.52  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697  238 DHN-PPQLELIKPFCEDLDQWLS-EDDNHVAAIHCKAGKGRTGVMICAYLLHRgKFLKAQEALDFYGEVRT-RDKKGVTI 314
Cdd:smart00404  12 DHGvPESPDSILELLRAVKKNLNqSESSGPVVVHCSAGVGRTGTFVAIDILLQ-QLEAEAGEVDIFDTVKElRSQRPGMV 90

                           90
                   ....*....|....*
gi 1167750697  315 PSQRRYVYYYSYLLK 329
Cdd:smart00404  91 QTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 238-329 1.03e-10

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: 58.52  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697  238 DHN-PPQLELIKPFCEDLDQWLS-EDDNHVAAIHCKAGKGRTGVMICAYLLHRgKFLKAQEALDFYGEVRT-RDKKGVTI 314
Cdd:smart00012  12 DHGvPESPDSILELLRAVKKNLNqSESSGPVVVHCSAGVGRTGTFVAIDILLQ-QLEAEAGEVDIFDTVKElRSQRPGMV 90

                           90
                   ....*....|....*
gi 1167750697  315 PSQRRYVYYYSYLLK 329
Cdd:smart00012  91 QTEEQYLFLYRALLE 105
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 188-322 3.73e-10

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: 58.81  E-value: 3.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 188 LEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAErhydTAKFNCRVAQYPFEDHN-PPQLELIKPFCEDLDQWLSEDDNhvA 266
Cdd:cd14505    36 LEELKDQGVDDVVTLCTDGELEELGVPDLLEQ----YQQAGITWHHLPIPDGGvPSDIAQWQELLEELLSALENGKK--V 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1167750697 267 AIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDfygEVRTRDKKGVTIPSQRRYVY 322
Cdd:cd14505   110 LIHCKGGLGRTGLIAACLLLELGDTLDPEQAIA---AVRALRPGAIQTPKQENFLH 162
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 193-307 4.28e-09

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: 55.69  E-value: 4.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 193 RNNIDDVVRfldskhknhykiynlCAERHYDTAKF---NCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVA--A 267
Cdd:cd14500    35 KYNVTDLVR---------------VCEPTYDKEPLekaGIKVHDWPFDDGSPPPDDVVDDWLDLLKTRFKEEGKPGAciA 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1167750697 268 IHCKAGKGRTGVMICAYLLHRGkfLKAQEALDFygeVRTR 307
Cdd:cd14500   100 VHCVAGLGRAPVLVAIALIELG--MKPEDAVEF---IRKK 134
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 171-326 2.22e-08

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: 53.05  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 171 LTYIYPNIIA-MGFPaeRLEGVYRNNIDDVVRFLDS--KHKNHYKIYNlcaerhydtaKFNCRVAQYPFEDHNPPQLELI 247
Cdd:cd14504     1 FSWVIPGKLAgMAFP--RLPEHYAYLNENGIRHVVTltEEPPPEHSDT----------CPGLRYHHIPIEDYTPPTLEQI 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 248 KPFcedLDQWLSED-DNHVAAIHCKAGKGRTGVMICAYLLHRGKFlKAQEALDfygEVRTRDKKGV-TIPSQRRYVYYYS 325
Cdd:cd14504    69 DEF---LDIVEEANaKNEAVLVHCLAGKGRTGTMLACYLVKTGKI-SAVDAIN---EIRRIRPGSIeTSEQEKFVIQFAK 141


                  .
gi 1167750697 326 Y 326
Cdd:cd14504   142 T 142
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 193-309 3.72e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 47.32  E-value: 3.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 193 RNNIDDVVRfldskhknhykiynlCAERHYDTAKF---NCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSED--DNHVAA 267
Cdd:PTZ00242   38 RYNVTHLVR---------------VCGPTYDAELLeknGIEVHDWPFDDGAPPPKAVIDNWLRLLDQEFAKQstPPETIA 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1167750697 268 IHCKAGKGRTGVMICAYLLHRGKFlkaqEALDFYGEVRTRDK 309
Cdd:PTZ00242  103 VHCVAGLGRAPILVALALVEYGGM----EPLDAVGFVREKRK 140
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
233-305 4.96e-06

