NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|74934476|sp|Q8T9S7|]
View 

RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN; AltName: Full=Inositol polyphosphate 3-phosphatase; AltName: Full=Pten 3-phosphoinositide phosphatase alpha

Protein Classification

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; ...
 24-180 8.70e-114

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: 333.79  E-value: 8.70e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  24 DLAYITDNIVAMGFPSEKVEGVFRNPMKDVQRFLDQYHKDHFKVYNLCSERVYDHSKFYGRVGYYPFDDHNAPQFEMIDA 103
Cdd:cd14509   1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLCSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74934476 104 FCRDVDAWMKEDSKNIAVIHCKAGKGRTGLMICCWLMYCGMWKNTEDSLRFYAALRTYNQKGVTIPSQIRYVGYFGR 180
Cdd:cd14509  81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTKNKKGVTIPSQRRYVYYYSR 157
PTEN_C2 super family cl11068
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 331-403 1.72e-17

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.


The actual alignment was detected with superfamily member pfam10409:

Pssm-ID: 463081  Cd Length: 133  Bit Score: 78.86  E-value: 1.72e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74934476   331 NDEYISFEIGALsLAGDIRIEFTNKQ-----DDRMFMFWVNTSFVQQLEII-PKSGLDKAHKDKNHKAFPEDFHVELTF 403
Cdd:pfam10409  54 DDCVILFPKGIP-VQGDVLVEFYHKGsdllsEEKMFRFWFNTSFIEDNTLTlPKNELDKADKDKKDKRFPKDFKVELLF 131
 
Name Accession Description Interval E-value
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 24-180 8.70e-114

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: 333.79  E-value: 8.70e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  24 DLAYITDNIVAMGFPSEKVEGVFRNPMKDVQRFLDQYHKDHFKVYNLCSERVYDHSKFYGRVGYYPFDDHNAPQFEMIDA 103
Cdd:cd14509   1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLCSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74934476 104 FCRDVDAWMKEDSKNIAVIHCKAGKGRTGLMICCWLMYCGMWKNTEDSLRFYAALRTYNQKGVTIPSQIRYVGYFGR 180
Cdd:cd14509  81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTKNKKGVTIPSQRRYVYYYSR 157
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 331-403 1.72e-17

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: 78.86  E-value: 1.72e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74934476   331 NDEYISFEIGALsLAGDIRIEFTNKQ-----DDRMFMFWVNTSFVQQLEII-PKSGLDKAHKDKNHKAFPEDFHVELTF 403
Cdd:pfam10409  54 DDCVILFPKGIP-VQGDVLVEFYHKGsdllsEEKMFRFWFNTSFIEDNTLTlPKNELDKADKDKKDKRFPKDFKVELLF 131
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
67-182 4.40e-15

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 72.31  E-value: 4.40e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  67 VYNLCSERVYDHSKFYGR---VGYYPFDDHNAPQFEMIDAFCRDVDAWMKEDSKNiaVIHCKAGKGRTGLMICCWLMYCG 143
Cdd:COG2453  29 VVSLTEEEELLLGLLEEAgleYLHLPIPDFGAPDDEQLQEAVDFIDEALREGKKV--LVHCRGGIGRTGTVAAAYLVLLG 106

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 74934476 144 MwkNTEDSLrfyAALRTYNQKGVTIPSQIRYVGYFGRSI 182
Cdd:COG2453 107 L--SAEEAL---ARVRAARPGAVETPAQRAFLERFAKRL 140
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 72-140 3.32e-06

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


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 47.31  E-value: 3.32e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74934476    72 SERVYDHSKFYG-RVGYY--PFDDHNAPQFEMIDAFcrdVDAwMKEDSKNIA-VIHCKAGKGRTGL-MICCWLM 140
Cdd:pfam14566  87 PEEVYERLKAEGpGVDYRriPITDEKAPLEEDFDAL---ISI-VKDAPEDTAlVFNCQMGRGRTTTaMVIADLV 156
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
87-175 2.05e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 43.50  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476     87 YYPFDDHNAPQF--EMIDaFCRDVDAWMK--EDSKNIaVIHCKAGKGRTGLMICCWLMYCGMWKNTE--DSLRFYAALRt 160
Cdd:smart00404   7 YTGWPDHGVPESpdSILE-LLRAVKKNLNqsESSGPV-VVHCSAGVGRTGTFVAIDILLQQLEAEAGevDIFDTVKELR- 83

