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Conserved domains on  [gi|1002623460|ref|NP_001307615|]
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tyrosine-protein phosphatase non-receptor type 20 isoform 8 [Homo sapiens]

Protein Classification

protein-tyrosine phosphatase family protein( domain architecture ID 1000023)

cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 127-333 1.46e-140

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.


The actual alignment was detected with superfamily member cd14596:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 207  Bit Score: 396.43  E-value: 1.46e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 206
Cdd:cd14596     1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 207 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCVD 286
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICVD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1002623460 287 VVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 333
Cdd:cd14596   161 VLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
 
Name Accession Description Interval E-value
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 127-333 1.46e-140

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: 396.43  E-value: 1.46e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 206
Cdd:cd14596     1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 207 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCVD 286
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICVD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1002623460 287 VVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 333
Cdd:cd14596   161 VLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
78-330 4.30e-112

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 326.15  E-value: 4.30e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460   78 IMQEFMAL-ELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPL----GKSKDYINASYIRIVNCGEEYfyIATQGPLL 152
Cdd:smart00194   2 LEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLkpppGEGSDYINASYIDGPNGPKAY--IATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  153 STIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSV 232
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  233 KQLQFTKWPDHGTPASADSFIKYIRYARK--SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQ 310
Cdd:smart00194 160 THYHYTNWPDHGVPESPESILDLIRAVRKsqSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                          250       260
                   ....*....|....*....|
gi 1002623460  311 RSGMVQTKEQYHFCYDIVLE 330
Cdd:smart00194 240 RPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
102-330 4.00e-108

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 314.95  E-value: 4.00e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 102 NREKNRYRDILPYDSTRVPLGKSK---DYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIE 178
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPgpsDYINASYIDGYK--KPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 179 GGIIKCYHYWPISLKKPLELKHFRVFLENY-QILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIR 257
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002623460 258 YARKSHL---TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 330
Cdd:pfam00102 159 KVRKSSLdgrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
98-337 7.26e-50

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 167.96  E-value: 7.26e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  98 NQPSNREKNRYRDILPYDSTRVplGKSKDYINASYIRIvncGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREI 177
Cdd:COG5599    38 QNINGSPLNRFRDIQPYKETAL--RANLGYLNANYIQV---IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 178 EGG--IIKCYHYWPIS---LKKPLELKHfrvfLENYQILQYFIIRMFQVVEKSTG-TSHSVKQLQFTKWPDHGTPaSADS 251
Cdd:COG5599   113 EISkpKVKMPVYFRQDgeyGKYEVSSEL----TESIQLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAI-SAEA 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 252 FIKYIRYARKSHLT-----GPMVVHCSAGIGRTGVFLCVDVVFCAI--VKNCSFNIMDIVAQMREQR-SGMVQTKEQYHF 323
Cdd:COG5599   188 LKNLADLIDKKEKIkdpdkLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRnGGMVQTSEQLDV 267

                         250
                  ....*....|....
gi 1002623460 324 CYDIVLEVLRKLLT 337
Cdd:COG5599   268 LVKLAEQQIRPLLR 281
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 78-339 2.15e-47

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 162.48  E-value: 2.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  78 IMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPL----GKSKDYINASYIRIVNcgEEYFYIATQGPLLS 153
Cdd:PHA02747   27 IRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILdsggGSTSDYIHANWIDGFE--DDKKFIATQGPFAE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 154 TIDDFWQMVLENNSNVIAMIT-REIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSV 232
Cdd:PHA02747  105 TCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKI 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 233 KQLQFTKWPDHGTPASADSFIKYIR------------YARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNI 300
Cdd:PHA02747  185 SHFQCSEWFEDETPSDHPDFIKFIKiidinrkksgklFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICL 264

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1002623460 301 MDIVAQMREQRSGMVQTKEQYHF---CYDIVLEVLRKLLTLD 339
Cdd:PHA02747  265 AKTAEKIREQRHAGIMNFDDYLFiqpGYEVLHYFLSKIKAID 306
 
Name Accession Description Interval E-value
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 127-333 1.46e-140

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: 396.43  E-value: 1.46e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 206
Cdd:cd14596     1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 207 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCVD 286
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICVD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1002623460 287 VVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 333
Cdd:cd14596   161 VLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 127-332 5.92e-136

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: 384.80  E-value: 5.92e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPL-ELKHFRVFL 205
Cdd:cd14538     1 YINASHIRIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLiCGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 206 ENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCV 285
Cdd:cd14538    81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNSGPIVVHCSAGIGRTGVLITI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1002623460 286 DVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 332
Cdd:cd14538   161 DVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
78-330 4.30e-112

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 326.15  E-value: 4.30e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460   78 IMQEFMAL-ELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPL----GKSKDYINASYIRIVNCGEEYfyIATQGPLL 152
Cdd:smart00194   2 LEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLkpppGEGSDYINASYIDGPNGPKAY--IATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  153 STIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSV 232
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  233 KQLQFTKWPDHGTPASADSFIKYIRYARK--SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQ 310
Cdd:smart00194 160 THYHYTNWPDHGVPESPESILDLIRAVRKsqSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                          250       260
                   ....*....|....*....|
gi 1002623460  311 RSGMVQTKEQYHFCYDIVLE 330
Cdd:smart00194 240 RPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
102-330 4.00e-108

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 314.95  E-value: 4.00e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 102 NREKNRYRDILPYDSTRVPLGKSK---DYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIE 178
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPgpsDYINASYIDGYK--KPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 179 GGIIKCYHYWPISLKKPLELKHFRVFLENY-QILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIR 257
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002623460 258 YARKSHL---TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 330
Cdd:pfam00102 159 KVRKSSLdgrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 102-332 6.12e-100

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: 294.43  E-value: 6.12e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 102 NREKNRYRDILPYDSTRVPLGKSKDYINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGI 181
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPLGDEGGYINASFIKMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEGGK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 182 IKCYHYWPISLKKPLEL-KHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR 260
Cdd:cd14597    83 IKCQRYWPEILGKTTMVdNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFISYMR 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002623460 261 KSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 332
Cdd:cd14597   163 HIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILYVL 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 127-326 3.97e-86

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: 257.98  E-value: 3.97e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 206
Cdd:cd00047     1 YINASYIDGYRGPKEY--IATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 207 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKS--HLTGPMVVHCSAGIGRTGVFLC 284
Cdd:cd00047    79 SEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEarKPNGPIVVHCSAGVGRTGTFIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1002623460 285 VDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 326
Cdd:cd00047   159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 78-325 2.22e-74

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: 230.71  E-value: 2.22e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  78 IMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPLGK-----SKDYINASYIrivncgEEY----FYIATQ 148
Cdd:cd14543     5 IYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKrngdeRTDYINANFM------DGYkqknAYIATQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 149 GPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGT 228
Cdd:cd14543    79 GPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 229 SHSVKQLQFTKWPDHGTPASADSFIKYIRYAR--------------KSHLTG-PMVVHCSAGIGRTGVFLCVDVVFCAIV 293
Cdd:cd14543   159 SRQVTHFQFTSWPDFGVPSSAAALLDFLGEVRqqqalavkamgdrwKGHPPGpPIVVHCSAGIGRTGTFCTLDICLSQLE 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1002623460 294 KNCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 325
Cdd:cd14543   239 DVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 107-323 4.47e-72

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: 223.00  E-value: 4.47e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 107 RYRDILPYDSTRVPLGKS-----KDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGI 181
Cdd:cd14548     1 RYTNILPYDHSRVKLIPIneeegSDYINANYIPGYNSPREF--IATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 182 IKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQVveKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARK 261
Cdd:cd14548    79 VKCDHYWPFD-QDPVYYGDITVTMLSESVLPDWTIREFKL--ERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002623460 262 S--HLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHF 323
Cdd:cd14548   156 YikQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 127-326 1.69e-70

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: 218.66  E-value: 1.69e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIrIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRV-FL 205
Cdd:cd18533     1 YINASYI-TLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWP-SGEYEGEYGDLTVeLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 206 ENYQI-LQYFIIRMFQVVeKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARK----SHLTGPMVVHCSAGIGRTG 280
Cdd:cd18533    79 SEEENdDGGFIVREFELS-KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElndsASLDPPIIVHCSAGVGRTG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002623460 281 VFLCVDVVF---------CAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 326
Cdd:cd18533   158 TFIALDSLLdelkrglsdSQDLEDSEDPVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 98-325 2.12e-69

