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Conserved domains on  [gi|1041121613|ref|XP_017284727|]
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receptor-type tyrosine-protein phosphatase T isoform X2 [Kryptolebias marmoratus]

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 ...
 985-1221 1.09e-176

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: 526.52  E-value: 1.09e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  985 DENRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNL 1064
Cdd:cd14630      1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1065 VEVGRVKCVRYWPDETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQV 1144
Cdd:cd14630     81 VEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQV 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1041121613 1145 KFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACLC 1221
Cdd:cd14630    161 KFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEACLC 237
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1306-1511 5.07e-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: 5.07e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQLCMQYWPEKNSCCYGPIQVEFISADIDE 1385
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTSCCYGPIQVEFVSADIDE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1386 DIINRIFRICNMARPQDGYRLVQHFQFIGWPAYRDTPLSKRSILQLVRRLAKWQEQYDGGDGRTVVHCLTGGGRSGTFCA 1465
Cdd:cd14634     81 DIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1041121613 1466 ICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1511
Cdd:cd14634    161 ICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 27-188 7.87e-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: 179.85  E-value: 7.87e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613    27 FPGGCTFEESySSCGYSVSLgTNGFTWEQVNSWEK---PTMDPALPTGSFMVVNASGRASGQKAHLYMPTLKEN-DTHCV 102
Cdd:smart00137    2 SPGNCDFEEG-STCGWHQDS-NDDGHWERVSSATGipgPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613   103 DFLYSLSsrdGASPGTLNVYVKVNGGAQGNPVWNASDTVTEGWVKAELAISTfWPNSYQIIFEAVSVQGHPGFIAVDDIR 182
Cdd:smart00137   80 TFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDIL 155


                    ....*.
gi 1041121613   183 VLAHPC 188
Cdd:smart00137  156 LSNGPC 161
fn3 pfam00041
Fibronectin type III domain;
501-576 1.07e-10

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.35  E-value: 1.07e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1041121613  501 IFMQWKAPNETNGAITLYEITYKALSSLDPSADLTTqrgrvfkLKNETHHLFVGLYPGTTYFFTLKASTNKGFGPP 576
Cdd:pfam00041   16 LTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITV-------PGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 389-479 3.65e-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: 46.72  E-value: 3.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  389 PQNVNVVDVRARQLTVQWETFGYAVTRCHSYnlTVQYQYVFNQQEFAAEELIQTSSHYTLRGLRPFVTVRLRLVLANPEG 468
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGY--VVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 1041121613  469 -SKESEEIVKQT 479
Cdd:cd00063     82 eSPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 288-359 5.52e-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: 42.99  E-value: 5.52e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1041121613   288 PTPIAPPELLAVGATYL---WIKPNANSiiGDGPIILKEVEYRTTTGNWAETHVVDAPT-YKLWHLDPDVEYEIKV 359
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVtlsWEPPPDDG--ITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRV 74
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 195-280 2.69e-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: 38.33  E-value: 2.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  195 LRLQNVEVNVGQNATFQCTAGGKWSQHDKLWLQQwNGRDTALMVTRVVNHRRFSATVSVGDTSQRSTSRYRCVIRSDGGS 274
Cdd:pfam00047    1 SAPPTVTVLEGDSATLTCSASTGSPGPDVTWSKE-GGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79


                   ....*.
gi 1041121613  275 GVSNYA 280
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 ...
 985-1221 1.09e-176

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: 526.52  E-value: 1.09e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  985 DENRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNL 1064
Cdd:cd14630      1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1065 VEVGRVKCVRYWPDETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQV 1144
Cdd:cd14630     81 VEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQV 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1041121613 1145 KFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACLC 1221
Cdd:cd14630    161 KFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEACLC 237
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1306-1511 5.07e-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: 5.07e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQLCMQYWPEKNSCCYGPIQVEFISADIDE 1385
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTSCCYGPIQVEFVSADIDE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1386 DIINRIFRICNMARPQDGYRLVQHFQFIGWPAYRDTPLSKRSILQLVRRLAKWQEQYDGGDGRTVVHCLTGGGRSGTFCA 1465
Cdd:cd14634     81 DIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1041121613 1466 ICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1511
Cdd:cd14634    161 ICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
963-1217 1.07e-124

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 388.94  E-value: 1.07e-124
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613   963 GFKEEYEALAEGQTA--PWETAKKDENRNKNRYGNIIAYDHTRVRLQLLDGDPhSDYINANYIDGYHRPRHYIATQGPMQ 1040
Cdd:smart00194    1 GLEEEFEKLDRLKPDdeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  1041 ETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE---TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIREL 1117
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  1118 RQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQ 1197
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                           250       260
                    ....*....|....*....|
gi 1041121613  1198 RVNMVQTEEQYVFVHDAILE 1217
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
987-1217 1.16e-116

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 365.80  E-value: 1.16e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  987 NRNKNRYGNIIAYDHTRVRLQllDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVE 1066
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1067 VGRVKCVRYWPDETE---VYGDIKVTLIETEP-LAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIR 1142
Cdd:pfam00102   79 KGREKCAQYWPEEEGeslEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1041121613 1143 QV-KFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:pfam00102  159 KVrKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1249-1511 1.11e-84

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 277.62  E-value: 1.11e-84
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  1249 QIKDEFQTLNIVTPRvrPEDCSVGLLPRNHDKNRSMDVLSADRCLPFLISVDGESSNYINAALMDSHKQPAAFIVTQHPL 1328
Cdd:smart00194    1 GLEEEFEKLDRLKPD--DESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  1329 PNTMGDFWRLVFDYNCSSIVMLNEMDAAQL--CMQYWPEKN--SCCYGPIQVEFISADIDEDIINRIFRICNMARPQDgy 1404
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGRekCAQYWPDEEgePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-- 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  1405 RLVQHFQFIGWPaYRDTPLSKRSILQLVRRLAKWQEQYdggDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHT 1484
Cdd:smart00194  157 RTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQSTS---TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEI 232

                           250       260
                    ....*....|....*....|....*..
gi 1041121613  1485 VKTLRNNKTNMVETMEQYKFCYEVALE 1511
Cdd:smart00194  233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1277-1511 1.35e-82

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 270.65  E-value: 1.35e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1277 NHDKNRSMDVLSADRCLPFLISVDGeSSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD-- 1354
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG-PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEek 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1355 AAQLCMQYWPEKN--SCCYGPIQVEFISADIDE-DIINRIFRICNMARPQdgYRLVQHFQFIGWPAyRDTPLSKRSILQL 1431
Cdd:pfam00102   80 GREKCAQYWPEEEgeSLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGSEE--TRTVKHFHYTGWPD-HGVPESPNSLLDL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1432 VRRLAKWQEqyDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1511
Cdd:pfam00102  157 LRKVRKSSL--DGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 27-188 7.87e-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: 179.85  E-value: 7.87e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613    27 FPGGCTFEESySSCGYSVSLgTNGFTWEQVNSWEK---PTMDPALPTGSFMVVNASGRASGQKAHLYMPTLKEN-DTHCV 102
Cdd:smart00137    2 SPGNCDFEEG-STCGWHQDS-NDDGHWERVSSATGipgPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613   103 DFLYSLSsrdGASPGTLNVYVKVNGGAQGNPVWNASDTVTEGWVKAELAISTfWPNSYQIIFEAVSVQGHPGFIAVDDIR 182
Cdd:smart00137   80 TFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDIL 155


                    ....*.
gi 1041121613   183 VLAHPC 188
Cdd:smart00137  156 LSNGPC 161
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 944-1212 1.56e-51

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 184.43  E-value: 1.56e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  944 IRVADLLQHITQMKCgQGYGFKEEYEALAEGQTAPWETAKKDENRNKNRYGNIIAYDHTRVRLQLLDGDPhSDYINANYI 1023
Cdd:PHA02747     9 CRAIDFLKRRNQLNC-FGIIRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGGGST-SDYIHANWI 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1024 DGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEV-GRVKCVRYW---PDETEVYGDIKVTLIETEPLAEY 1099
Cdd:PHA02747    87 DGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGTnGEEKCYQYWclnEDGNIDMEDFRIETLKTSVRAKY 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1100 VIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFI------RQV--KFLNPPDA--GPIVVHCSAGAGRTGCF 1169
Cdd:PHA02747   167 ILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKFIkiidinRKKsgKLFNPKDAllCPIVVHCSDGVGKTGIF 246

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1041121613 1170 IAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1212
Cdd:PHA02747   247 CAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
986-1208 1.25e-49

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 177.98  E-value: 1.25e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  986 ENRNKNRYGNIIAYDHTRVRlqlldgdPHSDYINANYIDGYhRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLV 1065
Cdd:COG5599     41 NGSPLNRFRDIQPYKETALR-------ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1066 EVG--RVKCVRYWP-DETEVYGDIKVTLIETEPLAEYV-IRTFTVQKKGH-HEIRELRQFHFTSWPDHGVPCYAT--GLL 1138
Cdd:COG5599    113 EISkpKVKMPVYFRqDGEYGKYEVSSELTESIQLRDGIeARTYVLTIKGTgQKKIEIPVLHVKNWPDHGAISAEAlkNLA 192

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1041121613 1139 GFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDM--AENEGVVDIFNCIRELRSQRVN-MVQTEEQY 1208
Cdd:COG5599    193 DLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMRTSRNGgMVQTSEQL 265
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 31-188 4.17e-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: 148.68  E-value: 4.17e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613   31 CTFEESYssCGYSVSLgTNGFTWEQVNSWEKPTMDPAL-----PTGSFMVVNASGRASGQKAHLYMPTLKEN-DTHCVDF 104
Cdd:cd06263      1 CDFEDGL--CGWTQDS-TDDFDWTRVSGSTPSPGTPPDhthgtGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCLSF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  105 LYSLSsrdGASPGTLNVYVKVNGGAQGNPVWNASDTVTEGWVKAELAISTFWpNSYQIIFEAVSVQGHPGFIAVDDIRVL 184
Cdd:cd06263     78 WYHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDISLS 153


                   ....
gi 1041121613  185 AHPC 188
Cdd:cd06263    154 PGPC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 31-189 1.53e-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: 138.65  E-value: 1.53e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613   31 CTFEESySSCGYSVSLGTnGFTWEQVNSWE---KPTMDPALPT--GSFMVVNASGRASGQKAHLYMPTLKENDT-HCVDF 104
Cdd:pfam00629    1 CDFEDG-NLCGWTQDSSD-DFDWERVSGPSvktGPSSDHTQGTgsGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  105 LYSLSsrdGASPGTLNVYVKVNGGAQGNPVWNASDTVTEGWVKAELAISTFwPNSYQIIFEAVSVQGHPGFIAVDDIRVL 184
Cdd:pfam00629   79 WYHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDISLS 154


                   ....*
gi 1041121613  185 AHPCR 189
Cdd:pfam00629  155 SGPCP 159
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1275-1510 3.70e-30

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 122.42  E-value: 3.70e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1275 PRNHDKNRSMDVLSADRCLPFLISVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN--- 1351
Cdd:PHA02747    49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTptk 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1352 EMDAAQLCMQYW--PEKNSCCYGPIQVEFISADIDEDIINRIFRICNmaRPQDGYRLVQHFQFIGWPAYrDTPLSKRSIL 1429
Cdd:PHA02747   129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD--KILKDSRKISHFQCSEWFED-ETPSDHPDFI 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1430 QLV----RRLAKWQEQYDGGDG---RTVVHCLTGGGRSGTFCAI-CSINEMIQQQNIVdVFHTVKTLRNNKTNMVETMEQ 1501
Cdd:PHA02747   206 KFIkiidINRKKSGKLFNPKDAllcPIVVHCSDGVGKTGIFCAVdICLNQLVKRKAIC-LAKTAEKIREQRHAGIMNFDD 284

                          250
                   ....*....|..
gi 1041121613 1502 YKF---CYEVAL 1510
Cdd:PHA02747   285 YLFiqpGYEVLH 296
fn3 pfam00041
Fibronectin type III domain;
501-576 1.07e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.35  E-value: 1.07e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1041121613  501 IFMQWKAPNETNGAITLYEITYKALSSLDPSADLTTqrgrvfkLKNETHHLFVGLYPGTTYFFTLKASTNKGFGPP 576
Cdd:pfam00041   16 LTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITV-------PGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 501-579 2.52e-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: 55.58  E-value: 2.52e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1041121613  501 IFMQWKAPNETNGAITLYEITYKALSSlDPSADLTTQRGrvfklkNETHHLFVGLYPGTTYFFTLKASTNKGFGPPVTT 579
Cdd:cd00063     17 VTLSWTPPEDDGGPITGYVVEYREKGS-GDWKEVEVTPG------SETSYTLTGLKPGTEYEFRVRAVNGGGESPPSES 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 389-479 3.65e-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: 46.72  E-value: 3.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  389 PQNVNVVDVRARQLTVQWETFGYAVTRCHSYnlTVQYQYVFNQQEFAAEELIQTSSHYTLRGLRPFVTVRLRLVLANPEG 468
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGY--VVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 1041121613  469 -SKESEEIVKQT 479
Cdd:cd00063     82 eSPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 288-359 5.52e-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: 42.99  E-value: 5.52e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1041121613   288 PTPIAPPELLAVGATYL---WIKPNANSiiGDGPIILKEVEYRTTTGNWAETHVVDAPT-YKLWHLDPDVEYEIKV 359
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVtlsWEPPPDDG--ITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRV 74
fn3 pfam00041
Fibronectin type III domain;
293-359 1.47e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 42.02  E-value: 1.47e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1041121613  293 PPELL---AVGATYL---WIKPNAnsiiGDGPIILKEVEYRTTTGNWAETHVVDAPT---YKLWHLDPDVEYEIKV 359
Cdd:pfam00041    2 APSNLtvtDVTSTSLtvsWTPPPD----GNGPITGYEVEYRPKNSGEPWNEITVPGTttsVTLTGLKPGTEYEVRV 73
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 501-574 1.79e-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: 41.83  E-value: 1.79e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1041121613   501 IFMQWKAPNETNGaiTLYEITYKALSSldpsaDLTTQRGRVFKLKNETHHLFVGLYPGTTYFFTLKASTNKGFG 574
Cdd:smart00060   17 VTLSWEPPPDDGI--TGYIVGYRVEYR-----EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 389-469 1.07e-03

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: 39.52  E-value: 1.07e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613   389 PQNVNVVDVRARQLTVQWETFGYAVTRchSYNLTVQYQYVFNQQEFAAEELIQTSSHYTLRGLRPFVTVRLRLVLANPEG 468
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    .
gi 1041121613   469 S 469
Cdd:smart00060   82 E 82
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 195-280 2.69e-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: 38.33  E-value: 2.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  195 LRLQNVEVNVGQNATFQCTAGGKWSQHDKLWLQQwNGRDTALMVTRVVNHRRFSATVSVGDTSQRSTSRYRCVIRSDGGS 274
Cdd:pfam00047    1 SAPPTVTVLEGDSATLTCSASTGSPGPDVTWSKE-GGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79


                   ....*.
gi 1041121613  275 GVSNYA 280
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 ...
 985-1221 1.09e-176

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: 526.52  E-value: 1.09e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  985 DENRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNL 1064
Cdd:cd14630      1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1065 VEVGRVKCVRYWPDETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQV 1144
Cdd:cd14630     81 VEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQV 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1041121613 1145 KFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACLC 1221
Cdd:cd14630    161 KFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEACLC 237
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 948-1220 1.90e-168

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: 506.50  E-value: 1.90e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  948 DLLQHITQMKCGQGYGFKEEYEALAEGQTAPWETAKKDENRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGYH 1027
Cdd:cd14633      1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1028 RPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEVYGDIKVTLIETEPLAEYVIRTFTVQ 1107
Cdd:cd14633     81 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1108 KKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDI 1187
Cdd:cd14633    161 KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDI 240

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1041121613 1188 FNCIRELRSQRVNMVQTEEQYVFVHDAILEACL 1220
Cdd:cd14633    241 YNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1306-1511 5.07e-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: 5.07e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQLCMQYWPEKNSCCYGPIQVEFISADIDE 1385
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTSCCYGPIQVEFVSADIDE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1386 DIINRIFRICNMARPQDGYRLVQHFQFIGWPAYRDTPLSKRSILQLVRRLAKWQEQYDGGDGRTVVHCLTGGGRSGTFCA 1465
Cdd:cd14634     81 DIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1041121613 1466 ICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1511
Cdd:cd14634    161 ICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1017-1220 1.33e-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: 448.21  E-value: 1.33e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEVYGDIKVTLIETEPL 1096
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTLVETEPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1097 AEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAVDIML 1176
Cdd:cd14555     81 AEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVIDIML 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1041121613 1177 DMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACL 1220
Cdd:cd14555    161 DMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1003-1220 8.24e-129

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: 398.62  E-value: 8.24e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1003 RVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEV 1082
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1083 YGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAG 1162
Cdd:cd14631     81 YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAG 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1041121613 1163 AGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACL 1220
Cdd:cd14631    161 AGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 987-1221 3.72e-128

