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Conserved domains on  [gi|2462518410|ref|XP_054221460|]
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tyrosine-protein phosphatase non-receptor type 20 isoform X32 [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 ...
 241-447 3.67e-141

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: 402.59  E-value: 3.67e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 320
Cdd:cd14596     1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 321 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCVD 400
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICVD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462518410 401 VVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 447
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 ...
 241-447 3.67e-141

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: 402.59  E-value: 3.67e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 320
Cdd:cd14596     1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 321 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCVD 400
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICVD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462518410 401 VVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 447
Cdd:cd14596   161 VLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
131-444 2.33e-100

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 300.73  E-value: 2.33e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410  131 IMQEFMAL-ELKNLPGEFNSGNQPSNREKNRYRDILPLkaampppseeidatlpeetfitspefvalqdiadssqdsqpp 209
Cdd:smart00194   2 LEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPY------------------------------------------ 39

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410  210 sfiasrpitrlksqqalkdDSTRVPL----GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIA 285
Cdd:smart00194  40 -------------------DHTRVKLkpppGEGSDYINASYIDGPNGPKAY--IATQGPLPSTVEDFWRMVWEQKVTVIV 98

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410  286 MITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADS 365
Cdd:smart00194  99 MLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPES 178

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410  366 FIKYIRYARK--SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVL 443
Cdd:smart00194 179 ILDLIRAVRKsqSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAIL 258


                   .
gi 2462518410  444 E 444
Cdd:smart00194 259 E 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
229-444 4.43e-97

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 291.07  E-value: 4.43e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPLGKSK---DYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIS 305
Cdd:pfam00102  14 DHTRVKLTGDPgpsDYINASYIDGYK--KPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGREKCAQYWPEE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 306 LKKPLELKHFRVFLENY-QILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL---TGP 381
Cdd:pfam00102  92 EGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRKSSLdgrSGP 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462518410 382 MVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:pfam00102 172 IVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
175-451 4.09e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 153.32  E-value: 4.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 175 SEEIDATLPEETFITSPEFVALQDIADSSQDSQPPSFIASRPITRLKSQQALKDDStrvpLGKSKDYINASYIRIvncGE 254
Cdd:COG5599     3 PKNPIAIKSEEEKINSRLSTLTNELAPSHNDPQYLQNINGSPLNRFRDIQPYKETA----LRANLGYLNANYIQV---IG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 255 EYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGG--IIKCYHYWPIS---LKKPLELKHfrvfLENYQILQYFI 329
Cdd:COG5599    76 NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYFRQDgeyGKYEVSSEL----TESIQLRDGIE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 330 IRMFQVVEKSTG-TSHSVKQLQFTKWPDHGTPaSADSFIKYIRYARKSHLT-----GPMVVHCSAGIGRTGVFLCVDVVF 403
Cdd:COG5599   152 ARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKEKIkdpdkLLPVVHCRAGVGRTGTLIACLALS 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462518410 404 CAI--VKNCSFNIMDIVAQMREQR-SGMVQTKEQYHFCYDIVLEVLRKLLT 451
Cdd:COG5599   231 KSInaLVQITLSVEEIVIDMRTSRnGGMVQTSEQLDVLVKLAEQQIRPLLR 281
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 229-444 5.57e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 142.83  E-value: 5.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPLGKSK---DYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIS 305
Cdd:PHA02742   65 DRNRVILKIEDggdDFINASYVDGHNAKGRF--ICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPH 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 306 LKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTG----- 380
Cdd:PHA02742  143 ERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVREADLKAdvdik 222

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462518410 381 --------PMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:PHA02742  223 genivkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
 
Name Accession Description Interval E-value
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 241-447 3.67e-141

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: 402.59  E-value: 3.67e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 320
Cdd:cd14596     1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 321 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCVD 400
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICVD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462518410 401 VVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 447
Cdd:cd14596   161 VLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 241-446 2.03e-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: 390.20  E-value: 2.03e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPL-ELKHFRVFL 319
Cdd:cd14538     1 YINASHIRIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLiCGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 320 ENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCV 399
Cdd:cd14538    81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNSGPIVVHCSAGIGRTGVLITI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462518410 400 DVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 446
Cdd:cd14538   161 DVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
131-444 2.33e-100

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 300.73  E-value: 2.33e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410  131 IMQEFMAL-ELKNLPGEFNSGNQPSNREKNRYRDILPLkaampppseeidatlpeetfitspefvalqdiadssqdsqpp 209
Cdd:smart00194   2 LEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPY------------------------------------------ 39

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410  210 sfiasrpitrlksqqalkdDSTRVPL----GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIA 285
Cdd:smart00194  40 -------------------DHTRVKLkpppGEGSDYINASYIDGPNGPKAY--IATQGPLPSTVEDFWRMVWEQKVTVIV 98

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410  286 MITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADS 365
Cdd:smart00194  99 MLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPES 178

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410  366 FIKYIRYARK--SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVL 443
Cdd:smart00194 179 ILDLIRAVRKsqSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAIL 258


                   .
gi 2462518410  444 E 444
Cdd:smart00194 259 E 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
229-444 4.43e-97

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 291.07  E-value: 4.43e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPLGKSK---DYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIS 305
Cdd:pfam00102  14 DHTRVKLTGDPgpsDYINASYIDGYK--KPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGREKCAQYWPEE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 306 LKKPLELKHFRVFLENY-QILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL---TGP 381
Cdd:pfam00102  92 EGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRKSSLdgrSGP 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462518410 382 MVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:pfam00102 172 IVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 229-446 6.37e-89

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: 270.55  E-value: 6.37e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPLGKSKDYINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKK 308
Cdd:cd14597    16 DTTRVPLGDEGGYINASFIKMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEGGKIKCQRYWPEILGK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 309 PLEL-KHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTGPMVVHCS 387
Cdd:cd14597    96 TTMVdNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFISYMRHIHKSGPIITHCS 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462518410 388 AGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 446
Cdd:cd14597   176 AGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILYVL 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 241-440 1.34e-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: 262.99  E-value: 1.34e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 320
Cdd:cd00047     1 YINASYIDGYRGPKEY--IATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 321 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKS--HLTGPMVVHCSAGIGRTGVFLC 398
Cdd:cd00047    79 SEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEarKPNGPIVVHCSAGVGRTGTFIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462518410 399 VDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 440
Cdd:cd00047   159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 241-440 4.70e-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: 220.97  E-value: 4.70e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIrIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRV-FL 319
Cdd:cd18533     1 YINASYI-TLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWP-SGEYEGEYGDLTVeLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 320 ENYQI-LQYFIIRMFQVVeKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARK----SHLTGPMVVHCSAGIGRTG 394
Cdd:cd18533    79 SEEENdDGGFIVREFELS-KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElndsASLDPPIIVHCSAGVGRTG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462518410 395 VFLCVDVVF---------CAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 440
Cdd:cd18533   158 TFIALDSLLdelkrglsdSQDLEDSEDPVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 229-437 5.33e-65

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: 208.36  E-value: 5.33e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPLGKS-----KDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP 303
Cdd:cd14548     9 DHSRVKLIPIneeegSDYINANYIPGYNSPREF--IATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVKCDHYWP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 304 ISlKKPLELKHFRVFLENYQILQYFIIRMFQVveKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKS--HLTGP 381
Cdd:cd14548    87 FD-QDPVYYGDITVTMLSESVLPDWTIREFKL--ERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYikQEKGP 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462518410 382 MVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHF 437
Cdd:cd14548   164 TIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 131-439 7.36e-63