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 46.12  E-value: 4.96e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167750697  233 QYPFEDHN----PPQLELIKPFCEDldqwlSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKfLKAQEALDFYGEVR 305
Cdd:smart00195  49 GVPIDDNTetkiSPYFPEAVEFIED-----AESKGGKVLVHCQAGVSRSATLIIAYLMKTRN-MSLNDAYDFVKDRR 119
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 200-305 5.21e-06

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 47.28  E-value: 5.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 200 VRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPF-EDHNPPQ--LELIKpFCEDLDQWlSEDDNHVAAIHCKAGKGR 276
Cdd:cd00047    75 VTLVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGwPDHGVPSspEDLLA-LVRRVRKE-ARKPNGPIVVHCSAGVGR 152

                          90       100       110
                  ....*....|....*....|....*....|
gi 1167750697 277 TGVMICA-YLLHRgkfLKAQEALDFYGEVR 305
Cdd:cd00047   153 TGTFIAIdILLER---LEAEGEVDVFEIVK 179
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 238-305 6.38e-06

RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes baculovirus RNA 5'-triphosphatase, dual specificity protein phosphatase 11 (DUSP11), and the RNA triphosphatase domains of metazoan and plant mRNA capping enzymes. RNA/polynucleotide 5'-triphosphatase (EC 3.1.3.33) catalyzes the removal of the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end. mRNA capping enzyme is a bifunctional enzyme that catalyzes the first two steps of cap formation. DUSP11 has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity.


Pssm-ID: 350352 [Multi-domain]  Cd Length: 167  Bit Score: 46.50  E-value: 6.38e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 238 DHNPPQLELIKPFCEDLDQWLSEDDNH-VAAIHCKAGKGRTGVMICAYLL-HRGkfLKAQEALDFYGEVR 305
Cdd:cd14502    85 RKEPPDAEEVNKFIELVDKFLAEDNPDkLIAVHCTHGFNRTGFMIVSYLVeRLG--LTVEQALEAFAQAR 152
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 234-321 7.91e-06

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: 46.96  E-value: 7.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 234 YPFEDHNPPQLELIKPFCEDLDQWLSEddNHVAAIHCKAGKGRTGVMICAYLLHRGKfLKAQEALDFygeVRTRDKKGVT 313
Cdd:cd14506    82 FGWKDYGVPSLTTILDIVKVMAFALQE--GGKVAVHCHAGLGRTGVLIACYLVYALR-MSADQAIRL---VRSKRPNSIQ 155


                  ....*...
gi 1167750697 314 IPSQRRYV 321
Cdd:cd14506   156 TRGQVLCV 163
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 239-305 3.40e-05

dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar proteins; dual specificity protein phosphatase 11 (DUSP11), also known as RNA/RNP complex-1-interacting phosphatase or phosphatase that interacts with RNA/RNP complex 1 (PIR1), has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity. It has activity for short RNAs but is less active toward mononucleotide triphosphates, suggesting that its primary function in vivo is to dephosphorylate RNA 5'-ends. It may play a role in nuclear mRNA metabolism. Also included in this subfamily is baculovirus RNA 5'-triphosphatase for Autographa californica nuclear polyhedrosis virus.


Pssm-ID: 350503  Cd Length: 169  Bit Score: 44.57  E-value: 3.40e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167750697 239 HNPPQLELIKPFCEDLDQWLSE--DDNHVAAIHCKAGKGRTGVMICAYLLHRGKFlKAQEALDFYGEVR 305
Cdd:cd17665    87 HQVPDDKTIQSFKDAVKDFLEKnkDNDKLIGVHCTHGLNRTGYLICRYLIDVDGM-SPDDAIEAFEQAR 154
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 224-305 4.29e-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: 43.42  E-value: 4.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 224 TAKFNCRVaqYPFEDHNPPQLELIKPFCEDLDQ---WLSE--DDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEAL 298
Cdd:cd14527    34 TAELPRPR--KRQAYRCVPLLDLVAPTPEQLERavaWIEElrAQGGPVLVHCALGYGRSATVVAAWLLAYGRAKSVAEAE 111