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: 397.54  E-value: 3.72e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  987 NRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVE 1066
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1067 VGRVKCVRYWP-DETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVK 1145
Cdd:cd14553     83 RSRVKCDQYWPtRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1041121613 1146 FLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACLC 1221
Cdd:cd14553    163 ACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAVTC 238
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
963-1217 1.07e-124

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 388.94  E-value: 1.07e-124
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613   963 GFKEEYEALAEGQTA--PWETAKKDENRNKNRYGNIIAYDHTRVRLQLLDGDPhSDYINANYIDGYHRPRHYIATQGPMQ 1040
Cdd:smart00194    1 GLEEEFEKLDRLKPDdeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  1041 ETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE---TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIREL 1117
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  1118 RQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQ 1197
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                           250       260
                    ....*....|....*....|
gi 1041121613  1198 RVNMVQTEEQYVFVHDAILE 1217
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1017-1221 1.97e-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: 380.55  E-value: 1.97e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEVYGDIKVTLIETEPL 1096
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTETL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1097 AEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAVDIML 1176
Cdd:cd14632     81 AEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDVML 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1041121613 1177 DMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACLC 1221
Cdd:cd14632    161 DMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1306-1507 7.47e-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: 370.58  E-value: 7.47e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD-AAQLCMQYWPEKNSCCYGPIQVEFISADID 1384
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDpKDQSCPQYWPDEGSGTYGPIQVEFVSTTID 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1385 EDIINRIFRICNMARPQDGYRLVQHFQFIGWPAYRDTPLSKRSILQLVRRLAKWQEQYdgGDGRTVVHCLTGGGRSGTFC 1464
Cdd:cd14556     81 EDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQS--GEGPIVVHCLNGVGRSGVFC 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1041121613 1465 AICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1507
Cdd:cd14556    159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
987-1217 1.16e-116

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 365.80  E-value: 1.16e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  987 NRNKNRYGNIIAYDHTRVRLQllDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVE 1066
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1067 VGRVKCVRYWPDETE---VYGDIKVTLIETEP-LAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIR 1142
Cdd:pfam00102   79 KGREKCAQYWPEEEGeslEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1041121613 1143 QV-KFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:pfam00102  159 KVrKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 947-1221 8.38e-116

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: 365.51  E-value: 8.38e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  947 ADLLQHITQMKCGQGYGFKEEYEALAEGQTAPWETAKKDENRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGY 1026
Cdd:cd14626      1 SDLADNIERLKANDGLKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1027 HRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLIETEPLAEYVIRTFT 1105
Cdd:cd14626     81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRgTETYGMIQVTLLDTVELATYSVRTFA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1106 VQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVV 1185
Cdd:cd14626    161 LYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTV 240

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1041121613 1186 DIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACLC 1221
Cdd:cd14626    241 DIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATC 276
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1306-1511 4.34e-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: 4.34e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQLCMQYWPEKNSCCYGPIQVEFISADIDE 1385
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1386 DIINRIFRICNMARPQDGYRLVQHFQFIGWPAYRDTPLSKRSILQLVRRLAKWQEQYDGGDGRTVVHCLTGGGRSGTFCA 1465
Cdd:cd14635     81 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1041121613 1466 ICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1511
Cdd:cd14635    161 ISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 941-1221 3.95e-108

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: 344.77  E-value: 3.95e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  941 QPAIRVADLLQHITQMKCGQGYGFKEEYEALAEGQTAPWETAKKDENRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYINA 1020
Cdd:cd14625      1 HPPIPISELAEHTERLKANDNLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1021 NYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLIETEPLAEY 1099
Cdd:cd14625     81 NYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRgTETYGMIQVTLLDTIELATF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1100 VIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMA 1179
Cdd:cd14625    161 CVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERI 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1041121613 1180 ENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACLC 1221
Cdd:cd14625    241 KHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 941-1223 4.08e-108

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: 344.79  E-value: 4.08e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  941 QPAIRVADLLQHITQMKCGQGYGFKEEYEALAEGQTAPWETAKKDENRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYINA 1020
Cdd:cd14624      1 HPPIPILELADHIERLKANDNLKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1021 NYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLIETEPLAEY 1099
Cdd:cd14624     81 NYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRgTETYGLIQVTLLDTVELATY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1100 VIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMA 1179
Cdd:cd14624    161 CVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERI 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1041121613 1180 ENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACLCGN 1223
Cdd:cd14624    241 KHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCGN 284
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1306-1511 2.77e-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: 336.23  E-value: 2.77e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQLCMQYWPEKNSCCYGPIQVEFISADIDE 1385
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGMLRYGPIQVECMSCSMDC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1386 DIINRIFRICNMARPQDGYRLVQHFQFIGWPAYRDTPLSKRSILQLVRRLAKWQEQYDGGDGRTVVHCLTGGGRSGTFCA 1465
Cdd:cd14636     81 DVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLNGGGRSGMFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1041121613 1466 ICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1511
Cdd:cd14636    161 ISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1017-1213 5.90e-102

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: 323.85  E-value: 5.90e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETE---VYGDIKVTLIET 1093
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGkplEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1094 EPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAVD 1173
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1041121613 1174 IMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHD 1213
Cdd:cd00047    161 ILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1017-1213 5.71e-101

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: 321.22  E-value: 5.71e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLIETEP 1095
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEgTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1096 LAEYVIRTFTVQ------KKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCF 1169
Cdd:cd14549     81 LATYTVRTFSLKnlklkkVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1041121613 1170 IAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHD 1213
Cdd:cd14549    161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 992-1212 1.33e-99

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: 318.14  E-value: 1.33e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  992 RYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVK 1071
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1072 CVRYWP-DETEV-YGDIKVTLIETEPLAEYVIRTFTVQkkGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNP 1149
Cdd:cd14548     81 CDHYWPfDQDPVyYGDITVTMLSESVLPDWTIREFKLE--RGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1041121613 1150 PDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1212
Cdd:cd14548    159 QEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1306-1511 8.21e-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: 315.31  E-value: 8.21e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD---AAQLCMQYWPEKNSCCYGPIQVEFISAD 1382
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNqsnSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1383 IDEDIINRIFRICNMARPQDGYRLVQHFQFIGWPAYRDTPLSKRSILQLVRRLAKWQEQydGGDGRTVVHCLTGGGRSGT 1462
Cdd:cd14637     81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRE--SGEGRTVVHCLNGGGRSGT 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1041121613 1463 FCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1511
Cdd:cd14637    159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 980-1220 4.50e-92

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: 299.26  E-value: 4.50e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  980 ETAKKDENRNKNRYGNIIAYDHTRVRLQLLDG--DPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSAS 1057
Cdd:cd17667     20 EHSNHPDNKHKNRYINILAYDHSRVKLRPLPGkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGI 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1058 IVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLIETEPLAEYVIRTFTVQK-----------KGHHEIRELRQFHFTSW 1125
Cdd:cd17667    100 IVMITNLVEKGRRKCDQYWPTEnSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpKGRQNERTVIQYHYTQW 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1126 PDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTE 1205
Cdd:cd17667    180 PDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 259

                          250
                   ....*....|....*
gi 1041121613 1206 EQYVFVHDAILEACL 1220
Cdd:cd17667    260 EQYIFIHDALLEAIL 274
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 963-1212 1.65e-90

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: 294.66  E-value: 1.65e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  963 GFKEEYEAL-AEGQTAPWETAKKDENRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQE 1041
Cdd:cd14543      4 GIYEEYEDIrREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1042 TVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE---TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELR 1118
Cdd:cd14543     84 TYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEegsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVT 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1119 QFHFTSWPDHGVPCYATGLLGFIRQVK--------FLNPPDAG-----PIVVHCSAGAGRTGCFIAVDIMLDMAENEGVV 1185
Cdd:cd14543    164 HFQFTSWPDFGVPSSAAALLDFLGEVRqqqalavkAMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTL 243

                          250       260
                   ....*....|....*....|....*..
gi 1041121613 1186 DIFNCIRELRSQRVNMVQTEEQYVFVH 1212
Cdd:cd14543    244 NVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 942-1226 3.22e-88

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: 289.23  E-value: 3.22e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  942 PAIRVADLLQHITQMKCGQGYGFKEEYEALAEGQ-TAPWETAKKDENRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYINA 1020
Cdd:cd14621      6 PPLPVDKLEEEINRRMADDNKLFREEFNALPACPiQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINA 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1021 NYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLIETEPLAEY 1099
Cdd:cd14621     86 SFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQgCWTYGNIRVSVEDVTVLVDY 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1100 VIRTFTVQKKG----HHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAVDIM 1175
Cdd:cd14621    166 TVRKFCIQQVGdvtnKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAM 245

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1041121613 1176 LDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEACLCGNTAI 1226
Cdd:cd14621    246 LDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 991-1217 5.27e-87

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: 283.25  E-value: 5.27e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  991 NRYGNIIAYDHTRVRLqLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRV 1070
Cdd:cd14615      1 NRYNNVLPYDISRVKL-SVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1071 KCVRYWPDE-TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGF---IRQVKF 1146
Cdd:cd14615     80 KCEEYWPSKqKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFrhlVREYMK 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1041121613 1147 LNPPDaGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:cd14615    160 QNPPN-SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1249-1511 1.11e-84

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 277.62  E-value: 1.11e-84
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  1249 QIKDEFQTLNIVTPRvrPEDCSVGLLPRNHDKNRSMDVLSADRCLPFLISVDGESSNYINAALMDSHKQPAAFIVTQHPL 1328
Cdd:smart00194    1 GLEEEFEKLDRLKPD--DESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  1329 PNTMGDFWRLVFDYNCSSIVMLNEMDAAQL--CMQYWPEKN--SCCYGPIQVEFISADIDEDIINRIFRICNMARPQDgy 1404
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGRekCAQYWPDEEgePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-- 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  1405 RLVQHFQFIGWPaYRDTPLSKRSILQLVRRLAKWQEQYdggDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHT 1484
Cdd:smart00194  157 RTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQSTS---TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEI 232

                           250       260
                    ....*....|....*....|....*..
gi 1041121613  1485 VKTLRNNKTNMVETMEQYKFCYEVALE 1511
Cdd:smart00194  233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 993-1217 5.45e-84

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: 274.51  E-value: 5.45e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  993 YGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKC 1072
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1073 VRYWPDE-TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELR---QFHFTSWPDHGVPCYATGLLGFIRQVKFLN 1148
Cdd:cd14620     81 YQYWPDQgCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAPRlvtQLHFTSWPDFGVPFTPIGMLKFLKKVKSVN 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1041121613 1149 PPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:cd14620    161 PVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 987-1215 7.76e-84

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: 275.11  E-value: 7.76e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  987 NRNKNRYGNIIAYDHTRVRLQLLDGD-PHSDYINANYI-----DGYHRP--RHYIATQGPMQETVRDFWRMVWQENSASI 1058
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIrneneGPTTDEnaKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1059 VMVTNLVEVGRVKCVRYWPDE--TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHE-IRELRQFHFTSWPDHGVPCYAT 1135
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPDEgmQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDpIREIWHYQYLSWPDHGVPSDPG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1136 GLLGFIRQV--KFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGV---VDIFNCIRELRSQRVNMVQTEEQYVF 1210
Cdd:cd14544    161 GVLNFLEDVnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKF 240


                   ....*
gi 1041121613 1211 VHDAI 1215
Cdd:cd14544    241 IYVAV 245
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1277-1511 1.35e-82

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 270.65  E-value: 1.35e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1277 NHDKNRSMDVLSADRCLPFLISVDGeSSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD-- 1354
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG-PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEek 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1355 AAQLCMQYWPEKN--SCCYGPIQVEFISADIDE-DIINRIFRICNMARPQdgYRLVQHFQFIGWPAyRDTPLSKRSILQL 1431
Cdd:pfam00102   80 GREKCAQYWPEEEgeSLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGSEE--TRTVKHFHYTGWPD-HGVPESPNSLLDL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1432 VRRLAKWQEqyDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1511
Cdd:pfam00102  157 LRKVRKSSL--DGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 991-1212 5.55e-81

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: 265.80  E-value: 5.55e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  991 NRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGY-HRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEvGR 1069
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1070 VKCVRYWPDE-TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGhhEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFL- 1147
Cdd:cd14547     80 EKCAQYWPEEeNETYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEAr 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1041121613 1148 -NPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1212
Cdd:cd14547    158 qTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 987-1216 7.90e-81

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: 265.93  E-value: 7.90e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  987 NRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVE 1066
Cdd:cd14554      6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLRE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1067 VGRVKCVRYWPDETEVygdiKVTLIETEPLAE-----YVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFI 1141
Cdd:cd14554     86 MGREKCHQYWPAERSA----RYQYFVVDPMAEynmpqYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFI 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1041121613 1142 RQVK--FLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAIL 1216
Cdd:cd14554    162 GQVHktKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 991-1212 1.53e-80

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: 264.47  E-value: 1.53e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  991 NRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRV 1070
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1071 KCVRYWPDETE--VYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEI-RELRQFHFTSWPDHGVPCYATGLLGFIRQVK-F 1146
Cdd:cd14617     81 KCDHYWPADQDslYYGDLIVQMLSESVLPEWTIREFKICSEEQLDApRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRdY 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1041121613 1147 LN-PPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1212
Cdd:cd14617    161 INrTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 991-1217 1.84e-79

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: 261.75  E-value: 1.84e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  991 NRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRV 1070
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1071 KCVRYWP-DETE-VYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVK-FL 1147
Cdd:cd14619     81 KCEHYWPlDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRqWL 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1041121613 1148 NPP-DAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:cd14619    161 DQTmSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 991-1216 2.06e-78

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: 258.72  E-value: 2.06e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  991 NRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRV 1070
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1071 KCVRYWPDETE--VYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVK--F 1146
Cdd:cd14618     81 LCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVRehV 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1147 LNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAIL 1216
Cdd:cd14618    161 QATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 986-1215 2.06e-77

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: 256.87  E-value: 2.06e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  986 ENRNKNRYGNIIAYDHTRVRLQllDGDPH---SDYINANYIDGYH-------RP-RHYIATQGPMQETVRDFWRMVWQEN 1054
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLH--DGDPNepvSDYINANIIMPEFetkcnnsKPkKSYIATQGCLQNTVNDFWRMVFQEN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1055 SASIVMVTNLVEVGRVKCVRYWPDETEV--YGDIKVTLIETEPLAEYVIRTFTVQKKGHHEI-RELRQFHFTSWPDHGVP 1131
Cdd:cd14605     79 SRVIVMTTKEVERGKSKCVKYWPDEYALkeYGVMRVRNVKESAAHDYILRELKLSKVGQGNTeRTVWQYHFRTWPDHGVP 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1132 CYATGLLGFIRQVKFLNP--PDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGV---VDIFNCIRELRSQRVNMVQTEE 1206
Cdd:cd14605    159 SDPGGVLDFLEEVHHKQEsiMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEA 238


                   ....*....
gi 1041121613 1207 QYVFVHDAI 1215
Cdd:cd14605    239 QYRFIYMAV 247
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 978-1216 2.40e-77

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: 256.35  E-value: 2.40e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  978 PWETAKKDENRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSAS 1057
Cdd:cd14614      3 PHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1058 IVMVTNLVEVGRVKCVRYWP--DETEVYGDIKVTLIETEPLAEYVIRTFTVQKKghHEIRELRQFHFTSWPDHGVPCY-- 1133
Cdd:cd14614     83 IVMLTQCNEKRRVKCDHYWPftEEPVAYGDITVEMLSEEEQPDWAIREFRVSYA--DEVQDVMHFNYTAWPDHGVPTAna 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1134 ATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHD 1213
Cdd:cd14614    161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                   ...
gi 1041121613 1214 AIL 1216
Cdd:cd14614    241 CVQ 243
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1017-1212 6.75e-77

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: 253.30  E-value: 6.75e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETE-VYGDIKVTLIETEP 1095
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCwTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1096 LAEYVIRTFTVQKK----GHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIA 1171
Cdd:cd14551     81 LVDYTTRKFCIQKVnrgiGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTFIV 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1041121613 1172 VDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1212
Cdd:cd14551    161 IDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1017-1216 1.51e-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: 249.51  E-value: 1.51e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLIETEP 1095
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADgSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1096 LAEYVIRTFTVQ--------KKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTG 1167
Cdd:cd17668     81 LAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1041121613 1168 CFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAIL 1216
Cdd:cd17668    161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1017-1213 8.95e-74

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: 244.47  E-value: 8.95e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYID-GYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETE--VYGDIKVTLIET 1093
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYegEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1094 E--PLAEYVIRTFTVQKKGhHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLN--PPDAGPIVVHCSAGAGRTGCF 1169
Cdd:cd18533     81 EenDDGGFIVREFELSKED-GKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNdsASLDPPIIVHCSAGVGRTGTF 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1041121613 1170 IAVDIMLDMAEN--------EGVVD-IFNCIRELRSQRVNMVQTEEQYVFVHD 1213
Cdd:cd18533    160 IALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 970-1217 1.78e-71