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: 204.52  E-value: 7.36e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 131 IMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPLkaampppseeidatlpeetfitspefvalqdiadssqdsqpps 210
Cdd:cd14543     5 IYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCL------------------------------------------- 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 211 fiasrpitrlksqqalkdDSTRVPLGK-----SKDYINASYIrivncgEEY----FYIATQGPLLSTIDDFWQMVLENNS 281
Cdd:cd14543    42 ------------------DQSRVKLPKrngdeRTDYINANFM------DGYkqknAYIATQGPLPKTYSDFWRMVWEQKV 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 282 NVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPA 361
Cdd:cd14543    98 LVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFGVPS 177

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 362 SADSFIKYIRYAR--------------KSHLTG-PMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRS 426
Cdd:cd14543   178 SAAALLDFLGEVRqqqalavkamgdrwKGHPPGpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRA 257

                         330
                  ....*....|...
gi 2462518410 427 GMVQTKEQYHFCY 439
Cdd:cd14543   258 FSIQTPDQYYFCY 270
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 241-446 2.40e-62

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: 201.53  E-value: 2.40e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKK--PLELKHFRVF 318
Cdd:cd14540     1 YINASHITATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEhdALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 319 LENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR--KSHLTG---------PMVVHCS 387
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINsvRRHTNQdvaghnrnpPTLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462518410 388 AGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 446
Cdd:cd14540   161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 213-439 1.22e-60

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: 197.75  E-value: 1.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 213 ASRPITRLKSQ--QALKDDSTRVPLG-----KSKDYINASYIRivncGEEY--FYIATQGPLLSTIDDFWQMVLENNSNV 283
Cdd:cd14554     1 ANLPCNKFKNRlvNILPYESTRVCLQpirgvEGSDYINASFID----GYRQrgAYIATQGPLAETTEDFWRMLWEHNSTI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 284 IAMITREIEGGIIKCYHYWPisLKKPLELKHFRVF-LENYQILQYfIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPAS 362
Cdd:cd14554    77 IVMLTKLREMGREKCHQYWP--AERSARYQYFVVDpMAEYNMPQY-ILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 363 ADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFC 438
Cdd:cd14554   154 GEGFIDFIGQVHKTKeqfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFC 233


                  .
gi 2462518410 439 Y 439
Cdd:cd14554   234 Y 234
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 241-440 1.99e-59

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: 193.34  E-value: 1.99e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPisLKKPLELKHFRVFLE 320
Cdd:cd14549     1 YINANYVDGYNKARAY--IATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWP--KEGTETYGNIQVTLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 321 NYQILQYFIIRMFQV------VEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIR--YARKSHLTGPMVVHCSAGIGR 392
Cdd:cd14549    77 STEVLATYTVRTFSLknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRksSAANPPGAGPIVVHCSAGVGR 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2462518410 393 TGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 440
Cdd:cd14549   157 TGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 229-439 2.25e-59

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


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 194.15  E-value: 2.25e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPL-GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLK 307
Cdd:cd14545    13 DRSRVKLkQGDNDYINASLVEVEEAKRSY--ILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIKCAQYWPQGEG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 308 KPLELKH--FRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL----TGP 381
Cdd:cd14545    91 NAMIFEDtgLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKVRESGSlssdVGP 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 382 MVVHCSAGIGRTGVFLCVDVVFCAIVKN--CSFNIMDIVAQMREQRSGMVQTKEQYHFCY 439
Cdd:cd14545   171 PVVHCSAGIGRSGTFCLVDTCLVLIEKGnpSSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 240-445 6.17e-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: 192.54  E-value: 6.17e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 240 DYINASYIR-------IVNcgeeyFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPiSLKKPLEL 312
Cdd:cd14541     1 DYINANYVNmeipgsgIVN-----RYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWP-DLGETMQF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 313 KHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTG--PMVVHCSAGI 390
Cdd:cd14541    75 GNLQITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMvePTVVHCSAGI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462518410 391 GRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEV 445
Cdd:cd14541   155 GRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 229-444 6.88e-59

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: 193.00  E-value: 6.88e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPLGKSK-----DYINASYI---RIVNCgeeyfYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYH 300
Cdd:cd14553    16 DHSRVILQPIEgvpgsDYINANYCdgyRKQNA-----YIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEERSRVKCDQ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 301 YWPISLKKPLELKHfrVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL-- 378
Cdd:cd14553    91 YWPTRGTETYGLIQ--VTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKACNPpd 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462518410 379 TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:cd14553   169 AGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 226-437 6.93e-58

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: 189.92  E-value: 6.93e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 226 LKDDSTRVPLGKSKD-----YINASYIRIVNcGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGiIKCYH 300
Cdd:cd14547     7 LPNEHSRVCLPSVDDdplssYINANYIRGYD-GEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK-EKCAQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 301 YWPIslKKPLELKHFRVFLENYQILQYFIIRmfQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIR----YARKS 376
Cdd:cd14547    85 YWPE--EENETYGDFEVTVQSVKETDGYTVR--KLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQeveeARQTE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462518410 377 HLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHF 437
Cdd:cd14547   161 PHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 229-448 1.89e-55

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


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 185.44  E-value: 1.89e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPLGKSKDYINASYIRI----VNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPi 304
Cdd:cd14600    53 DATRVVLQGNEDYINASYVNMeipsANIVNKY--IATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWP- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 305 SLKKPLELKHFRVFL--ENYQILqyFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTG-P 381
Cdd:cd14600   130 DPPDVMEYGGFRVQChsEDCTIA--YVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENeP 207

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462518410 382 MVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLRK 448
Cdd:cd14600   208 VLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 274
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 229-446 2.02e-55

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: 183.94  E-value: 2.02e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPLGKSK-----DYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP 303
Cdd:cd14619    10 DWSRVPLKPIHeepgsDYINANYMPGYWSSQEF--IATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRVKCEHYWP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 304 ISlKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARK---SHL-T 379
Cdd:cd14619    88 LD-YTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQwldQTMsG 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462518410 380 GPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 446
Cdd:cd14619   167 GPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 155-439 2.07e-55

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: 184.59  E-value: 2.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 155 NREKNRYRDILPLkaampppseeiDATLpeetfitspefVALQDIadssqDSQPPSfiasrpitrlksqqalkddstrvp 234
Cdd:cd14544     1 NKGKNRYKNILPF-----------DHTR-----------VILKDR-----DPNVPG------------------------ 29

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 235 lgksKDYINASYIRIVNCGEEYF-----YIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKP 309
Cdd:cd14544    30 ----SDYINANYIRNENEGPTTDenaktYIATQGCLENTVSDFWSMVWQENSRVIVMTTKEVERGKNKCVRYWPDEGMQK 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 310 lELKHFRVFLENYQILQYFIIRMFQVVEKSTGTS-HSVKQLQFTKWPDHGTPASAD---SFIKYIRYaRKSHL--TGPMV 383
Cdd:cd14544   106 -QYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPiREIWHYQYLSWPDHGVPSDPGgvlNFLEDVNQ-RQESLphAGPIV 183