                           90
                   ....*....|....*
gi 74934476    161 yNQKGVTIPSQIRYV 175
Cdd:smart00404  84 -SQRPGMVQTEEQYL 97
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 64-144 5.99e-05

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 43.47  E-value: 5.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476   64 HFKVYNL--CSERVYDHSKFYGR---VGYYPFDDHNAPQFEMIDAFCRDVDAWMKEDSK-NIAV-IHCKAGKGRTGLMIC 136
Cdd:PTZ00242  38 RYNVTHLvrVCGPTYDAELLEKNgieVHDWPFDDGAPPPKAVIDNWLRLLDQEFAKQSTpPETIaVHCVAGLGRAPILVA 117


                 ....*....
gi 74934476  137 CWLM-YCGM 144
Cdd:PTZ00242 118 LALVeYGGM 126
 
Name Accession Description Interval E-value
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 24-180 8.70e-114

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: 333.79  E-value: 8.70e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  24 DLAYITDNIVAMGFPSEKVEGVFRNPMKDVQRFLDQYHKDHFKVYNLCSERVYDHSKFYGRVGYYPFDDHNAPQFEMIDA 103
Cdd:cd14509   1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLCSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74934476 104 FCRDVDAWMKEDSKNIAVIHCKAGKGRTGLMICCWLMYCGMWKNTEDSLRFYAALRTYNQKGVTIPSQIRYVGYFGR 180
Cdd:cd14509  81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTKNKKGVTIPSQRRYVYYYSR 157
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 10-178 1.09e-81

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: 252.28  E-value: 1.09e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  10 SKQKRRYQKNGYDLDLAYITDNIVAMGFPSEKVEGVFRNPMKDVQRFLDQYHKDHFKVYNLCSERVYDHSKFYGRVGYYP 89
Cdd:cd14510   1 SENKRRYQKDGFDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLCSERGYDPKYFHNRVERVP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  90 FDDHNAPQFEMIDAFCRDVDAWMKEDSKNIAVIHCKAGKGRTGLMICCWLMYCGMWKNTEDSLRFYAALRTYNQ-----K 164
Cdd:cd14510  81 IDDHNVPTLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTDKSvsskfQ 160

                       170
                ....*....|....
gi 74934476 165 GVTIPSQIRYVGYF 178
Cdd:cd14510 161 GVETPSQSRYVGYF 174
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 24-178 5.72e-73

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: 229.00  E-value: 5.72e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  24 DLAYITDNIVAMGFPSEKV-EGVFRNPMKDVQRFLDQYHKDHFKVYNLCSERVYDHSKFYGRVGYYPFDDHNAPQFEMID 102
Cdd:cd14497   1 DLSYITPRIIAMSFPATGYpESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDDDSKFEGRVLHYGFPDHHPPPLGLLL 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74934476 103 AFCRDVDAWMKEDSKNIAVIHCKAGKGRTGLMICCWLMYCGMWKNTEDSLRFYAALRTYNQK-GVTIPSQIRYVGYF 178
Cdd:cd14497  81 EIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKRFKEGLpGVTIPSQLRYLQYF 157
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
 16-179 7.30e-44

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: 152.89  E-value: 7.30e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  16 YQKNgyDLDLAYITDNIVAMGFPSEKVE-GVFRNPMKDVQRFLDQYHKDHFKVYNLcSERVYDHSKFYGRVGYYPFDDHN 94
Cdd:cd14511   4 YARN--DLDISYITSRIIVMPFPAEGIEsTYRKNNIEDVRAFLDSRHPQKYSVYNL-SPRSYPTLRLPSRVVECSWPYRR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  95 APQFEMIDAFCRDVDAWMKEDSKNIAVIHCKAGKGRTGLMICCWLMYCGMWKNTEDSLRFYAALRTynQKGVTiPSQIRY 174
Cdd:cd14511  81 APSLHALYALCRDIYQWLNKDPKNVIVIHCTDGKAASATVVCALLVYCGLFKTPEDALQMFAVKRC--PPGLS-PSELRY 157