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: 216.62  E-value: 2.12e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  98 NQPSNREKNRYRDILPYDSTRVPLG-----KSKDYINASYIRivncGEEY--FYIATQGPLLSTIDDFWQMVLENNSNVI 170
Cdd:cd14554     2 NLPCNKFKNRLVNILPYESTRVCLQpirgvEGSDYINASFID----GYRQrgAYIATQGPLAETTEDFWRMLWEHNSTII 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 171 AMITREIEGGIIKCYHYWPisLKKPLELKHFRVF-LENYQILQYfIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASA 249
Cdd:cd14554    78 VMLTKLREMGREKCHQYWP--AERSARYQYFVVDpMAEYNMPQY-ILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 250 DSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 325
Cdd:cd14554   155 EGFIDFIGQVHKTKeqfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCY 234
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 99-334 8.70e-68

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: 213.94  E-value: 8.70e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  99 QPSNREKNRYRDILPYDSTRVPLGKSKDYINASYIRI----VNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMIT 174
Cdd:cd14600    37 LPQNMDKNRYKDVLPYDATRVVLQGNEDYINASYVNMeipsANIVNKY--IATQGPLPHTCAQFWQVVWEQKLSLIVMLT 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 175 REIEGGIIKCYHYWPiSLKKPLELKHFRVFL--ENYQILqyFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSF 252
Cdd:cd14600   115 TLTERGRTKCHQYWP-DPPDVMEYGGFRVQChsEDCTIA--YVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDF 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 253 IKYIRYARKSHLTG-PMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEV 331
Cdd:cd14600   192 LEFVNYVRSKRVENePVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRV 271


                  ...
gi 1002623460 332 LRK 334
Cdd:cd14600   272 YEE 274
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 102-330 2.59e-67

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: 211.49  E-value: 2.59e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 102 NREKNRYRDILPYDSTRVPLGKSK-----DYINASYI---RIVNCgeeyfYIATQGPLLSTIDDFWQMVLENNSNVIAMI 173
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEgvpgsDYINANYCdgyRKQNA-----YIATQGPLPETFGDFWRMVWEQRSATIVMM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 174 TREIEGGIIKCYHYWPISLKKPLELKHfrVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFI 253
Cdd:cd14553    78 TKLEERSRVKCDQYWPTRGTETYGLIQ--VTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002623460 254 KYIRYARKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 330
Cdd:cd14553   156 AFLRRVKACNPpdAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 105-325 2.79e-67

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: 211.10  E-value: 2.79e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 105 KNRYRDILPYDSTRVPL---GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGI 181
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVklkQGDNDYINASLVEVEEAKRSY--ILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 182 IKCYHYWPISLKKPLELKH--FRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYA 259
Cdd:cd14545    79 IKCAQYWPQGEGNAMIFEDtgLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002623460 260 RKSHL----TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKN--CSFNIMDIVAQMREQRSGMVQTKEQYHFCY 325
Cdd:cd14545   159 RESGSlssdVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGnpSSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 95-331 1.23e-66

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: 210.45  E-value: 1.23e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  95 NSGNQPSNREKNRYRDILPYDSTRVPL------GKSkDYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSN 168
Cdd:cd14603    23 VAGGRKENVKKNRYKDILPYDQTRVILsllqeeGHS-DYINANFIKGVD--GSRAYIATQGPLSHTVLDFWRMIWQYGVK 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 169 VIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRV-FLENYQILQYFIIRMFQVVEKStgTSHSVKQLQFTKWPDHGTPA 247
Cdd:cd14603   100 VILMACREIEMGKKKCERYWA-QEQEPLQTGPFTItLVKEKRLNEEVILRTLKVTFQK--ESRSVSHFQYMAWPDHGIPD 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 248 SADSFIKYIRYARKSHLTG--PMVVHCSAGIGRTGVFLCVDVVFCAIVKNC---SFNIMDIVAQMREQRSGMVQTKEQYH 322
Cdd:cd14603   177 SPDCMLAMIELARRLQGSGpePLCVHCSAGCGRTGVICTVDYVRQLLLTQRippDFSIFDVVLEMRKQRPAAVQTEEQYE 256


                  ....*....
gi 1002623460 323 FCYDIVLEV 331
Cdd:cd14603   257 FLYHTVAQM 265
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 102-325 4.72e-66

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: 208.47  E-value: 4.72e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 102 NREKNRYRDILPYDSTRVPLG------KSKDYINASYIRIVNCGEEYF-----YIATQGPLLSTIDDFWQMVLENNSNVI 170
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKdrdpnvPGSDYINANYIRNENEGPTTDenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 171 AMITREIEGGIIKCYHYWPISLKKPlELKHFRVFLENYQILQYFIIRMFQVVEKSTGTS-HSVKQLQFTKWPDHGTPASA 249
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQK-QYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPiREIWHYQYLSWPDHGVPSDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 250 D---SFIKYIRYaRKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKN---CSFNIMDIVAQMREQRSGMVQTKEQY 321
Cdd:cd14544   160 GgvlNFLEDVNQ-RQESLphAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKgldCDIDIQKTIQMVRSQRSGMVQTEAQY 238


                  ....
gi 1002623460 322 HFCY 325
Cdd:cd14544   239 KFIY 242
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 106-323 1.52e-65

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: 206.48  E-value: 1.52e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 106 NRYRDILPYDSTRVPLGKSKD-----YINASYIRIVNcGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGG 180
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDdplssYINANYIRGYD-GEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 181 iIKCYHYWPIslKKPLELKHFRVFLENYQILQYFIIRmfQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIR--- 257
Cdd:cd14547    80 -EKCAQYWPE--EENETYGDFEVTVQSVKETDGYTVR--KLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQeve 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002623460 258 -YARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHF 323
Cdd:cd14547   155 eARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 106-332 9.90e-64

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: 202.04  E-value: 9.90e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 106 NRYRDILPYDSTRVPLGKSK-----DYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGG 180
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHeepgsDYINANYMPGYWSSQEF--IATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 181 IIKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR 260
Cdd:cd14619    79 RVKCEHYWPLD-YTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002623460 261 K---SHL-TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 332
Cdd:cd14619   158 QwldQTMsGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 67-333 1.40e-63

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: 203.30  E-value: 1.40e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  67 KILEEKTAAYDIMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPLGKSKD----YINASYIRIVNCGEEY 142
Cdd:cd14599     3 KTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKEnntgYINASHIKVTVGGEEW 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 143 FYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPislkkPLELKHFRVFLENYQILQYF-------I 215
Cdd:cd14599    83 HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWP-----KLGSKHSSATYGKFKVTTKFrtdsgcyA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 216 IRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKY---IRYARK---------SHLTGPMVVHCSAGIGRTGVFL 283
Cdd:cd14599   158 TTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYleeIQSVRRhtnsmldstKNCNPPIVVHCSAGVGRTGVVI 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002623460 284 CVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 333
Cdd:cd14599   238 LTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 83-332 1.83e-63

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: 203.43  E-value: 1.83e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  83 MALELKNLP------GEFNSGNQPSNREKNRYRDILPYDSTRVPLG-----KSKDYINASYIRivNCGEEYFYIATQGPL 151
Cdd:cd14627    28 MELEFKRLAnskahtSRFISANLPCNKFKNRLVNIMPYETTRVCLQpirgvEGSDYINASFID--GYRQQKAYIATQGPL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 152 LSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVF-LENYQILQYfIIRMFQVVEKSTGTSH 230
Cdd:cd14627   106 AETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPA--ERSARYQYFVVDpMAEYNMPQY-ILREFKVTDARDGQSR 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 231 SVKQLQFTKWPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQ 306
Cdd:cd14627   183 TVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKeqfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKM 262

                         250       260
                  ....*....|....*....|....*.
gi 1002623460 307 MREQRSGMVQTKEQYHFCYDIVLEVL 332
Cdd:cd14627   263 LRTQRPAMVQTEDEYQFCYQAALEYL 288
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 127-332 3.34e-63