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462518410 384 VHCSAGIGRTGVFLCVDVVFCAIVKN---CSFNIMDIVAQMREQRSGMVQTKEQYHFCY 439
Cdd:cd14544   184 VHCSAGIGRTGTFIVIDMLLDQIKRKgldCDIDIQKTIQMVRSQRSGMVQTEAQYKFIY 242
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 241-439 8.02e-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: 181.47  E-value: 8.02e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 320
Cdd:cd14542     1 YINANFIKGVS--GSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 321 NYQILQY-FIIRMFQVveKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARK--SHLTGPMVVHCSAGIGRTGVFL 397
Cdd:cd14542    79 KEKRVGPdFLIRTLKV--TFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDyqGSEDVPICVHCSAGCGRTGTIC 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462518410 398 CVDVVFCAI---VKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 439
Cdd:cd14542   157 AIDYVWNLLktgKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 229-445 1.26e-53

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: 180.41  E-value: 1.26e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPL------GKSkDYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYW 302
Cdd:cd14603    43 DQTRVILsllqeeGHS-DYINANFIKGVD--GSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYW 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 303 PiSLKKPLELKHFRV-FLENYQILQYFIIRMFQVVEKStgTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTG- 380
Cdd:cd14603   120 A-QEQEPLQTGPFTItLVKEKRLNEEVILRTLKVTFQK--ESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGp 196

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462518410 381 -PMVVHCSAGIGRTGVFLCVDVVFCAIVKNC---SFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEV 445
Cdd:cd14603   197 ePLCVHCSAGCGRTGVICTVDYVRQLLLTQRippDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQM 265
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 229-439 2.61e-53

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: 178.19  E-value: 2.61e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPLGK-----SKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP 303
Cdd:cd14617    10 DSTRVKLSNvdddpCSDYINASYIPGNNFRREY--IATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 304 ISlKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHS-VKQLQFTKWPDHGTPASADSFIKYIR----YARKSHL 378
Cdd:cd14617    88 AD-QDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRlVRHFHYTVWPDHGVPETTQSLIQFVRtvrdYINRTPG 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462518410 379 TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 439
Cdd:cd14617   167 SGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 213-446 1.42e-52

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: 178.39  E-value: 1.42e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 213 ASRPITRLKSQ--QALKDDSTRVPLG-----KSKDYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIA 285
Cdd:cd14627    48 ANLPCNKFKNRlvNIMPYETTRVCLQpirgvEGSDYINASFID--GYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVV 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 286 MITREIEGGIIKCYHYWPIslKKPLELKHFRVF-LENYQILQYfIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASAD 364
Cdd:cd14627   126 MLTKLREMGREKCHQYWPA--ERSARYQYFVVDpMAEYNMPQY-ILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 365 SFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 440
Cdd:cd14627   203 GFIDFIGQVHKTKeqfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQ 282


                  ....*.
gi 2462518410 441 IVLEVL 446
Cdd:cd14627   283 AALEYL 288
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 202-446 6.85e-51

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: 174.15  E-value: 6.85e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 202 SSQDSQPPSFI-ASRPITRLKSQ--QALKDDSTRVPLG-----KSKDYINASYIRivNCGEEYFYIATQGPLLSTIDDFW 273
Cdd:cd14628    35 ASSKAHTSRFIsANLPCNKFKNRlvNIMPYESTRVCLQpirgvEGSDYINASFID--GYRQQKAYIATQGPLAETTEDFW 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 274 QMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVF-LENYQILQYfIIRMFQVVEKSTGTSHSVKQLQFT 352
Cdd:cd14628   113 RMLWEHNSTIVVMLTKLREMGREKCHQYWPA--ERSARYQYFVVDpMAEYNMPQY-ILREFKVTDARDGQSRTVRQFQFT 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 353 KWPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGM 428
Cdd:cd14628   190 DWPEQGVPKSGEGFIDFIGQVHKTKeqfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAM 269

                         250
                  ....*....|....*...
gi 2462518410 429 VQTKEQYHFCYDIVLEVL 446
Cdd:cd14628   270 VQTEDQYQFCYRAALEYL 287
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 240-448 8.24e-51

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 171.28  E-value: 8.24e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 240 DYINASYI--RIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRV 317
Cdd:cd14601     1 DYINANYInmEIPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP-EPSGSSSYGGFQV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 318 FLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR--KSHLTGPMVVHCSAGIGRTGV 395
Cdd:cd14601    80 TCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRnkRAGKDEPVVVHCSAGIGRTGV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462518410 396 FLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLRK 448
Cdd:cd14601   160 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 229-437 1.83e-50

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: 170.77  E-value: 1.83e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPLG----KSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPI 304
Cdd:cd14615    10 DISRVKLSvqshSTDDYINANYMPGYNSKKEF--IAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 305 SLKKplELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYiRYARKSHLT----- 379
Cdd:cd14615    88 KQKK--DYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINF-RHLVREYMKqnppn 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462518410 380 GPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHF 437
Cdd:cd14615   165 SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 241-440 1.83e-50

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: 169.87  E-value: 1.83e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIR-IVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFL 319
Cdd:cd14539     1 YINASLIEdLTPYCPRF--IATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 320 ENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIR-----YARKSHLTGPMVVHCSAGIGRTG 394
Cdd:cd14539    79 QSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEevhshYLQQRSLQTPIVVHCSSGVGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462518410 395 VFlCvdVVFCAIVK----NCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 440
Cdd:cd14539   159 AF-C--LLYAAVQEieagNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 120-447 3.50e-50

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: 172.10  E-value: 3.50e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 120 KILEEKTAAYDIMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPLkaampppseeidatlpeetfitspefvalqdi 199
Cdd:cd14599     3 KTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPY-------------------------------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 200 adssqdsqppsfiasrpitrlksqqalkdDSTRVPLGKSKD----YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQM 275
Cdd:cd14599    51 -----------------------------EENRVELVPTKEnntgYINASHIKVTVGGEEWHYIATQGPLPHTCHDFWQM 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 276 VLENNSNVIAMITREIEGGIIKCYHYWPislkkPLELKHFRVFLENYQILQYF-------IIRMFQVVEKSTGTSHSVKQ 348
Cdd:cd14599   102 VWEQGVNVIAMVTAEEEGGRSKSHRYWP-----KLGSKHSSATYGKFKVTTKFrtdsgcyATTGLKVKHLLSGQERTVWH 176

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 349 LQFTKWPDHGTPASADSFIKY---IRYARK---------SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMD 416
Cdd:cd14599   177 LQYTDWPDHGCPEEVQGFLSYleeIQSVRRhtnsmldstKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPV 256

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2462518410 417 IVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 447
Cdd:cd14599   257 MLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 208-439 1.53e-49

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: 169.25  E-value: 1.53e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 208 PPSFI----------ASRpiTRLKSqqALKDDSTRVPLGKSK------DYINASYIRIVNcGEEYFYIATQGPLLSTIDD 271
Cdd:cd14612     1 PPNFVspeeldipghASK--DRYKT--ILPNPQSRVCLRRAGsqeeegSYINANYIRGYD-GKEKAYIATQGPMLNTVSD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 272 FWQMVLENNSNVIAMITREIEGGiIKCYHYWPislKKPLELKHFRVFLENYQILQYFIIRmfQVVEKSTGTSHSVKQLQF 351
Cdd:cd14612    76 FWEMVWQEECPIIVMITKLKEKK-EKCVHYWP---EKEGTYGRFEIRVQDMKECDGYTIR--DLTIQLEEESRSVKHYWF 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 352 TKWPDHGTPASADSFIKYIRYARKSHLT----GPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSG 427
Cdd:cd14612   150 SSWPDHQTPESAGPLLRLVAEVEESRQTaaspGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGG 229

