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Conserved domains on  [gi|1949412791|ref|XP_038153481|]
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receptor-type tyrosine-protein phosphatase T isoform X11 [Cyprinodon tularosa]

Protein Classification

fibronectin type III domain-containing protein( domain architecture ID 13891661)

fibronectin type III (FN3) domain-containing protein may be involved in specific interactions with other molecules through its FN3 domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 942-1181 1.08e-174

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


:

Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 520.74  E-value: 1.08e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  942 DENRNKNRYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMV 1021
Cdd:cd14630      1 DENRNKNRYGNIISY---DHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1022 TNLVEVGRVKCVRYWPDETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFI 1101
Cdd:cd14630     78 TNLVEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFV 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1102 RQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACLC 1181
Cdd:cd14630    158 RQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEACLC 237
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1266-1471 2.56e-160

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


:

Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 481.44  E-value: 2.56e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQLCMQYWPEKNSCCYGPIQVEFISADIDE 1345
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTSCCYGPIQVEFVSADIDE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1346 DIINRIFRICNMARPQDGYRLVQHFQFIGWPAYRDTPLSKRSILQLVRRLAKWQEQYDGGDGRTVVHCLTGGGRSGTFCA 1425
Cdd:cd14634     81 DIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1949412791 1426 ICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1471
Cdd:cd14634    161 ICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 24-185 1.62e-52

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 181.77  E-value: 1.62e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791    24 FPGGCTFEESySSCGYSVSLgTNGFTWEQVNSWEK---PTMDPALPTGSFMVVNASGRASGQKAHLYMPTLKEN-DTHCI 99
Cdd:smart00137    2 SPGNCDFEEG-STCGWHQDS-NDDGHWERVSSATGipgPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791   100 DFLYSLSsrdGASPGTLNVYIKVNGGAQGNPVWNASDTVTEGWVKAELAISTfWPNSYQVIFEAVSVQGHPGFIAIDDIR 179
Cdd:smart00137   80 TFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDIL 155


                    ....*.
gi 1949412791   180 VLAHPC 185
Cdd:smart00137  156 LSNGPC 161
fn3 pfam00041
Fibronectin type III domain;
498-573 1.88e-10

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 1.88e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949412791  498 IFMQWKAPNETNGVITLYEITYKALSSLDPSADLTTqrgrvfkLRNETHHLFVSLYPGTTYFFTLKASTNKGFGPP 573
Cdd:pfam00041   16 LTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITV-------PGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 386-476 2.60e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 2.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  386 PQNVNVVDVRARQLTVQWETFGYAVTRCHSYnlTVQYQYVFNQQEFAAEELIQTSSHYTLRGLRPFVTVRLRLVLANPEG 465
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGY--VVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 1949412791  466 -SKESEEIVKQT 476
Cdd:cd00063     82 eSPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 285-356 3.89e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


:

Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 43.37  E-value: 3.89e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949412791   285 PTPIAPPELLAVGATYL---WIKPNANSiiGDGPIILKEVEYRTTTGNWAETHVVDAPT-YKLWHLDPDVEYEIKV 356
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVtlsWEPPPDDG--ITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRV 74
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 192-277 6.96e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam00047:

Pssm-ID: 472250  Cd Length: 86  Bit Score: 37.17  E-value: 6.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  192 LRLQNVEVNVGQNATFQCTAGGKWSQHDKLWLQQwNGKDTALMVTRVVNHRRFSATVSVGDTSQRSTSRYRCVIRSDGGS 271
Cdd:pfam00047    1 SAPPTVTVLEGDSATLTCSASTGSPGPDVTWSKE-GGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79


                   ....*.
gi 1949412791  272 GVSNYA 277
Cdd:pfam00047   80 ATLSTS 85
 
Name Accession Description Interval E-value
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 942-1181 1.08e-174

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 520.74  E-value: 1.08e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  942 DENRNKNRYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMV 1021
Cdd:cd14630      1 DENRNKNRYGNIISY---DHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1022 TNLVEVGRVKCVRYWPDETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFI 1101
Cdd:cd14630     78 TNLVEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFV 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1102 RQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACLC 1181
Cdd:cd14630    158 RQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEACLC 237
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1266-1471 2.56e-160

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 481.44  E-value: 2.56e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQLCMQYWPEKNSCCYGPIQVEFISADIDE 1345
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTSCCYGPIQVEFVSADIDE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1346 DIINRIFRICNMARPQDGYRLVQHFQFIGWPAYRDTPLSKRSILQLVRRLAKWQEQYDGGDGRTVVHCLTGGGRSGTFCA 1425
Cdd:cd14634     81 DIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1949412791 1426 ICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1471
Cdd:cd14634    161 ICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
920-1177 5.96e-122

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 380.85  E-value: 5.96e-122
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791   920 GFKEEYEALAEGQTA--PWETAKKDENRNKNRYGNIIAYptdDHTRVRLQLLDGDPhSDYINANYIDGYHRPRHYIATQG 997
Cdd:smart00194    1 GLEEEFEKLDRLKPDdeSCTVAAFPENRDKNRYKDVLPY---DHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQG 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791   998 PMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE---TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEI 1074
Cdd:smart00194   77 PLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  1075 RELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIREL 1154
Cdd:smart00194  157 RTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKEL 236

                           250       260
                    ....*....|....*....|...
gi 1949412791  1155 RSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:smart00194  237 RSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
944-1177 3.64e-114

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 358.86  E-value: 3.64e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  944 NRNKNRYGNIIAYptdDHTRVRLQllDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTN 1023
Cdd:pfam00102    1 NLEKNRYKDVLPY---DHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTE 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1024 LVEVGRVKCVRYWPDETE---VYGDIKVTLIETEP-LAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLG 1099
Cdd:pfam00102   76 LEEKGREKCAQYWPEEEGeslEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLD 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949412791 1100 FIRQV-KFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:pfam00102  156 LLRKVrKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1209-1471 6.30e-85

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 278.39  E-value: 6.30e-85
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  1209 QIKDEFQTLNIVTPRvrPEDCSVGLLPRNHDKNRSMDVLSADRCLPFLISVDGESSNYINAALMDSHKQPAAFIVTQHPL 1288
Cdd:smart00194    1 GLEEEFEKLDRLKPD--DESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  1289 PNTMGDFWRLVFDYNCSSIVMLNEMDAAQL--CMQYWPEKN--SCCYGPIQVEFISADIDEDIINRIFRICNMARPQDgy 1364
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGRekCAQYWPDEEgePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-- 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  1365 RLVQHFQFIGWPaYRDTPLSKRSILQLVRRLAKWQEQYdggDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHT 1444
Cdd:smart00194  157 RTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQSTS---TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEI 232

                           250       260
                    ....*....|....*....|....*..
gi 1949412791  1445 VKTLRNNKTNMVETMEQYKFCYEVALE 1471
Cdd:smart00194  233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1237-1471 6.56e-83

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 271.42  E-value: 6.56e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1237 NHDKNRSMDVLSADRCLPFLISVDGeSSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD-- 1314
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG-PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEek 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1315 AAQLCMQYWPEKN--SCCYGPIQVEFISADIDE-DIINRIFRICNMARPQdgYRLVQHFQFIGWPAyRDTPLSKRSILQL 1391
Cdd:pfam00102   80 GREKCAQYWPEEEgeSLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGSEE--TRTVKHFHYTGWPD-HGVPESPNSLLDL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1392 VRRLAKWQEqyDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1471
Cdd:pfam00102  157 LRKVRKSSL--DGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 24-185 1.62e-52

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 181.77  E-value: 1.62e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791    24 FPGGCTFEESySSCGYSVSLgTNGFTWEQVNSWEK---PTMDPALPTGSFMVVNASGRASGQKAHLYMPTLKEN-DTHCI 99
Cdd:smart00137    2 SPGNCDFEEG-STCGWHQDS-NDDGHWERVSSATGipgPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791   100 DFLYSLSsrdGASPGTLNVYIKVNGGAQGNPVWNASDTVTEGWVKAELAISTfWPNSYQVIFEAVSVQGHPGFIAIDDIR 179
Cdd:smart00137   80 TFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDIL 155


                    ....*.
gi 1949412791   180 VLAHPC 185
Cdd:smart00137  156 LSNGPC 161
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 901-1172 2.59e-49

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 178.27  E-value: 2.59e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  901 IRVADLLQHITQMKCgQGYGFKEEYEALAEGQTAPWETAKKDENRNKNRYGNIiayPTDDHTRVRLQLLDGDPhSDYINA 980
Cdd:PHA02747     9 CRAIDFLKRRNQLNC-FGIIRDEHHQIILKPFDGLIANFEKPENQPKNRYWDI---PCWDHNRVILDSGGGST-SDYIHA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  981 NYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEV-GRVKCVRYW---PDETEVYGDIKVTLIETEPL 1056
Cdd:PHA02747    84 NWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGTnGEEKCYQYWclnEDGNIDMEDFRIETLKTSVR 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1057 AEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFI------RQV--KFLNPPDA--GPIAVHCSAGAGRT 1126
Cdd:PHA02747   164 AKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKFIkiidinRKKsgKLFNPKDAllCPIVVHCSDGVGKT 243

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1949412791 1127 GCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1172
Cdd:PHA02747   244 GIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
943-1168 3.05e-47

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 171.04  E-value: 3.05e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  943 ENRNKNRYGNIIAYptdDHTRVRlqlldgdPHSDYINANYIDGYhRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVT 1022
Cdd:COG5599     41 NGSPLNRFRDIQPY---KETALR-------ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLA 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1023 NLVEVG--RVKCVRYWP-DETEVYGDIKVTLIETEPLAEYV-IRTFTVQKKGH-HEIRELRQFHFTSWPDHGVPCYAT-- 1095
Cdd:COG5599    110 SDDEISkpKVKMPVYFRqDGEYGKYEVSSELTESIQLRDGIeARTYVLTIKGTgQKKIEIPVLHVKNWPDHGAISAEAlk 189

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949412791 1096 GLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDM--AENEGVVDIFNCIRELRSQRVN-MVQTEEQY 1168
Cdd:COG5599    190 NLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMRTSRNGgMVQTSEQL 265
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 28-185 5.97e-41

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 148.29  E-value: 5.97e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791   28 CTFEESYssCGYSVSLgTNGFTWEQVNSWEKPTMDPAL-----PTGSFMVVNASGRASGQKAHLYMPTLKEN-DTHCIDF 101
Cdd:cd06263      1 CDFEDGL--CGWTQDS-TDDFDWTRVSGSTPSPGTPPDhthgtGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCLSF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  102 LYSLSsrdGASPGTLNVYIKVNGGAQGNPVWNASDTVTEGWVKAELAISTFWpNSYQVIFEAVSVQGHPGFIAIDDIRVL 181
Cdd:cd06263     78 WYHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDISLS 153


                   ....
gi 1949412791  182 AHPC 185
Cdd:cd06263    154 PGPC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 28-186 2.45e-37

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 137.88  E-value: 2.45e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791   28 CTFEESySSCGYSVSLGTnGFTWEQVNSWE---KPTMDPALPT--GSFMVVNASGRASGQKAHLYMPTLKENDT-HCIDF 101
Cdd:pfam00629    1 CDFEDG-NLCGWTQDSSD-DFDWERVSGPSvktGPSSDHTQGTgsGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  102 LYSLSsrdGASPGTLNVYIKVNGGAQGNPVWNASDTVTEGWVKAELAISTFwPNSYQVIFEAVSVQGHPGFIAIDDIRVL 181
Cdd:pfam00629   79 WYHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDISLS 154


                   ....*
gi 1949412791  182 AHPCR 186
Cdd:pfam00629  155 SGPCP 159
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1235-1470 3.20e-30

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 122.80  E-value: 3.20e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1235 PRNHDKNRSMDVLSADRCLPFLISVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN--- 1311
Cdd:PHA02747    49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTptk 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1312 EMDAAQLCMQYW--PEKNSCCYGPIQVEFISADIDEDIINRIFRICNmaRPQDGYRLVQHFQFIGWPAYrDTPLSKRSIL 1389
Cdd:PHA02747   129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD--KILKDSRKISHFQCSEWFED-ETPSDHPDFI 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1390 QLV----RRLAKWQEQYDGGDG---RTVVHCLTGGGRSGTFCAI-CSINEMIQQQNIVdVFHTVKTLRNNKTNMVETMEQ 1461
Cdd:PHA02747   206 KFIkiidINRKKSGKLFNPKDAllcPIVVHCSDGVGKTGIFCAVdICLNQLVKRKAIC-LAKTAEKIREQRHAGIMNFDD 284

                          250
                   ....*....|..
gi 1949412791 1462 YKF---CYEVAL 1470
Cdd:PHA02747   285 YLFiqpGYEVLH 296
fn3 pfam00041
Fibronectin type III domain;
498-573 1.88e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 1.88e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949412791  498 IFMQWKAPNETNGVITLYEITYKALSSLDPSADLTTqrgrvfkLRNETHHLFVSLYPGTTYFFTLKASTNKGFGPP 573
Cdd:pfam00041   16 LTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITV-------PGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 498-580 5.00e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 54.81  E-value: 5.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  498 IFMQWKAPNETNGVITLYEITYKALSSlDPSADLTTQRGrvfklrNETHHLFVSLYPGTTYFFTLKASTNKGFGPPVTTR 577
Cdd:cd00063     17 VTLSWTPPEDDGGPITGYVVEYREKGS-GDWKEVEVTPG------SETSYTLTGLKPGTEYEFRVRAVNGGGESPPSESV 89


                   ...
gi 1949412791  578 ITT 580
Cdd:cd00063     90 TVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 386-476 2.60e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 2.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  386 PQNVNVVDVRARQLTVQWETFGYAVTRCHSYnlTVQYQYVFNQQEFAAEELIQTSSHYTLRGLRPFVTVRLRLVLANPEG 465
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGY--VVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 1949412791  466 -SKESEEIVKQT 476
Cdd:cd00063     82 eSPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 285-356 3.89e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 43.37  E-value: 3.89e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949412791   285 PTPIAPPELLAVGATYL---WIKPNANSiiGDGPIILKEVEYRTTTGNWAETHVVDAPT-YKLWHLDPDVEYEIKV 356
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVtlsWEPPPDDG--ITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRV 74
fn3 pfam00041
Fibronectin type III domain;
290-356 1.03e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 42.40  E-value: 1.03e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949412791  290 PPELL---AVGATYL---WIKPNAnsiiGDGPIILKEVEYRTTTGNWAETHVVDAPT---YKLWHLDPDVEYEIKV 356
Cdd:pfam00041    2 APSNLtvtDVTSTSLtvsWTPPPD----GNGPITGYEVEYRPKNSGEPWNEITVPGTttsVTLTGLKPGTEYEVRV 73
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 498-571 5.31e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 40.29  E-value: 5.31e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949412791   498 IFMQWKAPNETNGV--ITLYEITYKalssldpsaDLTTQRGRVFKLRNETHHLFVSLYPGTTYFFTLKASTNKGFG 571
Cdd:smart00060   17 VTLSWEPPPDDGITgyIVGYRVEYR---------EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 386-466 8.08e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 39.91  E-value: 8.08e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791   386 PQNVNVVDVRARQLTVQWETFGYAVTRchSYNLTVQYQYVFNQQEFAAEELIQTSSHYTLRGLRPFVTVRLRLVLANPEG 465
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    .
gi 1949412791   466 S 466
Cdd:smart00060   82 E 82
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 192-277 6.96e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 37.17  E-value: 6.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  192 LRLQNVEVNVGQNATFQCTAGGKWSQHDKLWLQQwNGKDTALMVTRVVNHRRFSATVSVGDTSQRSTSRYRCVIRSDGGS 271
Cdd:pfam00047    1 SAPPTVTVLEGDSATLTCSASTGSPGPDVTWSKE-GGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79


                   ....*.
gi 1949412791  272 GVSNYA 277
Cdd:pfam00047   80 ATLSTS 85
 
Name Accession Description Interval E-value
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 942-1181 1.08e-174

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 520.74  E-value: 1.08e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  942 DENRNKNRYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMV 1021
Cdd:cd14630      1 DENRNKNRYGNIISY---DHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1022 TNLVEVGRVKCVRYWPDETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFI 1101
Cdd:cd14630     78 TNLVEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFV 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1102 RQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACLC 1181
Cdd:cd14630    158 RQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEACLC 237
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 905-1180 1.50e-166

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 500.72  E-value: 1.50e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  905 DLLQHITQMKCGQGYGFKEEYEALAEGQTAPWETAKKDENRNKNRYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYID 984
Cdd:cd14633      1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAY---DHSRVRLQPIEGETSSDYINGNYID 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  985 GYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEVYGDIKVTLIETEPLAEYVIRTF 1064
Cdd:cd14633     78 GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTF 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1065 TVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGV 1144
Cdd:cd14633    158 AVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV 237

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1949412791 1145 VDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACL 1180
Cdd:cd14633    238 VDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1266-1471 2.56e-160

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 481.44  E-value: 2.56e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQLCMQYWPEKNSCCYGPIQVEFISADIDE 1345
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTSCCYGPIQVEFVSADIDE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1346 DIINRIFRICNMARPQDGYRLVQHFQFIGWPAYRDTPLSKRSILQLVRRLAKWQEQYDGGDGRTVVHCLTGGGRSGTFCA 1425
Cdd:cd14634     81 DIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1949412791 1426 ICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1471
Cdd:cd14634    161 ICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 977-1180 1.27e-147

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 447.83  E-value: 1.27e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEVYGDIKVTLIETEPL 1056
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTLVETEPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1057 AEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIML 1136
Cdd:cd14555     81 AEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVIDIML 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1949412791 1137 DMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACL 1180
Cdd:cd14555    161 DMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 963-1180 1.14e-128