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: 199.99  E-value: 3.34e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKK--PLELKHFRVF 204
Cdd:cd14540     1 YINASHITATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEhdALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 205 LENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR--KSHLTG---------PMVVHCS 273
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINsvRRHTNQdvaghnrnpPTLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002623460 274 AGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 332
Cdd:cd14540   161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 106-325 1.36e-61

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: 196.29  E-value: 1.36e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 106 NRYRDILPYDSTRVPLGK-----SKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGG 180
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNvdddpCSDYINASYIPGNNFRREY--IATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 181 IIKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHS-VKQLQFTKWPDHGTPASADSFIKYIR-- 257
Cdd:cd14617    79 RVKCDHYWPAD-QDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRlVRHFHYTVWPDHGVPETTQSLIQFVRtv 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 258 --YARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 325
Cdd:cd14617   158 rdYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 83-332 2.57e-61

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: 197.65  E-value: 2.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  83 MALELKNLPG------EFNSGNQPSNREKNRYRDILPYDSTRVPLG-----KSKDYINASYIRivNCGEEYFYIATQGPL 151
Cdd:cd14628    27 MELEFKRLASskahtsRFISANLPCNKFKNRLVNIMPYESTRVCLQpirgvEGSDYINASFID--GYRQQKAYIATQGPL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 152 LSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVF-LENYQILQYfIIRMFQVVEKSTGTSH 230
Cdd:cd14628   105 AETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPA--ERSARYQYFVVDpMAEYNMPQY-ILREFKVTDARDGQSR 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 231 SVKQLQFTKWPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQ 306
Cdd:cd14628   182 TVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKeqfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKM 261

                         250       260
                  ....*....|....*....|....*.
gi 1002623460 307 MREQRSGMVQTKEQYHFCYDIVLEVL 332
Cdd:cd14628   262 LRTQRPAMVQTEDQYQFCYRAALEYL 287
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 127-326 9.00e-60

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: 190.64  E-value: 9.00e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPisLKKPLELKHFRVFLE 206
Cdd:cd14549     1 YINANYVDGYNKARAY--IATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWP--KEGTETYGNIQVTLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 207 NYQILQYFIIRMFQV------VEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIR--YARKSHLTGPMVVHCSAGIGR 278
Cdd:cd14549    77 STEVLATYTVRTFSLknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRksSAANPPGAGPIVVHCSAGVGR 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1002623460 279 TGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 326
Cdd:cd14549   157 TGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 126-331 1.77e-59

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: 190.23  E-value: 1.77e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 126 DYINASYIR-------IVNcgeeyFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPiSLKKPLEL 198
Cdd:cd14541     1 DYINANYVNmeipgsgIVN-----RYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWP-DLGETMQF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 199 KHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTG--PMVVHCSAGI 276
Cdd:cd14541    75 GNLQITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMvePTVVHCSAGI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002623460 277 GRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEV 331
Cdd:cd14541   155 GRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 83-332 6.94e-59

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: 191.48  E-value: 6.94e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  83 MALELKNLPG------EFNSGNQPSNREKNRYRDILPYDSTRVPLG-----KSKDYINASYIRivNCGEEYFYIATQGPL 151
Cdd:cd14629    28 MELEFKLLANskahtsRFISANLPCNKFKNRLVNIMPYELTRVCLQpirgvEGSDYINASFID--GYRQQKAYIATQGPL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 152 LSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVF-LENYQILQYfIIRMFQVVEKSTGTSH 230
Cdd:cd14629   106 AETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPA--ERSARYQYFVVDpMAEYNMPQY-ILREFKVTDARDGQSR 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 231 SVKQLQFTKWPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQ 306
Cdd:cd14629   183 TIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKeqfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKT 262

                         250       260
                  ....*....|....*....|....*.
gi 1002623460 307 MREQRSGMVQTKEQYHFCYDIVLEVL 332
Cdd:cd14629   263 LRTQRPAMVQTEDQYQLCYRAALEYL 288
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 106-323 3.48e-58

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: 187.72  E-value: 3.48e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 106 NRYRDILPYDSTRVPLG----KSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGI 181
Cdd:cd14615     1 NRYNNVLPYDISRVKLSvqshSTDDYINANYMPGYNSKKEF--IAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 182 IKCYHYWPISLKKplELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYiRYARK 261
Cdd:cd14615    79 TKCEEYWPSKQKK--DYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINF-RHLVR 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002623460 262 SHLT-----GPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHF 323
Cdd:cd14615   156 EYMKqnppnSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 96-329 4.73e-58

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: 187.79  E-value: 4.73e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  96 SGNQPSNREKNRYRDILPYDSTRVPL-----GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVI 170
Cdd:cd14614     6 AADLPVNRCKNRYTNILPYDFSRVKLvsmheEEGSDYINANYIPGYNSPQEY--IATQGPLPETRNDFWKMVLQQKSQII 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 171 AMITREIEGGIIKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQVveKSTGTSHSVKQLQFTKWPDHGTPA--S 248
Cdd:cd14614    84 VMLTQCNEKRRVKCDHYWPFT-EEPVAYGDITVEMLSEEEQPDWAIREFRV--SYADEVQDVMHFNYTAWPDHGVPTanA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 249 ADSFIKYIRYARKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 326
Cdd:cd14614   161 AESILQFVQMVRQQAVksKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                  ...
gi 1002623460 327 IVL 329
Cdd:cd14614   241 CVQ 243
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 95-336 9.28e-58

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: 188.60  E-value: 9.28e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  95 NSGNQPSNREKNRYRDILPYDSTRVPL-----GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNV 169
Cdd:cd14604    50 ATGEKEENVKKNRYKDILPFDHSRVKLtlktsSQDSDYINANFIKGVYGPKAY--IATQGPLANTVIDFWRMIWEYNVAI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 170 IAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVveKSTGTSHSVKQLQFTKWPDHGTPASA 249
Cdd:cd14604   128 IVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLL--EFQNETRRLYQFHYVNWPDHDVPSSF 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 250 DSFIKYIRYARK--SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNC---SFNIMDIVAQMREQRSGMVQTKEQYHFC 324
Cdd:cd14604   206 DSILDMISLMRKyqEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELV 285

                         250
                  ....*....|..
gi 1002623460 325 YDIVLEVLRKLL 336
Cdd:cd14604   286 HRAIAQLFEKQL 297
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 98-332 1.14e-57

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: 187.94  E-value: 1.14e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  98 NQPSNREKNRYRDILPYDSTRVPL-------GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVI 170
Cdd:cd17667    23 NHPDNKHKNRYINILAYDHSRVKLrplpgkdSKHSDYINANYVDGYNKAKAY--IATQGPLKSTFEDFWRMIWEQNTGII 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 171 AMITREIEGGIIKCYHYWPISLKKplELKHFRVFLENYQILQYFIIRMFQVVE-----------KSTGTSHSVKQLQFTK 239
Cdd:cd17667   101 VMITNLVEKGRRKCDQYWPTENSE--EYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpKGRQNERTVIQYHYTQ 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 240 WPDHGTPASADSFIKYIRY---ARKSHLtGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQ 316
Cdd:cd17667   179 WPDMGVPEYALPVLTFVRRssaARTPEM-GPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQ 257

                         250
                  ....*....|....*.
gi 1002623460 317 TKEQYHFCYDIVLEVL 332
Cdd:cd17667   258 TEEQYIFIHDALLEAI 273
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 102-325 2.16e-57

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: 186.38  E-value: 2.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 102 NREKNRYRDILPYDSTRV------PLGKSKDYINASYI------RIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNV 169
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVvlhdgdPNEPVSDYINANIImpefetKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 170 IAMITREIEGGIIKCYHYWP--ISLKkplELKHFRVFLENYQILQYFIIRMFQVVEKSTG-TSHSVKQLQFTKWPDHGTP 246
Cdd:cd14605    82 IVMTTKEVERGKSKCVKYWPdeYALK---EYGVMRVRNVKESAAHDYILRELKLSKVGQGnTERTVWQYHFRTWPDHGVP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 247 ASAD---SFIKYIRYARKSHL-TGPMVVHCSAGIGRTGVFLCVDVVFCAIVK---NCSFNIMDIVAQMREQRSGMVQTKE 319
Cdd:cd14605   159 SDPGgvlDFLEEVHHKQESIMdAGPVVVHCSAGIGRTGTFIVIDILIDIIREkgvDCDIDVPKTIQMVRSQRSGMVQTEA 238