                         250
                  ....*....|..
gi 2462518410 428 MVQTKEQYHFCY 439
Cdd:cd14612   230 MIQTSEQYQFLH 241
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 241-444 2.77e-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: 167.02  E-value: 2.77e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKpleLKHFRVFLE 320
Cdd:cd14555     1 YINANYIDGYH--RPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV---YGDIKVTLV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 321 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGVFLC 398
Cdd:cd14555    76 ETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNppSAGPIVVHCSAGAGRTGCYIV 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462518410 399 VDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:cd14555   156 IDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 168-446 7.79e-49

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: 168.75  E-value: 7.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 168 KAAMPPPSEEIDATlpeetfitSPEFVALqdiadSSQDSQPPSFI-ASRPITRLKSQ--QALKDDSTRVPLG-----KSK 239
Cdd:cd14629    15 KLTQVPPGESVTAM--------ELEFKLL-----ANSKAHTSRFIsANLPCNKFKNRlvNIMPYELTRVCLQpirgvEGS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 240 DYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVF- 318
Cdd:cd14629    82 DYINASFID--GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPA--ERSARYQYFVVDp 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 319 LENYQILQYfIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTG 394
Cdd:cd14629   158 MAEYNMPQY-ILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKeqfgQDGPITVHCSAGVGRTG 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462518410 395 VFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 446
Cdd:cd14629   237 VFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 241-439 8.97e-49

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: 165.72  E-value: 8.97e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEG-GIIKCYHYWPISLKKPLELKHFRVFL 319
Cdd:cd17658     1 YINASLVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNySTAKCADYFPAEENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 320 ENYQILQYFI-IRMFQVVE-KSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRyaRKSHL---TGPMVVHCSAGIGRTG 394
Cdd:cd17658    81 KKLKHSQHSItLRVLEVQYiESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLK--RLYGIppsAGPIVVHCSAGIGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462518410 395 VFLCVDVVFCAIVKN--CSFNIMDIVAQMREQRSGMVQTKEQYHFCY 439
Cdd:cd17658   159 AYCTIHNTIRRILEGdmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 209-443 1.27e-48

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: 166.60  E-value: 1.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 209 PSFIASRPITRLKSQ--QALKDDSTRVPL-----GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNS 281
Cdd:cd14614     3 PHFAADLPVNRCKNRytNILPYDFSRVKLvsmheEEGSDYINANYIPGYNSPQEY--IATQGPLPETRNDFWKMVLQQKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 282 NVIAMITREIEGGIIKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQVveKSTGTSHSVKQLQFTKWPDHGTPA 361
Cdd:cd14614    81 QIIVMLTQCNEKRRVKCDHYWPFT-EEPVAYGDITVEMLSEEEQPDWAIREFRV--SYADEVQDVMHFNYTAWPDHGVPT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 362 --SADSFIKYIRYARKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHF 437
Cdd:cd14614   158 anAAESILQFVQMVRQQAVksKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237


                  ....*.
gi 2462518410 438 CYDIVL 443
Cdd:cd14614   238 IHQCVQ 243
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 241-440 1.76e-48

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: 165.15  E-value: 1.76e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPisLKKPLELKHFRVFLE 320
Cdd:cd17668     1 YINANYVDGYN--KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP--ADGSEEYGNFLVTQK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 321 NYQILQYFIIRMFQV--------VEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR--KSHLTGPMVVHCSAGI 390
Cdd:cd17668    77 SVQVLAYYTVRNFTLrntkikkgSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASyaKRHAVGPVVVHCSAGV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462518410 391 GRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 440
Cdd:cd17668   157 GRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 197-444 2.51e-47

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: 164.43  E-value: 2.51e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 197 QDIADSSQDSqpPSFIASRPitRLKSQQALKD----DSTRVPLGKS-KDYINASYIRIVNCGEEYfyIATQGPLLSTIDD 271
Cdd:cd14608     6 QDIRHEASDF--PCRVAKLP--KNKNRNRYRDvspfDHSRIKLHQEdNDYINASLIKMEEAQRSY--ILTQGPLPNTCGH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 272 FWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPL--ELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQL 349
Cdd:cd14608    80 FWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMifEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 350 QFTKWPDHGTPASADSFIKYIRYARKSHLT----GPMVVHCSAGIGRTGVFLCVDVVFCAIVKN---CSFNIMDIVAQMR 422
Cdd:cd14608   160 HYTTWPDFGVPESPASFLNFLFKVRESGSLspehGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDIKKVLLEMR 239

                         250       260
                  ....*....|....*....|..
gi 2462518410 423 EQRSGMVQTKEQYHFCYDIVLE 444
Cdd:cd14608   240 KFRMGLIQTADQLRFSYLAVIE 261
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 229-439 3.34e-47

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: 163.26  E-value: 3.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRV------PLGKSKDYINASYI------RIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGII 296
Cdd:cd14605    15 DHTRVvlhdgdPNEPVSDYINANIImpefetKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERGKS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 297 KCYHYWP--ISLKkplELKHFRVFLENYQILQYFIIRMFQVVEKSTG-TSHSVKQLQFTKWPDHGTPASAD---SFIKYI 370
Cdd:cd14605    95 KCVKYWPdeYALK---EYGVMRVRNVKESAAHDYILRELKLSKVGQGnTERTVWQYHFRTWPDHGVPSDPGgvlDFLEEV 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462518410 371 RYARKSHL-TGPMVVHCSAGIGRTGVFLCVDVVFCAIVK---NCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 439
Cdd:cd14605   172 HHKQESIMdAGPVVVHCSAGIGRTGTFIVIDILIDIIREkgvDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIY 244
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 229-446 3.35e-47

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: 163.67  E-value: 3.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPL-------GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHY 301
Cdd:cd17667    40 DHSRVKLrplpgkdSKHSDYINANYVDGYNKAKAY--IATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQY 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 302 WPISLKKplELKHFRVFLENYQILQYFIIRMFQVVE-----------KSTGTSHSVKQLQFTKWPDHGTPASADSFIKYI 370
Cdd:cd17667   118 WPTENSE--EYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFV 195

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462518410 371 RY---ARKSHLtGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 446
Cdd:cd17667   196 RRssaARTPEM-GPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 273
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 148-450 4.30e-47

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: 164.34  E-value: 4.30e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 148 NSGNQPSNREKNRYRDILPlkaampppseeidatlpeetfitspefvalqdiadssqdsqppsFIASRPITRLKSQQalk 227
Cdd:cd14604    50 ATGEKEENVKKNRYKDILP--------------------------------------------FDHSRVKLTLKTSS--- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 228 ddstrvplgKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLK 307
Cdd:cd14604    83 ---------QDSDYINANFIKGVYGPKAY--IATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 308 KPLELKHFRVFLENYQILQYFIIRMFQVveKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARK--SHLTGPMVVH 385
Cdd:cd14604   152 EPMTFGPFRISCEAEQARTDYFIRTLLL--EFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKyqEHEDVPICIH 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462518410 386 CSAGIGRTGVFLCVDVVFCAIVKNC---SFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLRKLL 450
Cdd:cd14604   230 CSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQL 297
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 241-447 5.99e-47

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: 5.99e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPislkkPLELKHFRVFLE 320
Cdd:cd14598     1 YINASHIKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWP-----RLGSRHNTVTYG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 321 NYQILQYF-------IIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKY---IRYARKsHLTG---------P 381
Cdd:cd14598    76 RFKITTRFrtdsgcyATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeIQSVRR-HTNStidpkspnpP 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462518410 382 MVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 447
Cdd:cd14598   155 VLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 229-444 9.28e-47

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: 161.35  E-value: 9.28e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPL-----GKSKDYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP 303
Cdd:cd14630    16 DHSRVRLqlldgDPHSDYINANYIDGYH--RPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEVGRVKCVRYWP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 304 ISLKKPLELKhfrVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR--KSHLTGP 381
Cdd:cd14630    94 DDTEVYGDIK---VTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQVKflNPPDAGP 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462518410 382 MVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:cd14630   171 IVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 224-444 2.15e-46

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: 159.80  E-value: 2.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 224 QALKDDStrvplgkSKDYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP 303
Cdd:cd14631     5 QPVEDDP-------SSDYINANYID--GYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 304 islkKPLEL-KHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSH--LTG 380
Cdd:cd14631    76 ----DDTEVyGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNppSAG 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462518410 381 PMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:cd14631   152 PIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 241-439 2.55e-46

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: 160.08  E-value: 2.55e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNcGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIiKCYHYWPislKKPLELKHFRVFLE 320
Cdd:cd14611    30 YINANYIRGYG-GKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWP---EKRGIYGKVEVLVN 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 321 NYQILQYFIIRmfQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKY---IRYARKSHLT-GPMVVHCSAGIGRTGVF 396
Cdd:cd14611   105 SVKECDNYTIR--NLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLmldVEEDRLASPGrGPVVVHCSAGIGRTGCF 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462518410 397 LCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 439
Cdd:cd14611   183 IATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 241-444 2.73e-46

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: 159.15  E-value: 2.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIrIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPislKKPLELKH-FRVFL 319
Cdd:cd14546     1 YINASTI-YDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP---EEGSEVYHiYEVHL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 320 ENYQIL-QYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGVF 396
Cdd:cd14546    77 VSEHIWcDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYrgRSCPIVVHCSDGAGRTGTY 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462518410 397 LCVDVVFCAIVKncSFNIMDIVA---QMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:cd14546   157 ILIDMVLNRMAK--GAKEIDIAAtleHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 210-444 4.85e-46

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: 160.99  E-value: 4.85e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 210 SFIASRP--ITRLKSQQALKDDSTRVPLG-----KSKDYINASYIrIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSN 282
Cdd:cd14610    36 TNVAQREenVQKNRSLAVLPYDHSRIILKaenshSHSDYINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWESGCV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 283 VIAMITREIEGGIIKCYHYWPislKKPLELKH-FRVFLENYQI-LQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTP 360
Cdd:cd14610   115 VIVMLTPLAENGVKQCYHYWP---DEGSNLYHiYEVNLVSEHIwCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVP 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 361 ASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNC-SFNIMDIVAQMREQRSGMVQTKEQYHF 437
Cdd:cd14610   192 ASTRSLLDFRRKVNKCYrgRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAkEIDIAATLEHLRDQRPGMVQTKEQFEF 271


                  ....*..
gi 2462518410 438 CYDIVLE 444
Cdd:cd14610   272 ALTAVAE 278
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 241-442 1.29e-45

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: 1.29e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVFLE 320
Cdd:cd14552     1 YINASFIDGYR--QKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPE--DGSVSSGDITVELK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 321 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL---TGPMVVHCSAGIGRTGVFL 397
Cdd:cd14552    77 DQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQqsgNHPITVHCSAGAGRTGTFC 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462518410 398 CVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIV 442
Cdd:cd14552   157 ALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 229-445 1.82e-45

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: 158.08  E-value: 1.82e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPLG-----KSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP 303
Cdd:cd14602    11 DHSRVELSlitsdEDSDYINANFIKGVYGPRAY--IATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGKKKCERYWA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 304 ISLKKPLELKHFRVFLENYQILQYFIIRMFQVveKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR--KSHLTGP 381
Cdd:cd14602    89 EPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKV--KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRcyQEDDSVP 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462518410 382 MVVHCSAGIGRTGVFLCVDVVFC----AIVKNCsFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEV 445
Cdd:cd14602   167 ICIHCSAGCGRTGVICAIDYTWMllkdGIIPEN-FSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 229-444 1.40e-44

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: 156.74  E-value: 1.40e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPL-----GKSKDYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP 303
Cdd:cd14633    53 DHSRVRLqpiegETSSDYINGNYIDGYH--RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 304 ISLKKpleLKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRY--ARKSHLTGP 381
Cdd:cd14633   131 DDTEI---YKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQvkSKSPPNAGP 207

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462518410 382 MVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:cd14633   208 LVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 203-439 1.85e-44

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: 155.89  E-value: 1.85e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 203 SQDSQPPSFIASRPITRLKSQqaLKD----DSTRVPLGKSK-DYINASYIRIVNCgeEYFYIATQGPLLSTIDDFWQMVL 277
Cdd:cd14607     9 NESHDYPHRVAKYPENRNRNR--YRDvspyDHSRVKLQNTEnDYINASLVVIEEA--QRSYILTQGPLPNTCCHFWLMVW 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 278 ENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKH--FRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWP 355
Cdd:cd14607    85 QQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 356 DHGTPASADSFIKYIRYARKSHL----TGPMVVHCSAGIGRTGVFLCVD--VVFCAIVKNCSFNIMDIVAQMREQRSGMV 429
Cdd:cd14607   165 DFGVPESPASFLNFLFKVRESGSlspeHGPAVVHCSAGIGRSGTFSLVDtcLVLMEKKDPDSVDIKQVLLDMRKYRMGLI 244

                         250
                  ....*....|
gi 2462518410 430 QTKEQYHFCY 439
Cdd:cd14607   245 QTPDQLRFSY 254
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 229-444 1.92e-44

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: 156.73  E-value: 1.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPLGK-----SKDYINASYI---RIVNCgeeyfYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYH 300
Cdd:cd14626    54 DHSRVILTSvdgvpGSDYINANYIdgyRKQNA-----YIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQ 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 301 YWPISLKKPLELkhFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL-- 378
Cdd:cd14626   129 YWPIRGTETYGM--IQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPpd 206

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462518410 379 TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:cd14626   207 AGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 241-435 2.40e-44

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: 153.83  E-value: 2.40e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 320
Cdd:cd14557     1 YINASYID--GFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKIN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 321 NYQILQYFIIRMFQVV-EKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRY--ARKSHLTGPMVVHCSAGIGRTGVFL 397
Cdd:cd14557    79 EEKICPDYIIRKLNINnKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRvnAFNNFFSGPIVVHCSAGVGRTGTYI 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462518410 398 CVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQY 435
Cdd:cd14557   159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 241-444 2.41e-44

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: 2.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKhfrVFLE 320
Cdd:cd14632     1 YINANYIDGYH--RSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIK---ITLL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 321 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL--TGPMVVHCSAGIGRTGVFLC 398
Cdd:cd14632    76 KTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPpdAGPVVVHCSAGAGRTGCYIV 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462518410 399 VDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:cd14632   156 LDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 240-437 2.52e-44

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: 154.68  E-value: 2.52e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 240 DYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISlKKPLElkhfrVF- 318
Cdd:cd14616    26 DYINASYISGYLCPNEF--IATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRIRCHQYWPED-NKPVT-----VFg 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 319 -------LENYQIlqYFIIRMFQvVEKStGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR--KSHLTGPMVVHCSAG 389
Cdd:cd14616    98 divitklMEDVQI--DWTIRDLK-IERH-GDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRasRAHDNTPMIVHCSAG 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2462518410 390 IGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHF 437
Cdd:cd14616   174 VGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 226-444 4.60e-44