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: 240.11  E-value: 1.78e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  970 ALAEGQTAPWETAKKDENRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRM 1049
Cdd:cd14603     13 AFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRM 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1050 VWQENSASIVMVTNLVEVGRVKCVRYWP--DETEVYGDIKVTLI-ETEPLAEYVIRTFTVQKKghHEIRELRQFHFTSWP 1126
Cdd:cd14603     93 IWQYGVKVILMACREIEMGKKKCERYWAqeQEPLQTGPFTITLVkEKRLNEEVILRTLKVTFQ--KESRSVSHFQYMAWP 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1127 DHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVD---IFNCIRELRSQRVNMVQ 1203
Cdd:cd14603    171 DHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPAAVQ 250

                          250
                   ....*....|....
gi 1041121613 1204 TEEQYVFVHDAILE 1217
Cdd:cd14603    251 TEEQYEFLYHTVAQ 264
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1017-1212 1.79e-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: 237.42  E-value: 1.79e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWP---DETEVYGDIKVTLIET 1093
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmeEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1094 EPLAEYVIRTFTVQKKGHH-EIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAV 1172
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKgSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1041121613 1173 DIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1212
Cdd:cd14557    161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 983-1217 2.75e-71

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: 239.78  E-value: 2.75e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  983 KKDENRNKNRYGNIIAYDHTRVRLQLLDGD-PHSDYINANYIDGY-----HRPRHYIATQGPMQETVRDFWRMVWQENSA 1056
Cdd:cd14606     14 QRPENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNQllgpdENAKTYIASQGCLEATVNDFWQMAWQENSR 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1057 SIVMVTNLVEVGRVKCVRYWPD--ETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHE-IRELRQFHFTSWPDHGVPCY 1133
Cdd:cd14606     94 VIVMTTREVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGElIREIWHYQYLSWPDHGVPSE 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1134 ATGLLGFIRQV--KFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGV---VDIFNCIRELRSQRVNMVQTEEQY 1208
Cdd:cd14606    174 PGGVLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQY 253


                   ....*....
gi 1041121613 1209 VFVHDAILE 1217
Cdd:cd14606    254 KFIYVAIAQ 262
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 942-1217 4.40e-71

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: 240.02  E-value: 4.40e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  942 PAIRVADLLQHITQMKCGQGY-GFKEEYEALA--EGQTAPWETAKKDENRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYI 1018
Cdd:cd14628      4 PARNLYAYIQKLTQIETGENVtGMELEFKRLAssKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYI 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1019 NANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEVygdiKVTLIETEPLAE 1098
Cdd:cd14628     84 NASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA----RYQYFVVDPMAE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1099 -----YVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPP--DAGPIVVHCSAGAGRTGCFIA 1171
Cdd:cd14628    160 ynmpqYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFIT 239

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1041121613 1172 VDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:cd14628    240 LSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 990-1215 1.53e-70

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: 237.07  E-value: 1.53e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  990 KNRYGNIIAYDHTRVRLQLLD-GDPHSDYINANYIDGY-HRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEV 1067
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDqDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1068 GRvKCVRYWPDETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGhhEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFL 1147
Cdd:cd14613    108 NE-KCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVEEA 184

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1041121613 1148 N---PPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAI 1215
Cdd:cd14613    185 RqqaEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 942-1217 1.41e-69

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: 235.78  E-value: 1.41e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  942 PAIRVADLLQHITQMKCGQGY-GFKEEYEALA--EGQTAPWETAKKDENRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYI 1018
Cdd:cd14627      5 PARNLYSYIQKLAQVEVGEHVtGMELEFKRLAnsKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYI 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1019 NANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEVygdiKVTLIETEPLAE 1098
Cdd:cd14627     85 NASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSA----RYQYFVVDPMAE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1099 -----YVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPP--DAGPIVVHCSAGAGRTGCFIA 1171
Cdd:cd14627    161 ynmpqYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFIT 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1041121613 1172 VDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:cd14627    241 LSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 978-1215 3.70e-69

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: 234.83  E-value: 3.70e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  978 PWETAKKDENRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSAS 1057
Cdd:cd14604     48 PTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAI 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1058 IVMVTNLVEVGRVKCVRYWP---DETEVYGDIKVTLIETEPLAEYVIRTFTVQKKghHEIRELRQFHFTSWPDHGVPCYA 1134
Cdd:cd14604    128 IVMACREFEMGRKKCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQ--NETRRLYQFHYVNWPDHDVPSSF 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1135 TGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGV---VDIFNCIRELRSQRVNMVQTEEQYVFV 1211
Cdd:cd14604    206 DSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELV 285


                   ....
gi 1041121613 1212 HDAI 1215
Cdd:cd14604    286 HRAI 289
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1017-1218 8.28e-69

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: 230.34  E-value: 8.28e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYI------DGYHrprhYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETE----VYGDI 1086
Cdd:cd14538      1 YINASHIripvggDTYH----YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNkpliCGGRL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1087 KVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNppDAGPIVVHCSAGAGRT 1166
Cdd:cd14538     77 EVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRT 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1041121613 1167 GCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEA 1218
Cdd:cd14538    155 GVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 991-1212 3.36e-68

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: 229.02  E-value: 3.36e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  991 NRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRV 1070
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1071 KCVRYWPDETE---VYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIreLRQFHFTSWPDHGVPCYATGLLGFIRQVKFL 1147
Cdd:cd14616     81 RCHQYWPEDNKpvtVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMM--VRQCNFTSWPEHGVPESSAPLIHFVKLVRAS 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1041121613 1148 NPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1212
Cdd:cd14616    159 RAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 942-1217 4.03e-67

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: 228.84  E-value: 4.03e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  942 PAIRVADLLQHITQMKCGQGYGFKE-EYEALA--EGQTAPWETAKKDENRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYI 1018
Cdd:cd14629      5 PARNLYAHIQKLTQVPPGESVTAMElEFKLLAnsKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYI 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1019 NANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEVygdiKVTLIETEPLAE 1098
Cdd:cd14629     85 NASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA----RYQYFVVDPMAE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1099 -----YVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPP--DAGPIVVHCSAGAGRTGCFIA 1171
Cdd:cd14629    161 ynmpqYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFIT 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1041121613 1172 VDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:cd14629    241 LSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 990-1217 1.33e-66

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: 225.10  E-value: 1.33e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  990 KNRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGR 1069
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1070 VKCVRYWP---DETEVYGDIKVTLIETEPLAEYVIRTFTVQKKghHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKF 1146
Cdd:cd14602     81 KKCERYWAepgEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1041121613 1147 LNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAEnEGVV----DIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:cd14602    159 YQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1017-1213 3.05e-66

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: 222.65  E-value: 3.05e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEVYGDIKVTLIETEPL 1096
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1097 AEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVK------FLNPPDAGPIVVHCSAGAGRTGCFI 1170
Cdd:cd14558     81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKqklpykNSKHGRSVPIVVHCSDGSSRTGIFC 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1041121613 1171 AVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHD 1213
Cdd:cd14558    161 ALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1017-1215 3.49e-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: 3.49e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEV-YGDIKVTLIETEP 1095
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVsSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1096 LAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQV-KFLNPPDAGPIVVHCSAGAGRTGCFIAVDI 1174
Cdd:cd14552     81 YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHPITVHCSAGAGRTGTFCALST 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1041121613 1175 MLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAI 1215
Cdd:cd14552    161 VLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 990-1212 1.75e-65

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: 222.40  E-value: 1.75e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  990 KNRYGNIIAYDHTRVRLQLLDG-DPHSDYINANYIDGYH-RPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEv 1067
Cdd:cd14612     18 KDRYKTILPNPQSRVCLRRAGSqEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE- 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1068 GRVKCVRYWPDETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGhhEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVK-- 1145
Cdd:cd14612     97 KKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEE--ESRSVKHYWFSSWPDHQTPESAGPLLRLVAEVEes 174

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1041121613 1146 FLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1212
Cdd:cd14612    175 RQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1306-1507 2.89e-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: 219.85  E-value: 2.89e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN---EMDAAQlCMQYWPEKNS--CCYGPIQVEFIS 1380
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTnlvEKGREK-CERYWPEEGGkpLEYGDITVTLVS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1381 ADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAyRDTPLSKRSILQLVRRlakWQEQYDGGDGRTVVHCLTGGGRS 1460
Cdd:cd00047     80 EEELSDYTIRTLELSPKGCSES--REVTHLHYTGWPD-HGVPSSPEDLLALVRR---VRKEARKPNGPIVVHCSAGVGRT 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1041121613 1461 GTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1507
Cdd:cd00047    154 GTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 990-1212 4.67e-65

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: 220.17  E-value: 4.67e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  990 KNRYGNIIAYDHTRVRLQLLD-GDPHSDYINANYIDGYH-RPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEV 1067
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1068 GRvKCVRYWPDETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHeiRELRQFHFTSWPDHGVPCYATGLLGFIRQVK-- 1145
Cdd:cd14611     82 NE-KCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQS--RSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEed 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1041121613 1146 FLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1212
Cdd:cd14611    159 RLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 992-1217 6.10e-65

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: 219.92  E-value: 6.10e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  992 RYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVK 1071
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1072 CVRYWP-DETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPP 1150
Cdd:cd14623     81 CAQYWPsDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQ 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1041121613 1151 DAG-PIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:cd14623    161 SGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 986-1216 1.94e-64

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: 218.93  E-value: 1.94e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  986 ENRNKNRYGNIIAYDHTRVRLqlldGDPHsDYINANYI-----DGYHRprhYIATQGPMQETVRDFWRMVWQENSASIVM 1060
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPL----GDEG-GYINASFIkmpvgDEEFV---YIACQGPLPTTVADFWQMVWEQKSTVIAM 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1061 VTNLVEVGRVKCVRYWPDE----TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATG 1136
Cdd:cd14597     74 MTQEVEGGKIKCQRYWPEIlgktTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQ 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1137 LLGFIRQVKFLNppDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAIL 1216
Cdd:cd14597    154 LLTFISYMRHIH--KSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1017-1212 4.64e-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: 216.52  E-value: 4.64e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETE---VYGDIKVTLIET 1093
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEeqlQFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1094 EPLAE-YVIRTFTVQKKghHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAV 1172
Cdd:cd14542     81 KRVGPdFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAI 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1041121613 1173 DIMLDMAENEGVVD---IFNCIRELRSQRVNMVQTEEQYVFVH 1212
Cdd:cd14542    159 DYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1016-1218 1.17e-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: 215.66  E-value: 1.17e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1016 DYINANYIDgYHRPRH-----YIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPD--ETEVYGDIKV 1088
Cdd:cd14541      1 DYINANYVN-MEIPGSgivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlgETMQFGNLQI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1089 TLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGC 1168
Cdd:cd14541     80 TCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGV 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1169 FIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEA 1218
Cdd:cd14541    160 LITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 964-1217 4.91e-63

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: 216.85  E-value: 4.91e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  964 FKEEYEALAEGQTAPWET--AKKDENRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGyHRPRH--YIATQGPM 1039
Cdd:cd14610     19 LEKEWEALCAYQAEPNATnvAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMD-HDPRNpaYIATQGPL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1040 QETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLIETEPLAE-YVIRTFTVQKKGHHEIREL 1117
Cdd:cd14610     98 PATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEgSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQTNETRTV 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1118 RQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLD-MAENEGVVDIFNCIRELRS 1196
Cdd:cd14610    178 TQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNkMAKGAKEIDIAATLEHLRD 257

                          250       260
                   ....*....|....*....|.
gi 1041121613 1197 QRVNMVQTEEQYVFVHDAILE 1217
Cdd:cd14610    258 QRPGMVQTKEQFEFALTAVAE 278
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 990-1210 1.52e-62

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: 213.02  E-value: 1.52e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  990 KNRYGNIIAYDHTRVRLQLLDGDphSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGR 1069
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1070 VKCVRYWPDEtEVYGDI------KVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQ 1143
Cdd:cd14545     79 IKCAQYWPQG-EGNAMIfedtglKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQK 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1041121613 1144 VK---FLNpPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGV--VDIFNCIRELRSQRVNMVQTEEQYVF 1210
Cdd:cd14545    158 VResgSLS-SDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 966-1217 1.07e-61

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: 212.59  E-value: 1.07e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  966 EEYEALAEGQTAP--WETAKKDENRNKNRYGNIIAYDHTRVRLQLLDGDPHSDYINANYIDGyHRPR--HYIATQGPMQE 1041
Cdd:cd14609     19 KEWQALCAYQAEPntCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE-HDPRmpAYIATQGPLSH 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1042 TVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLIETEPLAE-YVIRTFTVQKKGHHEIRELRQ 1119
Cdd:cd14609     98 TIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEgSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQ 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1120 FHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLD-MAENEGVVDIFNCIRELRSQR 1198
Cdd:cd14609    178 FHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQR 257

                          250
                   ....*....|....*....
gi 1041121613 1199 VNMVQTEEQYVFVHDAILE 1217
Cdd:cd14609    258 PGMVRTKDQFEFALTAVAE 276
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1016-1215 2.42e-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: 202.93  E-value: 2.42e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1016 DYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETEV-YGDIKVTLIETE 1094
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVtHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1095 PLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQV-KFLNPPDAGPIVVHCSAGAGRTGCFIAVD 1173
Cdd:cd14622     81 LLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFIALS 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1041121613 1174 IMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAI 1215
Cdd:cd14622    161 NILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 973-1226 6.32e-59

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: 204.49  E-value: 6.32e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  973 EGQTAPWETAKKDENRNKNRYGNIIAYDHTRVRLQLLDgdphSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQ 1052
Cdd:cd14608     11 EASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED----NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWE 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1053 ENSASIVMVTNLVEVGRVKCVRYWPDETE---VYGD--IKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPD 1127
Cdd:cd14608     87 QKSRGVVMLNRVMEKGSLKCAQYWPQKEEkemIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPD 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1128 HGVPCYATGLLGF---IRQVKFLNpPDAGPIVVHCSAGAGRTGCFIAVD---IMLDMAENEGVVDIFNCIRELRSQRVNM 1201
Cdd:cd14608    167 FGVPESPASFLNFlfkVRESGSLS-PEHGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMGL 245

                          250       260
                   ....*....|....*....|....*..
gi 1041121613 1202 VQTEEQYVFVHDAILEAC--LCGNTAI 1226
Cdd:cd14608    246 IQTADQLRFSYLAVIEGAkfIMGDSSV 272
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 982-1216 5.97e-57

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: 198.92  E-value: 5.97e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  982 AKKDENRNKNRYGNIIAYDHTRVrlqLLDGDphSDYINANYID----GYHRPRHYIATQGPMQETVRDFWRMVWQENSAS 1057
Cdd:cd14600     35 AKLPQNMDKNRYKDVLPYDATRV---VLQGN--EDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSL 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1058 IVMVTNLVEVGRVKCVRYWPDETEV--YGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYAT 1135
Cdd:cd14600    110 IVMLTTLTERGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1136 GLLGFIRQVKFLNpPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAI 1215
Cdd:cd14600    190 DFLEFVNYVRSKR-VENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAI 268


                   .
gi 1041121613 1216 L 1216
Cdd:cd14600    269 L 269
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1017-1217 1.34e-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: 192.67  E-value: 1.34e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGY--HRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-----TEVYGDIKVT 1089
Cdd:cd14540      1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLggehdALTFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1090 LIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFL-----------NPPdaGPIVVH 1158
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVrrhtnqdvaghNRN--PPTLVH 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1041121613 1159 CSAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
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 ...
 1017-1217 1.35e-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: 192.27  E-value: 1.35e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGyHRPRH--YIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE-TEVYGDIKVTLI-E 1092
Cdd:cd14546      1 YINASTIYD-HDPRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEgSEVYHIYEVHLVsE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1093 TEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAV 1172
Cdd:cd14546     80 HIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILI 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1041121613 1173 DIMLD-MAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:cd14546    160 DMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 973-1215 6.51e-55

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: 192.49  E-value: 6.51e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  973 EGQTAPWETAKKDENRNKNRYGNIIAYDHTRVRLQLLDgdphSDYINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQ 1052
Cdd:cd14607     10 ESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTE----NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQ 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1053 ENSASIVMVTNLVEVGRVKCVRYWPDETE---VYGD--IKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPD 1127
Cdd:cd14607     86 QKTKAVVMLNRIVEKDSVKCAQYWPTDEEevlSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPD 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1128 HGVPCYATGLLGF---IRQVKFLNpPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEG--VVDIFNCIRELRSQRVNMV 1202
Cdd:cd14607    166 FGVPESPASFLNFlfkVRESGSLS-PEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLI 244

                          250
                   ....*....|...
gi 1041121613 1203 QTEEQYVFVHDAI 1215
Cdd:cd14607    245 QTPDQLRFSYMAV 257
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1017-1213 1.53e-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: 186.07  E-value: 1.53e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVtNLVEVGRVKCVRYWPDETE-VYGDIKVTLIETEp 1095
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSgTYGPIQVEFVSTT- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1096 LAEYVI-RTFTVQ--KKGHHEIRELRQFHFTSWPDHG-VPCYATGLLGFIRQV-KFLNPPDAGPIVVHCSAGAGRTGCFI 1170
Cdd:cd14556     79 IDEDVIsRIFRLQntTRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGEGPIVVHCLNGVGRSGVFC 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1041121613 1171 AVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHD 1213
Cdd:cd14556    159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1017-1218 8.73e-53