                  ....*..
gi 1167750697 299 DFYGEVR 305
Cdd:cd14527   112 ALIRAAR 118
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 219-305 6.03e-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: 43.45  E-value: 6.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 219 ERHYDTA---KFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGkfLKAQ 295
Cdd:cd18536    47 DATYDKApveKEGIQVLDWPFDDGAPPPNQIVDDWLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECG--MKYE 124

                          90
                  ....*....|
gi 1167750697 296 EALDFYGEVR 305
Cdd:cd18536   125 DAVQFIRQKR 134
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 231-336 6.12e-05

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: 43.47  E-value: 6.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 231 VAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGkfLKAQEALDFygevrTRDKK 310
Cdd:cd18535    61 VVDWPFDDGAPPPGKVVEDWLSLLKTKFCEDPGCCVAVHCVAGLGRAPVLVALALIESG--MKYEDAIQF-----IRQKR 133

                          90       100
                  ....*....|....*....|....*.
gi 1167750697 311 GVTIPSQRryvyyYSYLLKnhldYRP 336
Cdd:cd18535   134 RGAINSKQ-----LTYLEK----YRP 150
Mce1_N cd17664
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ...
 220-285 1.18e-04

N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as RNA guanylyltransferase and 5'-phosphatase (RNGTT) or mammalian mRNA capping enzyme (Mce1) in mammals, is a bifunctional enzyme that catalyzes the first two steps of cap formation: (1) by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end using the polynucleotide 5'-phosphatase activity (EC 3.1.3.33) of the N-terminal triphosphatase domain; and (2) by transferring the GMP moiety of GTP to the 5'-diphosphate terminus through the C-terminal mRNA guanylyltransferase domain (EC 2.7.7.50). The enzyme is also referred to as CEL-1 in Caenorhabditis elegans.


Pssm-ID: 350502  Cd Length: 167  Bit Score: 42.67  E-value: 1.18e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 220 RHYDTA---KFNCRVAQYPFEDHN-PPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYL 285
Cdd:cd17664    64 RFYDRNeveKEGCKYIKLQCKGHGeCPSPEQTETFIRLCENFIEKNPLELIGVHCTHGFNRTGFLICAYL 133
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 242-305 2.05e-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: 41.48  E-value: 2.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167750697 242 PQLELIKPFCEDLDQwlsedDNHVAAIHCKAGKGRTGVMICAYLLHRGKfLKAQEALDFYGEVR 305
Cdd:pfam00782  53 KYLEEAVEFIDDARQ-----KGGKVLVHCQAGISRSATLIIAYLMKTRN-LSLNEAYSFVKERR 110
PRK12361 PRK12361
hypothetical protein; Provisional
 235-305 2.38e-04

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 43.84  E-value: 2.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167750697 235 PFEDHNPPQLELIKPFCEDLDQWLSEDDNHVaaIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVR 305
Cdd:PRK12361  149 PILDHSVPTLAQLNQAINWIHRQVRANKSVV--VHCALGRGRSVLVLAAYLLCKDPDLTVEEVLQQIKQIR 217
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 213-305 3.07e-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: 41.60  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 213 IYNLCaERHYDTA---KFNCRVAQYPFEDHNPPQLELIkpfcedlDQWLS-------EDDNHVAAIHCKAGKGRTGVMIC 282
Cdd:cd18537    45 VVRVC-EATYDTTlveKEGIQVLDWPFDDGAPPSNQIV-------DDWLNllkvkfrEEPGCCIAVHCVAGLGRAPVLVA 116

                          90       100
                  ....*....|....*....|...
gi 1167750697 283 AYLLHRGkfLKAQEALDFYGEVR 305
Cdd:cd18537   117 LALIECG--MKYEDAVQFIRQKR 137
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 256-286 4.73e-04