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: 153.94  E-value: 4.60e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 226 LKDDSTRVPL-----GKSKDYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYH 300
Cdd:cd14620     5 LPYDHSRVILsqldgIPCSDYINASYID--GYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 301 YWPIslKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHS---VKQLQFTKWPDHG---TPASADSFIKYIRYAR 374
Cdd:cd14620    83 YWPD--QGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAprlVTQLHFTSWPDFGvpfTPIGMLKFLKKVKSVN 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 375 KSHlTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:cd14620   161 PVH-AGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 229-443 6.54e-44

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: 153.56  E-value: 6.54e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPLGK-----SKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP 303
Cdd:cd14618    10 DHSRVRLSQlggepHSDYINANFIPGYTSPQEF--IATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRVLCDHYWP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 304 ISLkKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARK----SHLT 379
Cdd:cd14618    88 SES-TPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREhvqaTKGK 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462518410 380 GPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVL 443
Cdd:cd14618   167 GPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 240-446 8.76e-44

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: 154.87  E-value: 8.76e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 240 DYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPislKKPLELKHF-RVF 318
Cdd:cd14625    76 DYINANYID--GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP---SRGTETYGMiQVT 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 319 LENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL--TGPMVVHCSAGIGRTGVF 396
Cdd:cd14625   151 LLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPpdAGPIVVHCSAGVGRTGCF 230

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462518410 397 LCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 446
Cdd:cd14625   231 IVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
175-451 4.09e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 153.32  E-value: 4.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 175 SEEIDATLPEETFITSPEFVALQDIADSSQDSQPPSFIASRPITRLKSQQALKDDStrvpLGKSKDYINASYIRIvncGE 254
Cdd:COG5599     3 PKNPIAIKSEEEKINSRLSTLTNELAPSHNDPQYLQNINGSPLNRFRDIQPYKETA----LRANLGYLNANYIQV---IG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 255 EYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGG--IIKCYHYWPIS---LKKPLELKHfrvfLENYQILQYFI 329
Cdd:COG5599    76 NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYFRQDgeyGKYEVSSEL----TESIQLRDGIE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 330 IRMFQVVEKSTG-TSHSVKQLQFTKWPDHGTPaSADSFIKYIRYARKSHLT-----GPMVVHCSAGIGRTGVFLCVDVVF 403
Cdd:COG5599   152 ARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKEKIkdpdkLLPVVHCRAGVGRTGTLIACLALS 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462518410 404 CAI--VKNCSFNIMDIVAQMREQR-SGMVQTKEQYHFCYDIVLEVLRKLLT 451
Cdd:COG5599   231 KSInaLVQITLSVEEIVIDMRTSRnGGMVQTSEQLDVLVKLAEQQIRPLLR 281
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 150-444 6.96e-43

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: 151.96  E-value: 6.96e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 150 GNQPSNREKNRYRDILPlkaampppseeidatlpeetfitspefvalqdiadssqdsqppsFIASRPItrlksqqaLKDD 229
Cdd:cd14606    13 GQRPENKSKNRYKNILP--------------------------------------------FDHSRVI--------LQGR 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 230 STRVPlgkSKDYINASYIR---IVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPiSL 306
Cdd:cd14606    41 DSNIP---GSDYINANYVKnqlLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWP-EV 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 307 KKPLELKHFRVFLENYQILQYFIIRMFQV-VEKSTGTSHSVKQLQFTKWPDHGTPASAD---SFIKYIRYARKS-HLTGP 381
Cdd:cd14606   117 GMQRAYGPYSVTNCGEHDTTEYKLRTLQVsPLDNGELIREIWHYQYLSWPDHGVPSEPGgvlSFLDQINQRQESlPHAGP 196

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462518410 382 MVVHCSAGIGRTGVFLCVDVVFCAIVK---NCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:cd14606   197 IIVHCSAGIGRTGTIIVIDMLMENISTkglDCDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQ 262
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 241-440 9.17e-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: 149.85  E-value: 9.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKhfrVFLE 320
Cdd:cd14558     1 YINASFIDGYWGPKSL--IATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIE---VELK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 321 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR--------KSHLTGPMVVHCSAGIGR 392
Cdd:cd14558    76 DTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKqklpyknsKHGRSVPIVVHCSDGSSR 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 393 TGvflcvdvVFCAIvkncsFNIMD------------IVAQMREQRSGMVQTKEQYHFCYD 440
Cdd:cd14558   156 TG-------IFCAL-----WNLLEsaetekvvdvfqVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 229-446 3.56e-42

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: 150.65  E-value: 3.56e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPLGK-----SKDYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP 303
Cdd:cd14624    60 DHSRVLLSAiegipGSDYINANYID--GYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWP 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 304 ISLKKPLELkhFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL--TGP 381
Cdd:cd14624   138 SRGTETYGL--IQVTLLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPpdAGP 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462518410 382 MVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 446
Cdd:cd14624   216 MVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 241-439 1.23e-41

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: 146.60  E-value: 1.23e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKplELKHFRVFLE 320
Cdd:cd14551     1 YINASYID--GYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW--TYGNLRVRVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 321 NYQILQYFIIRMFQVVEKSTGTSHS----VKQLQFTKWPDHGTPASADSFIKYIRYArKSHLT---GPMVVHCSAGIGRT 393
Cdd:cd14551    77 DTVVLVDYTTRKFCIQKVNRGIGEKrvrlVTQFHFTSWPDFGVPFTPIGMLKFLKKV-KSANPpraGPIVVHCSAGVGRT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462518410 394 GVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 439
Cdd:cd14551   156 GTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 240-442 2.93e-40

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: 143.22  E-value: 2.93e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 240 DYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVFL 319
Cdd:cd14622     1 DYINASFID--GYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPS--EGSVTHGEITIEI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 320 ENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL-TG--PMVVHCSAGIGRTGVF 396
Cdd:cd14622    77 KNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQqTGnhPIVVHCSAGAGRTGTF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462518410 397 LCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIV 442
Cdd:cd14622   157 IALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 240-444 5.75e-40

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: 144.79  E-value: 5.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 240 DYINASYIrIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPislKKPLELKH-FRVF 318
Cdd:cd14609    71 DYINASPI-IEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWP---DEGSSLYHiYEVN 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 319 LENYQI-LQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGV 395
Cdd:cd14609   147 LVSEHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYrgRSCPIIVHCSDGAGRTGT 226

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462518410 396 FLCVDVVFCAIVKNC-SFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:cd14609   227 YILIDMVLNRMAKGVkEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 226-442 1.31e-39

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: 143.08  E-value: 1.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 226 LKDDSTRVPLgKSKD-------YINASYIRIVNcGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIKC 298
Cdd:cd14613    35 LPNPHSRVCL-TSPDqddplssYINANYIRGYG-GEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMIT-NIEEMNEKC 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 299 YHYWP----------ISLKKPLELKHFRvflenyqilqyfiIRMFQVveKSTGTSHSVKQLQFTKWPDHGTPASADSFIK 368
Cdd:cd14613   112 TEYWPeeqvtyegieITVKQVIHADDYR-------------LRLITL--KSGGEERGLKHYWYTSWPDQKTPDNAPPLLQ 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 369 YIR-------YARKSHltGPMVVHCSAGIGRTGVFLCVDVVfCAIVKNCS-FNIMDIVAQMREQRSGMVQTKEQYHFCYD 440
Cdd:cd14613   177 LVQeveearqQAEPNC--GPVIVHCSAGIGRTGCFIATSIC-CKQLRNEGvVDILRTTCQLRLDRGGMIQTCEQYQFVHH 253