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 397.47  E-value: 1.14e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  963 RVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEV 1042
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1043 YGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAG 1122
Cdd:cd14631     81 YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAG 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1949412791 1123 AGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACL 1180
Cdd:cd14631    161 AGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 944-1181 1.21e-125

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 390.22  E-value: 1.21e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  944 NRNKNRYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTN 1023
Cdd:cd14553      3 NKPKNRYANVIAY---DHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1024 LVEVGRVKCVRYWP-DETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIR 1102
Cdd:cd14553     80 LEERSRVKCDQYWPtRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLR 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949412791 1103 QVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACLC 1181
Cdd:cd14553    160 RVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAVTC 238
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
920-1177 5.96e-122

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 380.85  E-value: 5.96e-122
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791   920 GFKEEYEALAEGQTA--PWETAKKDENRNKNRYGNIIAYptdDHTRVRLQLLDGDPhSDYINANYIDGYHRPRHYIATQG 997
Cdd:smart00194    1 GLEEEFEKLDRLKPDdeSCTVAAFPENRDKNRYKDVLPY---DHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQG 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791   998 PMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE---TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEI 1074
Cdd:smart00194   77 PLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  1075 RELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIREL 1154
Cdd:smart00194  157 RTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKEL 236

                           250       260
                    ....*....|....*....|...
gi 1949412791  1155 RSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:smart00194  237 RSQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 977-1181 6.68e-122

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 378.62  E-value: 6.68e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEVYGDIKVTLIETEPL 1056
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTETL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1057 AEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIML 1136
Cdd:cd14632     81 AEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDVML 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1949412791 1137 DMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACLC 1181
Cdd:cd14632    161 DMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1266-1467 2.88e-119

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 371.35  E-value: 2.88e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD-AAQLCMQYWPEKNSCCYGPIQVEFISADID 1344
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDpKDQSCPQYWPDEGSGTYGPIQVEFVSTTID 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1345 EDIINRIFRICNMARPQDGYRLVQHFQFIGWPAYRDTPLSKRSILQLVRRLAKWQEQYdgGDGRTVVHCLTGGGRSGTFC 1424
Cdd:cd14556     81 EDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQS--GEGPIVVHCLNGVGRSGVFC 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1949412791 1425 AICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1467
Cdd:cd14556    159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
944-1177 3.64e-114

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 358.86  E-value: 3.64e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  944 NRNKNRYGNIIAYptdDHTRVRLQllDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTN 1023
Cdd:pfam00102    1 NLEKNRYKDVLPY---DHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTE 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1024 LVEVGRVKCVRYWPDETE---VYGDIKVTLIETEP-LAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLG 1099
Cdd:pfam00102   76 LEEKGREKCAQYWPEEEGeslEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLD 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949412791 1100 FIRQV-KFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:pfam00102  156 LLRKVrKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 904-1181 1.92e-113

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 358.58  E-value: 1.92e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  904 ADLLQHITQMKCGQGYGFKEEYEALAEGQTAPWETAKKDENRNKNRYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYI 983
Cdd:cd14626      1 SDLADNIERLKANDGLKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAY---DHSRVILTSVDGVPGSDYINANYI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  984 DGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLIETEPLAEYVIR 1062
Cdd:cd14626     78 DGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRgTETYGMIQVTLLDTVELATYSVR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1063 TFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENE 1142
Cdd:cd14626    158 TFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHE 237

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1949412791 1143 GVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACLC 1181
Cdd:cd14626    238 KTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATC 276
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1266-1471 2.63e-113

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 355.15  E-value: 2.63e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQLCMQYWPEKNSCCYGPIQVEFISADIDE 1345
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1346 DIINRIFRICNMARPQDGYRLVQHFQFIGWPAYRDTPLSKRSILQLVRRLAKWQEQYDGGDGRTVVHCLTGGGRSGTFCA 1425
Cdd:cd14635     81 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1949412791 1426 ICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1471
Cdd:cd14635    161 ISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1266-1471 1.59e-106

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 336.61  E-value: 1.59e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQLCMQYWPEKNSCCYGPIQVEFISADIDE 1345
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGMLRYGPIQVECMSCSMDC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1346 DIINRIFRICNMARPQDGYRLVQHFQFIGWPAYRDTPLSKRSILQLVRRLAKWQEQYDGGDGRTVVHCLTGGGRSGTFCA 1425
Cdd:cd14636     81 DVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLNGGGRSGMFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1949412791 1426 ICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1471
Cdd:cd14636    161 ISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 898-1183 5.87e-106

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 338.24  E-value: 5.87e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  898 QPAIRVADLLQHITQMKCGQGYGFKEEYEALAEGQTAPWETAKKDENRNKNRYGNIIAYptdDHTRVRLQLLDGDPHSDY 977
Cdd:cd14624      1 HPPIPILELADHIERLKANDNLKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAY---DHSRVLLSAIEGIPGSDY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  978 INANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLIETEPL 1056
Cdd:cd14624     78 INANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRgTETYGLIQVTLLDTVEL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1057 AEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIML 1136
Cdd:cd14624    158 ATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAML 237

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1949412791 1137 DMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACLCGN 1183
Cdd:cd14624    238 ERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCGN 284
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 898-1181 7.83e-106

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 337.84  E-value: 7.83e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  898 QPAIRVADLLQHITQMKCGQGYGFKEEYEALAEGQTAPWETAKKDENRNKNRYGNIIAYptdDHTRVRLQLLDGDPHSDY 977
Cdd:cd14625      1 HPPIPISELAEHTERLKANDNLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAY---DHSRVILQPIEGIMGSDY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  978 INANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLIETEPL 1056
Cdd:cd14625     78 INANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRgTETYGMIQVTLLDTIEL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1057 AEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIML 1136
Cdd:cd14625    158 ATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAML 237

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1949412791 1137 DMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACLC 1181
Cdd:cd14625    238 ERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 977-1173 2.76e-101

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: 321.93  E-value: 2.76e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETE---VYGDIKVTLIET 1053
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGkplEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1054 EPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVD 1133
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1949412791 1134 IMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHD 1173
Cdd:cd00047    161 ILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 977-1173 1.82e-100

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 319.68  E-value: 1.82e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLIETEP 1055
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEgTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1056 LAEYVIRTFTVQ------KKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCF 1129
Cdd:cd14549     81 LATYTVRTFSLKnlklkkVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1949412791 1130 IAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHD 1173
Cdd:cd14549    161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1266-1471 4.15e-99

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 316.08  E-value: 4.15e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD---AAQLCMQYWPEKNSCCYGPIQVEFISAD 1342
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNqsnSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1343 IDEDIINRIFRICNMARPQDGYRLVQHFQFIGWPAYRDTPLSKRSILQLVRRLAKWQEQydGGDGRTVVHCLTGGGRSGT 1422
Cdd:cd14637     81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRE--SGEGRTVVHCLNGGGRSGT 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1949412791 1423 FCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1471
Cdd:cd14637    159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 949-1172 2.79e-97

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are 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. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 311.60  E-value: 2.79e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  949 RYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVG 1028
Cdd:cd14548      1 RYTNILPY---DHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1029 RVKCVRYWP-DETEV-YGDIKVTLIETEPLAEYVIRTFTVQkkGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKF 1106
Cdd:cd14548     78 RVKCDHYWPfDQDPVyYGDITVTMLSESVLPDWTIREFKLE--RGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD 155

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949412791 1107 LNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1172
Cdd:cd14548    156 YIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 937-1180 1.15e-89

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 292.32  E-value: 1.15e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  937 ETAKKDENRNKNRYGNIIAYptdDHTRVRLQLLDG--DPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQEN 1014
Cdd:cd17667     20 EHSNHPDNKHKNRYINILAY---DHSRVKLRPLPGkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQN 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1015 SASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLIETEPLAEYVIRTFTVQK-----------KGHHEIRELRQFHF 1082
Cdd:cd17667     97 TGIIVMITNLVEKGRRKCDQYWPTEnSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpKGRQNERTVIQYHY 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1083 TSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMV 1162
Cdd:cd17667    177 TQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLV 256

                          250
                   ....*....|....*...
gi 1949412791 1163 QTEEQYVFVHDAILEACL 1180
Cdd:cd17667    257 QTEEQYIFIHDALLEAIL 274
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 920-1172 8.44e-88

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


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 286.95  E-value: 8.44e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  920 GFKEEYEAL-AEGQTAPWETAKKDENRNKNRYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGP 998
Cdd:cd14543      4 GIYEEYEDIrREPPAGTFLCSLAPANQEKNRYGDVLCL---DQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  999 MQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE---TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIR 1075
Cdd:cd14543     81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEegsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1076 ELRQFHFTSWPDHGVPCYATGLLGFIRQVK--------FLNPPDAG-----PIAVHCSAGAGRTGCFIAVDIMLDMAENE 1142
Cdd:cd14543    161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRqqqalavkAMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                          250       260       270
                   ....*....|....*....|....*....|
gi 1949412791 1143 GVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1172
Cdd:cd14543    241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 899-1186 8.77e-86

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 282.30  E-value: 8.77e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  899 PAIRVADLLQHITQMKCGQGYGFKEEYEALAEGQ-TAPWETAKKDENRNKNRYGNIIAYptdDHTRVRLQLLDGDPHSDY 977
Cdd:cd14621      6 PPLPVDKLEEEINRRMADDNKLFREEFNALPACPiQATCEAASKEENKEKNRYVNILPY---DHSRVHLTPVEGVPDSDY 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  978 INANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLIETEPL 1056
Cdd:cd14621     83 INASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQgCWTYGNIRVSVEDVTVL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1057 AEYVIRTFTVQKKG----HHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAV 1132
Cdd:cd14621    163 VDYTVRKFCIQQVGdvtnKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVI 242

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1949412791 1133 DIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACLCGNTAI 1186
Cdd:cd14621    243 DAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1209-1471 6.30e-85

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 278.39  E-value: 6.30e-85
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  1209 QIKDEFQTLNIVTPRvrPEDCSVGLLPRNHDKNRSMDVLSADRCLPFLISVDGESSNYINAALMDSHKQPAAFIVTQHPL 1288
Cdd:smart00194    1 GLEEEFEKLDRLKPD--DESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  1289 PNTMGDFWRLVFDYNCSSIVMLNEMDAAQL--CMQYWPEKN--SCCYGPIQVEFISADIDEDIINRIFRICNMARPQDgy 1364
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGRekCAQYWPDEEgePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-- 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  1365 RLVQHFQFIGWPaYRDTPLSKRSILQLVRRLAKWQEQYdggDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHT 1444
Cdd:smart00194  157 RTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQSTS---TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEI 232

                           250       260
                    ....*....|....*....|....*..
gi 1949412791  1445 VKTLRNNKTNMVETMEQYKFCYEVALE 1471
Cdd:smart00194  233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 948-1177 7.14e-85

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ 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 (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 277.08  E-value: 7.14e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  948 NRYGNIIAYptdDHTRVRLqLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEV 1027
Cdd:cd14615      1 NRYNNVLPY---DISRVKL-SVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1028 GRVKCVRYWPDE-TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGF---IRQ 1103
Cdd:cd14615     77 GRTKCEEYWPSKqKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFrhlVRE 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949412791 1104 VKFLNPPDaGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14615    157 YMKQNPPN-SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1237-1471 6.56e-83

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 271.42  E-value: 6.56e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1237 NHDKNRSMDVLSADRCLPFLISVDGeSSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD-- 1314
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG-PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEek 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1315 AAQLCMQYWPEKN--SCCYGPIQVEFISADIDE-DIINRIFRICNMARPQdgYRLVQHFQFIGWPAyRDTPLSKRSILQL 1391
Cdd:pfam00102   80 GREKCAQYWPEEEgeSLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGSEE--TRTVKHFHYTGWPD-HGVPESPNSLLDL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1392 VRRLAKWQEqyDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1471
Cdd:pfam00102  157 LRKVRKSSL--DGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 950-1177 1.52e-81

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 267.58  E-value: 1.52e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  950 YGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGR 1029
Cdd:cd14620      1 YPNILPY---DHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1030 VKCVRYWPDE-TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELR---QFHFTSWPDHGVPCYATGLLGFIRQVK 1105
Cdd:cd14620     78 EKCYQYWPDQgCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAPRlvtQLHFTSWPDFGVPFTPIGMLKFLKKVK 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949412791 1106 FLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14620    158 SVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 944-1175 2.57e-81

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 267.79  E-value: 2.57e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  944 NRNKNRYGNIIAYptdDHTRVRLQLLDGD-PHSDYINANYI-----DGYHRP--RHYIATQGPMQETVRDFWRMVWQENS 1015
Cdd:cd14544      1 NKGKNRYKNILPF---DHTRVILKDRDPNvPGSDYINANYIrneneGPTTDEnaKTYIATQGCLENTVSDFWSMVWQENS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1016 ASIVMVTNLVEVGRVKCVRYWPDE--TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHE-IRELRQFHFTSWPDHGVPC 1092
Cdd:cd14544     78 RVIVMTTKEVERGKNKCVRYWPDEgmQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDpIREIWHYQYLSWPDHGVPS 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1093 YATGLLGFIRQV--KFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGV---VDIFNCIRELRSQRVNMVQTEEQ 1167
Cdd:cd14544    158 DPGGVLNFLEDVnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQ 237


                   ....*...
gi 1949412791 1168 YVFVHDAI 1175
Cdd:cd14544    238 YKFIYVAV 245
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 944-1176 2.04e-79

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 261.69  E-value: 2.04e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  944 NRNKNRYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTN 1023
Cdd:cd14554      6 NKFKNRLVNILPY---ESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1024 LVEVGRVKCVRYWPDETEVygdiKVTLIETEPLAE-----YVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLL 1098
Cdd:cd14554     83 LREMGREKCHQYWPAERSA----RYQYFVVDPMAEynmpqYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1099 GFIRQVK--FLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAIL 1176
Cdd:cd14554    159 DFIGQVHktKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 948-1172 3.25e-79

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 260.79  E-value: 3.25e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  948 NRYGNIIAYPtddHTRVRLQLLDGDPHSDYINANYIDGY-HRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVE 1026
Cdd:cd14547      1 NRYKTILPNE---HSRVCLPSVDDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1027 vGRVKCVRYWPDE-TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGhhEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVK 1105
Cdd:cd14547     78 -AKEKCAQYWPEEeNETYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVE 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949412791 1106 FL--NPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1172
Cdd:cd14547    155 EArqTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 948-1172 3.85e-78

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: 257.92  E-value: 3.85e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  948 NRYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEV 1027
Cdd:cd14617      1 NRYNNILPY---DSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1028 GRVKCVRYWPDETE--VYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEI-RELRQFHFTSWPDHGVPCYATGLLGFIRQV 1104
Cdd:cd14617     78 GRVKCDHYWPADQDslYYGDLIVQMLSESVLPEWTIREFKICSEEQLDApRLVRHFHYTVWPDHGVPETTQSLIQFVRTV 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1105 K-FLN-PPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1172
Cdd:cd14617    158 RdYINrTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 948-1177 4.09e-77

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH 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 localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 255.20  E-value: 4.09e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  948 NRYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEV 1027
Cdd:cd14619      1 NRFRNVLPY---DWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1028 GRVKCVRYWP-DETE-VYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVK 1105
Cdd:cd14619     78 GRVKCEHYWPlDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949412791 1106 -FLNPP-DAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14619    158 qWLDQTmSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 948-1176 1.22e-76

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-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. PTPRV 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. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 253.71  E-value: 1.22e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  948 NRYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEV 1027
Cdd:cd14618      1 NRYPHVLPY---DHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMEN 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1028 GRVKCVRYWPDETE--VYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVK 1105
Cdd:cd14618     78 GRVLCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949412791 1106 --FLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAIL 1176
Cdd:cd14618    158 ehVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 977-1172 3.46e-76

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 250.99  E-value: 3.46e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETE-VYGDIKVTLIETEP 1055
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCwTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1056 LAEYVIRTFTVQKK----GHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIA 1131
Cdd:cd14551     81 LVDYTTRKFCIQKVnrgiGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTFIV 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1949412791 1132 VDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1172
Cdd:cd14551    161 IDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 977-1176 2.64e-75

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 248.74  E-value: 2.64e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLIETEP 1055
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADgSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1056 LAEYVIRTFTVQ--------KKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTG 1127
Cdd:cd17668     81 LAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1949412791 1128 CFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAIL 1176
Cdd:cd17668    161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 935-1176 3.67e-75

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO 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 essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 249.81  E-value: 3.67e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  935 PWETAKKDENRNKNRYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQEN 1014
Cdd:cd14614      3 PHFAADLPVNRCKNRYTNILPY---DFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1015 SASIVMVTNLVEVGRVKCVRYWP--DETEVYGDIKVTLIETEPLAEYVIRTFTVQKKghHEIRELRQFHFTSWPDHGVPC 1092
Cdd:cd14614     80 SQIIVMLTQCNEKRRVKCDHYWPftEEPVAYGDITVEMLSEEEQPDWAIREFRVSYA--DEVQDVMHFNYTAWPDHGVPT 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1093 Y--ATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVF 1170
Cdd:cd14614    158 AnaAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237


                   ....*.
gi 1949412791 1171 VHDAIL 1176
Cdd:cd14614    238 IHQCVQ 243
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 943-1175 7.58e-75