                ....*
gi 74934476 175 VGYFG 179
Cdd:cd14511 158 LYYFS 162
PTP_tensin cd14508
protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular ...
 24-180 7.95e-36

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: 130.97  E-value: 7.95e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  24 DLAYITDNIVAMGFPSEKVEGVFRNPMKDVQRFLDQYHKDHFKVYNLcSERVYDHSKFYGRVGYYPFDDHNAPQFEMIDA 103
Cdd:cd14508   1 DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNL-SERRHDLRSLNPKVLDFGWPELHAPPLEKLCS 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74934476 104 FCRDVDAWMKEDSKNIAVIHCKAGKGRTGLMICCWLMYCGMWKNTEDSLRFYAALRTYNQK--GVTIPSQIRYVGYFGR 180
Cdd:cd14508  80 ICKNMDSWLNADPQNVVVLHCKGGKGRLGVVVSAYMHYSKISATADQALDRFAMKRFYDDKvgPLGQPSQKRYVGYFSG 158
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 22-177 2.70e-33

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: 124.25  E-value: 2.70e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  22 DLDLAYITDNIVAMGFPSEKVEGVFRNPMKDVQRFLDQYHKDHFKVYNLCsERVYDHSKFYGRVGYYPFDDHNAPQFEMI 101
Cdd:cd14564   8 DLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLS-QRTYRPSRFHNRVSECGWPARRAPNLQNL 86

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74934476 102 DAFCRDVDAWMKEDSKNIAVIHCKAGKGRTGLMICCWLMYCGMWKNTEDSLRFYAALRTynQKGVTiPSQIRYVGY 177
Cdd:cd14564  87 YSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKRC--PPGIW-PSHKRYIEY 159
PTP_tensin-1 cd14560
protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin ...
 24-178 1.67e-32

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: 122.01  E-value: 1.67e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  24 DLAYITDNIVAMGFPSEKVEGVFRNPMKDVQRFLDQYHKDHFKVYNLcSERVYDHSKFYGRVGYYPFDDHNAPQFEMIDA 103
Cdd:cd14560   1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNL-SERRHDISKLHPKVLDFGWPDLHAPALEKICS 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74934476 104 FCRDVDAWMKEDSKNIAVIHCKAGKGRTGLMICCWLMYCGMWKNTEDSLRFYAALRTYNQKGVTI--PSQIRYVGYF 178
Cdd:cd14560  80 ICKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRFYEDKVVPVgqPSQKRYVHYF 156
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 22-177 3.09e-31

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: 118.83  E-value: 3.09e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  22 DLDLAYITDNIVAMGFPSEKVEGVFRNPMKDVQRFLDQYHKDHFKVYNLcSERVYDHSKFYGRVGYYPFDDHNAPQFEMI 101
Cdd:cd14563   8 ELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNL-SQKSYRSAKFHNRVSECSWPVRQAPSLHNL 86

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74934476 102 DAFCRDVDAWMKEDSKNIAVIHCKAGKGRTGLMICCWLMYCGMWKNTEDSLRFYAALRTynqKGVTIPSQIRYVGY 177
Cdd:cd14563  87 FAVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRP---GIGLWPSHRRYIGY 159
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 24-178 2.32e-25

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: 102.33  E-value: 2.32e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  24 DLAYITDNIVAMGFPSEKVEGVFRNPMKDVQRFLDQYHKDHFKVYNLcSERVYDHSKFYGRVGYYPFDDHNAPQFEMIDA 103
Cdd:cd14561   1 DLTYITERIIAVSFPADCSEETYLHNLQDVTRMLKSKHGDNYLVLNL-SEKRYELTKLNPKIMDVGWPDLHAPPLDKMCT 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74934476 104 FCRDVDAWMKEDSKNIAVIHCKAGKGRTGLMICCWLMYCGMWKNTEDSLRFYAALRTYNQK--GVTIPSQIRYVGYF 178
Cdd:cd14561  80 ICKAMESWLNSDPLHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMKKFYDDKvsALMQPSQKRYVQFL 156
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
 24-179 2.39e-25