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: 184.18  E-value: 8.73e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGY--HRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPD---ETEVYGDIKVTLI 1091
Cdd:cd14596      1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPEtlqEPMELENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1092 ETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNppDAGPIVVHCSAGAGRTGCFIA 1171
Cdd:cd14596     81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGRAGVLIC 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1041121613 1172 VDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILEA 1218
Cdd:cd14596    159 VDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 27-188 7.87e-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: 179.85  E-value: 7.87e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613    27 FPGGCTFEESySSCGYSVSLgTNGFTWEQVNSWEK---PTMDPALPTGSFMVVNASGRASGQKAHLYMPTLKEN-DTHCV 102
Cdd:smart00137    2 SPGNCDFEEG-STCGWHQDS-NDDGHWERVSSATGipgPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613   103 DFLYSLSsrdGASPGTLNVYVKVNGGAQGNPVWNASDTVTEGWVKAELAISTfWPNSYQIIFEAVSVQGHPGFIAVDDIR 182
Cdd:smart00137   80 TFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDIL 155


                    ....*.
gi 1041121613   183 VLAHPC 188
Cdd:smart00137  156 LSNGPC 161
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 944-1212 1.56e-51

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 184.43  E-value: 1.56e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  944 IRVADLLQHITQMKCgQGYGFKEEYEALAEGQTAPWETAKKDENRNKNRYGNIIAYDHTRVRLQLLDGDPhSDYINANYI 1023
Cdd:PHA02747     9 CRAIDFLKRRNQLNC-FGIIRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGGGST-SDYIHANWI 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1024 DGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEV-GRVKCVRYW---PDETEVYGDIKVTLIETEPLAEY 1099
Cdd:PHA02747    87 DGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGTnGEEKCYQYWclnEDGNIDMEDFRIETLKTSVRAKY 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1100 VIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFI------RQV--KFLNPPDA--GPIVVHCSAGAGRTGCF 1169
Cdd:PHA02747   167 ILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKFIkiidinRKKsgKLFNPKDAllCPIVVHCSDGVGKTGIF 246

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1041121613 1170 IAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVH 1212
Cdd:PHA02747   247 CAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1016-1217 1.89e-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: 180.53  E-value: 1.89e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1016 DYINANYIDgYHRP-----RHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDET--EVYGDIKV 1088
Cdd:cd14601      1 DYINANYIN-MEIPsssiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSgsSSYGGFQV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1089 TLIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGC 1168
Cdd:cd14601     80 TCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGV 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1041121613 1169 FIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:cd14601    160 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1306-1508 6.27e-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: 6.27e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD--AAQLCMQYWPEKNSCCYGPIQVEFISADI 1383
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKerSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1384 DEDIINRIFRICNmARPQDGyRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQEQydGGDGRTVVHCLTGGGRSGTF 1463
Cdd:cd14552     81 YEDYTLRDFLVTK-GKGGST-RTVRQFHFHGWPEV-GIPDNGKGMIDLIAAVQKQQQQ--SGNHPITVHCSAGAGRTGTF 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1041121613 1464 CAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEV 1508
Cdd:cd14552    156 CALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKV 200
PHA02738 PHA02738
hypothetical protein; Provisional
 965-1215 1.13e-50

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 182.43  E-value: 1.13e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  965 KEEYEALAEGQTAPWETAKKdeNRNKNRYGNIIAYDHTRVRLQLLDGdpHSDYINANYIDGYHRPRHYIATQGPMQETVR 1044
Cdd:PHA02738    29 REHQKVISEKVDGTFNAEKK--NRKLNRYLDAVCFDHSRVILPAERN--RGDYINANYVDGFEYKKKFICGQAPTRQTCY 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1045 DFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDETE---VYGDIKVTLIETEPLAEYVIRTFTVqKKGHHEIRELRQFH 1121
Cdd:PHA02738   105 DFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQgsiRFGKFKITTTQVETHPHYVKSTLLL-TDGTSATQTVTHFN 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1122 FTSWPDHGVPCYATGLLGFIRQVK----------------FLNPPdagPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVV 1185
Cdd:PHA02738   184 FTAWPDHDVPKNTSEFLNFVLEVRqcqkelaqeslqighnRLQPP---PIVVHCNAGLGRTPCYCVVDISISRFDACATV 260

                          250       260       270
                   ....*....|....*....|....*....|
gi 1041121613 1186 DIFNCIRELRSQRVNMVQTEEQYVFVHDAI 1215
Cdd:PHA02738   261 SIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1274-1510 2.12e-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: 178.49  E-value: 2.12e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1274 LPRNHDKNRSMDVLSADR---CLPFLISVDGesSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML 1350
Cdd:cd14554      3 LPCNKFKNRLVNILPYEStrvCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1351 ---NEMDAAQlCMQYWPEKNSCCYGPIQVEFISADIDEDIINRIFRICNmARpQDGYRLVQHFQFIGWPAyRDTPLSKRS 1427
Cdd:cd14554     81 tklREMGREK-CHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTD-AR-DGQSRTVRQFQFTDWPE-QGVPKSGEG 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1428 ILQLVRRLAKWQEQYdGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1507
Cdd:cd14554    157 FIDFIGQVHKTKEQF-GQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235


                   ...
gi 1041121613 1508 VAL 1510
Cdd:cd14554    236 AAL 238
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
986-1208 1.25e-49

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 177.98  E-value: 1.25e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  986 ENRNKNRYGNIIAYDHTRVRlqlldgdPHSDYINANYIDGYhRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLV 1065
Cdd:COG5599     41 NGSPLNRFRDIQPYKETALR-------ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1066 EVG--RVKCVRYWP-DETEVYGDIKVTLIETEPLAEYV-IRTFTVQKKGH-HEIRELRQFHFTSWPDHGVPCYAT--GLL 1138
Cdd:COG5599    113 EISkpKVKMPVYFRqDGEYGKYEVSSELTESIQLRDGIeARTYVLTIKGTgQKKIEIPVLHVKNWPDHGAISAEAlkNLA 192

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1041121613 1139 GFIRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAVDIMLDM--AENEGVVDIFNCIRELRSQRVN-MVQTEEQY 1208
Cdd:COG5599    193 DLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMRTSRNGgMVQTSEQL 265
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1305-1508 4.51e-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: 4.51e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1305 NYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQL--CMQYWPEKNSCCYGPIQVEFISAD 1382
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQekCVQYWPSEGSVTHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1383 IDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQEQydGGDGRTVVHCLTGGGRSGT 1462
Cdd:cd14622     81 LLETISIRDFLVTYNQEKQT--RLVRQFHFHGWPEI-GIPAEGKGMIDLIAAVQKQQQQ--TGNHPIVVHCSAGAGRTGT 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1041121613 1463 FCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEV 1508
Cdd:cd14622    156 FIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRV 201
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1268-1506 1.33e-48

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: 174.47  E-value: 1.33e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1268 DCSvgLLPRNHDKNRSMDVLSADRCLPFLISVDG-ESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSS 1346
Cdd:cd14543     22 LCS--LAPANQEKNRYGDVLCLDQSRVKLPKRNGdERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1347 IVMLNE-MDAAQL-CMQYWP-EKNSCC-YGPIQVEFISADIDEDIINRIFRICNMArpQDGYRLVQHFQFIGWPAYrDTP 1422
Cdd:cd14543    100 IVMTTRvVERGRVkCGQYWPlEEGSSLrYGDLTVTNLSVENKEHYKKTTLEIHNTE--TDESRQVTHFQFTSWPDF-GVP 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1423 LSKRS---ILQLVRRLAKWQEQYDGGDGR-------TVVHCLTGGGRSGTFCA--ICsineMIQQQNI--VDVFHTVKTL 1488
Cdd:cd14543    177 SSAAAlldFLGEVRQQQALAVKAMGDRWKghppgppIVVHCSAGIGRTGTFCTldIC----LSQLEDVgtLNVMQTVRRM 252

                          250
                   ....*....|....*...
gi 1041121613 1489 RNNKTNMVETMEQYKFCY 1506
Cdd:cd14543    253 RTQRAFSIQTPDQYYFCY 270
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 964-1217 1.70e-47

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 172.49  E-value: 1.70e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  964 FKEEYEALAEGqTAPWETAKKDENRN--KNRYGNIIAYDHTRVRLQLLDGDphSDYINANYIDGYHRPRHYIATQGPMQE 1041
Cdd:PHA02742    28 LKEEHEHIMQE-IVAFSCNESLELKNmkKCRYPDAPCFDRNRVILKIEDGG--DDFINASYVDGHNAKGRFICTQAPLEE 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1042 TVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYW-PDE--TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELR 1118
Cdd:PHA02742   105 TALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmPHErgKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIK 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1119 QFHFTSWPDHGVPCYATGLLGFIRQVKFL-----------NPPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDI 1187
Cdd:PHA02742   185 HFAYEDWPHGGLPRDPNKFLDFVLAVREAdlkadvdikgeNIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPL 264

                          250       260       270
                   ....*....|....*....|....*....|
gi 1041121613 1188 FNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:PHA02742   265 LSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1017-1213 3.06e-47

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: 168.33  E-value: 3.06e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGY--HRPRhYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPDE---TEVYGDIKVTLI 1091
Cdd:cd14539      1 YINASLIEDLtpYCPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgqALVYGAITVSLQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1092 ETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQV-KFLNP--PDAGPIVVHCSAGAGRTGC 1168
Cdd:cd14539     80 SVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVhSHYLQqrSLQTPIVVHCSSGVGRTGA 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1041121613 1169 F-IAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHD 1213
Cdd:cd14539    160 FcLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1017-1210 3.20e-47

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: 168.41  E-value: 3.20e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRH--YIATQGPMQETVRDFWRMVWQENSASIVMVTNLVE-VGRVKCVRYWPDE---TEVYGDIKVTl 1090
Cdd:cd17658      1 YINASLVETPASESLpkFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCADYFPAEeneSREFGRISVT- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1091 IETEPLAEYVI--RTFTVQKKGHHE-IRELRQFHFTSWPDHGVPCYATGLLGFIRQVkFLNPPDAGPIVVHCSAGAGRTG 1167
Cdd:cd17658     80 NKKLKHSQHSItlRVLEVQYIESEEpPLSVLHIQYPEWPDHGVPKDTRSVRELLKRL-YGIPPSAGPIVVHCSAGIGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1041121613 1168 CFIAVDIMLD--MAENEGVVDIFNCIRELRSQRVNMVQTEEQYVF 1210
Cdd:cd17658    159 AYCTIHNTIRriLEGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIF 203
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 967-1217 1.30e-46

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: 169.41  E-value: 1.30e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  967 EYEALAEGQT-APWETAKKDENRNKNRYGNIIAYDHTRVRLqLLDGDPHSDYINANYIDGYHRPR--HYIATQGPMQETV 1043
Cdd:cd14599     17 EYEQIPKKKAdGVFTTATLPENAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIKVTVGGEewHYIATQGPLPHTC 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1044 RDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWPD-----ETEVYGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELR 1118
Cdd:cd14599     96 HDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVW 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1119 QFHFTSWPDHGVPCYATGLLGFIRQV--------------KFLNPPdagpIVVHCSAGAGRTGCFIAVDIMLDMAENEGV 1184
Cdd:cd14599    176 HLQYTDWPDHGCPEEVQGFLSYLEEIqsvrrhtnsmldstKNCNPP----IVVHCSAGVGRTGVVILTELMIGCLEHNEK 251

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1041121613 1185 VDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:cd14599    252 VEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1306-1507 2.91e-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: 165.26  E-value: 2.91e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEM--DAAQLCMQYWPEKNSCcYGPIQVEFISADI 1383
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELkeGDQEQCAQYWGDEKKT-YGDIEVELKDTEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1384 DEDIINRIFRICNMARPQDgyRLVQHFQFIGWpAYRDTPLSKRSILQLVRRLAKWQEQYDGGDGRT---VVHCLTGGGRS 1460
Cdd:cd14558     80 SPTYTVRVFEITHLKRKDS--RTVYQYQYHKW-KGEELPEKPKDLVDMIKSIKQKLPYKNSKHGRSvpiVVHCSDGSSRT 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1041121613 1461 GTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1507
Cdd:cd14558    157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1302-1511 3.31e-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: 166.37  E-value: 3.31e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1302 ESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD--AAQLCMQYWPEKNSCCYGPIQVEFI 1379
Cdd:cd14623     22 ENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEerGQEKCAQYWPSDGSVSYGDITIELK 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1380 SADIDEDIINRIFRICNMArpQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQEQydGGDGRTVVHCLTGGGR 1459
Cdd:cd14623    102 KEEECESYTVRDLLVTNTR--ENKSRQIRQFHFHGWPEV-GIPSDGKGMINIIAAVQKQQQQ--SGNHPITVHCSAGAGR 176

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1041121613 1460 SGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1511
Cdd:cd14623    177 TGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1277-1515 3.36e-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: 166.42  E-value: 3.36e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1277 NHDKNRSMDVLSADRCLPFLISVDG-ESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN--EM 1353
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTklEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1354 DAAQLCMQYWPEKNSCCYGPIQVEFIsadideDIIN------RIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRS 1427
Cdd:cd14553     83 RSRVKCDQYWPTRGTETYGLIQVTLL------DTVElatytvRTFALHKNGSSEK--REVRQFQFTAWPDH-GVPEHPTP 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1428 ILQLVRRLaKWQEQYDGGDgrTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1507
Cdd:cd14553    154 FLAFLRRV-KACNPPDAGP--IVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHD 230


                   ....*...
gi 1041121613 1508 VALEALNS 1515
Cdd:cd14553    231 ALLEAVTC 238
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1282-1504 8.91e-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: 164.83  E-value: 8.91e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1282 RSMDVLSADRCLPFLISVDGES-SNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMDAAQ-L 1358
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEgSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLtQCMEKGRvK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1359 CMQYWPEKN-SCCYGPIQVEFISADIDEDIINRIFRICNmarpQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLak 1437
Cdd:cd14548     81 CDHYWPFDQdPVYYGDITVTMLSESVLPDWTIREFKLER----GDEVRSVRQFHFTAWPDH-GVPEAPDSLLRFVRLV-- 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1041121613 1438 wQEQYDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKF 1504
Cdd:cd14548    154 -RDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1223-1515 7.75e-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: 164.52  E-value: 7.75e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1223 NTAIPVCEFRAVYYNISRLDPQTNSSQIKDEFQTLniVTPRVRPEDCSVGLLPRNHDKNRSMDVL---SADRCLPFLISV 1299
Cdd:cd14627      1 NTEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRL--ANSKAHTSRFISANLPCNKFKNRLVNIMpyeTTRVCLQPIRGV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1300 DGesSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD--AAQLCMQYWPEKNSCCYGPIQVE 1377
Cdd:cd14627     79 EG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLRemGREKCHQYWPAERSARYQYFVVD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1378 FISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAyRDTPLSKRSILQLVRRLAKWQEQYdGGDGRTVVHCLTGG 1457
Cdd:cd14627    157 PMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQF-GQDGPISVHCSAGV 232

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1041121613 1458 GRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEALNS 1515
Cdd:cd14627    233 GRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1224-1516 4.23e-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: 162.59  E-value: 4.23e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1224 TAIPVCEFRAVYYNISRLDPQTNSSQIKDEFQTLniVTPRVRPEDCSVGLLPRNHDKNRSMDVL---SADRCLPFLISVD 1300
Cdd:cd14628      1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRL--ASSKAHTSRFISANLPCNKFKNRLVNIMpyeSTRVCLQPIRGVE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1301 GesSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD--AAQLCMQYWPEKNSCCYGPIQVEF 1378
Cdd:cd14628     79 G--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLRemGREKCHQYWPAERSARYQYFVVDP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1379 ISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAyRDTPLSKRSILQLVRRLAKWQEQYdGGDGRTVVHCLTGGG 1458
Cdd:cd14628    157 MAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQF-GQDGPISVHCSAGVG 232

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1041121613 1459 RSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEALNSF 1516
Cdd:cd14628    233 RTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGSF 290
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1223-1516 6.93e-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: 161.82  E-value: 6.93e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1223 NTAIPVCEFRAVYYNISRLDPQTNSSQIKDEFQTLniVTPRVRPEDCSVGLLPRNHDKNRSMDVLSADRCLPFLISVDG- 1301
Cdd:cd14629      1 NTEVPARNLYAHIQKLTQVPPGESVTAMELEFKLL--ANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGv 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1302 ESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD--AAQLCMQYWPEKNSCCYGPIQVEFI 1379
Cdd:cd14629     79 EGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLRemGREKCHQYWPAERSARYQYFVVDPM 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1380 SADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAyRDTPLSKRSILQLVRRLAKWQEQYdGGDGRTVVHCLTGGGR 1459
Cdd:cd14629    159 AEYNMPQYILREFKVTDARDGQS--RTIRQFQFTDWPE-QGVPKTGEGFIDFIGQVHKTKEQF-GQDGPITVHCSAGVGR 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1041121613 1460 SGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEALNSF 1516
Cdd:cd14629    235 TGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGSF 291
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1242-1515 4.13e-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: 4.13e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1242 DPQTNSSQIKDEFQTLniVTPRVRPEDCSVGLLPRNHDKNRSMDVLSADRCLPFLISVDGES-SNYINAA-LMDSHKQPA 1319
Cdd:cd14610     11 DHLKNKNRLEKEWEAL--CAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHShSDYINASpIMDHDPRNP 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1320 AFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEM--DAAQLCMQYWPEKNSCCYGPIQVEFISADI-DEDIINRIFRICN 1396
Cdd:cd14610     89 AYIATQGPLPATVADFWQMVWESGCVVIVMLTPLaeNGVKQCYHYWPDEGSNLYHIYEVNLVSEHIwCEDFLVRSFYLKN 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1397 MARPQDgyRLVQHFQFIGWPAyRDTPLSKRSILQLVRRLAKWqeqYDGGDGRTVVHCLTGGGRSGTFCAI-CSINEMIQQ 1475
Cdd:cd14610    169 LQTNET--RTVTQFHFLSWND-QGVPASTRSLLDFRRKVNKC---YRGRSCPIIVHCSDGAGRSGTYILIdMVLNKMAKG 242

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1041121613 1476 QNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEALNS 1515
Cdd:cd14610    243 AKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNA 282
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 31-188 4.17e-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: 148.68  E-value: 4.17e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613   31 CTFEESYssCGYSVSLgTNGFTWEQVNSWEKPTMDPAL-----PTGSFMVVNASGRASGQKAHLYMPTLKEN-DTHCVDF 104
Cdd:cd06263      1 CDFEDGL--CGWTQDS-TDDFDWTRVSGSTPSPGTPPDhthgtGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCLSF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  105 LYSLSsrdGASPGTLNVYVKVNGGAQGNPVWNASDTVTEGWVKAELAISTFWpNSYQIIFEAVSVQGHPGFIAVDDIRVL 184
Cdd:cd06263     78 WYHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDISLS 153


                   ....
gi 1041121613  185 AHPC 188
Cdd:cd06263    154 PGPC 157
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1116-1217 1.28e-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: 145.19  E-value: 1.28e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  1116 ELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNP--PDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENE-GVVDIFNCIR 1192
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1041121613  1193 ELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1116-1217 1.28e-40

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 145.19  E-value: 1.28e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  1116 ELRQFHFTSWPDHGVPCYATGLLGFIRQVKFLNP--PDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENE-GVVDIFNCIR 1192
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1041121613  1193 ELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1306-1507 2.70e-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: 148.27  E-value: 2.70e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD--AAQLCMQYWPEKNSCCYGPIQVEFISADI 1383
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVerGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1384 DEDIINRIFRICNM----ARPQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQEqydGGDGRTVVHCLTGGGR 1459
Cdd:cd14549     81 LATYTVRTFSLKNLklkkVKGRSSERVVYQYHYTQWPDH-GVPDYTLPVLSFVRKSSAANP---PGAGPIVVHCSAGVGR 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1041121613 1460 SGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1507
Cdd:cd14549    157 TGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1274-1507 5.82e-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: 148.88  E-value: 5.82e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1274 LPRNHDKNRSMDVLSADRCLPFLISV-DGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNE 1352
Cdd:cd14614      9 LPVNRCKNRYTNILPYDFSRVKLVSMhEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQ 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1353 MDAAQL--CMQYWP-EKNSCCYGPIQVEFISADIDEDIINRIFRICNMARPQDgyrlVQHFQFIGWPAYR-DTPLSKRSI 1428
Cdd:cd14614     89 CNEKRRvkCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD----VMHFNYTAWPDHGvPTANAAESI 164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1041121613 1429 LQLVRRLakwQEQYDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1507
Cdd:cd14614    165 LQFVQMV---RQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1277-1512 7.81e-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: 149.42  E-value: 7.81e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1277 NHDKNRSMDVLSADRCLPFLISVDG-ESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDA 1355
Cdd:cd14626     41 NKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1356 AQL--CMQYWPEKNSCCYGPIQVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQLVR 1433
Cdd:cd14626    121 KSRvkCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEK--REVRQFQFMAWPDH-GVPEYPTPILAFLR 197

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1041121613 1434 RLaKWQEQYDGGDgrTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEA 1512
Cdd:cd14626    198 RV-KACNPPDAGP--MVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEA 273
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1017-1217 9.88e-40

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: 147.43  E-value: 9.88e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRH--YIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYWP-----DETEVYGDIKVT 1089
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1090 LIETEPLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFL----------NPPDAgPIVVHC 1159
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVrrhtnstidpKSPNP-PVLVHC 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1041121613 1160 SAGAGRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:cd14598    160 SAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 984-1215 2.15e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 149.79  E-value: 2.15e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  984 KDENRNKNRYGNIIAYDHTRV-------------------RLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVR 1044
Cdd:PHA02746    48 KKENLKKNRFHDIPCWDHSRVvinaheslkmfdvgdsdgkKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1045 DFWRMVWQENSASIVMVTNlVEVGRVKCVRYW--PDETEV-YGDIKVTLIETEPLAEYVIRTFTVQKKGHHEIRELRQFH 1121
Cdd:PHA02746   128 DFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELaFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFW 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1122 FTSWPDHGVPcyaTGLLGFIRQVKFLN-------------PPDAGPIVVHCSAGAGRTGCFIAVDIMLDMAENEGVVDIF 1188
Cdd:PHA02746   207 FPDWPDNGIP---TGMAEFLELINKVNeeqaelikqadndPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLG 283

                          250       260
                   ....*....|....*....|....*..
gi 1041121613 1189 NCIRELRSQRVNMVQTEEQYVFVHDAI 1215
Cdd:PHA02746   284 EIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1281-1510 1.00e-38

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: 144.70  E-value: 1.00e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1281 NRSMDVLSADRCLPFLISVDGES-SNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNE-MDAAQ- 1357
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPhSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVgMENGRv 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1358 LCMQYWP-EKNSCCYGPIQVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQLvRRLA 1436
Cdd:cd14618     81 LCDHYWPsESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKE--RRVKHLHYTAWPDH-GIPESTSSLMAF-RELV 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1041121613 1437 KWQEQYDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVAL 1510
Cdd:cd14618    157 REHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1306-1507 2.22e-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: 143.16  E-value: 2.22e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAalmdSHKQPAA-----FIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN-EMDAAQL-CMQYWPEK-NSCCYGPIQVE 1377
Cdd:cd18533      1 YINA----SYITLPGtsskrYIATQGPLPATIGDFWKMIWQNNVGVIVMLTpLVENGREkCDQYWPSGeYEGEYGDLTVE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1378 FIS--ADIDEDIINRIFRicnMARPQDGYRLVQHFQFIGWPAYRdTPLSKRSILQLVrRLAKWQEQYDGGDGRTVVHCLT 1455
Cdd:cd18533     77 LVSeeENDDGGFIVREFE---LSKEDGKVKKVYHIQYKSWPDFG-VPDSPEDLLTLI-KLKRELNDSASLDPPIIVHCSA 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1041121613 1456 GGGRSGTFCAICSINEMIQQQNIVD---------VFHTVKTLRNNKTNMVETMEQYKFCYE 1507
Cdd:cd18533    152 GVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1281-1513 3.11e-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: 143.49  E-value: 3.11e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1281 NRSMDVLSADRC-LPFLISVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMDAAQL 1358
Cdd:cd14619      1 NRFRNVLPYDWSrVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLtNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1359 -CMQYWP-EKNSCCYGPIQVEFISADIDEDIINRIFRICNMArpQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLA 1436
Cdd:cd14619     81 kCEHYWPlDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVE--EQKTLSVRHFHFTAWPDH-GVPSSTDTLLAFRRLLR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1041121613 1437 KWQEQYDGGdGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEAL 1513
Cdd:cd14619    158 QWLDQTMSG-GPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1281-1511 3.19e-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: 143.42  E-value: 3.19e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1281 NRSMDVLSADRCLPFLISVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML---NEMDAAQ 1357
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLtkcVEQGRTK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1358 lCMQYWPEKNSCCYGPIQVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAK 1437
Cdd:cd14615     81 -CEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNES--RTVRHFHFTSWPDH-GVPETTDLLINFRHLVRE 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1041121613 1438 WQEQYDgGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1511
Cdd:cd14615    157 YMKQNP-PNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1306-1507 3.89e-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: 142.07  E-value: 3.89e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQLCMQYWPEK-NSCCYGPIQVEFISADI- 1383
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPIYWPTKeKPLECETFKVTLSGEDHs 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1384 ----DEDIINRIFRICNMarpQDGYRL-VQHFQFIGWPAyRDTPLSkrSILQLVRRLAKWQEQYDGGdgrTVVHCLTGGG 1458
Cdd:cd14550     81 clsnEIRLIVRDFILEST---QDDYVLeVRQFQCPSWPN-PCSPIH--TVFELINTVQEWAQQRDGP---IVVHDRYGGV 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1041121613 1459 RSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1507
Cdd:cd14550    152 QAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1242-1515 1.12e-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: 1.12e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1242 DPQTNSSQIKDEFQTLniVTPRVRPEDCSVGLLPRNHDKNRSMDVLSADRC-LPFLISVDGESSNYINAA-LMDSHKQPA 1319
Cdd:cd14609      9 DHLRNRDRLAKEWQAL--CAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHArIKLKAESNPSRSDYINASpIIEHDPRMP 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1320 AFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEM--DAAQLCMQYWPEKNSCCYGPIQVEFISADI-DEDIINRIFRICN 1396
Cdd:cd14609     87 AYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLveDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIwCEDFLVRSFYLKN 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1397 MaRPQDGYRLVQhFQFIGWPAyRDTPLSKRSILQLVRRLAKwqeQYDGGDGRTVVHCLTGGGRSGTFCAI-CSINEMIQQ 1475
Cdd:cd14609    167 V-QTQETRTLTQ-FHFLSWPA-EGIPSSTRPLLDFRRKVNK---CYRGRSCPIIVHCSDGAGRTGTYILIdMVLNRMAKG 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1041121613 1476 QNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEALNS 1515
Cdd:cd14609    241 VKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNA 280
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 31-189 1.53e-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: 138.65  E-value: 1.53e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613   31 CTFEESySSCGYSVSLGTnGFTWEQVNSWE---KPTMDPALPT--GSFMVVNASGRASGQKAHLYMPTLKENDT-HCVDF 104
Cdd:pfam00629    1 CDFEDG-NLCGWTQDSSD-DFDWERVSGPSvktGPSSDHTQGTgsGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  105 LYSLSsrdGASPGTLNVYVKVNGGAQGNPVWNASDTVTEGWVKAELAISTFwPNSYQIIFEAVSVQGHPGFIAVDDIRVL 184
Cdd:pfam00629   79 WYHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDISLS 154


                   ....*
gi 1041121613  185 AHPCR 189
Cdd:pfam00629  155 SGPCP 159
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1277-1512 3.16e-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: 140.55  E-value: 3.16e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1277 NHDKNRSMDVLSADRCLPFLISVDGES-SNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMD 1354
Cdd:cd14630      3 NRNKNRYGNIISYDHSRVRLQLLDGDPhSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVtNLVE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1355 AAQL-CMQYWPEKNSCcYGPIQVEFISADIDEDIINRIFRIcnMARPQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVR 1433
Cdd:cd14630     83 VGRVkCVRYWPDDTEV-YGDIKVTLIETEPLAEYVIRTFTV--QKKGYHEIREIRQFHFTSWPDH-GVPCYATGLLGFVR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1041121613 1434 RLaKWQEQYDGGDgrTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEA 1512
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 ...
 1285-1511 3.40e-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: 3.40e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1285 DVLSADRCLPFLISVDG-ESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD--AAQLCMQ 1361
Cdd:cd14620      3 NILPYDHSRVILSQLDGiPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKerKEEKCYQ 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1362 YWPEKNSCCYGPIQVEFISADIDEDIINRIFriCNMARPQDGY---RLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKW 1438
Cdd:cd14620     83 YWPDQGCWTYGNIRVAVEDCVVLVDYTIRKF--CIQPQLPDGCkapRLVTQLHFTSWPDF-GVPFTPIGMLKFLKKVKSV 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1041121613 1439 QEQYDGgdgRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1511
Cdd:cd14620    160 NPVHAG---PIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1306-1513 4.28e-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: 139.05  E-value: 4.28e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAalmdSH------KQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN-EMDAAQL-CMQYWPE---KNSCCYGPI 1374
Cdd:cd14538      1 YINA----SHiripvgGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTqDVEGGKVkCHRYWPDslnKPLICGGRL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1375 QVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQEqydggDGRTVVHCL 1454
Cdd:cd14538     77 EVSLEKYQSLQDFVIRRISLRDKETGEV--HHITHLNFTTWPDH-GTPQSADPLLRFIRYMRRIHN-----SGPIVVHCS 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1041121613 1455 TGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEAL 1513
Cdd:cd14538    149 AGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1306-1512 5.51e-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: 138.90  E-value: 5.51e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMDAAQL-CMQYWPEkNSCCYGPIQVEFISADI 1383
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVtNLVEVGRVkCSRYWPD-DTEVYGDIKVTLVETEP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1384 DEDIINRIFricnmARPQDGY---RLVQHFQFIGWPAYrDTPLSKRSILQLVRRLaKWQEQYDGGDgrTVVHCLTGGGRS 1460
Cdd:cd14555     80 LAEYVVRTF-----ALERRGYheiREVRQFHFTGWPDH-GVPYHATGLLGFIRRV-KASNPPSAGP--IVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1041121613 1461 GTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEA 1512
Cdd:cd14555    151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEA 202
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1281-1507 4.07e-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: 4.07e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1281 NRSMDVLSADRCLPFLISVDGES-SNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNE-MDAAQL 1358
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQcVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1359 -CMQYWP-EKNSCCYGPIQVEFISADIDEDIINRIFRICNMARpQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLA 1436
Cdd:cd14617     81 kCDHYWPaDQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQ-LDAPRLVRHFHYTVWPDH-GVPETTQSLIQFVRTVR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1041121613 1437 KWQEQYDGGdGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1507
Cdd:cd14617    159 DYINRTPGS-GPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1274-1513 4.10e-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: 4.10e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1274 LPRNHDKNRSMDVLSADRCLPFLISVDG-ESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNE 1352
Cdd:cd14625     44 LEVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1353 MDAAQL--CMQYWPEKNSCCYGPIQVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQ 1430
Cdd:cd14625    124 LEEKSRikCDQYWPSRGTETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEK--REVRQFQFTAWPDH-GVPEYPTPFLA 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1431 LVRRLaKWQEQYDGGDgrTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVAL 1510
Cdd:cd14625    201 FLRRV-KTCNPPDAGP--IVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALL 277


                   ...
gi 1041121613 1511 EAL 1513
Cdd:cd14625    278 EAV 280
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1279-1506 6.74e-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: 6.74e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1279 DKNRSMDVLSADRCLpflISVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNE-MDAAQ 1357
Cdd:cd14545      2 NRYRDRDPYDHDRSR---VKLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKlMEKGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1358 L-CMQYWP----EKNSCCYGPIQVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYR--DTPLSKRSILQ 1430
Cdd:cd14545     79 IkCAQYWPqgegNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQET--REVLHFHYTTWPDFGvpESPAAFLNFLQ 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1041121613 1431 LVRRLAkwqeQYDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNI--VDVFHTVKTLRNNKTNMVETMEQYKFCY 1506
Cdd:cd14545    157 KVRESG----SLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1017-1217 7.27e-36

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: 135.53  E-value: 7.27e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVtNLVEVGRVkCVRYWPDETE-VYGDIKVTLIETEP 1095
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDAAQL-CMQYWPEKTScCYGPIQVEFVSADI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1096 LAEYVIRTFTV--QKKGHHEIRELRQFHFTSWPDH-GVPCYATGLLGFIRQV-KFLNPPDA--GPIVVHCSAGAGRTGCF 1169
Cdd:cd14634     79 DEDIISRIFRIcnMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLeKWQEQYDGreGRTVVHCLNGGGRSGTF 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1041121613 1170 IAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:cd14634    159 CAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1306-1514 8.04e-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: 135.65  E-value: 8.04e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAA-LMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML---NEMDAAQlCMQYWPEKNSCCYGPIQVEFISA 1381
Cdd:cd14546      1 YINAStIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLtrlQENGVKQ-CARYWPEEGSEVYHIYEVHLVSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1382 DI-DEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAyRDTPLSKRSILQLVRRLAKwqeQYDGGDGRTVVHCLTGGGRS 1460
Cdd:cd14546     80 HIwCDDYLVRSFYLKNLQTSET--RTVTQFHFLSWPD-EGIPASAKPLLEFRRKVNK---SYRGRSCPIVVHCSDGAGRT 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1041121613 1461 GTFCAI-CSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEALN 1514
Cdd:cd14546    154 GTYILIdMVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEVN 208
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1275-1513 3.05e-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: 3.05e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1275 PRNHDKNRSMDVLSADRC---LPFLISVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN 1351
Cdd:cd17667     25 PDNKHKNRYINILAYDHSrvkLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1352 EM--DAAQLCMQYWPEKNSCCYGPIQVEFISADIDEDIINRIFRICN--MARPQDG-------YRLVQHFQFIGWPAYrD 1420
Cdd:cd17667    105 NLveKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkVKKGQKGnpkgrqnERTVIQYHYTQWPDM-G 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1421 TPLSKRSILQLVRRLAKWQEQYdggDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETME 1500
Cdd:cd17667    184 VPEYALPVLTFVRRSSAARTPE---MGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEE 260

                          250
                   ....*....|...
gi 1041121613 1501 QYKFCYEVALEAL 1513
Cdd:cd17667    261 QYIFIHDALLEAI 273
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1017-1217 3.39e-35

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: 133.61  E-value: 3.39e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMvtnLVEVGRVK-CVRYWPDETEV-YGDIKVTLIETE 1094
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM---LNEVDLAQgCPQYWPEEGMLrYGPIQVECMSCS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1095 PLAEYVIRTF-----TVQKKGHHEIRelrQFHFTSWPDH-GVPCYATGLLGFIRQV-KFLNPPDAGP--IVVHCSAGAGR 1165
Cdd:cd14636     78 MDCDVISRIFricnlTRPQEGYLMVQ---QFQYLGWASHrEVPGSKRSFLKLILQVeKWQEECDEGEgrTIIHCLNGGGR 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1041121613 1166 TGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:cd14636    155 SGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1306-1507 4.54e-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: 4.54e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMD--AAQLCMQYWPEKNSCCYGPIQV--EFISA 1381
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKerKEKKCSQYWPDQGCWTYGNLRVrvEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1382 DIDEDI----INRIFRICNMARPqdgyRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQEQYDGGdgrTVVHCLTGG 1457
Cdd:cd14551     81 LVDYTTrkfcIQKVNRGIGEKRV----RLVTQFHFTSWPDF-GVPFTPIGMLKFLKKVKSANPPRAGP---IVVHCSAGV 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1458 GRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1507
Cdd:cd14551    153 GRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1269-1511 4.74e-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: 4.74e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1269 CSVGLLPRNHDKNRSMDVLSADRCLPFLISVDG-ESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSI 1347
Cdd:cd14621     44 CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATI 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1348 VMLNEMDAAQ--LCMQYWPEKNSCCYGPIQVEFISADIDEDIINRIFRICNMA-----RPQdgyRLVQHFQFIGWPAYrD 1420
Cdd:cd14621    124 VMVTNLKERKecKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVGdvtnkKPQ---RLITQFHFTSWPDF-G 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1421 TPLSKRSILQLVRRLAKWQEQYDGGdgrTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETME 1500
Cdd:cd14621    200 VPFTPIGMLKFLKKVKNCNPQYAGA---IVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDM 276

                          250
                   ....*....|.
gi 1041121613 1501 QYKFCYEVALE 1511
Cdd:cd14621    277 QYVFIYQALLE 287
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1292-1504 7.94e-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: 133.29  E-value: 7.94e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1292 CLPflISVDGESSNYINAALMDSHK-QPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMDAAQLCMQYWPEKNSC 1369
Cdd:cd14547     15 CLP--SVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMItNLTEAKEKCAQYWPEEENE 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1370 CYGPIQVEFISADIDEDIINRIFRIcnmaRPQDGYRLVQHFQFIGWPAYRdTPLSKRSILQLVRRLAKWQEQyDGGDGRT 1449
Cdd:cd14547     93 TYGDFEVTVQSVKETDGYTVRKLTL----KYGGEKRYLKHYWYTSWPDHK-TPEAAQPLLSLVQEVEEARQT-EPHRGPI 166

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1041121613 1450 VVHCLTGGGRSGTFCAIcSINeMIQ--QQNIVDVFHTVKTLRNNKTNMVETMEQYKF 1504
Cdd:cd14547    167 VVHCSAGIGRTGCFIAT-SIG-CQQlrEEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1306-1512 1.17e-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: 1.17e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEM-DAAQL-CMQYWPEkNSCCYGPIQVEFISADI 1383
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLvEVGRVkCSKYWPD-DSDTYGDIKITLLKTET 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1384 DEDIINRIFricnmARPQDGYRL---VQHFQFIGWPAYrDTPLSKRSILQLVRRLaKWQEQYDGGDgrTVVHCLTGGGRS 1460
Cdd:cd14632     80 LAEYSVRTF-----ALERRGYSArheVKQFHFTSWPEH-GVPYHATGLLAFIRRV-KASTPPDAGP--VVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1041121613 1461 GTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEA 1512
Cdd:cd14632    151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEA 202
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1300-1512 1.29e-34

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: 132.45  E-value: 1.29e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1300 DGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMDAAQL-CMQYWPEkNSCCYGPIQVE 1377
Cdd:cd14631      9 DDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVtNLVEVGRVkCYKYWPD-DTEVYGDFKVT 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1378 FISADIDEDIINRIFRIcnMARPQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLakwQEQYDGGDGRTVVHCLTGG 1457
Cdd:cd14631     88 CVEMEPLAEYVVRTFTL--ERRGYNEIREVKQFHFTGWPDH-GVPYHATGLLSFIRRV---KLSNPPSAGPIVVHCSAGA 161

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1041121613 1458 GRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEA 1512
Cdd:cd14631    162 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 216
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1306-1507 1.60e-34

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: 131.74  E-value: 1.60e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDsHKQPAA--FIVTQHPLPNTMGDFWRLVFDYNCSSIVML--NEMDAAQLCMQYWPEK--NSCCYGPIQVEFI 1379
Cdd:cd14539      1 YINASLIE-DLTPYCprFIATQAPLPGTAADFWLMVYEQQVSVIVMLvsEQENEKQKVHRYWPTErgQALVYGAITVSLQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1380 SADIDEDIINRIFRICNmaRPQDGYRLVQHFQFIGWPAYRdTPLSKRSILQLVRRLAKWQEQYDGGDGRTVVHCLTGGGR 1459
Cdd:cd14539     80 SVRTTPTHVERIISIQH--KDTRLSRSVVHLQFTTWPELG-LPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHCSSGVGR 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1041121613 1460 SGTFC-AICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1507
Cdd:cd14539    157 TGAFClLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1017-1210 1.86e-34

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: 131.29  E-value: 1.86e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCvrYWPDETEV--YGDIKVTLIETE 1094
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPleCETFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1095 -----PLAEYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATglLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCF 1169
Cdd:cd14550     79 hsclsNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTV--FELINTVQEWAQQRDGPIVVHDRYGGVQAATF 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1041121613 1170 IAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVF 1210
Cdd:cd14550    157 CALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQF 197
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1271-1511 2.34e-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: 133.41  E-value: 2.34e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1271 VGLLPRNHDKNRSMDVLSADR---CLPFLisVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSI 1347
Cdd:cd14603     24 AGGRKENVKKNRYKDILPYDQtrvILSLL--QEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVI 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1348 VMLN---EMdAAQLCMQYWP-EKNSCCYGPIQVEFISAD-IDEDIINRIFRIcnmaRPQDGYRLVQHFQFIGWPAyRDTP 1422
Cdd:cd14603    102 LMACreiEM-GKKKCERYWAqEQEPLQTGPFTITLVKEKrLNEEVILRTLKV----TFQKESRSVSHFQYMAWPD-HGIP 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1423 LSKRSILQLVRRLAKWQeqydgGDGRT--VVHCLTGGGRSGTFCAICSINEMIQQQNIVD---VFHTVKTLRNNKTNMVE 1497
Cdd:cd14603    176 DSPDCMLAMIELARRLQ-----GSGPEplCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPAAVQ 250

                          250
                   ....*....|....
gi 1041121613 1498 TMEQYKFCYEVALE 1511
Cdd:cd14603    251 TEEQYEFLYHTVAQ 264
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1277-1512 2.41e-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: 133.63  E-value: 2.41e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1277 NHDKNRSMDVLSADRCLPFLISVDGES-SNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMD 1354
Cdd:cd14633     40 NRMKNRYGNIIAYDHSRVRLQPIEGETsSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVtNLVE 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1355 AAQL-CMQYWPEKNSCcYGPIQVEFISADIDEDIINRIFRIcnMARPQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVR 1433
Cdd:cd14633    120 VGRVkCCKYWPDDTEI-YKDIKVTLIETELLAEYVIRTFAV--EKRGVHEIREIRQFHFTGWPDH-GVPYHATGLLGFVR 195

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1041121613 1434 RLakwQEQYDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEA 1512
Cdd:cd14633    196 QV---KSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEA 271
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1017-1217 5.32e-33

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: 127.33  E-value: 5.32e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRV-KCVRYWPDE-TEVYGDIKVTLIETE 1094
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPgLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1095 PLAEYVIRTFTVQ-----KKGHHEIRelrQFHFTSW-PDHGVPCYATGLLGFIRQV-KFLNPPDAGPIVVHCSAGAGRTG 1167
Cdd:cd14637     81 ADEDIVTRLFRVQnitrlQEGHLMVR---HFQFLRWsAYRDTPDSKKAFLHLLASVeKWQRESGEGRTVVHCLNGGGRSG 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1168 CFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:cd14637    158 TYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1274-1513 5.51e-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: 129.85  E-value: 5.51e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1274 LPRNHDKNRSMDVLSADRCLPFLISVDG-ESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNE 1352
Cdd:cd14624     44 LEVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1353 MDAAQL--CMQYWPEKNSCCYGPIQVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQ 1430
Cdd:cd14624    124 LEERSRvkCDQYWPSRGTETYGLIQVTLLDTVELATYCVRTFALYKNGSSEK--REVRQFQFTAWPDH-GVPEHPTPFLA 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1431 LVRRLaKWQEQYDGGDgrTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVAL 1510
Cdd:cd14624    201 FLRRV-KTCNPPDAGP--MVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALL 277


                   ...
gi 1041121613 1511 EAL 1513
Cdd:cd14624    278 EAV 280
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1017-1217 1.15e-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: 126.34  E-value: 1.15e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVtNLVEVGRVkCVRYWPDE-TEVYGDIKVTLIETEP 1095
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVML-NDVDPAQL-CPQYWPENgVHRHGPIQVEFVSADL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1096 LAEYVIRTFTVQKKGHHE--IRELRQFHFTSWPDH-GVPCYATGLLGFIRQV-KFLNPPDAGP--IVVHCSAGAGRTGCF 1169
Cdd:cd14635     79 EEDIISRIFRIYNAARPQdgYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdKWQEEYNGGEgrTVVHCLNGGGRSGTF 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1041121613 1170 IAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAILE 1217
Cdd:cd14635    159 CAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1306-1506 1.88e-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: 125.61  E-value: 1.88e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMDAAQL-CMQYWPEK--NSCCYGPIQVEFISA 1381
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMAcREFEMGKKkCERYWPEEgeEQLQFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1382 D-IDEDIINRIFRicnmARPQDGYRLVQHFQFIGWPAyRDTPLSKRSILQLVRRLAKWQEQydgGDGRTVVHCLTGGGRS 1460
Cdd:cd14542     81 KrVGPDFLIRTLK----VTFQKESRTVYQFHYTAWPD-HGVPSSVDPILDLVRLVRDYQGS---EDVPICVHCSAGCGRT 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1041121613 1461 GTFCAICSINEMIQQQNIVD---VFHTVKTLRNNKTNMVETMEQYKFCY 1506
Cdd:cd14542    153 GTICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1306-1510 2.19e-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: 2.19e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEM-DAAQLCMQYWPEKNSccygPIQVE-FISADI 1383
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGqNMAEDEFVYWPNKDE----PINCEtFKVTLI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1384 DEDII------NRIFRICNMARPQDGYRL-VQHFQFIGWPAyRDTPLSKrsILQLVRRLakwQEQYDGGDGRTVVHCLTG 1456
Cdd:cd17669     77 AEEHKclsneeKLIIQDFILEATQDDYVLeVRHFQCPKWPN-PDSPISK--TFELISII---KEEAANRDGPMIVHDEHG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1041121613 1457 GGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVAL 1510
Cdd:cd17669    151 GVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1280-1508 1.26e-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: 1.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1280 KNRSMDVLSADRCLPFLISVDGES--SNYINAALMDSH-KQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMDA 1355
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMItNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1356 AQLCMQYWPEKNSCCYGpiqVEFISADI--DEDIINRIFRIcnmaRPQDGYRLVQHFQFIGWPAYRdTPLSKRSILQLVR 1433
Cdd:cd14613    108 NEKCTEYWPEEQVTYEG---IEITVKQVihADDYRLRLITL----KSGGEERGLKHYWYTSWPDQK-TPDNAPPLLQLVQ 179

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1041121613 1434 RLAKWQEQYDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEV 1508
Cdd:cd14613    180 EVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHV 254
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1269-1511 1.34e-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: 1.34e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1269 CSVGLLPRNHDKNRSMDVLSADRCLpflISVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIV 1348
Cdd:cd14608     17 CRVAKLPKNKNRNRYRDVSPFDHSR---IKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1349 MLNE-MDAAQL-CMQYWP--EKNSCCY--GPIQVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAY--RD 1420
Cdd:cd14608     94 MLNRvMEKGSLkCAQYWPqkEEKEMIFedTNLKLTLISEDIKSYYTVRQLELENLTTQET--REILHFHYTTWPDFgvPE 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1421 TPLSKRSILQLVRRLAKWQEQYdggdGRTVVHCLTGGGRSGTFCAICSINEMIQQQ---NIVDVFHTVKTLRNNKTNMVE 1497
Cdd:cd14608    172 SPASFLNFLFKVRESGSLSPEH----GPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDIKKVLLEMRKFRMGLIQ 247

                          250
                   ....*....|....
gi 1041121613 1498 TMEQYKFCYEVALE 1511
Cdd:cd14608    248 TADQLRFSYLAVIE 261
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1306-1507 1.84e-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: 122.96  E-value: 1.84e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALM--DSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQL---CMQYWP--EKNSCCYGPIQVEF 1378
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStakCADYFPaeENESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1379 ISADIDEDIINRIFRICNMARPQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAkwqeQYDGGDGRTVVHCLTGGG 1458
Cdd:cd17658     81 KKLKHSQHSITLRVLEVQYIESEEPPLSVLHIQYPEWPDH-GVPKDTRSVRELLKRLY----GIPPSAGPIVVHCSAGIG 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1041121613 1459 RSGTFCAICSINEMIQQQNI--VDVFHTVKTLRNNKTNMVETMEQYKFCYE 1507
Cdd:cd17658    156 RTGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1306-1502 3.05e-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: 122.24  E-value: 3.05e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN---EMDAAQlCMQYWP--EKNSCCYGPIQVEFIS 1380
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTrceEGNRNK-CAQYWPsmEEGSRAFGDVVVKINE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1381 ADIDEDIINRIFRICNmARPQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQeqyDGGDGRTVVHCLTGGGRS 1460
Cdd:cd14557     80 EKICPDYIIRKLNINN-KKEKGSGREVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFN---NFFSGPIVVHCSAGVGRT 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1041121613 1461 GTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQY 1502
Cdd:cd14557    155 GTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1304-1507 8.99e-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: 8.99e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1304 SNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNE-MDAAQL-CMQYWPEKNS--CCYGPIQVEFI 1379
Cdd:cd14616     25 SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQcFEKGRIrCHQYWPEDNKpvTVFGDIVITKL 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1380 SADIDEDIINRIFRIcnmARPQDgYRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLakwQEQYDGGDGRTVVHCLTGGGR 1459
Cdd:cd14616    105 MEDVQIDWTIRDLKI---ERHGD-YMMVRQCNFTSWPEH-GVPESSAPLIHFVKLV---RASRAHDNTPMIVHCSAGVGR 176

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1041121613 1460 SGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1507
Cdd:cd14616    177 TGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1306-1513 1.07e-30

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: 120.62  E-value: 1.07e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAA--LMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN-EMDAAQL-CMQYWPEKNSccyGPIQVEFISA 1381
Cdd:cd14596      1 YINASyiTMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTrEVERGKVkCHRYWPETLQ---EPMELENYQL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1382 DIDEDIINRIF--RICNMARPQDG-YRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQEQydggdGRTVVHCLTGGG 1458
Cdd:cd14596     78 RLENYQALQYFiiRIIKLVEKETGeNRLIKHLQFTTWPDH-GTPQSSDQLVKFICYMRKVHNT-----GPIVVHCSAGIG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1041121613 1459 RSGTFCAICSINEMIQQQ---NIVDVfhtVKTLRNNKTNMVETMEQYKFCYEVALEAL 1513
Cdd:cd14596    152 RAGVLICVDVLLSLIEKDlsfNIKDI---VREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1017-1216 3.42e-30

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: 119.33  E-value: 3.42e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVrYWP--DETEVYGDIKVTLIETE 1094
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPnkDEPINCETFKVTLIAEE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1095 PLA-----EYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATglLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCF 1169
Cdd:cd17669     80 HKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAANRDGPMIVHDEHGGVTAGTF 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1041121613 1170 IAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAIL 1216
Cdd:cd17669    158 CALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1275-1510 3.70e-30