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 249.55  E-value: 7.58e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  943 ENRNKNRYGNIIAYptdDHTRVRLQllDGDPH---SDYINANYIDGYH-------RP-RHYIATQGPMQETVRDFWRMVW 1011
Cdd:cd14605      1 ENKNKNRYKNILPF---DHTRVVLH--DGDPNepvSDYINANIIMPEFetkcnnsKPkKSYIATQGCLQNTVNDFWRMVF 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1012 QENSASIVMVTNLVEVGRVKCVRYWPDETEV--YGDIKVTLIETEPLAEYVIRTFTVQKKGHHEI-RELRQFHFTSWPDH 1088
Cdd:cd14605     76 QENSRVIVMTTKEVERGKSKCVKYWPDEYALkeYGVMRVRNVKESAAHDYILRELKLSKVGQGNTeRTVWQYHFRTWPDH 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1089 GVPCYATGLLGFIRQVKFLNP--PDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGV---VDIFNCIRELRSQRVNMVQ 1163
Cdd:cd14605    156 GVPSDPGGVLDFLEEVHHKQEsiMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQ 235

                          250
                   ....*....|..
gi 1949412791 1164 TEEQYVFVHDAI 1175
Cdd:cd14605    236 TEAQYRFIYMAV 247
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 977-1173 2.60e-73

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 243.31  E-value: 2.60e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYID-GYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETE--VYGDIKVTLIET 1053
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYegEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1054 E--PLAEYVIRTFTVQKKGhHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLN--PPDAGPIAVHCSAGAGRTGCF 1129
Cdd:cd18533     81 EenDDGGFIVREFELSKED-GKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNdsASLDPPIIVHCSAGVGRTGTF 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1949412791 1130 IAVDIMLDMAEN--------EGVVD-IFNCIRELRSQRVNMVQTEEQYVFVHD 1173
Cdd:cd18533    160 IALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 977-1172 6.04e-71

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 235.88  E-value: 6.04e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWP---DETEVYGDIKVTLIET 1053
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmeEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1054 EPLAEYVIRTFTVQKKGHH-EIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAV 1132
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKgSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1949412791 1133 DIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1172
Cdd:cd14557    161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 899-1177 6.26e-70

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 236.94  E-value: 6.26e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  899 PAIRVADLLQHITQMKCGQGY-GFKEEYEALA--EGQTAPWETAKKDENRNKNRYGNIIAYptdDHTRVRLQLLDGDPHS 975
Cdd:cd14628      4 PARNLYAYIQKLTQIETGENVtGMELEFKRLAssKAHTSRFISANLPCNKFKNRLVNIMPY---ESTRVCLQPIRGVEGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  976 DYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEVygdiKVTLIETEP 1055
Cdd:cd14628     81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA----RYQYFVVDP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1056 LAE-----YVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPP--DAGPIAVHCSAGAGRTGC 1128
Cdd:cd14628    157 MAEynmpqYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGV 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1949412791 1129 FIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14628    237 FITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 947-1175 1.44e-69

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific 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. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 234.37  E-value: 1.44e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  947 KNRYGNIIAYPtddHTRVRLQLLD-GDPHSDYINANYIDGY-HRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNL 1024
Cdd:cd14613     28 KNRYKTILPNP---HSRVCLTSPDqDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNI 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1025 VEVGRvKCVRYWPDETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGhhEIRELRQFHFTSWPDHGVPCYATGLLGFIRQV 1104
Cdd:cd14613    105 EEMNE-KCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWYTSWPDQKTPDNAPPLLQLVQEV 181

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949412791 1105 KFLN---PPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAI 1175
Cdd:cd14613    182 EEARqqaEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 927-1177 2.04e-69

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 234.33  E-value: 2.04e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  927 ALAEGQTAPWETAKKDENRNKNRYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDF 1006
Cdd:cd14603     13 AFKADYVCSTVAGGRKENVKKNRYKDILPY---DQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDF 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1007 WRMVWQENSASIVMVTNLVEVGRVKCVRYWP--DETEVYGDIKVTLI-ETEPLAEYVIRTFTVQKKghHEIRELRQFHFT 1083
Cdd:cd14603     90 WRMIWQYGVKVILMACREIEMGKKKCERYWAqeQEPLQTGPFTITLVkEKRLNEEVILRTLKVTFQ--KESRSVSHFQYM 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1084 SWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVD---IFNCIRELRSQRVN 1160
Cdd:cd14603    168 AWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPA 247

                          250
                   ....*....|....*..
gi 1949412791 1161 MVQTEEQYVFVHDAILE 1177
Cdd:cd14603    248 AVQTEEQYEFLYHTVAQ 264
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 940-1177 7.46e-69

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 232.85  E-value: 7.46e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  940 KKDENRNKNRYGNIIAYptdDHTRVRLQLLDGD-PHSDYINANYIDGY-----HRPRHYIATQGPMQETVRDFWRMVWQE 1013
Cdd:cd14606     14 QRPENKSKNRYKNILPF---DHSRVILQGRDSNiPGSDYINANYVKNQllgpdENAKTYIASQGCLEATVNDFWQMAWQE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1014 NSASIVMVTNLVEVGRVKCVRYWPD--ETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHE-IRELRQFHFTSWPDHGV 1090
Cdd:cd14606     91 NSRVIVMTTREVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGElIREIWHYQYLSWPDHGV 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1091 PCYATGLLGFIRQV--KFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGV---VDIFNCIRELRSQRVNMVQTE 1165
Cdd:cd14606    171 PSEPGGVLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTE 250

                          250
                   ....*....|..
gi 1949412791 1166 EQYVFVHDAILE 1177
Cdd:cd14606    251 AQYKFIYVAIAQ 262
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 899-1177 2.09e-68

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 232.32  E-value: 2.09e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  899 PAIRVADLLQHITQMKCGQGY-GFKEEYEALA--EGQTAPWETAKKDENRNKNRYGNIIAYptdDHTRVRLQLLDGDPHS 975
Cdd:cd14627      5 PARNLYSYIQKLAQVEVGEHVtGMELEFKRLAnsKAHTSRFISANLPCNKFKNRLVNIMPY---ETTRVCLQPIRGVEGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  976 DYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEVygdiKVTLIETEP 1055
Cdd:cd14627     82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSA----RYQYFVVDP 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1056 LAE-----YVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPP--DAGPIAVHCSAGAGRTGC 1128
Cdd:cd14627    158 MAEynmpqYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGV 237

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1949412791 1129 FIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14627    238 FITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 977-1178 5.39e-68

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


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 227.64  E-value: 5.39e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYI------DGYHrprhYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETE----VYGDI 1046
Cdd:cd14538      1 YINASHIripvggDTYH----YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNkpliCGGRL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1047 KVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNppDAGPIAVHCSAGAGRT 1126
Cdd:cd14538     77 EVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRT 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1949412791 1127 GCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEA 1178
Cdd:cd14538    155 GVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 935-1175 2.34e-67

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 229.43  E-value: 2.34e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  935 PWETAKKDENRNKNRYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQEN 1014
Cdd:cd14604     48 PTATGEKEENVKKNRYKDILPF---DHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYN 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1015 SASIVMVTNLVEVGRVKCVRYWP---DETEVYGDIKVTLIETEPLAEYVIRTFTVQKKghHEIRELRQFHFTSWPDHGVP 1091
Cdd:cd14604    125 VAIIVMACREFEMGRKKCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQ--NETRRLYQFHYVNWPDHDVP 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1092 CYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGV---VDIFNCIRELRSQRVNMVQTEEQY 1168
Cdd:cd14604    203 SSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQY 282


                   ....*..
gi 1949412791 1169 VFVHDAI 1175
Cdd:cd14604    283 ELVHRAI 289
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 977-1175 3.38e-66

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 222.53  E-value: 3.38e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEV-YGDIKVTLIETEP 1055
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVsSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1056 LAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQV-KFLNPPDAGPIAVHCSAGAGRTGCFIAVDI 1134
Cdd:cd14552     81 YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHPITVHCSAGAGRTGTFCALST 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1949412791 1135 MLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAI 1175
Cdd:cd14552    161 VLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 948-1172 3.57e-66

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ 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 (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 223.24  E-value: 3.57e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  948 NRYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEV 1027
Cdd:cd14616      1 NRFPNIKPY---NNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1028 GRVKCVRYWPDETE---VYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIreLRQFHFTSWPDHGVPCYATGLLGFIRQV 1104
Cdd:cd14616     78 GRIRCHQYWPEDNKpvtVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMM--VRQCNFTSWPEHGVPESSAPLIHFVKLV 155

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949412791 1105 KFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1172
Cdd:cd14616    156 RASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1266-1467 1.44e-65

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: 220.62  E-value: 1.44e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN---EMDAAQlCMQYWPEKNS--CCYGPIQVEFIS 1340
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTnlvEKGREK-CERYWPEEGGkpLEYGDITVTLVS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1341 ADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAyRDTPLSKRSILQLVRRlakWQEQYDGGDGRTVVHCLTGGGRS 1420
Cdd:cd00047     80 EEELSDYTIRTLELSPKGCSES--REVTHLHYTGWPD-HGVPSSPEDLLALVRR---VRKEARKPNGPIVVHCSAGVGRT 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1949412791 1421 GTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1467
Cdd:cd00047    154 GTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 977-1173 1.91e-65

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 220.34  E-value: 1.91e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEVYGDIKVTLIETEPL 1056
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1057 AEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVK------FLNPPDAGPIAVHCSAGAGRTGCFI 1130
Cdd:cd14558     81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKqklpykNSKHGRSVPIVVHCSDGSSRTGIFC 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1949412791 1131 AVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHD 1173
Cdd:cd14558    161 ALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 899-1177 1.99e-65

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 223.83  E-value: 1.99e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  899 PAIRVADLLQHITQMKCGQGYGFKE-EYEALA--EGQTAPWETAKKDENRNKNRYGNIIAYptdDHTRVRLQLLDGDPHS 975
Cdd:cd14629      5 PARNLYAHIQKLTQVPPGESVTAMElEFKLLAnsKAHTSRFISANLPCNKFKNRLVNIMPY---ELTRVCLQPIRGVEGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  976 DYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEVygdiKVTLIETEP 1055
Cdd:cd14629     82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA----RYQYFVVDP 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1056 LAE-----YVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPP--DAGPIAVHCSAGAGRTGC 1128
Cdd:cd14629    158 MAEynmpqYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRTGV 237

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1949412791 1129 FIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14629    238 FITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 947-1177 5.97e-65

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 220.10  E-value: 5.97e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  947 KNRYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVE 1026
Cdd:cd14602      1 KNRYKDILPY---DHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1027 VGRVKCVRYWP---DETEVYGDIKVTLIETEPLAEYVIRTFTVQKKghHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQ 1103
Cdd:cd14602     78 MGKKKCERYWAepgEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWD 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949412791 1104 VKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAEnEGVV----DIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14602    156 VRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 947-1172 2.15e-64

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-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. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 218.94  E-value: 2.15e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  947 KNRYGNIIAYPtddHTRVRLQLLDG-DPHSDYINANYIDGYH-RPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNL 1024
Cdd:cd14612     18 KDRYKTILPNP---QSRVCLRRAGSqEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKL 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1025 VEvGRVKCVRYWPDETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGhhEIRELRQFHFTSWPDHGVPCYATGLLGFIRQV 1104
Cdd:cd14612     95 KE-KKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEE--ESRSVKHYWFSSWPDHQTPESAGPLLRLVAEV 171

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1105 K--FLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1172
Cdd:cd14612    172 EesRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 947-1172 4.84e-64

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 217.09  E-value: 4.84e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  947 KNRYGNIIAYPtddHTRVRLQLLD-GDPHSDYINANYIDGYH-RPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNL 1024
Cdd:cd14611      2 KNRYKTILPNP---HSRVCLKPKNsNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1025 VEVGRvKCVRYWPDETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHeiRELRQFHFTSWPDHGVPCYATGLLGFIRQV 1104
Cdd:cd14611     79 KEKNE-KCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQS--RSVKHYWYTSWPDHKTPDSAQPLLQLMLDV 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1105 K--FLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1172
Cdd:cd14611    156 EedRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 977-1172 8.52e-64

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 215.75  E-value: 8.52e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETE---VYGDIKVTLIET 1053
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEeqlQFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1054 EPLAE-YVIRTFTVQKKghHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAV 1132
Cdd:cd14542     81 KRVGPdFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAI 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1949412791 1133 DIMLDMAENEGVVD---IFNCIRELRSQRVNMVQTEEQYVFVH 1172
Cdd:cd14542    159 DYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 949-1177 2.56e-63

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 215.29  E-value: 2.56e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  949 RYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVG 1028
Cdd:cd14623      1 RVLQIIPY---EFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1029 RVKCVRYWP-DETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFL 1107
Cdd:cd14623     78 QEKCAQYWPsDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQ 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949412791 1108 NPPDAG-PIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14623    158 QQQSGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 976-1178 6.46e-63

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 213.34  E-value: 6.46e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  976 DYINANYIDgYHRPRH-----YIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPD--ETEVYGDIKV 1048
Cdd:cd14541      1 DYINANYVN-MEIPGSgivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlgETMQFGNLQI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1049 TLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGC 1128
Cdd:cd14541     80 TCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGV 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1129 FIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEA 1178
Cdd:cd14541    160 LITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 943-1176 4.94e-62

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 212.00  E-value: 4.94e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  943 ENRNKNRYGNIIAYptdDHTRVRLqlldGDPHsDYINANYI-----DGYHRprhYIATQGPMQETVRDFWRMVWQENSAS 1017
Cdd:cd14597      2 ENRKKNRYKNILPY---DTTRVPL----GDEG-GYINASFIkmpvgDEEFV---YIACQGPLPTTVADFWQMVWEQKSTV 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1018 IVMVTNLVEVGRVKCVRYWPDE----TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCY 1093
Cdd:cd14597     71 IAMMTQEVEGGKIKCQRYWPEIlgktTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQ 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1094 ATGLLGFIRQVKFLNppDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHD 1173
Cdd:cd14597    151 PEQLLTFISYMRHIH--KSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQ 228


                   ...
gi 1949412791 1174 AIL 1176
Cdd:cd14597    229 VIL 231
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 921-1177 1.54e-60

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 209.53  E-value: 1.54e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  921 FKEEYEALAEGQTAPWET--AKKDENRNKNRYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGyHRPRH--YIATQ 996
Cdd:cd14610     19 LEKEWEALCAYQAEPNATnvAQREENVQKNRSLAVLPY---DHSRIILKAENSHSHSDYINASPIMD-HDPRNpaYIATQ 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  997 GPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLIETEPLAE-YVIRTFTVQKKGHHEI 1074
Cdd:cd14610     95 GPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEgSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQTNET 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1075 RELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLD-MAENEGVVDIFNCIRE 1153
Cdd:cd14610    175 RTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNkMAKGAKEIDIAATLEH 254

                          250       260
                   ....*....|....*....|....
gi 1949412791 1154 LRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14610    255 LRDQRPGMVQTKEQFEFALTAVAE 278
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 947-1170 1.22e-59

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 204.93  E-value: 1.22e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  947 KNRYGNIIAYptdDHTRVRLQLLDGDphSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVE 1026
Cdd:cd14545      1 LNRYRDRDPY---DHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLME 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1027 VGRVKCVRYWPDEtEVYGDI------KVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGF 1100
Cdd:cd14545     76 KGQIKCAQYWPQG-EGNAMIfedtglKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNF 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949412791 1101 IRQVK---FLNpPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGV--VDIFNCIRELRSQRVNMVQTEEQYVF 1170
Cdd:cd14545    155 LQKVResgSLS-SDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 923-1177 3.24e-59

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 205.66  E-value: 3.24e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  923 EEYEALAEGQTAP--WETAKKDENRNKNRYGNIIAYptdDHTRVRLQLLDGDPHSDYINANYIDGyHRPR--HYIATQGP 998
Cdd:cd14609     19 KEWQALCAYQAEPntCSTAQGEANVKKNRNPDFVPY---DHARIKLKAESNPSRSDYINASPIIE-HDPRmpAYIATQGP 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  999 MQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLIETEPLAE-YVIRTFTVQKKGHHEIRE 1076
Cdd:cd14609     95 LSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEgSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRT 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1077 LRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLD-MAENEGVVDIFNCIRELR 1155
Cdd:cd14609    175 LTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEHVR 254

                          250       260
                   ....*....|....*....|..
gi 1949412791 1156 SQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14609    255 DQRPGMVRTKDQFEFALTAVAE 276
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 976-1175 6.67e-59

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 201.77  E-value: 6.67e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  976 DYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEV-YGDIKVTLIETE 1054
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVtHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1055 PLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQV-KFLNPPDAGPIAVHCSAGAGRTGCFIAVD 1133
Cdd:cd14622     81 LLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFIALS 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1949412791 1134 IMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAI 1175
Cdd:cd14622    161 NILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 930-1186 2.31e-56

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 197.17  E-value: 2.31e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  930 EGQTAPWETAKKDENRNKNRYGNIIAYptdDHTRVRLQLLDgdphSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRM 1009
Cdd:cd14608     11 EASDFPCRVAKLPKNKNRNRYRDVSPF---DHSRIKLHQED----NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEM 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1010 VWQENSASIVMVTNLVEVGRVKCVRYWPDETE---VYGD--IKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTS 1084
Cdd:cd14608     84 VWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEkemIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTT 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1085 WPDHGVPCYATGLLGF---IRQVKFLNpPDAGPIAVHCSAGAGRTGCFIAVD---IMLDMAENEGVVDIFNCIRELRSQR 1158
Cdd:cd14608    164 WPDFGVPESPASFLNFlfkVRESGSLS-PEHGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSVDIKKVLLEMRKFR 242

                          250       260       270
                   ....*....|....*....|....*....|
gi 1949412791 1159 VNMVQTEEQYVFVHDAILEAC--LCGNTAI 1186
Cdd:cd14608    243 MGLIQTADQLRFSYLAVIEGAkfIMGDSSV 272
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 977-1177 3.72e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 191.52  E-value: 3.72e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGY--HRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-----TEVYGDIKVT 1049
Cdd:cd14540      1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLggehdALTFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1050 LIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFL-----------NPPdaGPIAVH 1118
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVrrhtnqdvaghNRN--PPTLVH 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1949412791 1119 CSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14540    159 CSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 977-1177 4.77e-55

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 190.73  E-value: 4.77e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGyHRPRH--YIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLI-E 1052
Cdd:cd14546      1 YINASTIYD-HDPRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEgSEVYHIYEVHLVsE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1053 TEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAV 1132
Cdd:cd14546     80 HIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILI 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1949412791 1133 DIMLD-MAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14546    160 DMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 939-1176 8.09e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 192.76  E-value: 8.09e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  939 AKKDENRNKNRYGNIIAYptdDHTRVrlqLLDGDphSDYINANYID----GYHRPRHYIATQGPMQETVRDFWRMVWQEN 1014
Cdd:cd14600     35 AKLPQNMDKNRYKDVLPY---DATRV---VLQGN--EDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQK 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1015 SASIVMVTNLVEVGRVKCVRYWPDETEV--YGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPC 1092
Cdd:cd14600    107 LSLIVMLTTLTERGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPD 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1093 YATGLLGFIRQVKFLNpPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1172
Cdd:cd14600    187 DSSDFLEFVNYVRSKR-VENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVC 265


                   ....
gi 1949412791 1173 DAIL 1176
Cdd:cd14600    266 EAIL 269
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 977-1173 6.83e-53

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 184.15  E-value: 6.83e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVtNLVEVGRVKCVRYWPDETE-VYGDIKVTLIETEp 1055
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSgTYGPIQVEFVSTT- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1056 LAEYVI-RTFTVQ--KKGHHEIRELRQFHFTSWPDHG-VPCYATGLLGFIRQV-KFLNPPDAGPIAVHCSAGAGRTGCFI 1130
Cdd:cd14556     79 IDEDVIsRIFRLQntTRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGEGPIVVHCLNGVGRSGVFC 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1949412791 1131 AVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHD 1173
Cdd:cd14556    159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 24-185 1.62e-52

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 181.77  E-value: 1.62e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791    24 FPGGCTFEESySSCGYSVSLgTNGFTWEQVNSWEK---PTMDPALPTGSFMVVNASGRASGQKAHLYMPTLKEN-DTHCI 99
Cdd:smart00137    2 SPGNCDFEEG-STCGWHQDS-NDDGHWERVSSATGipgPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791   100 DFLYSLSsrdGASPGTLNVYIKVNGGAQGNPVWNASDTVTEGWVKAELAISTfWPNSYQVIFEAVSVQGHPGFIAIDDIR 179
Cdd:smart00137   80 TFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDIL 155


                    ....*.
gi 1949412791   180 VLAHPC 185
Cdd:smart00137  156 LSNGPC 161
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 930-1175 1.99e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 185.17  E-value: 1.99e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  930 EGQTAPWETAKKDENRNKNRYGNIIAYptdDHTRVRLQLLDgdphSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRM 1009
Cdd:cd14607     10 ESHDYPHRVAKYPENRNRNRYRDVSPY---DHSRVKLQNTE----NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLM 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1010 VWQENSASIVMVTNLVEVGRVKCVRYWPDETE---VYGD--IKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTS 1084
Cdd:cd14607     83 VWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEevlSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTT 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1085 WPDHGVPCYATGLLGF---IRQVKFLNpPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEG--VVDIFNCIRELRSQRV 1159
Cdd:cd14607    163 WPDFGVPESPASFLNFlfkVRESGSLS-PEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRM 241

                          250
                   ....*....|....*.
gi 1949412791 1160 NMVQTEEQYVFVHDAI 1175
Cdd:cd14607    242 GLIQTPDQLRFSYMAV 257
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 977-1178 2.89e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 182.64  E-value: 2.89e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGY--HRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPD---ETEVYGDIKVTLI 1051
Cdd:cd14596      1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPEtlqEPMELENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1052 ETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNppDAGPIAVHCSAGAGRTGCFIA 1131
Cdd:cd14596     81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGRAGVLIC 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1949412791 1132 VDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEA 1178
Cdd:cd14596    159 VDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1266-1468 6.09e-51

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 178.62  E-value: 6.09e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD--AAQLCMQYWPEKNSCCYGPIQVEFISADI 1343
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKerSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1344 DEDIINRIFRICNmARPQDGyRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQEQydGGDGRTVVHCLTGGGRSGTF 1423
Cdd:cd14552     81 YEDYTLRDFLVTK-GKGGST-RTVRQFHFHGWPEV-GIPDNGKGMIDLIAAVQKQQQQ--SGNHPITVHCSAGAGRTGTF 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1949412791 1424 CAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEV 1468
Cdd:cd14552    156 CALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKV 200
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 976-1177 9.10e-51

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 178.60  E-value: 9.10e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  976 DYINANYIDgYHRP-----RHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDET--EVYGDIKV 1048
Cdd:cd14601      1 DYINANYIN-MEIPsssiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSgsSSYGGFQV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1049 TLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGC 1128
Cdd:cd14601     80 TCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGV 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1949412791 1129 FIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14601    160 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1234-1470 1.49e-50

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 178.87  E-value: 1.49e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1234 LPRNHDKNRSMDVLSADR---CLPFLISVDGesSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML 1310
Cdd:cd14554      3 LPCNKFKNRLVNILPYEStrvCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1311 ---NEMDAAQlCMQYWPEKNSCCYGPIQVEFISADIDEDIINRIFRICNmARpQDGYRLVQHFQFIGWPAyRDTPLSKRS 1387
Cdd:cd14554     81 tklREMGREK-CHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTD-AR-DGQSRTVRQFQFTDWPE-QGVPKSGEG 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1388 ILQLVRRLAKWQEQYdGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1467
Cdd:cd14554    157 FIDFIGQVHKTKEQF-GQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235


                   ...
gi 1949412791 1468 VAL 1470
Cdd:cd14554    236 AAL 238
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 901-1172 2.59e-49

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 178.27  E-value: 2.59e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  901 IRVADLLQHITQMKCgQGYGFKEEYEALAEGQTAPWETAKKDENRNKNRYGNIiayPTDDHTRVRLQLLDGDPhSDYINA 980
Cdd:PHA02747     9 CRAIDFLKRRNQLNC-FGIIRDEHHQIILKPFDGLIANFEKPENQPKNRYWDI---PCWDHNRVILDSGGGST-SDYIHA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  981 NYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEV-GRVKCVRYW---PDETEVYGDIKVTLIETEPL 1056
Cdd:PHA02747    84 NWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGTnGEEKCYQYWclnEDGNIDMEDFRIETLKTSVR 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1057 AEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFI------RQV--KFLNPPDA--GPIAVHCSAGAGRT 1126
Cdd:PHA02747   164 AKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKFIkiidinRKKsgKLFNPKDAllCPIVVHCSDGVGKT 243

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1949412791 1127 GCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1172
Cdd:PHA02747   244 GIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1265-1468 4.18e-49

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 173.65  E-value: 4.18e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1265 NYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQL--CMQYWPEKNSCCYGPIQVEFISAD 1342
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQekCVQYWPSEGSVTHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1343 IDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQEQydGGDGRTVVHCLTGGGRSGT 1422
Cdd:cd14622     81 LLETISIRDFLVTYNQEKQT--RLVRQFHFHGWPEI-GIPAEGKGMIDLIAAVQKQQQQ--TGNHPIVVHCSAGAGRTGT 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1949412791 1423 FCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEV 1468
Cdd:cd14622    156 FIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRV 201
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1228-1466 9.63e-49

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


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 174.86  E-value: 9.63e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1228 DCSvgLLPRNHDKNRSMDVLSADRCLPFLISVDG-ESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSS 1306
Cdd:cd14543     22 LCS--LAPANQEKNRYGDVLCLDQSRVKLPKRNGdERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1307 IVMLNE-MDAAQL-CMQYWP-EKNSCC-YGPIQVEFISADIDEDIINRIFRICNMArpQDGYRLVQHFQFIGWPAYrDTP 1382
Cdd:cd14543    100 IVMTTRvVERGRVkCGQYWPlEEGSSLrYGDLTVTNLSVENKEHYKKTTLEIHNTE--TDESRQVTHFQFTSWPDF-GVP 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1383 LSKRS---ILQLVRRLAKWQEQYDGGDGR-------TVVHCLTGGGRSGTFCA--ICsineMIQQQNI--VDVFHTVKTL 1448
Cdd:cd14543    177 SSAAAlldFLGEVRQQQALAVKAMGDRWKghppgppIVVHCSAGIGRTGTFCTldIC----LSQLEDVgtLNVMQTVRRM 252

                          250
                   ....*....|....*...
gi 1949412791 1449 RNNKTNMVETMEQYKFCY 1466
Cdd:cd14543    253 RTQRAFSIQTPDQYYFCY 270
PHA02738 PHA02738
hypothetical protein; Provisional
 922-1175 3.11e-48

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 175.11  E-value: 3.11e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  922 KEEYEALAEGQTAPWETAKKdeNRNKNRYGNIIAYptdDHTRVRLQLLDGdpHSDYINANYIDGYHRPRHYIATQGPMQE 1001
Cdd:PHA02738    29 REHQKVISEKVDGTFNAEKK--NRKLNRYLDAVCF---DHSRVILPAERN--RGDYINANYVDGFEYKKKFICGQAPTRQ 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1002 TVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETE---VYGDIKVTLIETEPLAEYVIRTFTVqKKGHHEIRELR 1078
Cdd:PHA02738   102 TCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQgsiRFGKFKITTTQVETHPHYVKSTLLL-TDGTSATQTVT 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1079 QFHFTSWPDHGVPCYATGLLGFIRQVK----------------FLNPPdagPIAVHCSAGAGRTGCFIAVDIMLDMAENE 1142
Cdd:PHA02738   181 HFNFTAWPDHDVPKNTSEFLNFVLEVRqcqkelaqeslqighnRLQPP---PIVVHCNAGLGRTPCYCVVDISISRFDAC 257

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1949412791 1143 GVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAI 1175
Cdd:PHA02738   258 ATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
943-1168 3.05e-47

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 171.04  E-value: 3.05e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  943 ENRNKNRYGNIIAYptdDHTRVRlqlldgdPHSDYINANYIDGYhRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVT 1022
Cdd:COG5599     41 NGSPLNRFRDIQPY---KETALR-------ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLA 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1023 NLVEVG--RVKCVRYWP-DETEVYGDIKVTLIETEPLAEYV-IRTFTVQKKGH-HEIRELRQFHFTSWPDHGVPCYAT-- 1095
Cdd:COG5599    110 SDDEISkpKVKMPVYFRqDGEYGKYEVSSELTESIQLRDGIeARTYVLTIKGTgQKKIEIPVLHVKNWPDHGAISAEAlk 189

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949412791 1096 GLLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCFIAVDIMLDM--AENEGVVDIFNCIRELRSQRVN-MVQTEEQY 1168
Cdd:COG5599    190 NLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMRTSRNGgMVQTSEQL 265
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 977-1173 1.66e-46

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 166.02  E-value: 1.66e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGY--HRPRhYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE---TEVYGDIKVTLI 1051
Cdd:cd14539      1 YINASLIEDLtpYCPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgqALVYGAITVSLQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1052 ETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQV-KFLNP--PDAGPIAVHCSAGAGRTGC 1128
Cdd:cd14539     80 SVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVhSHYLQqrSLQTPIVVHCSSGVGRTGA 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1949412791 1129 F-IAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHD 1173
Cdd:cd14539    160 FcLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 977-1170 1.70e-46

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 166.10  E-value: 1.70e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRH--YIATQGPMQETVRDFWRMVWQENSASIVMVTNLVE-VGRVKCVRYWPDE---TEVYGDIKVTl 1050
Cdd:cd17658      1 YINASLVETPASESLpkFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCADYFPAEeneSREFGRISVT- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1051 IETEPLAEYVI--RTFTVQKKGHHE-IRELRQFHFTSWPDHGVPCYATGLLGFIRQVkFLNPPDAGPIAVHCSAGAGRTG 1127
Cdd:cd17658     80 NKKLKHSQHSItlRVLEVQYIESEEpPLSVLHIQYPEWPDHGVPKDTRSVRELLKRL-YGIPPSAGPIVVHCSAGIGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1949412791 1128 CFIAVDIMLD--MAENEGVVDIFNCIRELRSQRVNMVQTEEQYVF 1170
Cdd:cd17658    159 AYCTIHNTIRriLEGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIF 203
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1266-1467 1.99e-46

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 165.64  E-value: 1.99e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEM--DAAQLCMQYWPEKNSCcYGPIQVEFISADI 1343
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELkeGDQEQCAQYWGDEKKT-YGDIEVELKDTEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1344 DEDIINRIFRICNMARPQDgyRLVQHFQFIGWpAYRDTPLSKRSILQLVRRLAKWQEQYDGGDGRT---VVHCLTGGGRS 1420
Cdd:cd14558     80 SPTYTVRVFEITHLKRKDS--RTVYQYQYHKW-KGEELPEKPKDLVDMIKSIKQKLPYKNSKHGRSvpiVVHCSDGSSRT 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1949412791 1421 GTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1467
Cdd:cd14558    157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1262-1471 2.22e-46

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 166.76  E-value: 2.22e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1262 ESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD--AAQLCMQYWPEKNSCCYGPIQVEFI 1339
Cdd:cd14623     22 ENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEerGQEKCAQYWPSDGSVSYGDITIELK 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1340 SADIDEDIINRIFRICNMArpQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQEQydGGDGRTVVHCLTGGGR 1419
Cdd:cd14623    102 KEEECESYTVRDLLVTNTR--ENKSRQIRQFHFHGWPEV-GIPSDGKGMINIIAAVQKQQQQ--SGNHPITVHCSAGAGR 176

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1949412791 1420 SGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1471
Cdd:cd14623    177 TGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1237-1475 2.58e-46

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 166.80  E-value: 2.58e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1237 NHDKNRSMDVLSADRCLPFLISVDG-ESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN--EM 1313
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTklEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1314 DAAQLCMQYWPEKNSCCYGPIQVEFIsadideDIIN------RIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRS 1387
Cdd:cd14553     83 RSRVKCDQYWPTRGTETYGLIQVTLL------DTVElatytvRTFALHKNGSSEK--REVRQFQFTAWPDH-GVPEHPTP 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1388 ILQLVRRLaKWQEQYDGGDgrTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1467
Cdd:cd14553    154 FLAFLRRV-KACNPPDAGP--IVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHD 230


                   ....*...
gi 1949412791 1468 VALEALNS 1475
Cdd:cd14553    231 ALLEAVTC 238
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1242-1464 5.88e-46

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are 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. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 165.22  E-value: 5.88e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1242 RSMDVLSADRCLPFLISVDGES-SNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMDAAQ-L 1318
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEgSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLtQCMEKGRvK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1319 CMQYWPEKN-SCCYGPIQVEFISADIDEDIINRIFRICNmarpQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLak 1397
Cdd:cd14548     81 CDHYWPFDQdPVYYGDITVTMLSESVLPDWTIREFKLER----GDEVRSVRQFHFTAWPDH-GVPEAPDSLLRFVRLV-- 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949412791 1398 wQEQYDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKF 1464
Cdd:cd14548    154 -RDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 921-1177 1.99e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 166.72  E-value: 1.99e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  921 FKEEYEALAEGqTAPWETAKKDENRN--KNRYGNIiayPTDDHTRVRLQLLDGDphSDYINANYIDGYHRPRHYIATQGP 998
Cdd:PHA02742    28 LKEEHEHIMQE-IVAFSCNESLELKNmkKCRYPDA---PCFDRNRVILKIEDGG--DDFINASYVDGHNAKGRFICTQAP 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  999 MQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYW-PDE--TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIR 1075
Cdd:PHA02742   102 LEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmPHErgKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASL 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1076 ELRQFHFTSWPDHGVPCYATGLLGFIRQVKFL-----------NPPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGV 1144
Cdd:PHA02742   182 DIKHFAYEDWPHGGLPRDPNKFLDFVLAVREAdlkadvdikgeNIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAI 261

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1949412791 1145 VDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:PHA02742   262 IPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1183-1475 4.74e-45

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 164.91  E-value: 4.74e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1183 NTAIPVCEFRAVYYNISRLDPQTNSSQIKDEFQTLniVTPRVRPEDCSVGLLPRNHDKNRSMDVL---SADRCLPFLISV 1259
Cdd:cd14627      1 NTEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRL--ANSKAHTSRFISANLPCNKFKNRLVNIMpyeTTRVCLQPIRGV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1260 DGesSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD--AAQLCMQYWPEKNSCCYGPIQVE 1337
Cdd:cd14627     79 EG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLRemGREKCHQYWPAERSARYQYFVVD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1338 FISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAyRDTPLSKRSILQLVRRLAKWQEQYdGGDGRTVVHCLTGG 1417
Cdd:cd14627    157 PMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQF-GQDGPISVHCSAGV 232

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1949412791 1418 GRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEALNS 1475
Cdd:cd14627    233 GRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1184-1476 2.37e-44

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 162.98  E-value: 2.37e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1184 TAIPVCEFRAVYYNISRLDPQTNSSQIKDEFQTLniVTPRVRPEDCSVGLLPRNHDKNRSMDVL---SADRCLPFLISVD 1260
Cdd:cd14628      1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRL--ASSKAHTSRFISANLPCNKFKNRLVNIMpyeSTRVCLQPIRGVE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1261 GesSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD--AAQLCMQYWPEKNSCCYGPIQVEF 1338
Cdd:cd14628     79 G--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLRemGREKCHQYWPAERSARYQYFVVDP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1339 ISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAyRDTPLSKRSILQLVRRLAKWQEQYdGGDGRTVVHCLTGGG 1418
Cdd:cd14628    157 MAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQF-GQDGPISVHCSAGVG 232