                  ....*.
gi 1002623460 320 QYHFCY 325
Cdd:cd14605   239 QYRFIY 244
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 100-325 2.71e-57

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: 185.81  E-value: 2.71e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 100 PSNREKNRYRDILPYDSTRVPLGKSK------DYINASYIRIVNcGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMI 173
Cdd:cd14612    13 PGHASKDRYKTILPNPQSRVCLRRAGsqeeegSYINANYIRGYD-GKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 174 TREIEGGiIKCYHYWPislKKPLELKHFRVFLENYQILQYFIIRmfQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFI 253
Cdd:cd14612    92 TKLKEKK-EKCVHYWP---EKEGTYGRFEIRVQDMKECDGYTIR--DLTIQLEEESRSVKHYWFSSWPDHQTPESAGPLL 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002623460 254 KYIRYARKSHLT----GPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 325
Cdd:cd14612   166 RLVAEVEESRQTaaspGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 100-330 8.35e-57

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: 185.61  E-value: 8.35e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 100 PSNREKNRYRDILPYDSTRVPLGKS-KDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIE 178
Cdd:cd14608    23 PKNKNRNRYRDVSPFDHSRIKLHQEdNDYINASLIKMEEAQRSY--ILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVME 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 179 GGIIKCYHYWPISLKKPL--ELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYI 256
Cdd:cd14608   101 KGSLKCAQYWPQKEEKEMifEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 257 RYARKSHLT----GPMVVHCSAGIGRTGVFLCVDVVFCAIVKN---CSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVL 329
Cdd:cd14608   181 FKVRESGSLspehGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVI 260


                  .
gi 1002623460 330 E 330
Cdd:cd14608   261 E 261
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 85-325 3.22e-56

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: 183.63  E-value: 3.22e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  85 LELKNLPGE--FNSGNQPSNREKNRYRDILPYDSTRVPLGKSK-DYINASYIRIVNCgeEYFYIATQGPLLSTIDDFWQM 161
Cdd:cd14607     5 LEIRNESHDypHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEnDYINASLVVIEEA--QRSYILTQGPLPNTCCHFWLM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 162 VLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKH--FRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTK 239
Cdd:cd14607    83 VWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 240 WPDHGTPASADSFIKYIRYARKSHL----TGPMVVHCSAGIGRTGVFLCVD--VVFCAIVKNCSFNIMDIVAQMREQRSG 313
Cdd:cd14607   163 WPDFGVPESPASFLNFLFKVRESGSlspeHGPAVVHCSAGIGRSGTFSLVDtcLVLMEKKDPDSVDIKQVLLDMRKYRMG 242

                         250
                  ....*....|..
gi 1002623460 314 MVQTKEQYHFCY 325
Cdd:cd14607   243 LIQTPDQLRFSY 254
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 127-325 3.18e-55

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: 179.16  E-value: 3.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 206
Cdd:cd14542     1 YINANFIKGVS--GSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 207 NYQILQY-FIIRMFQVveKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARK--SHLTGPMVVHCSAGIGRTGVFL 283
Cdd:cd14542    79 KEKRVGPdFLIRTLKV--TFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDyqGSEDVPICVHCSAGCGRTGTIC 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1002623460 284 CVDVVFCAI---VKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 325
Cdd:cd14542   157 AIDYVWNLLktgKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 105-331 9.69e-55

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: 178.88  E-value: 9.69e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 105 KNRYRDILPYDSTRVPLG-----KSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEG 179
Cdd:cd14602     1 KNRYKDILPYDHSRVELSlitsdEDSDYINANFIKGVYGPRAY--IATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 180 GIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVveKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYA 259
Cdd:cd14602    79 GKKKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKV--KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002623460 260 R--KSHLTGPMVVHCSAGIGRTGVFLCVDVVFC----AIVKNCsFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEV 331
Cdd:cd14602   157 RcyQEDDSVPICIHCSAGCGRTGVICAIDYTWMllkdGIIPEN-FSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 102-330 1.37e-54

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: 178.68  E-value: 1.37e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 102 NREKNRYRDILPYDSTRVPL-----GKSKDYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITRE 176
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLqlldgDPHSDYINANYIDGYH--RPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 177 IEGGIIKCYHYWPISLKKPLELKhfrVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYI 256
Cdd:cd14630    81 VEVGRVKCVRYWPDDTEVYGDIK---VTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFV 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002623460 257 RYAR--KSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 330
Cdd:cd14630   158 RQVKflNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 97-330 5.01e-54

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: 178.15  E-value: 5.01e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  97 GNQPSNREKNRYRDILPYDSTRVPLGKS------KDYINASYIR---IVNCGEEYFYIATQGPLLSTIDDFWQMVLENNS 167
Cdd:cd14606    13 GQRPENKSKNRYKNILPFDHSRVILQGRdsnipgSDYINANYVKnqlLGPDENAKTYIASQGCLEATVNDFWQMAWQENS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 168 NVIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRVFLENYQILQYFIIRMFQV-VEKSTGTSHSVKQLQFTKWPDHGTP 246
Cdd:cd14606    93 RVIVMTTREVEKGRNKCVPYWP-EVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVsPLDNGELIREIWHYQYLSWPDHGVP 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 247 ASAD---SFIKYIRYARKS-HLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVK---NCSFNIMDIVAQMREQRSGMVQTKE 319
Cdd:cd14606   172 SEPGgvlSFLDQINQRQESlPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTkglDCDIDIQKTIQMVRAQRSGMVQTEA 251

                         250
                  ....*....|.
gi 1002623460 320 QYHFCYDIVLE 330
Cdd:cd14606   252 QYKFIYVAIAQ 262
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 80-330 4.94e-53

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: 175.99  E-value: 4.94e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  80 QEFMALElknlPGE---FNSGNQPSNREKNRYRDILPYDSTRVPLGK-----SKDYINASYI---RIVNCgeeyfYIATQ 148
Cdd:cd14626    20 QEYESID----PGQqftWENSNLEVNKPKNRYANVIAYDHSRVILTSvdgvpGSDYINANYIdgyRKQNA-----YIATQ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 149 GPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELkhFRVFLENYQILQYFIIRMFQVVEKSTGT 228
Cdd:cd14626    91 GPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGM--IQVTLLDTVELATYSVRTFALYKNGSSE 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 229 SHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQ 306
Cdd:cd14626   169 KREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPpdAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTC 248

                         250       260
                  ....*....|....*....|....
gi 1002623460 307 MREQRSGMVQTKEQYHFCYDIVLE 330
Cdd:cd14626   249 MRSQRNYMVQTEDQYIFIHEALLE 272
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 91-330 6.66e-53

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: 175.63  E-value: 6.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  91 PGEFNSGNQPSNREKNRYRDILPYDSTRVPLG-----KSKDYINASYIrIVNCGEEYFYIATQGPLLSTIDDFWQMVLEN 165
Cdd:cd14610    33 PNATNVAQREENVQKNRSLAVLPYDHSRIILKaenshSHSDYINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWES 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 166 NSNVIAMITREIEGGIIKCYHYWPislKKPLELKH-FRVFLENYQI-LQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDH 243
Cdd:cd14610   112 GCVVIVMLTPLAENGVKQCYHYWP---DEGSNLYHiYEVNLVSEHIwCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQ 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 244 GTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNC-SFNIMDIVAQMREQRSGMVQTKEQ 320
Cdd:cd14610   189 GVPASTRSLLDFRRKVNKCYrgRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAkEIDIAATLEHLRDQRPGMVQTKEQ 268

                         250
                  ....*....|
gi 1002623460 321 YHFCYDIVLE 330
Cdd:cd14610   269 FEFALTAVAE 278
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 94-330 1.62e-52