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: 101.95  E-value: 2.39e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  24 DLAYITDNIVAMGFPSEKVEGVFRNPMKDVQRFLDQYHKDHFKVYNLcSERVYDHSKFYGRVGYYPFDDHNAPQFEMIDA 103
Cdd:cd14562   1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNL-SEKRHDITRLNPKVQDFGWPDLHAPPLDKICS 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74934476 104 FCRDVDAWMKEDSKNIAVIHCKAGKGRTGLMICCWLMYCGMWKNTEDSLRfYAALRTYNQKGVTI---PSQIRYVGYFG 179
Cdd:cd14562  80 ICKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALS-TLAMRKFCEDKVATslqPSQRRYISYFG 157
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 331-403 1.72e-17

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: 78.86  E-value: 1.72e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74934476   331 NDEYISFEIGALsLAGDIRIEFTNKQ-----DDRMFMFWVNTSFVQQLEII-PKSGLDKAHKDKNHKAFPEDFHVELTF 403
Cdd:pfam10409  54 DDCVILFPKGIP-VQGDVLVEFYHKGsdllsEEKMFRFWFNTSFIEDNTLTlPKNELDKADKDKKDKRFPKDFKVELLF 131
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
67-182 4.40e-15

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 72.31  E-value: 4.40e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  67 VYNLCSERVYDHSKFYGR---VGYYPFDDHNAPQFEMIDAFCRDVDAWMKEDSKNiaVIHCKAGKGRTGLMICCWLMYCG 143
Cdd:COG2453  29 VVSLTEEEELLLGLLEEAgleYLHLPIPDFGAPDDEQLQEAVDFIDEALREGKKV--LVHCRGGIGRTGTVAAAYLVLLG 106

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 74934476 144 MwkNTEDSLrfyAALRTYNQKGVTIPSQIRYVGYFGRSI 182
Cdd:COG2453 107 L--SAEEAL---ARVRAARPGAVETPAQRAFLERFAKRL 140
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 27-175 1.10e-11

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: 61.60  E-value: 1.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  27 YITD-NIVAMGFPSEKVEgvfrnpmkDVQRFLDQYHkdHFKVYNLCSErvydhskfygrvgyypfddhnapqfeMIDAFC 105
Cdd:cd14494   3 WIDPlRLIAGALPLSPLE--------ADSRFLKQLG--VTTIVDLTLA--------------------------MVDRFL 46

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476 106 RDVDAWMKEDSKniAVIHCKAGKGRTGLMICCWLMyCGMWKNTEDSLRFYAALRTynQKGVTIPSQIRYV 175
Cdd:cd14494  47 EVLDQAEKPGEP--VLVHCKAGVGRTGTLVACYLV-LLGGMSAEEAVRIVRLIRP--GGIPQTIEQLDFL 111
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 70-144 7.48e-11

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: 59.98  E-value: 7.48e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74934476  70 LCSERVYDHSKFYGRVGYY--PFDDHNAPQFEMIDAFCRDVDawmKEDSKNIAV-IHCKAGKGRTGLMICCWLMYCGM 144
Cdd:cd14504  35 LTEEPPPEHSDTCPGLRYHhiPIEDYTPPTLEQIDEFLDIVE---EANAKNEAVlVHCLAGKGRTGTMLACYLVKTGK 109
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 73-141 2.67e-10

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: 59.39  E-value: 2.67e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74934476  73 ERVYDHSKFYgRVGY----YPFDDHNAPQFEMIDAFCRDVDawmkEDSKNIAViHCKAGKGRTGLMICCWLMY 141
Cdd:cd14499  67 KKLYDAKRFT-DAGIrhydLYFPDGSTPSDDIVKKFLDICE----NEKGAIAV-HCKAGLGRTGTLIACYLMK 133
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 71-159 1.38e-09

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: 57.28  E-value: 1.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  71 CSERVYDHSKFYGRVGYY---PFDDHNAPQFEMIDAFCRDVDAWMKEDSKN--IAViHCKAGKGRTGLMICCWLM-YCGM 144
Cdd:cd14502  61 NTDRYYDPNDLDDDGYVYykkVCVRKEPPDAEEVNKFIELVDKFLAEDNPDklIAV-HCTHGFNRTGFMIVSYLVeRLGL 139

                        90
                ....*....|....*
gi 74934476 145 wkNTEDSLRFYAALR 159
Cdd:cd14502 140 --TVEQALEAFAQAR 152
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 38-175 3.02e-09

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: 56.12  E-value: 3.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  38 PSEKVEGVFRNPMKDVQRFLDQYHKDhfkVYNLCSE------RVYDHSKFYGRVG----YYPFDDHNAPQFEmidAFCRD 107
Cdd:cd14505  21 PGCKFKDHRRDLQADLEELKDQGVDD---VVTLCTDgeleelGVPDLLEQYQQAGitwhHLPIPDGGVPSDI---AQWQE 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74934476 108 VDAWMK---EDSKNIaVIHCKAGKGRTGLMICCWLMYCGMWKNTEDSLrfyAALRTYNQKGVTIPSQIRYV 175
Cdd:cd14505  95 LLEELLsalENGKKV-LIHCKGGLGRTGLIAACLLLELGDTLDPEQAI---AAVRALRPGAIQTPKQENFL 161
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 27-141 3.67e-09

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: 56.59  E-value: 3.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  27 YITDNIVAMGFPSEKVegvfrnpMKDVqRFLDQYHKDHFK-VYNL--------CSERVYDHSKFY--------GRVGYYP 89
Cdd:cd14506  10 WITDDILAMARPSTEL-------IDKY-GIIEQFKEKGIKtVINLqepgehasCGPGLEPESGFSylpeafmrAGIYFYN 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 74934476  90 F--DDHNAPQFEMIDAFCRDVDAWMKEDSKnIAViHCKAGKGRTGLMICCWLMY 141
Cdd:cd14506  82 FgwKDYGVPSLTTILDIVKVMAFALQEGGK-VAV-HCHAGLGRTGVLIACYLVY 133
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 59-144 1.39e-06

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: 48.37  E-value: 1.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  59 QYHKDHFKVYNL-----CSERVYDHSKFYG---RVGYYPFDDHNAPQFEMIDAFCRDVDAWMKEDSKN---IAViHCKAG 127
Cdd:cd14500  27 PLYIKELKKYNVtdlvrVCEPTYDKEPLEKagiKVHDWPFDDGSPPPDDVVDDWLDLLKTRFKEEGKPgacIAV-HCVAG 105

                        90
                ....*....|....*..
gi 74934476 128 KGRTGLMICCWLMYCGM 144
Cdd:cd14500 106 LGRAPVLVAIALIELGM 122
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 72-140 3.32e-06

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


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 47.31  E-value: 3.32e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74934476    72 SERVYDHSKFYG-RVGYY--PFDDHNAPQFEMIDAFcrdVDAwMKEDSKNIA-VIHCKAGKGRTGL-MICCWLM 140
Cdd:pfam14566  87 PEEVYERLKAEGpGVDYRriPITDEKAPLEEDFDAL---ISI-VKDAPEDTAlVFNCQMGRGRTTTaMVIADLV 156
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
87-175 2.05e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 43.50  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476     87 YYPFDDHNAPQF--EMIDaFCRDVDAWMK--EDSKNIaVIHCKAGKGRTGLMICCWLMYCGMWKNTE--DSLRFYAALRt 160
Cdd:smart00404   7 YTGWPDHGVPESpdSILE-LLRAVKKNLNqsESSGPV-VVHCSAGVGRTGTFVAIDILLQQLEAEAGevDIFDTVKELR- 83

                           90
                   ....*....|....*
gi 74934476    161 yNQKGVTIPSQIRYV 175
Cdd:smart00404  84 -SQRPGMVQTEEQYL 97
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 87-175 2.05e-05

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 43.50  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476     87 YYPFDDHNAPQF--EMIDaFCRDVDAWMK--EDSKNIaVIHCKAGKGRTGLMICCWLMYCGMWKNTE--DSLRFYAALRt 160
Cdd:smart00012   7 YTGWPDHGVPESpdSILE-LLRAVKKNLNqsESSGPV-VVHCSAGVGRTGTFVAIDILLQQLEAEAGevDIFDTVKELR- 83

                           90
                   ....*....|....*
gi 74934476    161 yNQKGVTIPSQIRYV 175
Cdd:smart00012  84 -SQRPGMVQTEEQYL 97
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
64-137 3.40e-05

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 45.85  E-value: 3.40e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74934476  64 HFKVYNLcseRVYDHSKFYGRVG---YYPFDDHNAPQFEMIDAFCRDVDAWMKEDS--KNIAVIHCKAGKGRTGLMICC 137
Cdd:COG5599 151 EARTYVL---TIKGTGQKKIEIPvlhVKNWPDHGAISAEALKNLADLIDKKEKIKDpdKLLPVVHCRAGVGRTGTLIAC 226
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 64-144 5.99e-05

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 43.47  E-value: 5.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476   64 HFKVYNL--CSERVYDHSKFYGR---VGYYPFDDHNAPQFEMIDAFCRDVDAWMKEDSK-NIAV-IHCKAGKGRTGLMIC 136
Cdd:PTZ00242  38 RYNVTHLvrVCGPTYDAELLEKNgieVHDWPFDDGAPPPKAVIDNWLRLLDQEFAKQSTpPETIaVHCVAGLGRAPILVA 117


                 ....*....
gi 74934476  137 CWLM-YCGM 144
Cdd:PTZ00242 118 LALVeYGGM 126
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 64-141 1.17e-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: 41.86  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476    64 HFKVYNLCSERVYDHSKFYGRVGYYPFDDHN---APQFEMIDAFCRDVdawmKEDSKNIAViHCKAGKGRTGLMICCWLM 140
Cdd:pfam00782  18 GITAVINVTREVDLYNSGILYLRIPVEDNHEtniSKYLEEAVEFIDDA----RQKGGKVLV-HCQAGISRSATLIIAYLM 92


                  .
gi 74934476   141 Y 141
Cdd:pfam00782  93 K 93
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 88-164 2.06e-04

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: 41.91  E-value: 2.06e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74934476  88 YPFDDHNAPQFEMIDAFCRDVDAWMKEDSKNIAVIHCKAGKGRTGLMICCWLMYCGMwkNTEDSLRFYAALR--TYNQK 164
Cdd:cd18536  65 WPFDDGAPPPNQIVDDWLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGM--KYEDAVQFIRQKRrgAFNSK 141
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 122-145 2.09e-04

protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or PTP localized to the mitochondrion 1 (PTPMT1), also called phosphoinositide lipid phosphatase (PLIP), phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1, or PTEN-like phosphatase, is a lipid phosphatase or phosphatidylglycerophosphatase (EC 3.1.3.27) which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). It is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. It is essential for the biosynthesis of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. PTPMT1 also plays a crucial role in hematopoietic stem cell (HSC) function, and has been shown to display activity toward phosphoprotein substrates.


Pssm-ID: 350374 [Multi-domain]  Cd Length: 149  Bit Score: 41.86  E-value: 2.09e-04
                        10        20
                ....*....|....*....|....
gi 74934476 122 IHCKAGKGRTGLMICCWLMYCGMW 145
Cdd:cd14524  94 VHCKAGRGRSATIVACYLIQHKGW 117
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
67-155 9.71e-04

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 39.57  E-value: 9.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476     67 VYNLCSERVYDHSKFYGRVGYYPFDDHNA---PQFEMIDAFCRDVdawmKEDSKNIAViHCKAGKGRTGLMICCWLMYCG 143
Cdd:smart00195  30 VINVTNEVPNYNGSDFTYLGVPIDDNTETkisPYFPEAVEFIEDA----ESKGGKVLV-HCQAGVSRSATLIIAYLMKTR 104

                           90
                   ....*....|..
gi 74934476    144 MWkNTEDSLRFY 155
Cdd:smart00195 105 NM-SLNDAYDFV 115
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 88-187 2.24e-03

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


Pssm-ID: 350513 [Multi-domain]  Cd Length: 167  Bit Score: 38.90  E-value: 2.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  88 YPFDDHNAPQFEMIDAFCRDVDAWMKEDSKNIAVIHCKAGKGRTGLMICCWLMYCGMwkNTEDSLRFYAALRtynqKGVT 167
Cdd:cd18537  68 WPFDDGAPPSNQIVDDWLNLLKVKFREEPGCCIAVHCVAGLGRAPVLVALALIECGM--KYEDAVQFIRQKR----RGAF 141

                        90       100
                ....*....|....*....|
gi 74934476 168 IPSQIRYVGYFGRSIRESIK 187
Cdd:cd18537 142 NSKQLLYLEKYRPKMRLRFK 161
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 92-152 2.96e-03

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: 39.19  E-value: 2.96e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74934476  92 DHNAPQ-FEMIDAFCRDVDAWMKEDSKNIaVIHCKAGKGRTGLMICCWLMYCGMWKNTEDSL 152
Cdd:cd00047 114 DHGVPSsPEDLLALVRRVRKEARKPNGPI-VVHCSAGVGRTGTFIAIDILLERLEAEGEVDV 174
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 88-175 3.20e-03

protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), also known as protein-tyrosine phosphatase of regenerating liver 3 (PRL-3), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It exerts its oncogenic functions through activation of PI3K/Akt, which is a key regulator of the rapamycin-sensitive mTOR complex 1. PRL-3 is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350511 [Multi-domain]  Cd Length: 154  Bit Score: 38.47  E-value: 3.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  88 YPFDDHNAPQFEMIDAFCRDVDAWMKEDSKNIAVIHCKAGKGRTGLMICCWLMYCGMwkNTEDSLRFYAALRtynqKGVT 167
Cdd:cd18535  64 WPFDDGAPPPGKVVEDWLSLLKTKFCEDPGCCVAVHCVAGLGRAPVLVALALIESGM--KYEDAIQFIRQKR----RGAI 137


                ....*...
gi 74934476 168 IPSQIRYV 175
Cdd:cd18535 138 NSKQLTYL 145
Mce1_N cd17664
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ...
 95-139 4.99e-03

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: 38.05  E-value: 4.99e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 74934476  95 APQFEMIDAFCRDVDAWMKEDSKNIAVIHCKAGKGRTGLMICCWL 139
Cdd:cd17664  89 CPSPEQTETFIRLCENFIEKNPLELIGVHCTHGFNRTGFLICAYL 133
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 3-159 5.03e-03

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 38.75  E-value: 5.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476   3 NLLRVAVSKQKRRYQKNGY---DLDLAYITDNIVAMgfPSEKVegvfrnpmkdvqrfLDQYHKDHFKVynlCSERVYDHS 79
Cdd:cd14617  67 NIVMVTQCVEKGRVKCDHYwpaDQDSLYYGDLIVQM--LSESV--------------LPEWTIREFKI---CSEEQLDAP 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74934476  80 KFYGRVGYYPFDDHNAPQF-EMIDAFCRDV-DAWMKEDSKNIAVIHCKAGKGRTGLMICCWLMYCGMwkNTEDSLRFYAA 157
Cdd:cd14617 128 RLVRHFHYTVWPDHGVPETtQSLIQFVRTVrDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQL--DSKDSVDIYGA 205


                ..
gi 74934476 158 LR 159
Cdd:cd14617 206 VH 207
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
 92-150 5.36e-03

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


Pssm-ID: 350345  Cd Length: 278  Bit Score: 38.89  E-value: 5.36e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74934476  92 DHNAPQFEMIDAFCRDV-----DAWMkedskniaVIHCKAGKGR-TGLMIccwlMYcGMWKNTED 150
Cdd:cd14495 164 DHVWPDDEEIDAFVAFYrslpaDAWL--------HFHCRAGKGRtTTFMV----MY-DMLKNPKD 215
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 121-185 7.66e-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: 37.35  E-value: 7.66e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74934476 121 VIHCKAGKGRTGLMICCWLMYCGMWKN--TEDSLRFYAALRTYnQKGVTIPSQIRYVGYFGRSIRES 185
Cdd:cd14529  93 LIHCKHGKDRTGLVSALYRIVYGGSKEeaNEDYRLSNRHLEGL-RSGIALDSKGGVKGRYLAAYFER 158
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 93-146 8.11e-03

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: 37.26  E-value: 8.11e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 74934476  93 HNAPQFEMIDAFCRDVDAWMKEDSKNIAVI--HCKAGKGRTGLMICCWLMYCGMWK 146
Cdd:cd17665  87 HQVPDDKTIQSFKDAVKDFLEKNKDNDKLIgvHCTHGLNRTGYLICRYLIDVDGMS 142
 
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