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1949412791 1419 RSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEALNSF 1476
Cdd:cd14628    233 RTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGSF 290
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 924-1177 3.02e-44

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 162.47  E-value: 3.02e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  924 EYEALAEGQT-APWETAKKDENRNKNRYGNIIAYptdDHTRVRLqLLDGDPHSDYINANYIDGYHRPR--HYIATQGPMQ 1000
Cdd:cd14599     17 EYEQIPKKKAdGVFTTATLPENAERNRIREVVPY---EENRVEL-VPTKENNTGYINASHIKVTVGGEewHYIATQGPLP 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1001 ETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPD-----ETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIR 1075
Cdd:cd14599     93 HTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQER 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1076 ELRQFHFTSWPDHGVPCYATGLLGFIRQV--------------KFLNPpdagPIAVHCSAGAGRTGCFIAVDIMLDMAEN 1141
Cdd:cd14599    173 TVWHLQYTDWPDHGCPEEVQGFLSYLEEIqsvrrhtnsmldstKNCNP----PIVVHCSAGVGRTGVVILTELMIGCLEH 248

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1949412791 1142 EGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14599    249 NEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1183-1476 4.66e-44

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 162.20  E-value: 4.66e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1183 NTAIPVCEFRAVYYNISRLDPQTNSSQIKDEFQTLniVTPRVRPEDCSVGLLPRNHDKNRSMDVLSADRCLPFLISVDG- 1261
Cdd:cd14629      1 NTEVPARNLYAHIQKLTQVPPGESVTAMELEFKLL--ANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGv 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1262 ESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD--AAQLCMQYWPEKNSCCYGPIQVEFI 1339
Cdd:cd14629     79 EGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLRemGREKCHQYWPAERSARYQYFVVDPM 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1340 SADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAyRDTPLSKRSILQLVRRLAKWQEQYdGGDGRTVVHCLTGGGR 1419
Cdd:cd14629    159 AEYNMPQYILREFKVTDARDGQS--RTIRQFQFTDWPE-QGVPKTGEGFIDFIGQVHKTKEQF-GQDGPITVHCSAGVGR 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1949412791 1420 SGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEALNSF 1476
Cdd:cd14629    235 TGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGSF 291
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1202-1475 4.00e-42

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 156.37  E-value: 4.00e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1202 DPQTNSSQIKDEFQTLniVTPRVRPEDCSVGLLPRNHDKNRSMDVLSADRCLPFLISVDGES-SNYINAA-LMDSHKQPA 1279
Cdd:cd14610     11 DHLKNKNRLEKEWEAL--CAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHShSDYINASpIMDHDPRNP 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1280 AFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEM--DAAQLCMQYWPEKNSCCYGPIQVEFISADI-DEDIINRIFRICN 1356
Cdd:cd14610     89 AYIATQGPLPATVADFWQMVWESGCVVIVMLTPLaeNGVKQCYHYWPDEGSNLYHIYEVNLVSEHIwCEDFLVRSFYLKN 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1357 MARPQDgyRLVQHFQFIGWPAyRDTPLSKRSILQLVRRLAKWqeqYDGGDGRTVVHCLTGGGRSGTFCAI-CSINEMIQQ 1435
Cdd:cd14610    169 LQTNET--RTVTQFHFLSWND-QGVPASTRSLLDFRRKVNKC---YRGRSCPIIVHCSDGAGRSGTYILIdMVLNKMAKG 242

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1949412791 1436 QNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEALNS 1475
Cdd:cd14610    243 AKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNA 282
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 28-185 5.97e-41

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 148.29  E-value: 5.97e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791   28 CTFEESYssCGYSVSLgTNGFTWEQVNSWEKPTMDPAL-----PTGSFMVVNASGRASGQKAHLYMPTLKEN-DTHCIDF 101
Cdd:cd06263      1 CDFEDGL--CGWTQDS-TDDFDWTRVSGSTPSPGTPPDhthgtGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCLSF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  102 LYSLSsrdGASPGTLNVYIKVNGGAQGNPVWNASDTVTEGWVKAELAISTFWpNSYQVIFEAVSVQGHPGFIAIDDIRVL 181
Cdd:cd06263     78 WYHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDISLS 153


                   ....
gi 1949412791  182 AHPC 185
Cdd:cd06263    154 PGPC 157
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1266-1467 1.73e-40

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 148.65  E-value: 1.73e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD--AAQLCMQYWPEKNSCCYGPIQVEFISADI 1343
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVerGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1344 DEDIINRIFRICNM----ARPQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQEqydGGDGRTVVHCLTGGGR 1419
Cdd:cd14549     81 LATYTVRTFSLKNLklkkVKGRSSERVVYQYHYTQWPDH-GVPDYTLPVLSFVRKSSAANP---PGAGPIVVHCSAGVGR 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1949412791 1420 SGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1467
Cdd:cd14549    157 TGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1234-1467 3.99e-40

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO 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 essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 149.27  E-value: 3.99e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1234 LPRNHDKNRSMDVLSADRCLPFLISV-DGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNE 1312
Cdd:cd14614      9 LPVNRCKNRYTNILPYDFSRVKLVSMhEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQ 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1313 MDAAQL--CMQYWP-EKNSCCYGPIQVEFISADIDEDIINRIFRICNMARPQDgyrlVQHFQFIGWPAYR-DTPLSKRSI 1388
Cdd:cd14614     89 CNEKRRvkCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD----VMHFNYTAWPDHGvPTANAAESI 164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949412791 1389 LQLVRRLakwQEQYDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1467
Cdd:cd14614    165 LQFVQMV---RQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1076-1177 4.95e-40

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: 143.65  E-value: 4.95e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  1076 ELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNP--PDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENE-GVVDIFNCIR 1152
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1949412791  1153 ELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1076-1177 4.95e-40

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 143.65  E-value: 4.95e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  1076 ELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNP--PDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENE-GVVDIFNCIR 1152
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1949412791  1153 ELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1237-1472 7.01e-40

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 149.80  E-value: 7.01e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1237 NHDKNRSMDVLSADRCLPFLISVDG-ESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDA 1315
Cdd:cd14626     41 NKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1316 AQL--CMQYWPEKNSCCYGPIQVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQLVR 1393
Cdd:cd14626    121 KSRvkCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEK--REVRQFQFMAWPDH-GVPEYPTPILAFLR 197

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949412791 1394 RLaKWQEQYDGGDgrTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEA 1472
Cdd:cd14626    198 RV-KACNPPDAGP--MVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEA 273
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 977-1177 2.07e-39

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 146.27  E-value: 2.07e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRH--YIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWP-----DETEVYGDIKVT 1049
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1050 LIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFL----------NPPDAgPIAVHC 1119
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVrrhtnstidpKSPNP-PVLVHC 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1949412791 1120 SAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14598    160 SAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1241-1470 5.25e-39

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-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. PTPRV 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. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 145.47  E-value: 5.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1241 NRSMDVLSADRCLPFLISVDGES-SNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNE-MDAAQ- 1317
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPhSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVgMENGRv 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1318 LCMQYWP-EKNSCCYGPIQVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQLvRRLA 1396
Cdd:cd14618     81 LCDHYWPsESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKE--RRVKHLHYTAWPDH-GIPESTSSLMAF-RELV 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949412791 1397 KWQEQYDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVAL 1470
Cdd:cd14618    157 REHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1266-1467 1.65e-38

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 143.54  E-value: 1.65e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAalmdSHKQPAA-----FIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN-EMDAAQL-CMQYWPEK-NSCCYGPIQVE 1337
Cdd:cd18533      1 YINA----SYITLPGtsskrYIATQGPLPATIGDFWKMIWQNNVGVIVMLTpLVENGREkCDQYWPSGeYEGEYGDLTVE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1338 FIS--ADIDEDIINRIFRicnMARPQDGYRLVQHFQFIGWPAYRdTPLSKRSILQLVrRLAKWQEQYDGGDGRTVVHCLT 1415
Cdd:cd18533     77 LVSeeENDDGGFIVREFE---LSKEDGKVKKVYHIQYKSWPDFG-VPDSPEDLLTLI-KLKRELNDSASLDPPIIVHCSA 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949412791 1416 GGGRSGTFCAICSINEMIQQQNIVD---------VFHTVKTLRNNKTNMVETMEQYKFCYE 1467
Cdd:cd18533    152 GVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1241-1471 2.10e-38

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ 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 (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 143.80  E-value: 2.10e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1241 NRSMDVLSADRCLPFLISVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML---NEMDAAQ 1317
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLtkcVEQGRTK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1318 lCMQYWPEKNSCCYGPIQVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAK 1397
Cdd:cd14615     81 -CEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNES--RTVRHFHFTSWPDH-GVPETTDLLINFRHLVRE 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949412791 1398 WQEQYDgGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1471
Cdd:cd14615    157 YMKQNP-PNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1241-1473 2.24e-38

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH 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 localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 143.88  E-value: 2.24e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1241 NRSMDVLSADRC-LPFLISVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMDAAQL 1318
Cdd:cd14619      1 NRFRNVLPYDWSrVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLtNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1319 -CMQYWP-EKNSCCYGPIQVEFISADIDEDIINRIFRICNMArpQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLA 1396
Cdd:cd14619     81 kCEHYWPlDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVE--EQKTLSVRHFHFTAWPDH-GVPSSTDTLLAFRRLLR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949412791 1397 KWQEQYDGGdGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEAL 1473
Cdd:cd14619    158 QWLDQTMSG-GPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1266-1467 2.67e-38

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 142.46  E-value: 2.67e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQLCMQYWPEK-NSCCYGPIQVEFISADI- 1343
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPIYWPTKeKPLECETFKVTLSGEDHs 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1344 ----DEDIINRIFRICNMarpQDGYRL-VQHFQFIGWPAyRDTPLSkrSILQLVRRLAKWQEQYDGGdgrTVVHCLTGGG 1418
Cdd:cd14550     81 clsnEIRLIVRDFILEST---QDDYVLeVRQFQCPSWPN-PCSPIH--TVFELINTVQEWAQQRDGP---IVVHDRYGGV 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1949412791 1419 RSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1467
Cdd:cd14550    152 QAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1202-1475 1.08e-37

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 143.64  E-value: 1.08e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1202 DPQTNSSQIKDEFQTLniVTPRVRPEDCSVGLLPRNHDKNRSMDVLSADRC-LPFLISVDGESSNYINAA-LMDSHKQPA 1279
Cdd:cd14609      9 DHLRNRDRLAKEWQAL--CAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHArIKLKAESNPSRSDYINASpIIEHDPRMP 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1280 AFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEM--DAAQLCMQYWPEKNSCCYGPIQVEFISADI-DEDIINRIFRICN 1356
Cdd:cd14609     87 AYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLveDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIwCEDFLVRSFYLKN 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1357 MaRPQDGYRLVQhFQFIGWPAyRDTPLSKRSILQLVRRLAKwqeQYDGGDGRTVVHCLTGGGRSGTFCAI-CSINEMIQQ 1435
Cdd:cd14609    167 V-QTQETRTLTQ-FHFLSWPA-EGIPSSTRPLLDFRRKVNK---CYRGRSCPIIVHCSDGAGRTGTYILIdMVLNRMAKG 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1949412791 1436 QNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEALNS 1475
Cdd:cd14609    241 VKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNA 280
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 28-186 2.45e-37

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 137.88  E-value: 2.45e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791   28 CTFEESySSCGYSVSLGTnGFTWEQVNSWE---KPTMDPALPT--GSFMVVNASGRASGQKAHLYMPTLKENDT-HCIDF 101
Cdd:pfam00629    1 CDFEDG-NLCGWTQDSSD-DFDWERVSGPSvktGPSSDHTQGTgsGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  102 LYSLSsrdGASPGTLNVYIKVNGGAQGNPVWNASDTVTEGWVKAELAISTFwPNSYQVIFEAVSVQGHPGFIAIDDIRVL 181
Cdd:pfam00629   79 WYHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDISLS 154


                   ....*
gi 1949412791  182 AHPCR 186
Cdd:pfam00629  155 SGPCP 159
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1237-1472 2.66e-37

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 140.93  E-value: 2.66e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1237 NHDKNRSMDVLSADRCLPFLISVDGES-SNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMD 1314
Cdd:cd14630      3 NRNKNRYGNIISYDHSRVRLQLLDGDPhSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVtNLVE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1315 AAQL-CMQYWPEKNSCcYGPIQVEFISADIDEDIINRIFRIcnMARPQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVR 1393
Cdd:cd14630     83 VGRVkCVRYWPDDTEV-YGDIKVTLIETEPLAEYVIRTFTV--QKKGYHEIREIRQFHFTSWPDH-GVPCYATGLLGFVR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949412791 1394 RLaKWQEQYDGGDgrTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEA 1472
Cdd:cd14630    159 QV-KFLNPPDAGP--IVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEA 234
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1245-1471 2.78e-37

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 140.46  E-value: 2.78e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1245 DVLSADRCLPFLISVDG-ESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD--AAQLCMQ 1321
Cdd:cd14620      3 NILPYDHSRVILSQLDGiPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKerKEEKCYQ 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1322 YWPEKNSCCYGPIQVEFISADIDEDIINRIFriCNMARPQDGY---RLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKW 1398
Cdd:cd14620     83 YWPDQGCWTYGNIRVAVEDCVVLVDYTIRKF--CIQPQLPDGCkapRLVTQLHFTSWPDF-GVPFTPIGMLKFLKKVKSV 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949412791 1399 QEQYDGgdgRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1471
Cdd:cd14620    160 NPVHAG---PIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1266-1473 2.80e-37

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


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 139.82  E-value: 2.80e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAalmdSH------KQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN-EMDAAQL-CMQYWPE---KNSCCYGPI 1334
Cdd:cd14538      1 YINA----SHiripvgGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTqDVEGGKVkCHRYWPDslnKPLICGGRL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1335 QVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQEqydggDGRTVVHCL 1414
Cdd:cd14538     77 EVSLEKYQSLQDFVIRRISLRDKETGEV--HHITHLNFTTWPDH-GTPQSADPLLRFIRYMRRIHN-----SGPIVVHCS 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1949412791 1415 TGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEAL 1473
Cdd:cd14538    149 AGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1266-1472 3.14e-37

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 139.28  E-value: 3.14e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMDAAQL-CMQYWPEkNSCCYGPIQVEFISADI 1343
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVtNLVEVGRVkCSRYWPD-DTEVYGDIKVTLVETEP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1344 DEDIINRIFricnmARPQDGY---RLVQHFQFIGWPAYrDTPLSKRSILQLVRRLaKWQEQYDGGDgrTVVHCLTGGGRS 1420
Cdd:cd14555     80 LAEYVVRTF-----ALERRGYheiREVRQFHFTGWPDH-GVPYHATGLLGFIRRV-KASNPPSAGP--IVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1949412791 1421 GTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEA 1472
Cdd:cd14555    151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEA 202
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 941-1175 5.18e-37

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 142.86  E-value: 5.18e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  941 KDENRNKNRYGNIiayPTDDHTRV-------------------RLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQE 1001
Cdd:PHA02746    48 KKENLKKNRFHDI---PCWDHSRVvinaheslkmfdvgdsdgkKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKED 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1002 TVRDFWRMVWQENSASIVMVTNlVEVGRVKCVRYW--PDETEV-YGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELR 1078
Cdd:PHA02746   125 TSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELaFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIH 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1079 QFHFTSWPDHGVPcyaTGLLGFIRQVKFLN-------------PPDAGPIAVHCSAGAGRTGCFIAVDIMLDMAENEGVV 1145
Cdd:PHA02746   204 HFWFPDWPDNGIP---TGMAEFLELINKVNeeqaelikqadndPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEV 280

                          250       260       270
                   ....*....|....*....|....*....|
gi 1949412791 1146 DIFNCIRELRSQRVNMVQTEEQYVFVHDAI 1175
Cdd:PHA02746   281 CLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1241-1467 2.93e-36

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: 137.36  E-value: 2.93e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1241 NRSMDVLSADRCLPFLISVDGES-SNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNE-MDAAQL 1318
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQcVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1319 -CMQYWP-EKNSCCYGPIQVEFISADIDEDIINRIFRICNMARpQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLA 1396
Cdd:cd14617     81 kCDHYWPaDQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQ-LDAPRLVRHFHYTVWPDH-GVPETTQSLIQFVRTVR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949412791 1397 KWQEQYDGGdGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1467
Cdd:cd14617    159 DYINRTPGS-GPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1234-1473 3.69e-36

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 139.07  E-value: 3.69e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1234 LPRNHDKNRSMDVLSADRCLPFLISVDG-ESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNE 1312
Cdd:cd14625     44 LEVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1313 MDAAQL--CMQYWPEKNSCCYGPIQVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQ 1390
Cdd:cd14625    124 LEEKSRikCDQYWPSRGTETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEK--REVRQFQFTAWPDH-GVPEYPTPFLA 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1391 LVRRLaKWQEQYDGGDgrTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVAL 1470
Cdd:cd14625    201 FLRRV-KTCNPPDAGP--IVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALL 277


                   ...
gi 1949412791 1471 EAL 1473
Cdd:cd14625    278 EAV 280
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1266-1474 5.73e-36