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: 42.00  E-value: 4.73e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1167750697 256 QWLSEDDNHVAAIHCKAGKGRTGVMICAYLL 286
Cdd:cd14559   161 SAINDKNKLLPVIHCRAGVGRTGQLAAAMEL 191
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
200-322 6.69e-04

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 41.49  E-value: 6.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697  200 VRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPF-EDHN-PPQLELIKPFCEDLDQWLSEDDNHVAaIHCKAGKGRT 277
Cdd:smart00194 130 VTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHYTNwPDHGvPESPESILDLIRAVRKSQSTSTGPIV-VHCSAGVGRT 208

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1167750697  278 GVMICA-YLLHRgkfLKAQEALDFYG---EVRTRDKKGVTIPSQRRYVY 322
Cdd:smart00194 209 GTFIAIdILLQQ---LEAGKEVDIFEivkELRSQRPGMVQTEEQYIFLY 254
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 268-323 1.54e-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: 39.17  E-value: 1.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 268 IHCKAGKGRTGVMICAYLL-HRGkfLKAQEALDFYGEVRTRdkkgVTI-PSQRRYV--YY 323
Cdd:cd14524    94 VHCKAGRGRSATIVACYLIqHKG--WSPEEAQEFLRSKRPH----ILLrLSQREVLeeFY 147
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 215-307 3.78e-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: 37.91  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 215 NLCAERHYDTAKFNCRVAQYPFEDHNPpqlELIKPFCEDLDQWLSE--DDNHVAAIHCKAGKGRTGVMICAYLLHRGKfL 292
Cdd:cd14498    32 NVAGEPPPNKFPDGIKYLRIPIEDSPD---EDILSHFEEAIEFIEEalKKGGKVLVHCQAGVSRSATIVIAYLMKKYG-W 107

                          90
                  ....*....|....*
gi 1167750697 293 KAQEALDFygeVRTR 307
Cdd:cd14498   108 SLEEALEL---VKSR 119
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
238-322 4.53e-03

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 38.76  E-value: 4.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 238 DHNPPQ--LELIKpFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRgkFLKAQEALDFYG---EVRTRDKKGV 312
Cdd:pfam00102 143 DHGVPEspNSLLD-LLRKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQ--QLEAEGEVDIFQivkELRSQRPGMV 219

                          90
                  ....*....|
gi 1167750697 313 TIPSQRRYVY 322
Cdd:pfam00102 220 QTLEQYIFLY 229
PFA-DSP_Siw14 cd14528
atypical dual specificity phosphatases similar to yeast Siw14; This subfamily contains ...
 189-281 6.69e-03

atypical dual specificity phosphatases similar to yeast Siw14; This subfamily contains Saccharomyces Siw14 and a novel phosphatase from the Arabidopsis thaliana gene locus At1g05000. Siw14, also known as Oca3, plays a role in actin filament organization and endocytosis. Siw14 has been shown to be an inositol pyrophosphate phosphatase, hydrolyzing the beta-phosphate from 5-diphosphoinositol pentakisphosphate (5PP-IP5or IP7). The At1g05000 protein, also called AtPFA-DSP1, has been shown to have highest activity toward olyphosphate (poly-P(12-13)) and deoxyribo- and ribonucleoside triphosphates, and less activity toward phosphoenolpyruvate, phosphotyrosine, phosphotyrosine-containing peptides, and phosphatidylinositols. This subfamily belongs to a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds called plant and fungi atypical dual-specificity phosphatases (PFA-DSPs).


Pssm-ID: 350377 [Multi-domain]  Cd Length: 148  Bit Score: 37.31  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167750697 189 EGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTA-----KFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDN 263
Cdd:cd14528    13 KGVYRSGYPNKKNFPFLRTLGLRSILYLCPEDYPESNleflkENGIKLFQFGIEGNKEPFVDIPEELIRDALKVLLDPRN 92

                          90
                  ....*....|....*...
gi 1167750697 264 HVAAIHCKAGKGRTGVMI 281
Cdd:cd14528    93 HPVLIHCNKGKHRTGCLV 110
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH