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Conserved domains on  [gi|564388256|ref|XP_006252829|]
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tyrosine-protein phosphatase non-receptor type 20 isoform X1 [Rattus norvegicus]

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 ...
 209-415 5.76e-125

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: 360.22  E-value: 5.76e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLE 288
Cdd:cd14596    1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 289 NFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHITGPLLVHCSAGVGRTGVFICVD 368
Cdd:cd14596   81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICVD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564388256 369 VVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVLQ 415
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 ...
 209-415 5.76e-125

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: 360.22  E-value: 5.76e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLE 288
Cdd:cd14596    1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 289 NFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHITGPLLVHCSAGVGRTGVFICVD 368
Cdd:cd14596   81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICVD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564388256 369 VVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVLQ 415
Cdd:cd14596  161 VLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
160-412 5.44e-114

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 334.24  E-value: 5.44e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256   160 IIREFLELEEM-IPPDDFKSGYELQNRDKNRYRDILPYDSTRVPL----GKNKDYINASYIRIVNHEEEYfyIATQGPLP 234
Cdd:smart00194   2 LEEEFEKLDRLkPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLkpppGEGSDYINASYIDGPNGPKAY--IATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256   235 DTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSV 314
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256   315 KHLQFIKWPDHGTPASADFFIKYVRYVRKSHI--TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQ 392
Cdd:smart00194 160 THYHYTNWPDHGVPESPESILDLIRAVRKSQStsTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                          250       260
                   ....*....|....*....|
gi 564388256   393 RFGMIQTKEQYQFCYEIVLE 412
Cdd:smart00194 240 RPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
184-412 2.37e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 323.81  E-value: 2.37e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256  184 NRDKNRYRDILPYDSTRVPLGK---NKDYINASYIRIvnHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIE 260
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGdpgPSDYINASYIDG--YKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256  261 GGVIKCCSYWPVSLKEPLEFKHFHV-LLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVR 339
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVtLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564388256  340 YVRKSHI---TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:pfam00102 159 KVRKSSLdgrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
187-405 5.45e-51

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 172.97  E-value: 5.45e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 187 KNRYRDILPYDSTRVplGKNKDYINASYIRIVNheeEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGV--I 264
Cdd:COG5599   45 LNRFRDIQPYKETAL--RANLGYLNANYIQVIG---NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKpkV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 265 KCCSYWPVS---LKEPLEFKhfhvLLENFQITQYFVIRIFQIVKKSTG-KSHSVKHLQFIKWPDHGTPaSADFFIKYVRY 340
Cdd:COG5599  120 KMPVYFRQDgeyGKYEVSSE----LTESIQLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAI-SAEALKNLADL 194

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388256 341 VRKSHIT-----GPLLVHCSAGVGRTGVFICVDVVFCTI--EKNYSFNIMNIVTQMRKQR-FGMIQTKEQYQF 405
Cdd:COG5599  195 IDKKEKIkdpdkLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRnGGMVQTSEQLDV 267
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 139-412 1.84e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 159.40  E-value: 1.84e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 139 SSSRAALRDCLKALQKKEELDIIREFLE--LEEMIPPDDFKSgYELQNRDKNRYRDILPYDSTRVPLGKNK---DYINAS 213
Cdd:PHA02742   6 SKKNSFAKNCEQLIEESNLAEILKEEHEhiMQEIVAFSCNES-LELKNMKKCRYPDAPCFDRNRVILKIEDggdDFINAS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 214 YIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLENFQIT 293
Cdd:PHA02742  85 YVD--GHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 294 QYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHITG-------------PLLVHCSAGVGR 360
Cdd:PHA02742 163 RNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVREADLKAdvdikgenivkepPILVHCSAGLDR 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564388256 361 TGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:PHA02742 243 AGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
 
Name Accession Description Interval E-value
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 209-415 5.76e-125

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: 360.22  E-value: 5.76e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLE 288
Cdd:cd14596    1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 289 NFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHITGPLLVHCSAGVGRTGVFICVD 368
Cdd:cd14596   81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICVD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564388256 369 VVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVLQ 415
Cdd:cd14596  161 VLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 209-414 5.76e-120

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: 347.44  E-value: 5.76e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPL-EFKHFHVLL 287
Cdd:cd14538    1 YINASHIRIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLiCGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 288 ENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHITGPLLVHCSAGVGRTGVFICV 367
Cdd:cd14538   81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNSGPIVVHCSAGIGRTGVLITI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564388256 368 DVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVL 414
Cdd:cd14538  161 DVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
160-412 5.44e-114

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 334.24  E-value: 5.44e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256   160 IIREFLELEEM-IPPDDFKSGYELQNRDKNRYRDILPYDSTRVPL----GKNKDYINASYIRIVNHEEEYfyIATQGPLP 234
Cdd:smart00194   2 LEEEFEKLDRLkPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLkpppGEGSDYINASYIDGPNGPKAY--IATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256   235 DTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSV 314
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256   315 KHLQFIKWPDHGTPASADFFIKYVRYVRKSHI--TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQ 392
Cdd:smart00194 160 THYHYTNWPDHGVPESPESILDLIRAVRKSQStsTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                          250       260
                   ....*....|....*....|
gi 564388256   393 RFGMIQTKEQYQFCYEIVLE 412
Cdd:smart00194 240 RPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
184-412 2.37e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 323.81  E-value: 2.37e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256  184 NRDKNRYRDILPYDSTRVPLGK---NKDYINASYIRIvnHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIE 260
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGdpgPSDYINASYIDG--YKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256  261 GGVIKCCSYWPVSLKEPLEFKHFHV-LLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVR 339
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVtLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564388256  340 YVRKSHI---TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:pfam00102 159 KVRKSSLdgrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 183-414 1.29e-97

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: 291.35  E-value: 1.29e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 183 QNRDKNRYRDILPYDSTRVPLGKNKDYINASYIRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGG 262
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPLGDEGGYINASFIKMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 263 VIKCCSYWPVSLKEPLEF-KHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYV 341
Cdd:cd14597   82 KIKCQRYWPEILGKTTMVdNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFISYM 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388256 342 RKSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVL 414
Cdd:cd14597  162 RHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILYVL 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 209-408 1.52e-87

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: 264.53  E-value: 1.52e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLE 288
Cdd:cd00047    1 YINASYIDGYRGPKEY--IATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 289 NFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHI--TGPLLVHCSAGVGRTGVFIC 366
Cdd:cd00047   79 SEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARkpNGPIVVHCSAGVGRTGTFIA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564388256 367 VDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 408
Cdd:cd00047  159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 160-407 4.16e-79

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: 245.35  E-value: 4.16e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 160 IIREFLELEEMIPPDDFKSGYELQNRDKNRYRDILPYDSTRVPLGK-----NKDYINASYIRivNHEEEYFYIATQGPLP 234
Cdd:cd14543    5 IYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKrngdeRTDYINANFMD--GYKQKNAYIATQGPLP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 235 DTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSV 314
Cdd:cd14543   83 KTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 315 KHLQFIKWPDHGTPASADFFIKYVRYVR--------------KSHITG-PLLVHCSAGVGRTGVFICVDVVFCTIEKNYS 379
Cdd:cd14543  163 THFQFTSWPDFGVPSSAAALLDFLGEVRqqqalavkamgdrwKGHPPGpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGT 242

                        250       260
                 ....*....|....*....|....*...
gi 564388256 380 FNIMNIVTQMRKQRFGMIQTKEQYQFCY 407
Cdd:cd14543  243 LNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 183-413 2.73e-75

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: 235.90  E-value: 2.73e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 183 QNRDKNRYRDILPYDSTRVPLGKNKDYINASYIR-------IVNHeeeyfYIATQGPLPDTIEDFWQMVLENNCNVIAMI 255
Cdd:cd14600   39 QNMDKNRYKDVLPYDATRVVLQGNEDYINASYVNmeipsanIVNK-----YIATQGPLPHTCAQFWQVVWEQKLSLIVML 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 256 TREIEGGVIKCCSYWPvSLKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFI 335
Cdd:cd14600  114 TTLTERGRTKCHQYWP-DPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFL 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564388256 336 KYVRYVRKSHITG-PLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEV 413
Cdd:cd14600  193 EFVNYVRSKRVENePVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRV 271
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 209-408 3.28e-73

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


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 228.29  E-value: 3.28e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRIVNHEEEYfYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPvSLKEPLEFKHFHV-LL 287
Cdd:cd18533    1 YINASYITLPGTSSKR-YIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWP-SGEYEGEYGDLTVeLV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 288 ENFQITQY-FVIRIFQiVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRK----SHITGPLLVHCSAGVGRTG 362
Cdd:cd18533   79 SEEENDDGgFIVREFE-LSKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElndsASLDPPIIVHCSAGVGRTG 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564388256 363 VFICVDVVFCTIEKNYSFN---------IMNIVTQMRKQRFGMIQTKEQYQFCYE 408
Cdd:cd18533  158 TFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 189-405 6.91e-72

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 225.31  E-value: 6.91e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 189 RYRDILPYDSTRVPL-----GKNKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGV 263
Cdd:cd14548    1 RYTNILPYDHSRVKLipineEEGSDYINANYIPGYNSPREF--IATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 264 IKCCSYWPVSlKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKstGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRK 343
Cdd:cd14548   79 VKCDHYWPFD-QDPVYYGDITVTMLSESVLPDWTIREFKLERG--DEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388256 344 S--HITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQF 405
Cdd:cd14548  156 YikQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 188-405 8.86e-70

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: 219.96  E-value: 8.86e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 188 NRYRDILPYDSTRVPLGKNKD-----YINASYIRIVNHEEEYfYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGG 262
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDdplssYINANYIRGYDGEEKA-YIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 263 ViKCCSYWPVslKEPLEFKHFHVLLENFQITQYFVIRifQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYV- 341
Cdd:cd14547   80 E-KCAQYWPE--EENETYGDFEVTVQSVKETDGYTVR--KLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVe 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388256 342 ---RKSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQF 405
Cdd:cd14547  155 earQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 187-407 7.25e-69

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: 217.64  E-value: 7.25e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 187 KNRYRDILPYDSTRVPLGKNK---DYINASyiRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGV 263
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQgdnDYINAS--LVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 264 IKCCSYWPVSLKEPLEFKH--FHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYV 341
Cdd:cd14545   79 IKCAQYWPQGEGNAMIFEDtgLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564388256 342 RKSHI----TGPLLVHCSAGVGRTGVFICVDVVFCTIEK-NYS-FNIMNIVTQMRKQRFGMIQTKEQYQFCY 407
Cdd:cd14545  159 RESGSlssdVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKgNPSsVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 208-413 3.43e-68

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


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 215.27  E-value: 3.43e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 208 DYINASYIR-------IVNHeeeyfYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVsLKEPLEF 280
Cdd:cd14541    1 DYINANYVNmeipgsgIVNR-----YIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPD-LGETMQF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 281 KHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHITG--PLLVHCSAGV 358
Cdd:cd14541   75 GNLQITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMvePTVVHCSAGI 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564388256 359 GRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEV 413
Cdd:cd14541  155 GRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 184-412 8.94e-68

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: 215.34  E-value: 8.94e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 184 NRDKNRYRDILPYDSTRVPLGK-----NKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITRE 258
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPiegvpGSDYINANYCD--GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 259 IEGGVIKCCSYWPVSLKEPLEFkhFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYV 338
Cdd:cd14553   81 EERSRVKCDQYWPTRGTETYGL--IQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564388256 339 RYVRKSHI--TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:cd14553  159 RRVKACNPpdAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 184-411 2.56e-67