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 136.04  E-value: 5.73e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAA-LMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML---NEMDAAQlCMQYWPEKNSCCYGPIQVEFISA 1341
Cdd:cd14546      1 YINAStIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLtrlQENGVKQ-CARYWPEEGSEVYHIYEVHLVSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1342 DI-DEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAyRDTPLSKRSILQLVRRLAKwqeQYDGGDGRTVVHCLTGGGRS 1420
Cdd:cd14546     80 HIwCDDYLVRSFYLKNLQTSET--RTVTQFHFLSWPD-EGIPASAKPLLEFRRKVNK---SYRGRSCPIVVHCSDGAGRT 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1949412791 1421 GTFCAI-CSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEALN 1474
Cdd:cd14546    154 GTYILIdMVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEVN 208
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1239-1466 6.54e-36

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 136.75  E-value: 6.54e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1239 DKNRSMDVLSADRCLpflISVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNE-MDAAQ 1317
Cdd:cd14545      2 NRYRDRDPYDHDRSR---VKLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKlMEKGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1318 L-CMQYWP----EKNSCCYGPIQVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYR--DTPLSKRSILQ 1390
Cdd:cd14545     79 IkCAQYWPqgegNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQET--REVLHFHYTTWPDFGvpESPAAFLNFLQ 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949412791 1391 LVRRLAkwqeQYDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNI--VDVFHTVKTLRNNKTNMVETMEQYKFCY 1466
Cdd:cd14545    157 KVRESG----SLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1235-1473 2.96e-35

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 136.32  E-value: 2.96e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1235 PRNHDKNRSMDVLSADRC---LPFLISVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN 1311
Cdd:cd17667     25 PDNKHKNRYINILAYDHSrvkLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1312 EM--DAAQLCMQYWPEKNSCCYGPIQVEFISADIDEDIINRIFRICN--MARPQDG-------YRLVQHFQFIGWPAYrD 1380
Cdd:cd17667    105 NLveKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkVKKGQKGnpkgrqnERTVIQYHYTQWPDM-G 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1381 TPLSKRSILQLVRRLAKWQEQYdggDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETME 1460
Cdd:cd17667    184 VPEYALPVLTFVRRSSAARTPE---MGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEE 260

                          250
                   ....*....|...
gi 1949412791 1461 QYKFCYEVALEAL 1473
Cdd:cd17667    261 QYIFIHDALLEAI 273
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 977-1177 3.43e-35

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 133.61  E-value: 3.43e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVtNLVEVGRVkCVRYWPDETE-VYGDIKVTLIETEP 1055
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDAAQL-CMQYWPEKTScCYGPIQVEFVSADI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1056 LAEYVIRTFTV--QKKGHHEIRELRQFHFTSWPDH-GVPCYATGLLGFIRQV-KFLNPPDA--GPIAVHCSAGAGRTGCF 1129
Cdd:cd14634     79 DEDIISRIFRIcnMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLeKWQEQYDGreGRTVVHCLNGGGRSGTF 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1949412791 1130 IAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14634    159 CAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1266-1467 4.32e-35

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 133.11  E-value: 4.32e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD--AAQLCMQYWPEKNSCCYGPIQV--EFISA 1341
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKerKEKKCSQYWPDQGCWTYGNLRVrvEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1342 DIDEDI----INRIFRICNMARPqdgyRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQEQYDGGdgrTVVHCLTGG 1417
Cdd:cd14551     81 LVDYTTrkfcIQKVNRGIGEKRV----RLVTQFHFTSWPDF-GVPFTPIGMLKFLKKVKSANPPRAGP---IVVHCSAGV 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1418 GRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1467
Cdd:cd14551    153 GRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1229-1471 4.50e-35

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 136.31  E-value: 4.50e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1229 CSVGLLPRNHDKNRSMDVLSADRCLPFLISVDG-ESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSI 1307
Cdd:cd14621     44 CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATI 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1308 VMLNEMDAAQ--LCMQYWPEKNSCCYGPIQVEFISADIDEDIINRIFRICNMA-----RPQdgyRLVQHFQFIGWPAYrD 1380
Cdd:cd14621    124 VMVTNLKERKecKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVGdvtnkKPQ---RLITQFHFTSWPDF-G 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1381 TPLSKRSILQLVRRLAKWQEQYDGGdgrTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETME 1460
Cdd:cd14621    200 VPFTPIGMLKFLKKVKNCNPQYAGA---IVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDM 276

                          250
                   ....*....|.
gi 1949412791 1461 QYKFCYEVALE 1471
Cdd:cd14621    277 QYVFIYQALLE 287
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1252-1464 6.30e-35

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 133.68  E-value: 6.30e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1252 CLPflISVDGESSNYINAALMDSHK-QPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMDAAQLCMQYWPEKNSC 1329
Cdd:cd14547     15 CLP--SVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMItNLTEAKEKCAQYWPEEENE 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1330 CYGPIQVEFISADIDEDIINRIFRIcnmaRPQDGYRLVQHFQFIGWPAYRdTPLSKRSILQLVRRLAKWQEQyDGGDGRT 1409
Cdd:cd14547     93 TYGDFEVTVQSVKETDGYTVRKLTL----KYGGEKRYLKHYWYTSWPDHK-TPEAAQPLLSLVQEVEEARQT-EPHRGPI 166

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1949412791 1410 VVHCLTGGGRSGTFCAIcSINeMIQ--QQNIVDVFHTVKTLRNNKTNMVETMEQYKF 1464
Cdd:cd14547    167 VVHCSAGIGRTGCFIAT-SIG-CQQlrEEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1266-1467 8.98e-35

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 132.51  E-value: 8.98e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDsHKQPAA--FIVTQHPLPNTMGDFWRLVFDYNCSSIVML--NEMDAAQLCMQYWPEK--NSCCYGPIQVEFI 1339
Cdd:cd14539      1 YINASLIE-DLTPYCprFIATQAPLPGTAADFWLMVYEQQVSVIVMLvsEQENEKQKVHRYWPTErgQALVYGAITVSLQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1340 SADIDEDIINRIFRICNmaRPQDGYRLVQHFQFIGWPAYRdTPLSKRSILQLVRRLAKWQEQYDGGDGRTVVHCLTGGGR 1419
Cdd:cd14539     80 SVRTTPTHVERIISIQH--KDTRLSRSVVHLQFTTWPELG-LPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHCSSGVGR 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1949412791 1420 SGTFC-AICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1467
Cdd:cd14539    157 TGAFClLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1260-1472 9.41e-35

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 132.84  E-value: 9.41e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1260 DGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMDAAQL-CMQYWPEkNSCCYGPIQVE 1337
Cdd:cd14631      9 DDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVtNLVEVGRVkCYKYWPD-DTEVYGDFKVT 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1338 FISADIDEDIINRIFRIcnMARPQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLakwQEQYDGGDGRTVVHCLTGG 1417
Cdd:cd14631     88 CVEMEPLAEYVVRTFTL--ERRGYNEIREVKQFHFTGWPDH-GVPYHATGLLSFIRRV---KLSNPPSAGPIVVHCSAGA 161

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1949412791 1418 GRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEA 1472
Cdd:cd14631    162 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 216
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 977-1177 1.05e-34

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 132.46  E-value: 1.05e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMvtnLVEVGRVK-CVRYWPDETEV-YGDIKVTLIETE 1054
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM---LNEVDLAQgCPQYWPEEGMLrYGPIQVECMSCS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1055 PLAEYVIRTF-----TVQKKGHHEIRelrQFHFTSWPDH-GVPCYATGLLGFIRQV-KFLNPPDAGP--IAVHCSAGAGR 1125
Cdd:cd14636     78 MDCDVISRIFricnlTRPQEGYLMVQ---QFQYLGWASHrEVPGSKRSFLKLILQVeKWQEECDEGEgrTIIHCLNGGGR 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1949412791 1126 TGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14636    155 SGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1266-1472 1.13e-34

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 132.10  E-value: 1.13e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEM-DAAQL-CMQYWPEkNSCCYGPIQVEFISADI 1343
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLvEVGRVkCSKYWPD-DSDTYGDIKITLLKTET 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1344 DEDIINRIFricnmARPQDGYRL---VQHFQFIGWPAYrDTPLSKRSILQLVRRLaKWQEQYDGGDgrTVVHCLTGGGRS 1420
Cdd:cd14632     80 LAEYSVRTF-----ALERRGYSArheVKQFHFTSWPEH-GVPYHATGLLAFIRRV-KASTPPDAGP--VVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1949412791 1421 GTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEA 1472
Cdd:cd14632    151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEA 202
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1237-1472 1.77e-34

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 134.01  E-value: 1.77e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1237 NHDKNRSMDVLSADRCLPFLISVDGES-SNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMD 1314
Cdd:cd14633     40 NRMKNRYGNIIAYDHSRVRLQPIEGETsSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVtNLVE 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1315 AAQL-CMQYWPEKNSCcYGPIQVEFISADIDEDIINRIFRIcnMARPQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVR 1393
Cdd:cd14633    120 VGRVkCCKYWPDDTEI-YKDIKVTLIETELLAEYVIRTFAV--EKRGVHEIREIRQFHFTGWPDH-GVPYHATGLLGFVR 195

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949412791 1394 RLakwQEQYDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEA 1472
Cdd:cd14633    196 QV---KSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEA 271
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1231-1471 1.80e-34

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 133.80  E-value: 1.80e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1231 VGLLPRNHDKNRSMDVLSADR---CLPFLisVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSI 1307
Cdd:cd14603     24 AGGRKENVKKNRYKDILPYDQtrvILSLL--QEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVI 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1308 VMLN---EMdAAQLCMQYWP-EKNSCCYGPIQVEFISAD-IDEDIINRIFRIcnmaRPQDGYRLVQHFQFIGWPAyRDTP 1382
Cdd:cd14603    102 LMACreiEM-GKKKCERYWAqEQEPLQTGPFTITLVKEKrLNEEVILRTLKV----TFQKESRSVSHFQYMAWPD-HGIP 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1383 LSKRSILQLVRRLAKWQeqydgGDGRT--VVHCLTGGGRSGTFCAICSINEMIQQQNIVD---VFHTVKTLRNNKTNMVE 1457
Cdd:cd14603    176 DSPDCMLAMIELARRLQ-----GSGPEplCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPAAVQ 250

                          250
                   ....*....|....
gi 1949412791 1458 TMEQYKFCYEVALE 1471
Cdd:cd14603    251 TEEQYEFLYHTVAQ 264
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 977-1170 1.07e-33

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 128.98  E-value: 1.07e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCvrYWPDETEV--YGDIKVTLIETE 1054
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPleCETFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1055 -----PLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATglLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCF 1129
Cdd:cd14550     79 hsclsNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTV--FELINTVQEWAQQRDGPIVVHDRYGGVQAATF 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1949412791 1130 IAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVF 1170
Cdd:cd14550    157 CALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQF 197
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1234-1473 4.13e-33

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 130.24  E-value: 4.13e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1234 LPRNHDKNRSMDVLSADRCLPFLISVDG-ESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNE 1312
Cdd:cd14624     44 LEVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1313 MDAAQL--CMQYWPEKNSCCYGPIQVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQ 1390
Cdd:cd14624    124 LEERSRvkCDQYWPSRGTETYGLIQVTLLDTVELATYCVRTFALYKNGSSEK--REVRQFQFTAWPDH-GVPEHPTPFLA 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1391 LVRRLaKWQEQYDGGDgrTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVAL 1470
Cdd:cd14624    201 FLRRV-KTCNPPDAGP--MVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALL 277


                   ...
gi 1949412791 1471 EAL 1473
Cdd:cd14624    278 EAV 280
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1266-1466 1.42e-32

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 126.00  E-value: 1.42e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMDAAQL-CMQYWPEK--NSCCYGPIQVEFISA 1341
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMAcREFEMGKKkCERYWPEEgeEQLQFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1342 D-IDEDIINRIFRicnmARPQDGYRLVQHFQFIGWPAyRDTPLSKRSILQLVRRLAKWQEQydgGDGRTVVHCLTGGGRS 1420
Cdd:cd14542     81 KrVGPDFLIRTLK----VTFQKESRTVYQFHYTAWPD-HGVPSSVDPILDLVRLVRDYQGS---EDVPICVHCSAGCGRT 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1949412791 1421 GTFCAICSINEMIQQQNIVD---VFHTVKTLRNNKTNMVETMEQYKFCY 1466
Cdd:cd14542    153 GTICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 977-1177 1.81e-32

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 125.79  E-value: 1.81e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRV-KCVRYWPDE-TEVYGDIKVTLIETE 1054
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPgLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1055 PLAEYVIRTFTVQ-----KKGHHEIRelrQFHFTSW-PDHGVPCYATGLLGFIRQV-KFLNPPDAGPIAVHCSAGAGRTG 1127
Cdd:cd14637     81 ADEDIVTRLFRVQnitrlQEGHLMVR---HFQFLRWsAYRDTPDSKKAFLHLLASVeKWQRESGEGRTVVHCLNGGGRSG 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1128 CFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14637    158 TYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1266-1470 2.13e-32

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 125.49  E-value: 2.13e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEM-DAAQLCMQYWPEKNSccygPIQVE-FISADI 1343
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGqNMAEDEFVYWPNKDE----PINCEtFKVTLI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1344 DEDII------NRIFRICNMARPQDGYRL-VQHFQFIGWPAyRDTPLSKrsILQLVRRLakwQEQYDGGDGRTVVHCLTG 1416
Cdd:cd17669     77 AEEHKclsneeKLIIQDFILEATQDDYVLeVRHFQCPKWPN-PDSPISK--TFELISII---KEEAANRDGPMIVHDEHG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1949412791 1417 GGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVAL 1470
Cdd:cd17669    151 GVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 977-1177 3.77e-32

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 124.80  E-value: 3.77e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVtNLVEVGRVkCVRYWPDE-TEVYGDIKVTLIETEP 1055
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVML-NDVDPAQL-CPQYWPENgVHRHGPIQVEFVSADL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1056 LAEYVIRTFTVQKKGHHE--IRELRQFHFTSWPDH-GVPCYATGLLGFIRQV-KFLNPPDAGP--IAVHCSAGAGRTGCF 1129
Cdd:cd14635     79 EEDIISRIFRIYNAARPQdgYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdKWQEEYNGGEgrTVVHCLNGGGRSGTF 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1949412791 1130 IAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1177
Cdd:cd14635    159 CAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1240-1468 1.01e-31

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific 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. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 125.36  E-value: 1.01e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1240 KNRSMDVLSADRCLPFLISVDGES--SNYINAALMDSH-KQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMDA 1315
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMItNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1316 AQLCMQYWPEKNSCCYGpiqVEFISADI--DEDIINRIFRIcnmaRPQDGYRLVQHFQFIGWPAYRdTPLSKRSILQLVR 1393
Cdd:cd14613    108 NEKCTEYWPEEQVTYEG---IEITVKQVihADDYRLRLITL----KSGGEERGLKHYWYTSWPDQK-TPDNAPPLLQLVQ 179

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949412791 1394 RLAKWQEQYDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEV 1468
Cdd:cd14613    180 EVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHV 254
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1229-1471 1.30e-31

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 125.91  E-value: 1.30e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1229 CSVGLLPRNHDKNRSMDVLSADRCLpflISVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIV 1308
Cdd:cd14608     17 CRVAKLPKNKNRNRYRDVSPFDHSR---IKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1309 MLNE-MDAAQL-CMQYWP--EKNSCCY--GPIQVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAY--RD 1380
Cdd:cd14608     94 MLNRvMEKGSLkCAQYWPqkEEKEMIFedTNLKLTLISEDIKSYYTVRQLELENLTTQET--REILHFHYTTWPDFgvPE 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1381 TPLSKRSILQLVRRLAKWQEQYdggdGRTVVHCLTGGGRSGTFCAICSINEMIQQQ---NIVDVFHTVKTLRNNKTNMVE 1457
Cdd:cd14608    172 SPASFLNFLFKVRESGSLSPEH----GPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDIKKVLLEMRKFRMGLIQ 247

                          250
                   ....*....|....
gi 1949412791 1458 TMEQYKFCYEVALE 1471
Cdd:cd14608    248 TADQLRFSYLAVIE 261
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1266-1467 1.31e-31

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 123.34  E-value: 1.31e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALM--DSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQL---CMQYWP--EKNSCCYGPIQVEF 1338
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStakCADYFPaeENESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1339 ISADIDEDIINRIFRICNMARPQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAkwqeQYDGGDGRTVVHCLTGGG 1418
Cdd:cd17658     81 KKLKHSQHSITLRVLEVQYIESEEPPLSVLHIQYPEWPDH-GVPKDTRSVRELLKRLY----GIPPSAGPIVVHCSAGIG 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1949412791 1419 RSGTFCAICSINEMIQQQNI--VDVFHTVKTLRNNKTNMVETMEQYKFCYE 1467
Cdd:cd17658    156 RTGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1266-1462 2.16e-31

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 122.63  E-value: 2.16e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN---EMDAAQlCMQYWP--EKNSCCYGPIQVEFIS 1340
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTrceEGNRNK-CAQYWPsmEEGSRAFGDVVVKINE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1341 ADIDEDIINRIFRICNmARPQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQeqyDGGDGRTVVHCLTGGGRS 1420
Cdd:cd14557     80 EKICPDYIIRKLNINN-KKEKGSGREVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFN---NFFSGPIVVHCSAGVGRT 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1949412791 1421 GTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQY 1462
Cdd:cd14557    155 GTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1266-1473 6.36e-31