                  ..
gi 2462518410 441 IV 442
Cdd:cd14613   254 VL 255
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 229-444 5.57e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 142.83  E-value: 5.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPLGKSK---DYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIS 305
Cdd:PHA02742   65 DRNRVILKIEDggdDFINASYVDGHNAKGRF--ICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPH 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 306 LKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTG----- 380
Cdd:PHA02742  143 ERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVREADLKAdvdik 222

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462518410 381 --------PMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:PHA02742  223 genivkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 229-453 7.10e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 142.83  E-value: 7.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPL----GKSKDYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMIT-REIEGGIIKCYHYWP 303
Cdd:PHA02747   64 DHNRVILdsggGSTSDYIHANWIDGFE--DDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWC 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 304 ISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIR------------ 371
Cdd:PHA02747  142 LNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKFIKiidinrkksgkl 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 372 YARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHF---CYDIVLEVLRK 448
Cdd:PHA02747  222 FNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFiqpGYEVLHYFLSK 301


                  ....*
gi 2462518410 449 LLTLD 453
Cdd:PHA02747  302 IKAID 306
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 237-444 1.03e-36

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: 134.40  E-value: 1.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 237 KSKDYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISlkKPLELKHFR 316
Cdd:cd14623    22 ENTDYVNASFID--GYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPSD--GSVSYGDIT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 317 VFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTG---PMVVHCSAGIGRT 393
Cdd:cd14623    98 IELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQSgnhPITVHCSAGAGRT 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462518410 394 GVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:cd14623   178 GTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 345-444 2.38e-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: 129.40  E-value: 2.38e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410  345 SVKQLQFTKWPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVfCAIVKNCS--FNIMDIV 418
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLnqseSSGPVVVHCSAGVGRTGTFVAIDIL-LQQLEAEAgeVDIFDTV 79

                           90       100
                   ....*....|....*....|....*.
gi 2462518410  419 AQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:smart00012  80 KELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
345-444 2.38e-36

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 129.40  E-value: 2.38e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410  345 SVKQLQFTKWPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVfCAIVKNCS--FNIMDIV 418
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLnqseSSGPVVVHCSAGVGRTGTFVAIDIL-LQQLEAEAgeVDIFDTV 79

                           90       100
                   ....*....|....*....|....*.
gi 2462518410  419 AQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:smart00404  80 KELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 240-444 6.45e-36

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: 134.38  E-value: 6.45e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 240 DYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVFL 319
Cdd:cd14621    81 DYINASFIN--GYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPD--QGCWTYGNIRVSV 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 320 ENYQILQYFIIRMF--QVVEKSTGTSHS--VKQLQFTKWPDHGTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRT 393
Cdd:cd14621   157 EDVTVLVDYTVRKFciQQVGDVTNKKPQrlITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNpqYAGAIVVHCSAGVGRT 236

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462518410 394 GVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:cd14621   237 GTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 241-440 8.83e-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: 125.60  E-value: 8.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIrivncgEEY----FYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIKCYHYWPIslKKPLELKHFR 316
Cdd:cd14556     1 YINAALL------DSYkqpaAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLN-QLDPKDQSCPQYWPD--EGSGTYGPIQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 317 VFLENYQILQYFIIRMFQVVE--KSTGTSHSVKQLQFTKWPDHG-TPASADSFIKYIRYARK---SHLTGPMVVHCSAGI 390
Cdd:cd14556    72 VEFVSTTIDEDVISRIFRLQNttRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKwqeQSGEGPIVVHCLNGV 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462518410 391 GRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 440
Cdd:cd14556   152 GRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PHA02738 PHA02738
hypothetical protein; Provisional
 229-442 9.44e-32

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 123.50  E-value: 9.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 229 DSTRVPLGKSK---DYINASYIRivncGEEYF--YIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP 303
Cdd:PHA02738   62 DHSRVILPAERnrgDYINANYVD----GFEYKkkFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWS 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 304 ISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEkSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR--------- 374
Cdd:PHA02738  138 DVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRqcqkelaqe 216

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462518410 375 ------KSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIV 442
Cdd:PHA02738  217 slqighNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 106-446 5.05e-31

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 121.67  E-value: 5.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 106 IFNFHEQT-AIKDCLKILEEKTAAYDImqefmalelkNLPGEFNSGNQPSNREKNRYRDILPLKAAmpppseeidatlpe 184
Cdd:PHA02746   11 AFDFFDKTnHAKFCEFVLLEHAEVMDI----------PIRGTTNHFLKKENLKKNRFHDIPCWDHS-------------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 185 ETFITSPEFVALQDIADSSQdsqppsfiasrpitrlKSQQALKDDStrvplgkSKDYINASYIRivNCGEEYFYIATQGP 264
Cdd:PHA02746   67 RVVINAHESLKMFDVGDSDG----------------KKIEVTSEDN-------AENYIHANFVD--GFKEANKFICAQGP 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 265 LLSTIDDFWQMVLENNSNVIAMITrEIEGGIIKCYHYWpiSLKKPLELKHFRVFLENYQILQ--YFIIRMFQVVEKSTGT 342
Cdd:PHA02746  122 KEDTSEDFFKLISEHESQVIVSLT-DIDDDDEKCFELW--TKEEDSELAFGRFVAKILDIIEelSFTKTRLMITDKISDT 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 343 SHSVKQLQFTKWPDHGTPASADSFIKYIRYARK------------SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNC 410
Cdd:PHA02746  199 SREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadndPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEK 278

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2462518410 411 SFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 446
Cdd:PHA02746  279 EVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAI 314
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 241-444 6.22e-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: 6.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIkCYHYWPisLKKPLELKHFRVFLE 320
Cdd:cd14634     1 YINAALMD--SHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN-EMDAAQL-CMQYWP--EKTSCCYGPIQVEFV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 321 NYQILQYFIIRMFQV--VEKSTGTSHSVKQLQFTKWPDH-GTPASADSFIKYIRYARKSHLT-----GPMVVHCSAGIGR 392
Cdd:cd14634    75 SADIDEDIISRIFRIcnMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgreGRTVVHCLNGGGR 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462518410 393 TGVFlcvdvvfCAIVKNCSF----NIMDI---VAQMREQRSGMVQTKEQYHFCYDIVLE 444
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 ...
 241-439 6.05e-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: 95.85  E-value: 6.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGiiKCYHYWPISlKKPLELKHFRVFL- 319
Cdd:cd14550     1 YINASYLQGYRRSNEF--IITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTK-EKPLECETFKVTLs 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 320 ---------ENYQILQYFIIRMFQ---VVEkstgtshsVKQLQFTKWPDHGTPASadSFIKYIRYARKSHLT--GPMVVH 385
Cdd:cd14550    76 gedhsclsnEIRLIVRDFILESTQddyVLE--------VRQFQCPSWPNPCSPIH--TVFELINTVQEWAQQrdGPIVVH 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462518410 386 -----CSAGigrtgvflcvdvVFCAI------VKNCsfNIMDI--VAQMREQ-RSGMVQTKEQYHFCY 439
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 ...
 241-444 1.74e-22