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 122.42  E-value: 3.70e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1275 PRNHDKNRSMDVLSADRCLPFLISVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN--- 1351
Cdd:PHA02747    49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTptk 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1352 EMDAAQLCMQYW--PEKNSCCYGPIQVEFISADIDEDIINRIFRICNmaRPQDGYRLVQHFQFIGWPAYrDTPLSKRSIL 1429
Cdd:PHA02747   129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD--KILKDSRKISHFQCSEWFED-ETPSDHPDFI 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1430 QLV----RRLAKWQEQYDGGDG---RTVVHCLTGGGRSGTFCAI-CSINEMIQQQNIVdVFHTVKTLRNNKTNMVETMEQ 1501
Cdd:PHA02747   206 KFIkiidINRKKSGKLFNPKDAllcPIVVHCSDGVGKTGIFCAVdICLNQLVKRKAIC-LAKTAEKIREQRHAGIMNFDD 284

                          250
                   ....*....|..
gi 1041121613 1502 YKF---CYEVAL 1510
Cdd:PHA02747   285 YLFiqpGYEVLH 296
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1264-1506 5.41e-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: 119.94  E-value: 5.41e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1264 VRPEDCSVgllPRNHDKNRSMDVLSADR---CLPFLISVDgESSNYINAA-LMDSHKQPAAFIVTQHPLPNTMGDFWRLV 1339
Cdd:cd14612      5 VSPEELDI---PGHASKDRYKTILPNPQsrvCLRRAGSQE-EEGSYINANyIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1340 FDYNCSSIVMLNEM-DAAQLCMQYWPEKNSCcYGPIQVEF-ISADIDEDIINRIfricnMARPQDGYRLVQHFQFIGWPA 1417
Cdd:cd14612     81 WQEECPIIVMITKLkEKKEKCVHYWPEKEGT-YGRFEIRVqDMKECDGYTIRDL-----TIQLEEESRSVKHYWFSSWPD 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1418 YRdTPLSKRSILQLVRRLAKwQEQYDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVE 1497
Cdd:cd14612    155 HQ-TPESAGPLLRLVAEVEE-SRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQ 232


                   ....*....
gi 1041121613 1498 TMEQYKFCY 1506
Cdd:cd14612    233 TSEQYQFLH 241
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1306-1507 3.02e-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: 116.62  E-value: 3.02e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEM--DAAQLCMQYWPEKNSCCYGPIQVEFISADI 1383
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLveKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1384 DEDIINRIFRICNM--------ARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQEQydgGDGRTVVHCLT 1455
Cdd:cd17668     81 LAYYTVRNFTLRNTkikkgsqkGRPSG--RVVTQYHYTQWPDM-GVPEYTLPVLTFVRKASYAKRH---AVGPVVVHCSA 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1041121613 1456 GGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1507
Cdd:cd17668    155 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1277-1513 6.32e-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: 116.47  E-value: 6.32e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1277 NHDKNRSMDVLSADRCLPFLisvdGESSNYINAAL--MDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEM 1353
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPL----GDEGGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMtQEV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1354 DAAQL-CMQYWPE---KNSCCYGPIQVEFISadiDEDIINRIFRICNMARPQDG-YRLVQHFQFIGWPAYrDTPLSKRSI 1428
Cdd:cd14597     79 EGGKIkCQRYWPEilgKTTMVDNRLQLTLVR---MQQLKNFVIRVLELEDIQTReVRHITHLNFTAWPDH-DTPSQPEQL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1429 LQLV---RRLAKwqeqydggDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFC 1505
Cdd:cd14597    155 LTFIsymRHIHK--------SGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFC 226


                   ....*...
gi 1041121613 1506 YEVALEAL 1513
Cdd:cd14597    227 YQVILYVL 234
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1306-1510 6.38e-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: 6.38e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML-NEMDAAQLCMQYWP--EKNSCCYGpIQVEFISAD 1382
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpDNQGLAEDEFVYWPsrEESMNCEA-FTVTLISKD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1383 I-----DEDIINRIFRicnMARPQDGYRL-VQHFQFIGWPAyRDTPLSkrSILQLVRRLakwQEQYDGGDGRTVVHCLTG 1456
Cdd:cd17670     80 RlclsnEEQIIIHDFI---LEATQDDYVLeVRHFQCPKWPN-PDAPIS--STFELINVI---KEEALTRDGPTIVHDEFG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1041121613 1457 GGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVAL 1510
Cdd:cd17670    151 AVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1278-1513 8.99e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 118.98  E-value: 8.99e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1278 HDKNRSMDVLSADRCLPFLISVDgESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAA- 1356
Cdd:PHA02746    73 HESLKMFDVGDSDGKKIEVTSED-NAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDd 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1357 QLCMQYW--PEKNSCCYGPIQVEFIsaDIDEDIINRIFRICNMARPQDGYRLVQHFQFIGWPAYrDTPLSKRSILQLV-- 1432
Cdd:PHA02746   152 EKCFELWtkEEDSELAFGRFVAKIL--DIIEELSFTKTRLMITDKISDTSREIHHFWFPDWPDN-GIPTGMAEFLELInk 228

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1433 -----RRLAKWQEQYDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYE 1507
Cdd:PHA02746   229 vneeqAELIKQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYK 308


                   ....*.
gi 1041121613 1508 VALEAL 1513
Cdd:PHA02746   309 ALKYAI 314
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1280-1511 9.13e-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: 116.09  E-value: 9.13e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1280 KNRSMDVLSADRC---LPFLISvdGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN---EM 1353
Cdd:cd14602      1 KNRYKDILPYDHSrveLSLITS--DEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACmefEM 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1354 DAAQlCMQYWPE--KNSCCYGPIQVEFISADIDEDIINRIFRicnmARPQDGYRLVQHFQFIGWPAYrDTPLSKRSILQL 1431
Cdd:cd14602     79 GKKK-CERYWAEpgEMQLEFGPFSVTCEAEKRKSDYIIRTLK----VKFNSETRTIYQFHYKNWPDH-DVPSSIDPILEL 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1432 VRRLAKWQEQydgGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNI---VDVFHTVKTLRNNKTNMVETMEQYKFCYEV 1508
Cdd:cd14602    153 IWDVRCYQED---DSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIpenFSVFSLIQEMRTQRPSLVQTKEQYELVYNA 229


                   ...
gi 1041121613 1509 ALE 1511
Cdd:cd14602    230 VIE 232
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1261-1506 9.68e-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: 9.68e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1261 TPRVRPEDcsVGLLPRNHDKNRSMDVLSADRC-LPFLISVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLV 1339
Cdd:cd14604     43 TEKIYPTA--TGEKEENVKKNRYKDILPFDHSrVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMI 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1340 FDYNCSSIVMLN---EMDAAQlCMQYWPeknscCYGPIQVEF----ISADIDEDIINRIFRICNMARPQDGYRLVQhFQF 1412
Cdd:cd14604    121 WEYNVAIIVMACrefEMGRKK-CERYWP-----LYGEEPMTFgpfrISCEAEQARTDYFIRTLLLEFQNETRRLYQ-FHY 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1413 IGWPAYrDTPLSKRSILQLVRRLAKWQEQydgGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNI---VDVFHTVKTLR 1489
Cdd:cd14604    194 VNWPDH-DVPSSFDSILDMISLMRKYQEH---EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMR 269

                          250
                   ....*....|....*..
gi 1041121613 1490 NNKTNMVETMEQYKFCY 1506
Cdd:cd14604    270 TQRHSAVQTKEQYELVH 286
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1277-1506 1.01e-28

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: 116.41  E-value: 1.01e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1277 NHDKNRSMDVLSADRCLPFLISVDGE--SSNYINA------ALMDSHKQPA-AFIVTQHPLPNTMGDFWRLVFDYNCSSI 1347
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNvpGSDYINAnyirneNEGPTTDENAkTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1348 VMLNEM--DAAQLCMQYWP-EKNSCCYGPIQVEFISADIDEDIINRIFRICNMARPQDGyRLVQHFQFIGWPAYrDTPLS 1424
Cdd:cd14544     81 VMTTKEveRGKNKCVRYWPdEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPI-REIWHYQYLSWPDH-GVPSD 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1425 KRSILQLVRRLAKWQEqYDGGDGRTVVHCLTGGGRSGTFCAICSINEMIQQQNI---VDVFHTVKTLRNNKTNMVETMEQ 1501
Cdd:cd14544    159 PGGVLNFLEDVNQRQE-SLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQ 237


                   ....*
gi 1041121613 1502 YKFCY 1506
Cdd:cd14544    238 YKFIY 242
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1017-1216 2.60e-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: 114.01  E-value: 2.60e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1017 YINANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVrYWPDETEVYG--DIKVTLIETE 1094
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFV-YWPSREESMNceAFTVTLISKD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1095 PLA-----EYVIRTFTVQKKGHHEIRELRQFHFTSWPDHGVPCYATglLGFIRQVKFLNPPDAGPIVVHCSAGAGRTGCF 1169
Cdd:cd17670     80 RLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEFGAVSAGTL 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1041121613 1170 IAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAIL 1216
Cdd:cd17670    158 CALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1298-1506 4.88e-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: 113.86  E-value: 4.88e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1298 SVDGESSNYINAALMDSHK-QPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEM-DAAQLCMQYWPEKNSCcYGPIQ 1375
Cdd:cd14611     22 NSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLkEKNEKCVLYWPEKRGI-YGKVE 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1376 VEFISADIDEDIINRifricNMARPQDGY-RLVQHFQFIGWPAYRdTPLSKRSILQLVRRLAKwQEQYDGGDGRTVVHCL 1454
Cdd:cd14611    101 VLVNSVKECDNYTIR-----NLTLKQGSQsRSVKHYWYTSWPDHK-TPDSAQPLLQLMLDVEE-DRLASPGRGPVVVHCS 173

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1041121613 1455 TGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCY 1506
Cdd:cd14611    174 AGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1277-1506 9.99e-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: 9.99e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1277 NHDKNRSMDVLSADRCLPFLISVD--GESSNYINAALM--------DSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSS 1346
Cdd:cd14605      2 NKNKNRYKNILPFDHTRVVLHDGDpnEPVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1347 IVMLN-EMDAAQ-LCMQYWPEKNSCC-YGPIQVEFISADIDEDIINRIFRICNMARpQDGYRLVQHFQFIGWPAYrDTPL 1423
Cdd:cd14605     82 IVMTTkEVERGKsKCVKYWPDEYALKeYGVMRVRNVKESAAHDYILRELKLSKVGQ-GNTERTVWQYHFRTWPDH-GVPS 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1424 SKRSILQLVRRLAKWQEQYDGGdGRTVVHCLTGGGRSGTFCAICSINEMIQQQNI---VDVFHTVKTLRNNKTNMVETME 1500
Cdd:cd14605    160 DPGGVLDFLEEVHHKQESIMDA-GPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEA 238


                   ....*.
gi 1041121613 1501 QYKFCY 1506
Cdd:cd14605    239 QYRFIY 244
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1272-1515 2.14e-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: 2.14e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1272 GLLPRNHDKNRSMDVLSADRCLPFLISVDGE-------SSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNC 1344
Cdd:cd14606     13 GQRPENKSKNRYKNILPFDHSRVILQGRDSNipgsdyiNANYVKNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENS 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1345 SSIVMLN-EMDAAQ-LCMQYWPEKNSC-CYGPIQVEFISADIDEDIINRIFRICNMARpQDGYRLVQHFQFIGWPAYrDT 1421
Cdd:cd14606     93 RVIVMTTrEVEKGRnKCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLRTLQVSPLDN-GELIREIWHYQYLSWPDH-GV 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1422 PLSKRSILQLVRRLAKWQEQYDGGdGRTVVHCLTGGGRSGTFCAICSINEMIQQQNI---VDVFHTVKTLRNNKTNMVET 1498
Cdd:cd14606    171 PSEPGGVLSFLDQINQRQESLPHA-GPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQT 249

                          250
                   ....*....|....*..
gi 1041121613 1499 MEQYKFCYEVALEALNS 1515
Cdd:cd14606    250 EAQYKFIYVAIAQFIET 266
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1306-1515 2.28e-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: 2.28e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAALMD----SHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEM--DAAQLCMQYWPEKN-SCCYGPIQVEF 1378
Cdd:cd14541      2 YINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLveRGRVKCHQYWPDLGeTMQFGNLQITC 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1379 ISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLAKWQEqydGGDGRTVVHCLTGGG 1458
Cdd:cd14541     82 VSEEVTPSFAFREFILTNTNTGEE--RHITQMQYLAWPDH-GVPDDSSDFLDFVKRVRQNRV---GMVEPTVVHCSAGIG 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1041121613 1459 RSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEALNS 1515
Cdd:cd14541    156 RTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVYEE 212
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1306-1513 5.25e-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: 107.54  E-value: 5.25e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAalmdSHKQPAA------FIVTQHPLPNTMGDFWRLVFDYNCSSIVML--NEMDAAQLCMQYWPEKNSCC----YGP 1373
Cdd:cd14540      1 YINA----SHITATVggkqrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVtaEEEGGREKCFRYWPTLGGEHdaltFGE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1374 IQVEFISADIDEDIINRIFRICNMarPQDGYRLVQHFQFIGWPAYrDTPLSKRSIL------QLVRRLAKwqeQYDGGDG 1447
Cdd:cd14540     77 YKVSTKFSVSSGCYTTTGLRVKHT--LSGQSRTVWHLQYTDWPDH-GCPEDVSGFLdfleeiNSVRRHTN---QDVAGHN 150

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1041121613 1448 R---TVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEAL 1513
Cdd:cd14540    151 RnppTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1407-1511 6.64e-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: 103.21  E-value: 6.64e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  1407 VQHFQFIGWPAyRDTPLSKRSILQLVRRLAKWQEQYDGGdGRTVVHCLTGGGRSGTFCAICSINEMI-QQQNIVDVFHTV 1485
Cdd:smart00012    2 VKHYHYTGWPD-HGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDTV 79

                            90       100
                    ....*....|....*....|....*.
gi 1041121613  1486 KTLRNNKTNMVETMEQYKFCYEVALE 1511
Cdd:smart00012   80 KELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1407-1511 6.64e-26

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 103.21  E-value: 6.64e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  1407 VQHFQFIGWPAyRDTPLSKRSILQLVRRLAKWQEQYDGGdGRTVVHCLTGGGRSGTFCAICSINEMI-QQQNIVDVFHTV 1485
Cdd:smart00404    2 VKHYHYTGWPD-HGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDTV 79

                            90       100
                    ....*....|....*....|....*.
gi 1041121613  1486 KTLRNNKTNMVETMEQYKFCYEVALE 1511
Cdd:smart00404   80 KELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1275-1506 9.87e-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: 105.05  E-value: 9.87e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1275 PRNHDKNRSMDVLSADRCLpflISVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN--- 1351
Cdd:cd14607     22 PENRNRNRYRDVSPYDHSR---VKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNriv 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1352 EMDAAQlCMQYWP--EKNSCCYGP--IQVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAY--RDTPLSK 1425
Cdd:cd14607     99 EKDSVK-CAQYWPtdEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGET--RTISHFHYTTWPDFgvPESPASF 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1426 RSILQLVRRLAKWQEQYdggdGRTVVHCLTGGGRSGTFCAICSINEMIQQQN--IVDVFHTVKTLRNNKTNMVETMEQYK 1503
Cdd:cd14607    176 LNFLFKVRESGSLSPEH----GPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQTPDQLR 251


                   ...
gi 1041121613 1504 FCY 1506
Cdd:cd14607    252 FSY 254
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1274-1510 8.71e-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: 8.71e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1274 LPRNHDKNRSMDVLSADRCLPFLisvdGESSNYINAALMDShKQPAA-----FIVTQHPLPNTMGDFWRLVFDYNCSSIV 1348
Cdd:cd14600     37 LPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVNM-EIPSAnivnkYIATQGPLPHTCAQFWQVVWEQKLSLIV 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1349 MLNEMD--AAQLCMQYWPEKNSCC-YGPIQVEFISADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSK 1425
Cdd:cd14600    112 MLTTLTerGRTKCHQYWPDPPDVMeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEE--RTVTHLQYVAWPDH-GVPDDS 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1426 RSILQLVRRLAKWQEQYDggdgRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFC 1505
Cdd:cd14600    189 SDFLEFVNYVRSKRVENE----PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFV 264


                   ....*
gi 1041121613 1506 YEVAL 1510
Cdd:cd14600    265 CEAIL 269
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1266-1511 5.45e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 101.23  E-value: 5.45e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1266 PEDCSVGLLPRNHDKNRSMDVLSADRCLPFLISVDGeSSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCS 1345
Cdd:PHA02742    41 AFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVR 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1346 SIVMLNEM--DAAQLCMQYW--PEKNSCCYGPIQVEfiSADIDEdiiNRIFRICNM--ARPQDGYRL-VQHFQFIGWPaY 1418
Cdd:PHA02742   120 VIVMITKImeDGKEACYPYWmpHERGKATHGEFKIK--TKKIKS---FRNYAVTNLclTDTNTGASLdIKHFAYEDWP-H 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1419 RDTPLSKRSILQLVRRLAKWQEQYD---GGDGRT-----VVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRN 1490
Cdd:PHA02742   194 GGLPRDPNKFLDFVLAVREADLKADvdiKGENIVkeppiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRK 273