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 121.39  E-value: 6.36e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAA--LMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN-EMDAAQL-CMQYWPEKNSccyGPIQVEFISA 1341
Cdd:cd14596      1 YINASyiTMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTrEVERGKVkCHRYWPETLQ---EPMELENYQL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1342 DIDEDIINRIF--RICNMARPQDG-YRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQEQydggdGRTVVHCLTGGG 1418
Cdd:cd14596     78 RLENYQALQYFiiRIIKLVEKETGeNRLIKHLQFTTWPDH-GTPQSSDQLVKFICYMRKVHNT-----GPIVVHCSAGIG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1949412791 1419 RSGTFCAICSINEMIQQQ---NIVDVfhtVKTLRNNKTNMVETMEQYKFCYEVALEAL 1473
Cdd:cd14596    152 RAGVLICVDVLLSLIEKDlsfNIKDI---VREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1264-1467 8.31e-31

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ 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 (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 121.55  E-value: 8.31e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1264 SNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNE-MDAAQL-CMQYWPEKNS--CCYGPIQVEFI 1339
Cdd:cd14616     25 SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQcFEKGRIrCHQYWPEDNKpvTVFGDIVITKL 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1340 SADIDEDIINRIFRIcnmARPQDgYRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLakwQEQYDGGDGRTVVHCLTGGGR 1419
Cdd:cd14616    105 MEDVQIDWTIRDLKI---ERHGD-YMMVRQCNFTSWPEH-GVPESSAPLIHFVKLV---RASRAHDNTPMIVHCSAGVGR 176

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1949412791 1420 SGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1467
Cdd:cd14616    177 TGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1235-1470 3.20e-30

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 122.80  E-value: 3.20e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1235 PRNHDKNRSMDVLSADRCLPFLISVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN--- 1311
Cdd:PHA02747    49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTptk 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1312 EMDAAQLCMQYW--PEKNSCCYGPIQVEFISADIDEDIINRIFRICNmaRPQDGYRLVQHFQFIGWPAYrDTPLSKRSIL 1389
Cdd:PHA02747   129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD--KILKDSRKISHFQCSEWFED-ETPSDHPDFI 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1390 QLV----RRLAKWQEQYDGGDG---RTVVHCLTGGGRSGTFCAI-CSINEMIQQQNIVdVFHTVKTLRNNKTNMVETMEQ 1461
Cdd:PHA02747   206 KFIkiidINRKKSGKLFNPKDAllcPIVVHCSDGVGKTGIFCAVdICLNQLVKRKAIC-LAKTAEKIREQRHAGIMNFDD 284

                          250
                   ....*....|..
gi 1949412791 1462 YKF---CYEVAL 1470
Cdd:PHA02747   285 YLFiqpGYEVLH 296
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1224-1466 4.37e-30

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-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. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 120.33  E-value: 4.37e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1224 VRPEDCSVgllPRNHDKNRSMDVLSADR---CLPFLISVDgESSNYINAA-LMDSHKQPAAFIVTQHPLPNTMGDFWRLV 1299
Cdd:cd14612      5 VSPEELDI---PGHASKDRYKTILPNPQsrvCLRRAGSQE-EEGSYINANyIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1300 FDYNCSSIVMLNEM-DAAQLCMQYWPEKNSCcYGPIQVEF-ISADIDEDIINRIfricnMARPQDGYRLVQHFQFIGWPA 1377
Cdd:cd14612     81 WQEECPIIVMITKLkEKKEKCVHYWPEKEGT-YGRFEIRVqDMKECDGYTIRDL-----TIQLEEESRSVKHYWFSSWPD 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1378 YRdTPLSKRSILQLVRRLAKwQEQYDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVE 1457
Cdd:cd14612    155 HQ-TPESAGPLLRLVAEVEE-SRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQ 232


                   ....*....
gi 1949412791 1458 TMEQYKFCY 1466
Cdd:cd14612    233 TSEQYQFLH 241
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 977-1176 1.27e-29

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 117.79  E-value: 1.27e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVrYWP--DETEVYGDIKVTLIETE 1054
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPnkDEPINCETFKVTLIAEE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1055 PLA-----EYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATglLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCF 1129
Cdd:cd17669     80 HKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAANRDGPMIVHDEHGGVTAGTF 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1949412791 1130 IAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAIL 1176
Cdd:cd17669    158 CALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1266-1467 1.70e-29

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 117.39  E-value: 1.70e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEM--DAAQLCMQYWPEKNSCCYGPIQVEFISADI 1343
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLveKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1344 DEDIINRIFRICNM--------ARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQEQydgGDGRTVVHCLT 1415
Cdd:cd17668     81 LAYYTVRNFTLRNTkikkgsqkGRPSG--RVVTQYHYTQWPDM-GVPEYTLPVLTFVRKASYAKRH---AVGPVVVHCSA 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1949412791 1416 GGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1467
Cdd:cd17668    155 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1237-1473 5.63e-29

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 116.85  E-value: 5.63e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1237 NHDKNRSMDVLSADRCLPFLisvdGESSNYINAAL--MDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEM 1313
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPL----GDEGGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMtQEV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1314 DAAQL-CMQYWPE---KNSCCYGPIQVEFISadiDEDIINRIFRICNMARPQDG-YRLVQHFQFIGWPAYrDTPLSKRSI 1388
Cdd:cd14597     79 EGGKIkCQRYWPEilgKTTMVDNRLQLTLVR---MQQLKNFVIRVLELEDIQTReVRHITHLNFTAWPDH-DTPSQPEQL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1389 LQLV---RRLAKwqeqydggDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFC 1465
Cdd:cd14597    155 LTFIsymRHIHK--------SGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFC 226


                   ....*...
gi 1949412791 1466 YEVALEAL 1473
Cdd:cd14597    227 YQVILYVL 234
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1266-1470 6.19e-29

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 115.55  E-value: 6.19e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMDAAQLCMQYWP--EKNSCCYGpIQVEFISAD 1342
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpDNQGLAEDEFVYWPsrEESMNCEA-FTVTLISKD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1343 I-----DEDIINRIFRicnMARPQDGYRL-VQHFQFIGWPAyRDTPLSkrSILQLVRRLakwQEQYDGGDGRTVVHCLTG 1416
Cdd:cd17670     80 RlclsnEEQIIIHDFI---LEATQDDYVLeVRHFQCPKWPN-PDAPIS--STFELINVI---KEEALTRDGPTIVHDEFG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1949412791 1417 GGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVAL 1470
Cdd:cd17670    151 AVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1240-1471 6.84e-29

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 116.48  E-value: 6.84e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1240 KNRSMDVLSADRC---LPFLISvdGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN---EM 1313
Cdd:cd14602      1 KNRYKDILPYDHSrveLSLITS--DEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACmefEM 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1314 DAAQlCMQYWPE--KNSCCYGPIQVEFISADIDEDIINRIFRicnmARPQDGYRLVQHFQFIGWPAYrDTPLSKRSILQL 1391
Cdd:cd14602     79 GKKK-CERYWAEpgEMQLEFGPFSVTCEAEKRKSDYIIRTLK----VKFNSETRTIYQFHYKNWPDH-DVPSSIDPILEL 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1392 VRRLAKWQEQydgGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHT---VKTLRNNKTNMVETMEQYKFCYEV 1468
Cdd:cd14602    153 IWDVRCYQED---DSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVfslIQEMRTQRPSLVQTKEQYELVYNA 229


                   ...
gi 1949412791 1469 ALE 1471
Cdd:cd14602    230 VIE 232
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1238-1473 7.27e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 118.98  E-value: 7.27e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1238 HDKNRSMDVLSADRCLPFLISVDgESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAA- 1316
Cdd:PHA02746    73 HESLKMFDVGDSDGKKIEVTSED-NAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDd 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1317 QLCMQYW--PEKNSCCYGPIQVEFIsaDIDEDIINRIFRICNMARPQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLV-- 1392
Cdd:PHA02746   152 EKCFELWtkEEDSELAFGRFVAKIL--DIIEELSFTKTRLMITDKISDTSREIHHFWFPDWPDN-GIPTGMAEFLELInk 228

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1393 -----RRLAKWQEQYDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1467
Cdd:PHA02746   229 vneeqAELIKQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYK 308


                   ....*.
gi 1949412791 1468 VALEAL 1473
Cdd:PHA02746   309 ALKYAI 314
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1237-1466 8.53e-29

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 116.79  E-value: 8.53e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1237 NHDKNRSMDVLSADRCLPFLISVDGE--SSNYINA------ALMDSHKQPA-AFIVTQHPLPNTMGDFWRLVFDYNCSSI 1307
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNvpGSDYINAnyirneNEGPTTDENAkTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1308 VMLNEM--DAAQLCMQYWP-EKNSCCYGPIQVEFISADIDEDIINRIFRICNMARPQDGyRLVQHFQFIGWPAYrDTPLS 1384
Cdd:cd14544     81 VMTTKEveRGKNKCVRYWPdEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPI-REIWHYQYLSWPDH-GVPSD 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1385 KRSILQLVRRLAKWQEqYDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNI---VDVFHTVKTLRNNKTNMVETMEQ 1461
Cdd:cd14544    159 PGGVLNFLEDVNQRQE-SLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQ 237


                   ....*
gi 1949412791 1462 YKFCY 1466
Cdd:cd14544    238 YKFIY 242
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1221-1466 9.38e-29

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 118.11  E-value: 9.38e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1221 TPRVRPEDcsVGLLPRNHDKNRSMDVLSADRC-LPFLISVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLV 1299
Cdd:cd14604     43 TEKIYPTA--TGEKEENVKKNRYKDILPFDHSrVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMI 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1300 FDYNCSSIVMLN---EMDAAQlCMQYWPeknscCYGPIQVEF----ISADIDEDIINRIFRICNMARPQDGYRLVQhFQF 1372
Cdd:cd14604    121 WEYNVAIIVMACrefEMGRKK-CERYWP-----LYGEEPMTFgpfrISCEAEQARTDYFIRTLLLEFQNETRRLYQ-FHY 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1373 IGWPAYrDTPLSKRSILQLVRRLAKWQEQydgGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNI---VDVFHTVKTLR 1449
Cdd:cd14604    194 VNWPDH-DVPSSFDSILDMISLMRKYQEH---EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMR 269

                          250
                   ....*....|....*..
gi 1949412791 1450 NNKTNMVETMEQYKFCY 1466
Cdd:cd14604    270 TQRHSAVQTKEQYELVH 286
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1258-1466 3.42e-28

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 114.24  E-value: 3.42e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1258 SVDGESSNYINAALMDSHK-QPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEM-DAAQLCMQYWPEKNSCcYGPIQ 1335
Cdd:cd14611     22 NSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLkEKNEKCVLYWPEKRGI-YGKVE 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1336 VEFISADIDEDIINRifricNMARPQDGY-RLVQHFQFIGWPAYRdTPLSKRSILQLVRRLAKwQEQYDGGDGRTVVHCL 1414
Cdd:cd14611    101 VLVNSVKECDNYTIR-----NLTLKQGSQsRSVKHYWYTSWPDHK-TPDSAQPLLQLMLDVEE-DRLASPGRGPVVVHCS 173

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1949412791 1415 TGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCY 1466
Cdd:cd14611    174 AGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1237-1466 9.69e-28

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 113.96  E-value: 9.69e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1237 NHDKNRSMDVLSADRCLPFLISVD--GESSNYINAALM--------DSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSS 1306
Cdd:cd14605      2 NKNKNRYKNILPFDHTRVVLHDGDpnEPVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1307 IVMLN-EMDAAQ-LCMQYWPEKNSCC-YGPIQVEFISADIDEDIINRIFRICNMARpQDGYRLVQHFQFIGWPAYrDTPL 1383
Cdd:cd14605     82 IVMTTkEVERGKsKCVKYWPDEYALKeYGVMRVRNVKESAAHDYILRELKLSKVGQ-GNTERTVWQYHFRTWPDH-GVPS 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1384 SKRSILQLVRRLAKWQEQYDGGdGRTVVHCLTGGGRSGTFCAICSINEMIQQQNI---VDVFHTVKTLRNNKTNMVETME 1460
Cdd:cd14605    160 DPGGVLDFLEEVHHKQESIMDA-GPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEA 238


                   ....*.
gi 1949412791 1461 QYKFCY 1466
Cdd:cd14605    239 QYRFIY 244
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 977-1176 9.72e-28

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 112.08  E-value: 9.72e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  977 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVrYWPDETEVYG--DIKVTLIETE 1054
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFV-YWPSREESMNceAFTVTLISKD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1055 PLA-----EYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATglLGFIRQVKFLNPPDAGPIAVHCSAGAGRTGCF 1129
Cdd:cd17670     80 RLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEFGAVSAGTL 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1949412791 1130 IAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAIL 1176
Cdd:cd17670    158 CALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1232-1475 1.73e-26

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 110.35  E-value: 1.73e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1232 GLLPRNHDKNRSMDVLSADRCLPFLISVDGE-------SSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNC 1304
Cdd:cd14606     13 GQRPENKSKNRYKNILPFDHSRVILQGRDSNipgsdyiNANYVKNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENS 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1305 SSIVMLN-EMDAAQ-LCMQYWPEKNSC-CYGPIQVEFISADIDEDIINRIFRICNMARpQDGYRLVQHFQFIGWPAYrDT 1381
Cdd:cd14606     93 RVIVMTTrEVEKGRnKCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLRTLQVSPLDN-GELIREIWHYQYLSWPDH-GV 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1382 PLSKRSILQLVRRLAKWQEQYDGGdGRTVVHCLTGGGRSGTFCAICSINEMIQQQNI---VDVFHTVKTLRNNKTNMVET 1458
Cdd:cd14606    171 PSEPGGVLSFLDQINQRQESLPHA-GPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQT 249

                          250
                   ....*....|....*..
gi 1949412791 1459 MEQYKFCYEVALEALNS 1475
Cdd:cd14606    250 EAQYKFIYVAIAQFIET 266
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1266-1475 1.86e-26

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 108.57  E-value: 1.86e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAALMD----SHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEM--DAAQLCMQYWPEKN-SCCYGPIQVEF 1338
Cdd:cd14541      2 YINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLveRGRVKCHQYWPDLGeTMQFGNLQITC 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1339 ISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQEqydGGDGRTVVHCLTGGG 1418
Cdd:cd14541     82 VSEEVTPSFAFREFILTNTNTGEE--RHITQMQYLAWPDH-GVPDDSSDFLDFVKRVRQNRV---GMVEPTVVHCSAGIG 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1949412791 1419 RSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEALNS 1475
Cdd:cd14541    156 RTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVYEE 212
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1266-1473 3.00e-26

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 108.31  E-value: 3.00e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAalmdSHKQPAA------FIVTQHPLPNTMGDFWRLVFDYNCSSIVML--NEMDAAQLCMQYWPEKNSCC----YGP 1333
Cdd:cd14540      1 YINA----SHITATVggkqrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVtaEEEGGREKCFRYWPTLGGEHdaltFGE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1334 IQVEFISADIDEDIINRIFRICNMarPQDGYRLVQHFQFIGWPAYrDTPLSKRSIL------QLVRRLAKwqeQYDGGDG 1407
Cdd:cd14540     77 YKVSTKFSVSSGCYTTTGLRVKHT--LSGQSRTVWHLQYTDWPDH-GCPEDVSGFLdfleeiNSVRRHTN---QDVAGHN 150

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949412791 1408 R---TVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEAL 1473
Cdd:cd14540    151 RnppTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1367-1471 4.97e-26

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: 103.59  E-value: 4.97e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  1367 VQHFQFIGWPAyRDTPLSKRSILQLVRRLAKWQEQYDGGdGRTVVHCLTGGGRSGTFCAICSINEMI-QQQNIVDVFHTV 1445
Cdd:smart00012    2 VKHYHYTGWPD-HGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDTV 79

                            90       100
                    ....*....|....*....|....*.
gi 1949412791  1446 KTLRNNKTNMVETMEQYKFCYEVALE 1471
Cdd:smart00012   80 KELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1367-1471 4.97e-26

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 103.59  E-value: 4.97e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  1367 VQHFQFIGWPAyRDTPLSKRSILQLVRRLAKWQEQYDGGdGRTVVHCLTGGGRSGTFCAICSINEMI-QQQNIVDVFHTV 1445
Cdd:smart00404    2 VKHYHYTGWPD-HGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDTV 79

                            90       100
                    ....*....|....*....|....*.
gi 1949412791  1446 KTLRNNKTNMVETMEQYKFCYEVALE 1471
Cdd:smart00404   80 KELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1235-1466 7.26e-25

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 105.43  E-value: 7.26e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1235 PRNHDKNRSMDVLSADRCLpflISVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN--- 1311
Cdd:cd14607     22 PENRNRNRYRDVSPYDHSR---VKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNriv 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1312 EMDAAQlCMQYWP--EKNSCCYGP--IQVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAY--RDTPLSK 1385
Cdd:cd14607     99 EKDSVK-CAQYWPtdEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGET--RTISHFHYTTWPDFgvPESPASF 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1386 RSILQLVRRLAKWQEQYdggdGRTVVHCLTGGGRSGTFCAICSINEMIQQQN--IVDVFHTVKTLRNNKTNMVETMEQYK 1463
Cdd:cd14607    176 LNFLFKVRESGSLSPEH----GPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQTPDQLR 251


                   ...
gi 1949412791 1464 FCY 1466
Cdd:cd14607    252 FSY 254
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1234-1470 6.99e-24

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 103.01  E-value: 6.99e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1234 LPRNHDKNRSMDVLSADRCLPFLisvdGESSNYINAALMDShKQPAA-----FIVTQHPLPNTMGDFWRLVFDYNCSSIV 1308
Cdd:cd14600     37 LPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVNM-EIPSAnivnkYIATQGPLPHTCAQFWQVVWEQKLSLIV 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1309 MLNEMD--AAQLCMQYWPEKNSCC-YGPIQVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSK 1385
Cdd:cd14600    112 MLTTLTerGRTKCHQYWPDPPDVMeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEE--RTVTHLQYVAWPDH-GVPDDS 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1386 RSILQLVRRLAKWQEQYDggdgRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFC 1465
Cdd:cd14600    189 SDFLEFVNYVRSKRVENE----PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFV 264