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: 1.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIkCYHYWP---ISLKKPLELKHFRV 317
Cdd:cd14635     1 YINAALMD--SYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLN-DVDPAQL-CPQYWPengVHRHGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 318 FLENYQILQYFiiRMFQVVEKSTGTsHSVKQLQFTKWPDH-GTPASADSFIKYIRYARKSHLT-----GPMVVHCSAGIG 391
Cdd:cd14635    77 DLEEDIISRIF--RIYNAARPQDGY-RMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynggeGRTVVHCLNGGG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462518410 392 RTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:cd14635   154 RSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 241-444 1.80e-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: 91.89  E-value: 1.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINA----SYIRIVNcgeeyfYIATQGPLLSTIDDFWQMVLENNSNVIAMITR-EIEGGIIKCYHYWP---ISLKKPLEL 312
Cdd:cd14637     1 YINAaltdSYTRSAA------FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQlNQSNSAWPCLQYWPepgLQQYGPMEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 313 KHFRVFLEnyqilQYFIIRMFQV--VEKSTGTSHSVKQLQFTKW-PDHGTPASADSFIKYI----RYARKSHlTGPMVVH 385
Cdd:cd14637    75 EFVSGSAD-----EDIVTRLFRVqnITRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLasveKWQRESG-EGRTVVH 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462518410 386 CSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:cd14637   149 CLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 241-444 9.40e-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: 90.08  E-value: 9.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITR-EIEGGiikCYHYWP---ISLKKPLELKHFR 316
Cdd:cd14636     1 YINAALMDSYR--QPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEvDLAQG---CPQYWPeegMLRYGPIQVECMS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 317 VFLENYQILQYFiiRMFQVVEKSTGTShSVKQLQFTKWPDH-GTPASADSFIKYIRYARK-----SHLTGPMVVHCSAGI 390
Cdd:cd14636    76 CSMDCDVISRIF--RICNLTRPQEGYL-MVQQFQYLGWASHrEVPGSKRSFLKLILQVEKwqeecDEGEGRTIIHCLNGG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462518410 391 GRTGVFLCVDVVfCAIVKNCsfNIMDI---VAQMREQRSGMVQTKEQYHFCYDIVLE 444
Cdd:cd14636   153 GRSGMFCAISIV-CEMIKRQ--NVVDVfhaVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 241-443 1.04e-20

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: 89.67  E-value: 1.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYhYWPiSLKKPLELKHFRVFL- 319
Cdd:cd17669     1 YINASYIMGYYQSNEF--IITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWP-NKDEPINCETFKVTLi 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 320 ---------ENYQILQYFIIRMFQ---VVEkstgtshsVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTGPMVVHCS 387
Cdd:cd17669    77 aeehkclsnEEKLIIQDFILEATQddyVLE--------VRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDE 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462518410 388 AGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVL 443
Cdd:cd17669   149 HGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 226-435 4.96e-19

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: 85.53  E-value: 4.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 226 LKDDSTRVPLGKSKDyINASYIRIvncGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMIT--REIEGGIIKCY---- 299
Cdd:cd14559     3 FTNIQTRVSTPVGKN-LNANRVQI---GNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLAsnKDIQRKGLPPYfrqs 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 300 -HYWPISLKKPLELKhfrvflenYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHgTPASADSFIK---YIRYARK 375
Cdd:cd14559    79 gTYGSVTVKSKKTGK--------DELVDGLKADMYNLKITDGNKTITIPVVHVTNWPDH-TAISSEGLKEladLVNKSAE 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462518410 376 SHLTGPM---------------VVHCSAGIGRTGVFLCvdvVFCAIVKNCSFNIMDIVAQMREQRSG-MVQTKEQY 435
Cdd:cd14559   150 EKRNFYKskgssaindknkllpVIHCRAGVGRTGQLAA---AMELNKSPNNLSVEDIVSDMRTSRNGkMVQKDEQL 222
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 241-443 1.80e-16

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: 1.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 241 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIKCYHYWPiSLKKPLELKHFRVFLE 320
Cdd:cd17670     1 YINASYIMGYYRSNEF--IITQHPLPHTTKDFWRMIWDHNAQIIVMLP-DNQGLAEDEFVYWP-SREESMNCEAFTVTLI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 321 NYQIL-----QYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASadSFIKYIRYARKSHLT--GPMVVHCSAGIGRT 393
Cdd:cd17670    77 SKDRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPIS--STFELINVIKEEALTrdGPTIVHDEFGAVSA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462518410 394 GVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVL 443
Cdd:cd17670   155 GTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 216-442 3.40e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 73.08  E-value: 3.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 216 PITRLKSQqalkddstRVPLGKSKDYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGgi 295
Cdd:PHA02740   61 HITRLLHR--------RIKLFNDEKVLDARFVDGYD--FEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK-- 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 296 iKCYH-YWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKStGTSHSVKQLQFTKWPDHGTPASADSFIKY----- 369
Cdd:PHA02740  129 -KCFNqFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDKF-GQAQKISHFQYTAWPADGFSHDPDAFIDFfcnid 206

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462518410 370 -----IRYARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIV 442
Cdd:PHA02740  207 dlcadLEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
354-437 8.45e-10

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 56.90  E-value: 8.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 354 WPDHGTP--ASADSFIKYIRYARKSHltGPMVVHCSAGIGRTGVFL-CVdvvfcAIVKNCSFNimDIVAQMREQRSGMVQ 430
Cdd:COG2453    55 IPDFGAPddEQLQEAVDFIDEALREG--KKVLVHCRGGIGRTGTVAaAY-----LVLLGLSAE--EALARVRAARPGAVE 125


                  ....*..
gi 2462518410 431 TKEQYHF 437
Cdd:COG2453   126 TPAQRAF 132
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 380-440 1.37e-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: 52.74  E-value: 1.37e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462518410 380 GPMVVHCSAGIGRTGVFLCvdvvfCAIVKNCSFNIMDIVAQMREQR-SGMVQTKEQYHFCYD 440
Cdd:cd14494    57 EPVLVHCKAGVGRTGTLVA-----CYLVLLGGMSAEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 364-437 2.45e-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: 52.66  E-value: 2.45e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462518410 364 DSFIKYIRYARKSHLtgPMVVHCSAGIGRTGVFLCvdvvfCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHF 437
Cdd:cd14504    69 DEFLDIVEEANAKNE--AVLVHCLAGKGRTGTMLA-----CYLVKTGKISAVDAINEIRRIRPGSIETSEQEKF 135
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 348-437 2.11e-05

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 44.63  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 348 QLQFTKWP--DHGTPASA--DSFIKYIR--YARKSHLTGPMVVHCSAGIGRTGVFLCVdvvfcAIVKNCSFNIMDIVAQM 421
Cdd:PTZ00242   61 GIEVHDWPfdDGAPPPKAviDNWLRLLDqeFAKQSTPPETIAVHCVAGLGRAPILVAL-----ALVEYGGMEPLDAVGFV 135

                          90
                  ....*....|....*.
gi 2462518410 422 REQRSGMVQTKeQYHF 437
Cdd:PTZ00242  136 REKRKGAINQT-QLQF 150
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 354-434 2.75e-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: 45.03  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518410 354 WPDHGTPASA---DSfIKYIRYARKshLTGPMVVHCSAGIGRTGVflcvdVVFCAIVKNCSFNIMDIVAQMREQRSGMVQ 430
Cdd:cd14506    84 WKDYGVPSLTtilDI-VKVMAFALQ--EGGKVAVHCHAGLGRTGV-----LIACYLVYALRMSADQAIRLVRSKRPNSIQ 155


                  ....
gi 2462518410 431 TKEQ 434
Cdd:cd14506   156 TRGQ 159
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 383-440 3.05e-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: 3.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462518410 383 VVHCSAGIGRTGVFL-CVdvvfcAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 440
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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