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: 174.46  E-value: 1.62e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  94 FNSGNQPSNREKNRYRDILPYDSTRVPL-----GKSKDYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSN 168
Cdd:cd14633    32 WDSAKKDENRMKNRYGNIIAYDHSRVRLqpiegETSSDYINGNYIDGYH--RPNHYIATQGPMQETIYDFWRMVWHENTA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 169 VIAMITREIEGGIIKCYHYWPISLKKpleLKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPAS 248
Cdd:cd14633   110 SIIMVTNLVEVGRVKCCKYWPDDTEI---YKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYH 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 249 ADSFIKYIRY--ARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 326
Cdd:cd14633   187 ATGLLGFVRQvkSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 266


                  ....
gi 1002623460 327 IVLE 330
Cdd:cd14633   267 AILE 270
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 105-325 3.64e-52

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: 172.02  E-value: 3.64e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 105 KNRYRDILPYDSTRVPLgKSKD-------YINASYIRIVNcGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREI 177
Cdd:cd14611     2 KNRYKTILPNPHSRVCL-KPKNsndslstYINANYIRGYG-GKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 178 EGGIiKCYHYWPislKKPLELKHFRVFLENYQILQYFIIRmfQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKY-- 255
Cdd:cd14611    80 EKNE-KCVLYWP---EKRGIYGKVEVLVNSVKECDNYTIR--NLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLml 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002623460 256 -IRYARKSHLT-GPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 325
Cdd:cd14611   154 dVEEDRLASPGrGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 126-334 3.69e-52

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: 171.67  E-value: 3.69e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 126 DYINASYI--RIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRV 203
Cdd:cd14601     1 DYINANYInmEIPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP-EPSGSSSYGGFQV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 204 FLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR--KSHLTGPMVVHCSAGIGRTGV 281
Cdd:cd14601    80 TCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRnkRAGKDEPVVVHCSAGIGRTGV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002623460 282 FLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLRK 334
Cdd:cd14601   160 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 80-332 8.98e-52

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: 172.97  E-value: 8.98e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  80 QEFMALElknlPGE---FNSGNQPSNREKNRYRDILPYDSTRVPLGK-----SKDYINASYIRivNCGEEYFYIATQGPL 151
Cdd:cd14625    26 QEYESID----PGQqftWEHSNLEVNKPKNRYANVIAYDHSRVILQPiegimGSDYINANYID--GYRKQNAYIATQGPL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 152 LSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPislKKPLELKHF-RVFLENYQILQYFIIRMFQVVEKSTGTSH 230
Cdd:cd14625   100 PETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP---SRGTETYGMiQVTLLDTIELATFCVRTFSLHKNGSSEKR 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 231 SVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMR 308
Cdd:cd14625   177 EVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPpdAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMR 256

                         250       260
                  ....*....|....*....|....
gi 1002623460 309 EQRSGMVQTKEQYHFCYDIVLEVL 332
Cdd:cd14625   257 SQRNYMVQTEDQYSFIHDALLEAV 280
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 127-326 1.82e-51

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: 169.49  E-value: 1.82e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIR-IVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFL 205
Cdd:cd14539     1 YINASLIEdLTPYCPRF--IATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 206 ENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIR-----YARKSHLTGPMVVHCSAGIGRTG 280
Cdd:cd14539    79 QSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEevhshYLQQRSLQTPIVVHCSSGVGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002623460 281 VFlCvdVVFCAIVK----NCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 326
Cdd:cd14539   159 AF-C--LLYAAVQEieagNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 106-329 2.97e-51

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: 169.74  E-value: 2.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 106 NRYRDILPYDSTRVPLGK-----SKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGG 180
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQlggepHSDYINANFIPGYTSPQEF--IATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 181 IIKCYHYWPISLkKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR 260
Cdd:cd14618    79 RVLCDHYWPSES-TPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002623460 261 K----SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVL 329
Cdd:cd14618   158 EhvqaTKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 80-332 1.98e-50

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: 169.53  E-value: 1.98e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  80 QEFMALElknlPGE---FNSGNQPSNREKNRYRDILPYDSTRVPLGK-----SKDYINASYIRivNCGEEYFYIATQGPL 151
Cdd:cd14624    26 QEYESID----PGQqftWEHSNLEVNKPKNRYANVIAYDHSRVLLSAiegipGSDYINANYID--GYRKQNAYIATQGAL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 152 LSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELkhFRVFLENYQILQYFIIRMFQVVEKSTGTSHS 231
Cdd:cd14624   100 PETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGL--IQVTLLDTVELATYCVRTFALYKNGSSEKRE 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 232 VKQLQFTKWPDHGTPASADSFIKYIRYARKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMRE 309
Cdd:cd14624   178 VRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPpdAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRA 257

                         250       260
                  ....*....|....*....|...
gi 1002623460 310 QRSGMVQTKEQYHFCYDIVLEVL 332
Cdd:cd14624   258 QRNYMVQTEDQYIFIHDALLEAV 280
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
98-337 7.26e-50

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 167.96  E-value: 7.26e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  98 NQPSNREKNRYRDILPYDSTRVplGKSKDYINASYIRIvncGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREI 177
Cdd:COG5599    38 QNINGSPLNRFRDIQPYKETAL--RANLGYLNANYIQV---IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 178 EGG--IIKCYHYWPIS---LKKPLELKHfrvfLENYQILQYFIIRMFQVVEKSTG-TSHSVKQLQFTKWPDHGTPaSADS 251
Cdd:COG5599   113 EISkpKVKMPVYFRQDgeyGKYEVSSEL----TESIQLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAI-SAEA 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 252 FIKYIRYARKSHLT-----GPMVVHCSAGIGRTGVFLCVDVVFCAI--VKNCSFNIMDIVAQMREQR-SGMVQTKEQYHF 323
Cdd:COG5599   188 LKNLADLIDKKEKIkdpdkLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRnGGMVQTSEQLDV 267

                         250
                  ....*....|....
gi 1002623460 324 CYDIVLEVLRKLLT 337
Cdd:COG5599   268 LVKLAEQQIRPLLR 281
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 127-325 8.67e-50

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: 165.33  E-value: 8.67e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEG-GIIKCYHYWPISLKKPLELKHFRVFL 205
Cdd:cd17658     1 YINASLVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNySTAKCADYFPAEENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 206 ENYQILQYFI-IRMFQVVE-KSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRyaRKSHL---TGPMVVHCSAGIGRTG 280
Cdd:cd17658    81 KKLKHSQHSItLRVLEVQYiESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLK--RLYGIppsAGPIVVHCSAGIGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1002623460 281 VFLCVDVVFCAIVKN--CSFNIMDIVAQMREQRSGMVQTKEQYHFCY 325
Cdd:cd17658   159 AYCTIHNTIRRILEGdmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 127-330 1.53e-49

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: 164.32  E-value: 1.53e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKpleLKHFRVFLE 206
Cdd:cd14555     1 YINANYIDGYH--RPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV---YGDIKVTLV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 207 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGVFLC 284
Cdd:cd14555    76 ETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNppSAGPIVVHCSAGAGRTGCYIV 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1002623460 285 VDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 330
Cdd:cd14555   156 IDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 127-326 2.65e-49

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: 164.00  E-value: 2.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPisLKKPLELKHFRVFLE 206
Cdd:cd17668     1 YINANYVDGYN--KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP--ADGSEEYGNFLVTQK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 207 NYQILQYFIIRMFQV--------VEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR--KSHLTGPMVVHCSAGI 276
Cdd:cd17668    77 SVQVLAYYTVRNFTLrntkikkgSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASyaKRHAVGPVVVHCSAGV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002623460 277 GRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 326
Cdd:cd17668   157 GRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 108-330 2.66e-49

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: 164.73  E-value: 2.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 108 YRDILPYDSTRVPL-----GKSKDYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGII 182
Cdd:cd14620     1 YPNILPYDHSRVILsqldgIPCSDYINASYID--GYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 183 KCYHYWPIslKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHS---VKQLQFTKWPDHG---TPASADSFIKYI 256
Cdd:cd14620    79 KCYQYWPD--QGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAprlVTQLHFTSWPDFGvpfTPIGMLKFLKKV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002623460 257 RYARKSHlTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 330
Cdd:cd14620   157 KSVNPVH-AGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 91-330 3.00e-49

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: 166.37  E-value: 3.00e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  91 PGEFNSGNQPSNREKNRYRDILPYDSTRVPLG-----KSKDYINASYIrIVNCGEEYFYIATQGPLLSTIDDFWQMVLEN 165
Cdd:cd14609    31 PNTCSTAQGEANVKKNRNPDFVPYDHARIKLKaesnpSRSDYINASPI-IEHDPRMPAYIATQGPLSHTIADFWQMVWEN 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 166 NSNVIAMITREIEGGIIKCYHYWPislKKPLELKH-FRVFLENYQI-LQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDH 243
Cdd:cd14609   110 GCTVIVMLTPLVEDGVKQCDRYWP---DEGSSLYHiYEVNLVSEHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 244 GTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNC-SFNIMDIVAQMREQRSGMVQTKEQ 320
Cdd:cd14609   187 GIPSSTRPLLDFRRKVNKCYrgRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVkEIDIAATLEHVRDQRPGMVRTKDQ 266

                         250
                  ....*....|
gi 1002623460 321 YHFCYDIVLE 330
Cdd:cd14609   267 FEFALTAVAE 276
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 106-323 4.43e-49

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: 163.92  E-value: 4.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 106 NRYRDILPYDSTRVPL-----GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGG 180
Cdd:cd14616     1 NRFPNIKPYNNNRVKLiadagVPGSDYINASYISGYLCPNEF--IATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 181 IIKCYHYWPISlKKPLElkhfrVF--------LENYQIlqYFIIRMFQvVEKStGTSHSVKQLQFTKWPDHGTPASADSF 252
Cdd:cd14616    79 RIRCHQYWPED-NKPVT-----VFgdivitklMEDVQI--DWTIRDLK-IERH-GDYMMVRQCNFTSWPEHGVPESSAPL 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002623460 253 IKYIRYAR--KSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHF 323
Cdd:cd14616   149 IHFVKLVRasRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 127-333 3.93e-48

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: 161.30  E-value: 3.93e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPislkkPLELKHFRVFLE 206
Cdd:cd14598     1 YINASHIKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWP-----RLGSRHNTVTYG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 207 NYQILQYF-------IIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKY---IRYARKsHLTG---------P 267
Cdd:cd14598    76 RFKITTRFrtdsgcyATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeIQSVRR-HTNStidpkspnpP 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002623460 268 MVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 333
Cdd:cd14598   155 VLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 80-330 1.75e-47

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: 162.12  E-value: 1.75e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  80 QEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPLGK-----SKDYINASYIRivNCGEEYFYIATQGPLLST 154
Cdd:cd14621    30 EEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPvegvpDSDYINASFIN--GYQEKNKFIAAQGPKEET 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 155 IDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVFLENYQILQYFIIRMF--QVVEKSTGTSHS- 231
Cdd:cd14621   108 VNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPD--QGCWTYGNIRVSVEDVTVLVDYTVRKFciQQVGDVTNKKPQr 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 232 -VKQLQFTKWPDHGTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMR 308
Cdd:cd14621   186 lITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNpqYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIR 265

                         250       260
                  ....*....|....*....|..
gi 1002623460 309 EQRSGMVQTKEQYHFCYDIVLE 330
Cdd:cd14621   266 AQRCQMVQTDMQYVFIYQALLE 287
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 78-339 2.15e-47

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 162.48  E-value: 2.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  78 IMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPL----GKSKDYINASYIRIVNcgEEYFYIATQGPLLS 153
Cdd:PHA02747   27 IRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILdsggGSTSDYIHANWIDGFE--DDKKFIATQGPFAE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 154 TIDDFWQMVLENNSNVIAMIT-REIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSV 232
Cdd:PHA02747  105 TCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKI 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 233 KQLQFTKWPDHGTPASADSFIKYIR------------YARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNI 300
Cdd:PHA02747  185 SHFQCSEWFEDETPSDHPDFIKFIKiidinrkksgklFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICL 264

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1002623460 301 MDIVAQMREQRSGMVQTKEQYHF---CYDIVLEVLRKLLTLD 339
Cdd:PHA02747  265 AKTAEKIREQRHAGIMNFDDYLFiqpGYEVLHYFLSKIKAID 306
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 124-330 6.89e-47

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: 158.26  E-value: 6.89e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 124 SKDYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPislkKPLEL-KHFR 202
Cdd:cd14631    12 SSDYINANYID--GYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP----DDTEVyGDFK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 203 VFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTG 280
Cdd:cd14631    86 VTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNppSAGPIVVHCSAGAGRTG 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002623460 281 VFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 330
Cdd:cd14631   166 CYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 127-330 8.54e-47

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: 157.61  E-value: 8.54e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIrIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPislKKPLELKH-FRVFL 205
Cdd:cd14546     1 YINASTI-YDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP---EEGSEVYHiYEVHL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 206 ENYQIL-QYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGVF 282
Cdd:cd14546    77 VSEHIWcDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYrgRSCPIVVHCSDGAGRTGTY 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002623460 283 LCVDVVFCAIVKncSFNIMDIVA---QMREQRSGMVQTKEQYHFCYDIVLE 330
Cdd:cd14546   157 ILIDMVLNRMAK--GAKEIDIAAtleHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 127-328 8.99e-47

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: 157.43  E-value: 8.99e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVFLE 206
Cdd:cd14552     1 YINASFIDGYR--QKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPE--DGSVSSGDITVELK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 207 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL---TGPMVVHCSAGIGRTGVFL 283
Cdd:cd14552    77 DQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQqsgNHPITVHCSAGAGRTGTFC 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1002623460 284 CVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIV 328
Cdd:cd14552   157 ALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 105-328 2.04e-46

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: 158.10  E-value: 2.04e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 105 KNRYRDILPYDSTRVPLgKSKD-------YINASYIRIVNcGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEI 177
Cdd:cd14613    28 KNRYKTILPNPHSRVCL-TSPDqddplssYINANYIRGYG-GEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMIT-NI 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 178 EGGIIKCYHYWP----------ISLKKPLELKHFRvflenyqilqyfiIRMFQVveKSTGTSHSVKQLQFTKWPDHGTPA 247
Cdd:cd14613   105 EEMNEKCTEYWPeeqvtyegieITVKQVIHADDYR-------------LRLITL--KSGGEERGLKHYWYTSWPDQKTPD 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 248 SADSFIKYIR-------YARKSHltGPMVVHCSAGIGRTGVFLCVDVVfCAIVKNCS-FNIMDIVAQMREQRSGMVQTKE 319
Cdd:cd14613   170 NAPPLLQLVQeveearqQAEPNC--GPVIVHCSAGIGRTGCFIATSIC-CKQLRNEGvVDILRTTCQLRLDRGGMIQTCE 246


                  ....*....
gi 1002623460 320 QYHFCYDIV 328
Cdd:cd14613   247 QYQFVHHVL 255
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 63-330 1.18e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 157.47  E-value: 1.18e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  63 KDCLKILEEKTAAYDIMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPLGKSK---DYINASYIRIVNCG 139
Cdd:PHA02742   13 KNCEQLIEESNLAEILKEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDggdDFINASYVDGHNAK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 140 EEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMF 219
Cdd:PHA02742   93 GRF--ICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 220 QVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTG-------------PMVVHCSAGIGRTGVFLCVD 286
Cdd:PHA02742  171 CLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVREADLKAdvdikgenivkepPILVHCSAGLDRAGAFCAID 250

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1002623460 287 VVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 330
Cdd:PHA02742  251 ICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 127-330 1.77e-45

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: 154.05  E-value: 1.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKhfrVFLE 206
Cdd:cd14632     1 YINANYIDGYH--RSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIK---ITLL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 207 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL--TGPMVVHCSAGIGRTGVFLC 284
Cdd:cd14632    76 KTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPpdAGPVVVHCSAGAGRTGCYIV 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1002623460 285 VDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 330
Cdd:cd14632   156 LDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 127-321 9.05e-45

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: 151.90  E-value: 9.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 206
Cdd:cd14557     1 YINASYID--GFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKIN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 207 NYQILQYFIIRMFQVV-EKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRY--ARKSHLTGPMVVHCSAGIGRTGVFL 283
Cdd:cd14557    79 EEKICPDYIIRKLNINnKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRvnAFNNFFSGPIVVHCSAGVGRTGTYI 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1002623460 284 CVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQY 321
Cdd:cd14557   159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 127-326 2.18e-43

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: 148.31  E-value: 2.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKhfrVFLE 206
Cdd:cd14558     1 YINASFIDGYWGPKSL--IATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIE---VELK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 207 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR--------KSHLTGPMVVHCSAGIGR 278
Cdd:cd14558    76 DTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKqklpyknsKHGRSVPIVVHCSDGSSR 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 279 TGvflcvdvVFCAIvkncsFNIMD------------IVAQMREQRSGMVQTKEQYHFCYD 326
Cdd:cd14558   156 TG-------IFCAL-----WNLLEsaetekvvdvfqVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 127-325 6.86e-42

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: 144.67  E-value: 6.86e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKplELKHFRVFLE 206
Cdd:cd14551     1 YINASYID--GYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW--TYGNLRVRVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 207 NYQILQYFIIRMFQVVEKSTGTSHS----VKQLQFTKWPDHGTPASADSFIKYIRYArKSHLT---GPMVVHCSAGIGRT 279
Cdd:cd14551    77 DTVVLVDYTTRKFCIQKVNRGIGEKrvrlVTQFHFTSWPDFGVPFTPIGMLKFLKKV-KSANPpraGPIVVHCSAGVGRT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1002623460 280 GVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 325
Cdd:cd14551   156 GTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 126-328 5.54e-41

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: 142.45  E-value: 5.54e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 126 DYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVFL 205
Cdd:cd14622     1 DYINASFID--GYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPS--EGSVTHGEITIEI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 206 ENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL-TG--PMVVHCSAGIGRTGVF 282
Cdd:cd14622    77 KNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQqTGnhPIVVHCSAGAGRTGTF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1002623460 283 LCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIV 328
Cdd:cd14622   157 IALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 107-330 5.61e-40

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: 140.57  E-value: 5.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 107 RYRDILPYDSTRV--PLGKSK---DYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGI 181
Cdd:cd14623     1 RVLQIIPYEFNRViiPVKRGEentDYVNASFID--GYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 182 IKCYHYWPISlkKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARK 261
Cdd:cd14623    79 EKCAQYWPSD--GSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQK 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002623460 262 SHLTG---PMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 330
Cdd:cd14623   157 QQQQSgnhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PHA02738 PHA02738
hypothetical protein; Provisional
 57-328 1.47e-37

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 136.59  E-value: 1.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  57 HEQTAIKDCLKILEEKTAAYDIMQEFMALELKNLPGEFNSgnQPSNREKNRYRDILPYDSTRVPLGKSK---DYINASYI 133
Cdd:PHA02738    6 FRELKYAEFLALMEKSDCEEVITREHQKVISEKVDGTFNA--EKKNRKLNRYLDAVCFDHSRVILPAERnrgDYINANYV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 134 RivncGEEYF--YIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQIL 211
Cdd:PHA02738   84 D----GFEYKkkFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 212 QYFIIRMFQVVEkSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR---------------KSHLTGPMVVHCSAGI 276
Cdd:PHA02738  160 PHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRqcqkelaqeslqighNRLQPPPIVVHCNAGL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002623460 277 GRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIV 328
Cdd:PHA02738  239 GRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 53-332 1.70e-36

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 134.00  E-value: 1.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  53 IFNFHEQT-AIKDCLKILEEKTAAYDImqefmalelkNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPLGK-------- 123
Cdd:PHA02746   11 AFDFFDKTnHAKFCEFVLLEHAEVMDI----------PIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 124 ------------SKD----YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIKCYHY 187
Cdd:PHA02746   81 vgdsdgkkievtSEDnaenYIHANFVD--GFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLT-DIDDDDEKCFEL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 188 WpiSLKKPLELKHFRVFLENYQILQ--YFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARK---- 261
Cdd:PHA02746  158 W--TKEEDSELAFGRFVAKILDIIEelSFTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqae 235

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002623460 262 --------SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 332
Cdd:PHA02746  236 likqadndPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAI 314
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
231-330 4.02e-36

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 126.32  E-value: 4.02e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  231 SVKQLQFTKWPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVfCAIVKNCS--FNIMDIV 304
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLnqseSSGPVVVHCSAGVGRTGTFVAIDIL-LQQLEAEAgeVDIFDTV 79

                           90       100
                   ....*....|....*....|....*.
gi 1002623460  305 AQMREQRSGMVQTKEQYHFCYDIVLE 330
Cdd:smart00404  80 KELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 231-330 4.02e-36

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: 126.32  E-value: 4.02e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  231 SVKQLQFTKWPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVfCAIVKNCS--FNIMDIV 304
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLnqseSSGPVVVHCSAGVGRTGTFVAIDIL-LQQLEAEAgeVDIFDTV 79

                           90       100
                   ....*....|....*....|....*.
gi 1002623460  305 AQMREQRSGMVQTKEQYHFCYDIVLE 330
Cdd:smart00012  80 KELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 127-326 2.42e-34

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: 124.83  E-value: 2.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIrivncgEEY----FYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIKCYHYWPIslKKPLELKHFR 202
Cdd:cd14556     1 YINAALL------DSYkqpaAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLN-QLDPKDQSCPQYWPD--EGSGTYGPIQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 203 VFLENYQILQYFIIRMFQVVE--KSTGTSHSVKQLQFTKWPDHG-TPASADSFIKYIRYARK---SHLTGPMVVHCSAGI 276
Cdd:cd14556    72 VEFVSTTIDEDVISRIFRLQNttRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKwqeQSGEGPIVVHCLNGV 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002623460 277 GRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 326
Cdd:cd14556   152 GRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 127-330 1.55e-24

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: 98.94  E-value: 1.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIkCYHYWPisLKKPLELKHFRVFLE 206
Cdd:cd14634     1 YINAALMD--SHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN-EMDAAQL-CMQYWP--EKTSCCYGPIQVEFV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 207 NYQILQYFIIRMFQV--VEKSTGTSHSVKQLQFTKWPDH-GTPASADSFIKYIRYARKSHLT-----GPMVVHCSAGIGR 278
Cdd:cd14634    75 SADIDEDIISRIFRIcnMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgreGRTVVHCLNGGGR 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002623460 279 TGVFlcvdvvfCAIVKNCSF----NIMDI---VAQMREQRSGMVQTKEQYHFCYDIVLE 330
Cdd:cd14634   155 SGTF-------CAICSVCEMiqqqNIIDVfhtVKTLRNNKSNMVETLEQYKFVYEVALE 206
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 127-325 2.66e-23

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: 95.47  E-value: 2.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGiiKCYHYWPISlKKPLELKHFRVFL- 205
Cdd:cd14550     1 YINASYLQGYRRSNEF--IITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTK-EKPLECETFKVTLs 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 206 ---------ENYQILQYFIIRMFQ---VVEkstgtshsVKQLQFTKWPDHGTPASadSFIKYIRYARKSHLT--GPMVVH 271
Cdd:cd14550    76 gedhsclsnEIRLIVRDFILESTQddyVLE--------VRQFQCPSWPNPCSPIH--TVFELINTVQEWAQQrdGPIVVH 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002623460 272 -----CSAGigrtgvflcvdvVFCAI------VKNCsfNIMDI--VAQMREQ-RSGMVQTKEQYHFCY 325
Cdd:cd14550   146 dryggVQAA------------TFCALttlhqqLEHE--SSVDVyqVAKLYHLmRPGVFTSKEDYQFLY 199
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 127-330 5.63e-23

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: 94.75  E-value: 5.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIkCYHYWP---ISLKKPLELKHFRV 203
Cdd:cd14635     1 YINAALMD--SYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLN-DVDPAQL-CPQYWPengVHRHGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 204 FLENYQILQYFiiRMFQVVEKSTGTsHSVKQLQFTKWPDH-GTPASADSFIKYIRYARKSHLT-----GPMVVHCSAGIG 277
Cdd:cd14635    77 DLEEDIISRIF--RIYNAARPQDGY-RMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynggeGRTVVHCLNGGG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002623460 278 RTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 330
Cdd:cd14635   154 RSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 127-330 1.51e-21

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: 90.74  E-value: 1.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINA----SYIRIVNcgeeyfYIATQGPLLSTIDDFWQMVLENNSNVIAMITR-EIEGGIIKCYHYWP---ISLKKPLEL 198
Cdd:cd14637     1 YINAaltdSYTRSAA------FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQlNQSNSAWPCLQYWPepgLQQYGPMEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 199 KHFRVFLEnyqilQYFIIRMFQV--VEKSTGTSHSVKQLQFTKW-PDHGTPASADSFIKYI----RYARKSHlTGPMVVH 271
Cdd:cd14637    75 EFVSGSAD-----EDIVTRLFRVqnITRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLasveKWQRESG-EGRTVVH 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002623460 272 CSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 330
Cdd:cd14637   149 CLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 127-329 2.85e-21

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: 90.05  E-value: 2.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYhYWPiSLKKPLELKHFRVFL- 205
Cdd:cd17669     1 YINASYIMGYYQSNEF--IITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWP-NKDEPINCETFKVTLi 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 206 ---------ENYQILQYFIIRMFQ---VVEkstgtshsVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTGPMVVHCS 273
Cdd:cd17669    77 aeehkclsnEEKLIIQDFILEATQddyVLE--------VRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDE 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002623460 274 AGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVL 329
Cdd:cd17669   149 HGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 127-330 7.12e-21

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: 88.93  E-value: 7.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITR-EIEGGiikCYHYWP---ISLKKPLELKHFR 202
Cdd:cd14636     1 YINAALMDSYR--QPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEvDLAQG---CPQYWPeegMLRYGPIQVECMS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 203 VFLENYQILQYFiiRMFQVVEKSTGTShSVKQLQFTKWPDH-GTPASADSFIKYIRYARK-----SHLTGPMVVHCSAGI 276
Cdd:cd14636    76 CSMDCDVISRIF--RICNLTRPQEGYL-MVQQFQYLGWASHrEVPGSKRSFLKLILQVEKwqeecDEGEGRTIIHCLNGG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002623460 277 GRTGVFLCVDVVfCAIVKNCsfNIMDI---VAQMREQRSGMVQTKEQYHFCYDIVLE 330
Cdd:cd14636   153 GRSGMFCAISIV-CEMIKRQ--NVVDVfhaVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 106-321 1.72e-20

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: 88.61  E-value: 1.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 106 NRYRDIlpydSTRVPLGKSKDyINASYIRIvncGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMIT--REIEGGIIK 183
Cdd:cd14559     1 NRFTNI----QTRVSTPVGKN-LNANRVQI---GNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLAsnKDIQRKGLP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 184 CY-----HYWPISLKKPLELKhfrvflenYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHgTPASADSFIK---Y 255
Cdd:cd14559    73 PYfrqsgTYGSVTVKSKKTGK--------DELVDGLKADMYNLKITDGNKTITIPVVHVTNWPDH-TAISSEGLKEladL 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 256 IRYARKSHLTGPM---------------VVHCSAGIGRTGVFLCvdvVFCAIVKNCSFNIMDIVAQMREQRSG-MVQTKE 319
Cdd:cd14559   144 VNKSAEEKRNFYKskgssaindknkllpVIHCRAGVGRTGQLAA---AMELNKSPNNLSVEDIVSDMRTSRNGkMVQKDE 220


                  ..
gi 1002623460 320 QY 321
Cdd:cd14559   221 QL 222
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 78-328 2.92e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 83.86  E-value: 2.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460  78 IMQEFMALelknLPGEFNSGNQPSNREKNRYRD------ILPYDSTRVPLGKSKDYINASYIRIVNcgEEYFYIATQGPL 151
Cdd:PHA02740   27 IIKEYRAI----VPEHEDEANKACAQAENKAKDenlalhITRLLHRRIKLFNDEKVLDARFVDGYD--FEQKFICIINLC 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 152 LSTIDDFWQMVLENNSNVIAMITREIEGgiiKCYH-YWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKStGTSH 230
Cdd:PHA02740  101 EDACDKFLQALSDNKVQIIVLISRHADK---KCFNqFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDKF-GQAQ 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 231 SVKQLQFTKWPDHGTPASADSFIKY----------IRYARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNI 300
Cdd:PHA02740  177 KISHFQYTAWPADGFSHDPDAFIDFfcniddlcadLEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSI 256

                         250       260
                  ....*....|....*....|....*...
gi 1002623460 301 MDIVAQMREQRSGMVQTKEQYHFCYDIV 328
Cdd:PHA02740  257 ANALKKVRQKKYGCMNCLDDYVFCYHLI 284
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 127-329 7.95e-17

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: 77.80  E-value: 7.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 127 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIKCYHYWPiSLKKPLELKHFRVFLE 206
Cdd:cd17670     1 YINASYIMGYYRSNEF--IITQHPLPHTTKDFWRMIWDHNAQIIVMLP-DNQGLAEDEFVYWP-SREESMNCEAFTVTLI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 207 NYQIL-----QYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASadSFIKYIRYARKSHLT--GPMVVHCSAGIGRT 279
Cdd:cd17670    77 SKDRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPIS--STFELINVIKEEALTrdGPTIVHDEFGAVSA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002623460 280 GVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVL 329
Cdd:cd17670   155 GTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
240-323 5.67e-10

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 56.90  E-value: 5.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 240 WPDHGTP--ASADSFIKYIRYARKSHltGPMVVHCSAGIGRTGVFL-CVdvvfcAIVKNCSFNimDIVAQMREQRSGMVQ 316
Cdd:COG2453    55 IPDFGAPddEQLQEAVDFIDEALREG--KKVLVHCRGGIGRTGTVAaAY-----LVLLGLSAE--EALARVRAARPGAVE 125


                  ....*..
gi 1002623460 317 TKEQYHF 323
Cdd:COG2453   126 TPAQRAF 132
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 250-323 2.12e-08

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 52.28  E-value: 2.12e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002623460 250 DSFIKYIRYARKSHLtgPMVVHCSAGIGRTGVFLCvdvvfCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHF 323
Cdd:cd14504    69 DEFLDIVEEANAKNE--AVLVHCLAGKGRTGTMLA-----CYLVKTGKISAVDAINEIRRIRPGSIETSEQEKF 135
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 266-326 3.24e-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: 51.20  E-value: 3.24e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002623460 266 GPMVVHCSAGIGRTGVFLCvdvvfCAIVKNCSFNIMDIVAQMREQR-SGMVQTKEQYHFCYD 326
Cdd:cd14494    57 EPVLVHCKAGVGRTGTLVA-----CYLVLLGGMSAEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 234-323 1.44e-05

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 44.63  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 234 QLQFTKWP--DHGTPASA--DSFIKYIR--YARKSHLTGPMVVHCSAGIGRTGVFLCVdvvfcAIVKNCSFNIMDIVAQM 307
Cdd:PTZ00242   61 GIEVHDWPfdDGAPPPKAviDNWLRLLDqeFAKQSTPPETIAVHCVAGLGRAPILVAL-----ALVEYGGMEPLDAVGFV 135

                          90
                  ....*....|....*.
gi 1002623460 308 REQRSGMVQTKeQYHF 323
Cdd:PTZ00242  136 REKRKGAINQT-QLQF 150
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 240-320 2.84e-05

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: 44.26  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002623460 240 WPDHGTPASA---DSfIKYIRYARKshLTGPMVVHCSAGIGRTGVflcvdVVFCAIVKNCSFNIMDIVAQMREQRSGMVQ 316
Cdd:cd14506    84 WKDYGVPSLTtilDI-VKVMAFALQ--EGGKVAVHCHAGLGRTGV-----LIACYLVYALRMSADQAIRLVRSKRPNSIQ 155


                  ....
gi 1002623460 317 TKEQ 320
Cdd:cd14506   156 TRGQ 159
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 269-326 2.10e-04

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: 41.09  E-value: 2.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002623460 269 VVHCSAGIGRTGVFL-CVdvvfcAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 326
Cdd:cd14505   110 LIHCKGGLGRTGLIAaCL-----LLELGDTLDPEQAIAAVRALRPGAIQTPKQENFLHQ 163
 
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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