                   ....*
gi 1949412791 1466 YEVAL 1470
Cdd:cd14600    265 CEAIL 269
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1226-1471 4.46e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 101.62  E-value: 4.46e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1226 PEDCSVGLLPRNHDKNRSMDVLSADRCLPFLISVDGeSSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCS 1305
Cdd:PHA02742    41 AFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVR 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1306 SIVMLNEM--DAAQLCMQYW--PEKNSCCYGPIQVEfiSADIDEdiiNRIFRICNM--ARPQDGYRL-VQHFQFIGWPaY 1378
Cdd:PHA02742   120 VIVMITKImeDGKEACYPYWmpHERGKATHGEFKIK--TKKIKS---FRNYAVTNLclTDTNTGASLdIKHFAYEDWP-H 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1379 RDTPLSKRSILQLVRRLAKWQEQYD---GGDGRT-----VVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRN 1450
Cdd:PHA02742   194 GGLPRDPNKFLDFVLAVREADLKADvdiKGENIVkeppiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRK 273

                          250       260
                   ....*....|....*....|.
gi 1949412791 1451 NKTNMVETMEQYKFCYEVALE 1471
Cdd:PHA02742   274 QRHNCLSLPQQYIFCYFIVLI 294
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1263-1471 2.02e-20

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 91.16  E-value: 2.02e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1263 SSNYINAALmDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQL--CMQYWPE-KNSCCYGPIQVEFI 1339
Cdd:cd14601      4 NANYINMEI-PSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRvkCHQYWPEpSGSSSYGGFQVTCH 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1340 SADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLakwQEQYDGGDGRTVVHCLTGGGR 1419
Cdd:cd14601     83 SEEGNPAYVFREMTLTNLEKNES--RPLTQIQYIAWPDH-GVPDDSSDFLDFVCLV---RNKRAGKDEPVVVHCSAGIGR 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1949412791 1420 SGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1471
Cdd:cd14601    157 TGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PHA02738 PHA02738
hypothetical protein; Provisional
 1236-1475 5.44e-19

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 89.98  E-value: 5.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1236 RNHDKNRSMDVLSADRCLPFLiSVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML--NEM 1313
Cdd:PHA02738    48 KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLckKKE 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1314 DAAQLCMQYWP--EKNSCCYGPIQVEFISAdidEDIINRIFRICNMARPQDGYRLVQHFQFIGWPAYrDTPLSKRSILQL 1391
Cdd:PHA02738   127 NGREKCFPYWSdvEQGSIRFGKFKITTTQV---ETHPHYVKSTLLLTDGTSATQTVTHFNFTAWPDH-DVPKNTSEFLNF 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1392 ---VRRLAK--WQEQYDGGDGRT-----VVHCLTGGGRSGTFCAI-CSINEMIQQQNiVDVFHTVKTLRNNKTNMVETME 1460
Cdd:PHA02738   203 vleVRQCQKelAQESLQIGHNRLqpppiVVHCNAGLGRTPCYCVVdISISRFDACAT-VSIPSIVSSIRNQRYYSLFIPF 281

                          250
                   ....*....|....*
gi 1949412791 1461 QYKFCYEVALEALNS 1475
Cdd:PHA02738   282 QYFFCYRAVKRYVNL 296
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1222-1473 5.60e-19

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 88.90  E-value: 5.60e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1222 PRVRPEDC-SVGLLPRNHDKNRSMDVLSADRCLPFLISVDGESSNYINAalmdSHKQPAA------FIVTQHPLPNTMGD 1294
Cdd:cd14599     22 PKKKADGVfTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINA----SHIKVTVggeewhYIATQGPLPHTCHD 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1295 FWRLVFDYNCSSIVMLN--EMDAAQLCMQYWP----EKNSCCYGPIQVefiSADIDED---IINRIFRICNMARPQDgyR 1365
Cdd:cd14599     98 FWQMVWEQGVNVIAMVTaeEEGGRSKSHRYWPklgsKHSSATYGKFKV---TTKFRTDsgcYATTGLKVKHLLSGQE--R 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1366 LVQHFQFIGWPAYrDTP------LSKRSILQLVRRLAkwQEQYDGGDGRT---VVHCLTGGGRSGTFCAICSINEMIQQQ 1436
Cdd:cd14599    173 TVWHLQYTDWPDH-GCPeevqgfLSYLEEIQSVRRHT--NSMLDSTKNCNppiVVHCSAGVGRTGVVILTELMIGCLEHN 249

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1949412791 1437 NIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEAL 1473
Cdd:cd14599    250 EKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFL 286
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1266-1473 1.18e-15

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 77.71  E-value: 1.18e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1266 YINAalmdSHKQPAA------FIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN--EMDAAQLCMQYWP----EKNSCCYGP 1333
Cdd:cd14598      1 YINA----SHIKVTVggkewdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTaeEEGGREKSFRYWPrlgsRHNTVTYGR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1334 IQvefISADIDED---IINRIFRICNMARPQDgyRLVQHFQFIGWPAY---RDTP--LSKRSILQLVRRLAKWQEQYDGG 1405
Cdd:cd14598     77 FK---ITTRFRTDsgcYATTGLKIKHLLTGQE--RTVWHLQYTDWPEHgcpEDLKgfLSYLEEIQSVRRHTNSTIDPKSP 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949412791 1406 DGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEAL 1473
Cdd:cd14598    152 NPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 901-1175 2.42e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 75.39  E-value: 2.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  901 IRVADLLQHITQmkcgqgygfkeEYEALAEGQTapwETAKKDENRNKNRYGN-IIAYPTDDHTRVRLQLLDGDphsDYIN 979
Cdd:PHA02740    18 INKPDLLSCIIK-----------EYRAIVPEHE---DEANKACAQAENKAKDeNLALHITRLLHRRIKLFNDE---KVLD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  980 ANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEvgrVKC-VRYWPDE---TEVYGDIKVTLIE--T 1053
Cdd:PHA02740    81 ARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHAD---KKCfNQFWSLKegcVITSDKFQIETLEiiI 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1054 EPLAEYVIRTFTVQKKghhEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFL--------NPPDAGPIAVHCSAGAGR 1125
Cdd:PHA02740   158 KPHFNLTLLSLTDKFG---QAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLcadlekhkADGKIAPIIIDCIDGISS 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1126 TGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAI 1175
Cdd:PHA02740   235 SAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 978-1169 7.50e-13

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: 69.74  E-value: 7.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  978 INANY--IDGYHRprhYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYW-PDETevYGDIKVTLIETE 1054
Cdd:cd14559     18 LNANRvqIGNKNV---AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFrQSGT--YGSVTVKSKKTG 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1055 PLA---EYVIRTFTVQKKGHHEIRELRQFHFTSWPDHG-VPCYATGLL-GFIRQV-----KFL--------NPPDAGPIA 1116
Cdd:cd14559     93 KDElvdGLKADMYNLKITDGNKTITIPVVHVTNWPDHTaISSEGLKELaDLVNKSaeekrNFYkskgssaiNDKNKLLPV 172

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1949412791 1117 VHCSAGAGRTGCFIAVDIMLDMAENEGVVDIfncIRELRSQR-VNMVQTEEQYV 1169
Cdd:cd14559    173 IHCRAGVGRTGQLAAAMELNKSPNNLSVEDI---VSDMRTSRnGKMVQKDEQLD 223
fn3 pfam00041
Fibronectin type III domain;
498-573 1.88e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 1.88e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949412791  498 IFMQWKAPNETNGVITLYEITYKALSSLDPSADLTTqrgrvfkLRNETHHLFVSLYPGTTYFFTLKASTNKGFGPP 573
Cdd:pfam00041   16 LTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITV-------PGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 498-580 5.00e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 54.81  E-value: 5.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  498 IFMQWKAPNETNGVITLYEITYKALSSlDPSADLTTQRGrvfklrNETHHLFVSLYPGTTYFFTLKASTNKGFGPPVTTR 577
Cdd:cd00063     17 VTLSWTPPEDDGGPITGYVVEYREKGS-GDWKEVEVTPG------SETSYTLTGLKPGTEYEFRVRAVNGGGESPPSESV 89


                   ...
gi 1949412791  578 ITT 580
Cdd:cd00063     90 TVT 92
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1267-1468 8.12e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 58.82  E-value: 8.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1267 INAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQLCMQYWPEKNSCC--YGPIQVEFIsadid 1344
Cdd:PHA02740    79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCFNQFWSLKEGCVitSDKFQIETL----- 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1345 eDIINRIFRICNMARPQDGY---RLVQHFQFIGWP---------AYRDTPLSKRSI-LQLVRRLAkwqeqyDGGDGRTVV 1411
Cdd:PHA02740   154 -EIIIKPHFNLTLLSLTDKFgqaQKISHFQYTAWPadgfshdpdAFIDFFCNIDDLcADLEKHKA------DGKIAPIII 226

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1949412791 1412 HCLTGGGRSGTFCA--ICSINemIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEV 1468
Cdd:PHA02740   227 DCIDGISSSAVFCVfdICATE--FDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHL 283
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1281-1463 1.13e-08

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: 57.41  E-value: 1.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1281 FIVTQHPLPNTMGDFWRLVFDYNCSSIVML---NEMDAAQLcmqywPE--KNSCCYGPIQV--EFISADIDEDIINriFR 1353
Cdd:cd14559     31 AIACQYPKNEQLEDHLKMLADNRTPCLVVLasnKDIQRKGL-----PPyfRQSGTYGSVTVksKKTGKDELVDGLK--AD 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1354 ICNMARPQDGYRL---VQHFQfiGWPAYrdTPLSKRSILQLVRRLAK-------------WQEQYDGGDGRTVVHCLTGG 1417
Cdd:cd14559    104 MYNLKITDGNKTItipVVHVT--NWPDH--TAISSEGLKELADLVNKsaeekrnfykskgSSAINDKNKLLPVIHCRAGV 179

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1949412791 1418 GRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKtnMVETMEQYK 1463
Cdd:cd14559    180 GRTGQLAAAMELNKSPNNLSVEDIVSDMRTSRNGK--MVQKDEQLD 223
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1085-1173 1.63e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 54.98  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1085 WPDHGVPCYATgLLGFIRQVKFLNPPDaGPIAVHCSAGAGRTGCFIAvdiMLDMAENEGVVDIFNCIRELRSQRvnmVQT 1164
Cdd:COG2453     55 IPDFGAPDDEQ-LQEAVDFIDEALREG-KKVLVHCRGGIGRTGTVAA---AYLVLLGLSAEEALARVRAARPGA---VET 126


                   ....*....
gi 1949412791 1165 EEQYVFVHD 1173
Cdd:COG2453    127 PAQRAFLER 135
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1080-1173 1.71e-08

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 56.20  E-value: 1.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1080 FHFTSWPDHGVPCYATgLLGFIRQVKFLnPPDAGPIAVHCSAGAGRTGCFIAVDIM--LDMAENEgvvdifnCIRELRSQ 1157
Cdd:cd14506     79 FYNFGWKDYGVPSLTT-ILDIVKVMAFA-LQEGGKVAVHCHAGLGRTGVLIACYLVyaLRMSADQ-------AIRLVRSK 149

                           90
                   ....*....|....*.
gi 1949412791 1158 RVNMVQTEEQYVFVHD 1173
Cdd:cd14506    150 RPNSIQTRGQVLCVRE 165
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 980-1173 2.50e-08

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: 53.51  E-value: 2.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  980 ANYIDgyhrPRHYIATQGPMqETVRDFWRMVWQENSASIVMVTNlvevgrvkcvrywpdetevygdikvtlieteplaey 1059
Cdd:cd14494      1 FNWID----PLRLIAGALPL-SPLEADSRFLKQLGVTTIVDLTL------------------------------------ 39

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1060 virtftvqkkghHEIRELRQFhftswpdhgvpcyatgllgfIRQvkFLNPPdaGPIAVHCSAGAGRTGCFIAVDIMLDMA 1139
Cdd:cd14494     40 ------------AMVDRFLEV--------------------LDQ--AEKPG--EPVLVHCKAGVGRTGTLVACYLVLLGG 83

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1949412791 1140 EnegvvDIFNCIRELRSQRVN-MVQTEEQYVFVHD 1173
Cdd:cd14494     84 M-----SAEEAVRIVRLIRPGgIPQTIEQLDFLIK 113
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 386-476 2.60e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 2.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  386 PQNVNVVDVRARQLTVQWETFGYAVTRCHSYnlTVQYQYVFNQQEFAAEELIQTSSHYTLRGLRPFVTVRLRLVLANPEG 465
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGY--VVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 1949412791  466 -SKESEEIVKQT 476
Cdd:cd00063     82 eSPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 285-356 3.89e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 43.37  E-value: 3.89e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949412791   285 PTPIAPPELLAVGATYL---WIKPNANSiiGDGPIILKEVEYRTTTGNWAETHVVDAPT-YKLWHLDPDVEYEIKV 356
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVtlsWEPPPDDG--ITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRV 74
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1043-1173 5.13e-05

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: 45.33  E-value: 5.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1043 YGDIKVTLIETEPLAEYVIRTF--TVQKKGhheireLRQFHFtSWPDHGVPcyatgllGFIRQVKFLNPP-----DAGP- 1114
Cdd:cd14505     43 GVDDVVTLCTDGELEELGVPDLleQYQQAG------ITWHHL-PIPDGGVP-------SDIAQWQELLEEllsalENGKk 108

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1949412791 1115 IAVHCSAGAGRTGcFIAVDIMLDMAENEGVVDIFNCIRELRSqrvNMVQTEEQYVFVHD 1173
Cdd:cd14505    109 VLIHCKGGLGRTG-LIAACLLLELGDTLDPEQAIAAVRALRP---GAIQTPKQENFLHQ 163
fn3 pfam00041
Fibronectin type III domain;
290-356 1.03e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 42.40  E-value: 1.03e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949412791  290 PPELL---AVGATYL---WIKPNAnsiiGDGPIILKEVEYRTTTGNWAETHVVDAPT---YKLWHLDPDVEYEIKV 356
Cdd:pfam00041    2 APSNLtvtDVTSTSLtvsWTPPPD----GNGPITGYEVEYRPKNSGEPWNEITVPGTttsVTLTGLKPGTEYEVRV 73
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1114-1171 1.04e-04

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: 43.81  E-value: 1.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1949412791 1114 PIAVHCSAGAGRTGCFIAVDIMldmaeNEGVVDIFNCIRELRSQRVNMVQTEEQYVFV 1171
Cdd:cd14504     84 AVLVHCLAGKGRTGTMLACYLV-----KTGKISAVDAINEIRRIRPGSIETSEQEKFV 136
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1389-1467 1.17e-04

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: 43.11  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1389 LQLVRRLAKWQEQYDGGDGRTVVHCLTGGGRSGTFCAIcsineMIQQQNIVDVFHTVKTLRNNKTN-MVETMEQYKFCYE 1467
Cdd:cd14494     39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVAC-----YLVLLGGMSAEEAVRIVRLIRPGgIPQTIEQLDFLIK 113
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 1113-1135 1.57e-04

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 43.98  E-value: 1.57e-04
                           10        20
                   ....*....|....*....|...
gi 1949412791 1113 GPIAVHCSAGAGRTGCFIAVDIM 1135
Cdd:cd14499    110 GAIAVHCKAGLGRTGTLIACYLM 132
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 498-571 5.31e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 40.29  E-value: 5.31e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949412791   498 IFMQWKAPNETNGV--ITLYEITYKalssldpsaDLTTQRGRVFKLRNETHHLFVSLYPGTTYFFTLKASTNKGFG 571
Cdd:smart00060   17 VTLSWEPPPDDGITgyIVGYRVEYR---------EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
 1046-1145 7.79e-04

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: 43.13  E-value: 7.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791 1046 IKVTLIETEplaEYVirtftVQKKGHHEIRELRQFHFtsWPDhgvPCYATGLLGFIRQvkflNPPDAGpIAVHCSAGAGR 1125
Cdd:cd14495    138 VKVESVRTE---EEL-----VKKKGAHYVRIAATDHV--WPD---DEEIDAFVAFYRS----LPADAW-LHFHCRAGKGR 199

                           90       100
                   ....*....|....*....|
gi 1949412791 1126 TGCFIAvdiMLDMAENEGVV 1145
Cdd:cd14495    200 TTTFMV---MYDMLKNPKDV 216
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 386-466 8.08e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 39.91  E-value: 8.08e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791   386 PQNVNVVDVRARQLTVQWETFGYAVTRchSYNLTVQYQYVFNQQEFAAEELIQTSSHYTLRGLRPFVTVRLRLVLANPEG 465
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    .
gi 1949412791   466 S 466
Cdd:smart00060   82 E 82
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 1100-1161 4.09e-03

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


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 38.78  E-value: 4.09e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949412791 1100 FIRQVKFLNppdaGPIAVHCSAGAGRTGCFIAVDIMldMAENEGVVDIFNCIRELRSQ-RVNM 1161
Cdd:pfam00782   61 FIDDARQKG----GKVLVHCQAGISRSATLIIAYLM--KTRNLSLNEAYSFVKERRPGiSPNF 117
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 192-277 6.96e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 37.17  E-value: 6.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949412791  192 LRLQNVEVNVGQNATFQCTAGGKWSQHDKLWLQQwNGKDTALMVTRVVNHRRFSATVSVGDTSQRSTSRYRCVIRSDGGS 271
Cdd:pfam00047    1 SAPPTVTVLEGDSATLTCSASTGSPGPDVTWSKE-GGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79


                   ....*.
gi 1949412791  272 GVSNYA 277
Cdd:pfam00047   80 ATLSTS 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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