                          250       260
                   ....*....|....*....|.
gi 1041121613 1491 NKTNMVETMEQYKFCYEVALE 1511
Cdd:PHA02742   274 QRHNCLSLPQQYIFCYFIVLI 294
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1303-1511 2.20e-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: 2.20e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1303 SSNYINAALmDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQL--CMQYWPE-KNSCCYGPIQVEFI 1379
Cdd:cd14601      4 NANYINMEI-PSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRvkCHQYWPEpSGSSSYGGFQVTCH 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1380 SADIDEDIINRIFRICNMARPQDgyRLVQHFQFIGWPAYrDTPLSKRSILQLVRRLakwQEQYDGGDGRTVVHCLTGGGR 1459
Cdd:cd14601     83 SEEGNPAYVFREMTLTNLEKNES--RPLTQIQYIAWPDH-GVPDDSSDFLDFVCLV---RNKRAGKDEPVVVHCSAGIGR 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1041121613 1460 SGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALE 1511
Cdd:cd14601    157 TGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PHA02738 PHA02738
hypothetical protein; Provisional
 1276-1515 6.83e-19

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 89.60  E-value: 6.83e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1276 RNHDKNRSMDVLSADRCLPFLiSVDGESSNYINAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVML--NEM 1353
Cdd:PHA02738    48 KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLckKKE 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1354 DAAQLCMQYWP--EKNSCCYGPIQVEFISAdidEDIINRIFRICNMARPQDGYRLVQHFQFIGWPAYrDTPLSKRSILQL 1431
Cdd:PHA02738   127 NGREKCFPYWSdvEQGSIRFGKFKITTTQV---ETHPHYVKSTLLLTDGTSATQTVTHFNFTAWPDH-DVPKNTSEFLNF 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1432 ---VRRLAK--WQEQYDGGDGRT-----VVHCLTGGGRSGTFCAI-CSINEMIQQQNiVDVFHTVKTLRNNKTNMVETME 1500
Cdd:PHA02738   203 vleVRQCQKelAQESLQIGHNRLqpppiVVHCNAGLGRTPCYCVVdISISRFDACAT-VSIPSIVSSIRNQRYYSLFIPF 281

                          250
                   ....*....|....*
gi 1041121613 1501 QYKFCYEVALEALNS 1515
Cdd:PHA02738   282 QYFFCYRAVKRYVNL 296
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1262-1513 7.72e-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: 88.52  E-value: 7.72e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1262 PRVRPEDC-SVGLLPRNHDKNRSMDVLSADRCLPFLISVDGESSNYINAalmdSHKQPAA------FIVTQHPLPNTMGD 1334
Cdd:cd14599     22 PKKKADGVfTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINA----SHIKVTVggeewhYIATQGPLPHTCHD 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1335 FWRLVFDYNCSSIVMLN--EMDAAQLCMQYWP----EKNSCCYGPIQVefiSADIDED---IINRIFRICNMARPQDgyR 1405
Cdd:cd14599     98 FWQMVWEQGVNVIAMVTaeEEGGRSKSHRYWPklgsKHSSATYGKFKV---TTKFRTDsgcYATTGLKVKHLLSGQE--R 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1406 LVQHFQFIGWPAYrDTP------LSKRSILQLVRRLAkwQEQYDGGDGRT---VVHCLTGGGRSGTFCAICSINEMIQQQ 1476
Cdd:cd14599    173 TVWHLQYTDWPDH-GCPeevqgfLSYLEEIQSVRRHT--NSMLDSTKNCNppiVVHCSAGVGRTGVVILTELMIGCLEHN 249

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1041121613 1477 NIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEAL 1513
Cdd:cd14599    250 EKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFL 286
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 944-1215 5.81e-16

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 80.40  E-value: 5.81e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  944 IRVADLLQHITQmkcgqgygfkeEYEALAEGQTapwETAKKDENRNKNRYGN------IIAYDHTRVRLQlldgdPHSDY 1017
Cdd:PHA02740    18 INKPDLLSCIIK-----------EYRAIVPEHE---DEANKACAQAENKAKDenlalhITRLLHRRIKLF-----NDEKV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1018 INANYIDGYHRPRHYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEvgrVKC-VRYWPDE---TEVYGDIKVTLIE- 1092
Cdd:PHA02740    79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHAD---KKCfNQFWSLKegcVITSDKFQIETLEi 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1093 -TEPLAEYVIRTFTVQKKghhEIRELRQFHFTSWPDHGVPCYATGLLGFIRQVKFL--------NPPDAGPIVVHCSAGA 1163
Cdd:PHA02740   156 iIKPHFNLTLLSLTDKFG---QAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLcadlekhkADGKIAPIIIDCIDGI 232

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1041121613 1164 GRTGCFIAVDIMLDMAENEGVVDIFNCIRELRSQRVNMVQTEEQYVFVHDAI 1215
Cdd:PHA02740   233 SSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1306-1513 1.21e-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: 1.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1306 YINAalmdSHKQPAA------FIVTQHPLPNTMGDFWRLVFDYNCSSIVMLN--EMDAAQLCMQYWP----EKNSCCYGP 1373
Cdd:cd14598      1 YINA----SHIKVTVggkewdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTaeEEGGREKSFRYWPrlgsRHNTVTYGR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1374 IQvefISADIDED---IINRIFRICNMARPQDgyRLVQHFQFIGWPAY---RDTP--LSKRSILQLVRRLAKWQEQYDGG 1445
Cdd:cd14598     77 FK---ITTRFRTDsgcYATTGLKIKHLLTGQE--RTVWHLQYTDWPEHgcpEDLKgfLSYLEEIQSVRRHTNSTIDPKSP 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1041121613 1446 DGRTVVHCLTGGGRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEVALEAL 1513
Cdd:cd14598    152 NPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1018-1209 6.95e-14

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: 72.82  E-value: 6.95e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1018 INANY--IDGYHRprhYIATQGPMQETVRDFWRMVWQENSASIVMVTNLVEVGRVKCVRYW-PDETevYGDIKVTLIETE 1094
Cdd:cd14559     18 LNANRvqIGNKNV---AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFrQSGT--YGSVTVKSKKTG 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1095 PLA---EYVIRTFTVQKKGHHEIRELRQFHFTSWPDHG-VPCYATGLL-GFIRQV-----KFL--------NPPDAGPIV 1156
Cdd:cd14559     93 KDElvdGLKADMYNLKITDGNKTITIPVVHVTNWPDHTaISSEGLKELaDLVNKSaeekrNFYkskgssaiNDKNKLLPV 172

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1041121613 1157 VHCSAGAGRTGCFIAVDIMLDMAENEGVVDIfncIRELRSQR-VNMVQTEEQYV 1209
Cdd:cd14559    173 IHCRAGVGRTGQLAAAMELNKSPNNLSVEDI---VSDMRTSRnGKMVQKDEQLD 223
fn3 pfam00041
Fibronectin type III domain;
501-576 1.07e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.35  E-value: 1.07e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1041121613  501 IFMQWKAPNETNGAITLYEITYKALSSLDPSADLTTqrgrvfkLKNETHHLFVGLYPGTTYFFTLKASTNKGFGPP 576
Cdd:pfam00041   16 LTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITV-------PGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 501-579 2.52e-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: 55.58  E-value: 2.52e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1041121613  501 IFMQWKAPNETNGAITLYEITYKALSSlDPSADLTTQRGrvfklkNETHHLFVGLYPGTTYFFTLKASTNKGFGPPVTT 579
Cdd:cd00063     17 VTLSWTPPEDDGGPITGYVVEYREKGS-GDWKEVEVTPG------SETSYTLTGLKPGTEYEFRVRAVNGGGESPPSES 88
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1307-1508 8.37e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 58.82  E-value: 8.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1307 INAALMDSHKQPAAFIVTQHPLPNTMGDFWRLVFDYNCSSIVMLNEMDAAQLCMQYWPEKNSCC--YGPIQVEFIsadid 1384
Cdd:PHA02740    79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCFNQFWSLKEGCVitSDKFQIETL----- 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1385 eDIINRIFRICNMARPQDGY---RLVQHFQFIGWP---------AYRDTPLSKRSI-LQLVRRLAkwqeqyDGGDGRTVV 1451
Cdd:PHA02740   154 -EIIIKPHFNLTLLSLTDKFgqaQKISHFQYTAWPadgfshdpdAFIDFFCNIDDLcADLEKHKA------DGKIAPIII 226

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1041121613 1452 HCLTGGGRSGTFCA--ICSINemIQQQNIVDVFHTVKTLRNNKTNMVETMEQYKFCYEV 1508
Cdd:PHA02740   227 DCIDGISSSAVFCVfdICATE--FDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHL 283
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1321-1503 1.16e-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: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1321 FIVTQHPLPNTMGDFWRLVFDYNCSSIVML---NEMDAAQLcmqywPE--KNSCCYGPIQV--EFISADIDEDIINriFR 1393
Cdd:cd14559     31 AIACQYPKNEQLEDHLKMLADNRTPCLVVLasnKDIQRKGL-----PPyfRQSGTYGSVTVksKKTGKDELVDGLK--AD 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1394 ICNMARPQDGYRL---VQHFQfiGWPAYrdTPLSKRSILQLVRRLAK-------------WQEQYDGGDGRTVVHCLTGG 1457
Cdd:cd14559    104 MYNLKITDGNKTItipVVHVT--NWPDH--TAISSEGLKELADLVNKsaeekrnfykskgSSAINDKNKLLPVIHCRAGV 179

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1041121613 1458 GRSGTFCAICSINEMIQQQNIVDVFHTVKTLRNNKtnMVETMEQYK 1503
Cdd:cd14559    180 GRTGQLAAAMELNKSPNNLSVEDIVSDMRTSRNGK--MVQKDEQLD 223
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1125-1213 1.22e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 55.36  E-value: 1.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1125 WPDHGVPCYATgLLGFIRQVKFLNPPDaGPIVVHCSAGAGRTGCFIAvdiMLDMAENEGVVDIFNCIRELRSQRvnmVQT 1204
Cdd:COG2453     55 IPDFGAPDDEQ-LQEAVDFIDEALREG-KKVLVHCRGGIGRTGTVAA---AYLVLLGLSAEEALARVRAARPGA---VET 126


                   ....*....
gi 1041121613 1205 EEQYVFVHD 1213
Cdd:COG2453    127 PAQRAFLER 135
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1020-1213 1.96e-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: 53.89  E-value: 1.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1020 ANYIDgyhrPRHYIATQGPMqETVRDFWRMVWQENSASIVMVTNlvevgrvkcvrywpdetevygdikvtlieteplaey 1099
Cdd:cd14494      1 FNWID----PLRLIAGALPL-SPLEADSRFLKQLGVTTIVDLTL------------------------------------ 39

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1100 virtftvqkkghHEIRELRQFhftswpdhgvpcyatgllgfIRQvkFLNPPdaGPIVVHCSAGAGRTGCFIAVDIMLDMA 1179
Cdd:cd14494     40 ------------AMVDRFLEV--------------------LDQ--AEKPG--EPVLVHCKAGVGRTGTLVACYLVLLGG 83

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1041121613 1180 EnegvvDIFNCIRELRSQRVN-MVQTEEQYVFVHD 1213
Cdd:cd14494     84 M-----SAEEAVRIVRLIRPGgIPQTIEQLDFLIK 113
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1120-1213 1.92e-07

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: 53.12  E-value: 1.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1120 FHFTSWPDHGVPCYATgLLGFIRQVKFLnPPDAGPIVVHCSAGAGRTGCFIAVDIM--LDMAENEgvvdifnCIRELRSQ 1197
Cdd:cd14506     79 FYNFGWKDYGVPSLTT-ILDIVKVMAFA-LQEGGKVAVHCHAGLGRTGVLIACYLVyaLRMSADQ-------AIRLVRSK 149

                           90
                   ....*....|....*.
gi 1041121613 1198 RVNMVQTEEQYVFVHD 1213
Cdd:cd14506    150 RPNSIQTRGQVLCVRE 165
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 389-479 3.65e-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: 46.72  E-value: 3.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  389 PQNVNVVDVRARQLTVQWETFGYAVTRCHSYnlTVQYQYVFNQQEFAAEELIQTSSHYTLRGLRPFVTVRLRLVLANPEG 468
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGY--VVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 1041121613  469 -SKESEEIVKQT 479
Cdd:cd00063     82 eSPPSESVTVTT 93
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1083-1213 1.99e-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: 46.49  E-value: 1.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1083 YGDIKVTLIETEPLAEYVIRTF--TVQKKGhheireLRQFHFtSWPDHGVPcyatgllGFIRQVKFLNPP-----DAGP- 1154
Cdd:cd14505     43 GVDDVVTLCTDGELEELGVPDLleQYQQAG------ITWHHL-PIPDGGVP-------SDIAQWQELLEEllsalENGKk 108

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1041121613 1155 IVVHCSAGAGRTGcFIAVDIMLDMAENEGVVDIFNCIRELRSqrvNMVQTEEQYVFVHD 1213
Cdd:cd14505    109 VLIHCKGGLGRTG-LIAACLLLELGDTLDPEQAIAAVRALRP---GAIQTPKQENFLHQ 163
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 288-359 5.52e-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: 42.99  E-value: 5.52e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1041121613   288 PTPIAPPELLAVGATYL---WIKPNANSiiGDGPIILKEVEYRTTTGNWAETHVVDAPT-YKLWHLDPDVEYEIKV 359
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVtlsWEPPPDDG--ITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRV 74
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1429-1507 1.34e-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: 42.72  E-value: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1429 LQLVRRLAKWQEQYDGGDGRTVVHCLTGGGRSGTFCAIcsineMIQQQNIVDVFHTVKTLRNNKTN-MVETMEQYKFCYE 1507
Cdd:cd14494     39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVAC-----YLVLLGGMSAEEAVRIVRLIRPGgIPQTIEQLDFLIK 113
fn3 pfam00041
Fibronectin type III domain;
293-359 1.47e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 42.02  E-value: 1.47e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1041121613  293 PPELL---AVGATYL---WIKPNAnsiiGDGPIILKEVEYRTTTGNWAETHVVDAPT---YKLWHLDPDVEYEIKV 359
Cdd:pfam00041    2 APSNLtvtDVTSTSLtvsWTPPPD----GNGPITGYEVEYRPKNSGEPWNEITVPGTttsVTLTGLKPGTEYEVRV 73
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1154-1211 1.57e-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: 43.42  E-value: 1.57e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1041121613 1154 PIVVHCSAGAGRTGCFIAVDIMldmaeNEGVVDIFNCIRELRSQRVNMVQTEEQYVFV 1211
Cdd:cd14504     84 AVLVHCLAGKGRTGTMLACYLV-----KTGKISAVDAINEIRRIRPGSIETSEQEKFV 136
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 501-574 1.79e-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: 41.83  E-value: 1.79e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1041121613   501 IFMQWKAPNETNGaiTLYEITYKALSSldpsaDLTTQRGRVFKLKNETHHLFVGLYPGTTYFFTLKASTNKGFG 574
Cdd:smart00060   17 VTLSWEPPPDDGI--TGYIVGYRVEYR-----EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
 1086-1185 2.69e-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: 44.67  E-value: 2.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613 1086 IKVTLIETEplaEYVirtftVQKKGHHEIRELRQFHFtsWPDhgvPCYATGLLGFIRQvkflNPPDAGpIVVHCSAGAGR 1165
Cdd:cd14495    138 VKVESVRTE---EEL-----VKKKGAHYVRIAATDHV--WPD---DEEIDAFVAFYRS----LPADAW-LHFHCRAGKGR 199

                           90       100
                   ....*....|....*....|
gi 1041121613 1166 TGCFIAvdiMLDMAENEGVV 1185
Cdd:cd14495    200 TTTFMV---MYDMLKNPKDV 216
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 389-469 1.07e-03

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: 39.52  E-value: 1.07e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613   389 PQNVNVVDVRARQLTVQWETFGYAVTRchSYNLTVQYQYVFNQQEFAAEELIQTSSHYTLRGLRPFVTVRLRLVLANPEG 468
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    .
gi 1041121613   469 S 469
Cdd:smart00060   82 E 82
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 195-280 2.69e-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: 38.33  E-value: 2.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041121613  195 LRLQNVEVNVGQNATFQCTAGGKWSQHDKLWLQQwNGRDTALMVTRVVNHRRFSATVSVGDTSQRSTSRYRCVIRSDGGS 274
Cdd:pfam00047    1 SAPPTVTVLEGDSATLTCSASTGSPGPDVTWSKE-GGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79


                   ....*.
gi 1041121613  275 GVSNYA 280
Cdd:pfam00047   80 ATLSTS 85
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 1153-1175 3.50e-03

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: 40.13  E-value: 3.50e-03
                           10        20
                   ....*....|....*....|...
gi 1041121613 1153 GPIVVHCSAGAGRTGCFIAVDIM 1175
Cdd:cd14499    110 GAIAVHCKAGLGRTGTLIACYLM 132
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 1140-1201 3.75e-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: 39.17  E-value: 3.75e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1041121613 1140 FIRQVKFLNppdaGPIVVHCSAGAGRTGCFIAVDIMldMAENEGVVDIFNCIRELRSQ-RVNM 1201
Cdd:pfam00782   61 FIDDARQKG----GKVLVHCQAGISRSATLIIAYLM--KTRNLSLNEAYSFVKERRPGiSPNF 117
 
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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