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: 213.93  E-value: 2.56e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 184 NRDKNRYRDILPYDSTRVPLG-----KNKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITRE 258
Cdd:cd14554    6 NKFKNRLVNILPYESTRVCLQpirgvEGSDYINASFID--GYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 259 IEGGVIKCCSYWPvsLKEPLEFKHFHV-LLENFQITQYfVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY 337
Cdd:cd14554   84 REMGREKCHQYWP--AERSARYQYFVVdPMAEYNMPQY-ILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388256 338 VRYVRKSH----ITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVL 411
Cdd:cd14554  161 IGQVHKTKeqfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 183-413 1.73e-66

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


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 212.76  E-value: 1.73e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 183 QNRDKNRYRDILPYDSTRVPLG-----KNKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITR 257
Cdd:cd14603   29 ENVKKNRYKDILPYDQTRVILSllqeeGHSDYINANFIKGVDGSRAY--IATQGPLSHTVLDFWRMIWQYGVKVILMACR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 258 EIEGGVIKCCSYWPvSLKEPLEFKHFHV-LLENFQITQYFVIRIFQIVKKStgKSHSVKHLQFIKWPDHGTPASADFFIK 336
Cdd:cd14603  107 EIEMGKKKCERYWA-QEQEPLQTGPFTItLVKEKRLNEEVILRTLKVTFQK--ESRSVSHFQYMAWPDHGIPDSPDCMLA 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 337 YVRYVRKSHITG--PLLVHCSAGVGRTGVFICVDVV---FCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVL 411
Cdd:cd14603  184 MIELARRLQGSGpePLCVHCSAGCGRTGVICTVDYVrqlLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVA 263


                 ..
gi 564388256 412 EV 413
Cdd:cd14603  264 QM 265
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 209-414 1.07e-65

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: 209.23  E-value: 1.07e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKE--PLEFKHFHVL 286
Cdd:cd14540    1 YINASHITATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEhdALTFGEYKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 287 LENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY---VRYVRKsHITG---------PLLVHC 354
Cdd:cd14540   81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeINSVRR-HTNQdvaghnrnpPTLVHC 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 355 SAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVL 414
Cdd:cd14540  160 SAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 150-415 4.48e-63

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


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 204.85  E-value: 4.48e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 150 KALQKK-EELDIIREFLELEEMIPPDDFKSGYELQNRDKNRYRDILPYDSTRVPLGKNKD----YINASYIRIVNHEEEY 224
Cdd:cd14599    3 KTLERKlEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKEnntgYINASHIKVTVGGEEW 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 225 FYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPvslkePLEFKHFHVLLENFQITQYF-------V 297
Cdd:cd14599   83 HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWP-----KLGSKHSSATYGKFKVTTKFrtdsgcyA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 298 IRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY---VRYVRK---------SHITGPLLVHCSAGVGRTGVFI 365
Cdd:cd14599  158 TTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYleeIQSVRRhtnsmldstKNCNPPIVVHCSAGVGRTGVVI 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 564388256 366 CVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVLQ 415
Cdd:cd14599  238 LTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 188-412 3.17e-62

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: 200.43  E-value: 3.17e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 188 NRYRDILPYDSTRVPLG----KNKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGV 263
Cdd:cd14615    1 NRYNNVLPYDISRVKLSvqshSTDDYINANYMPGYNSKKEF--IAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 264 IKCCSYWPVslKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY---VR- 339
Cdd:cd14615   79 TKCEEYWPS--KQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFrhlVRe 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388256 340 YVRKSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:cd14615  157 YMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 188-414 5.77e-62

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: 200.12  E-value: 5.77e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 188 NRYRDILPYDSTRVPLGKNK-----DYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGG 262
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHeepgsDYINANYMPGYWSSQEF--IATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 263 VIKCCSYWPVSlKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVR 342
Cdd:cd14619   79 RVKCEHYWPLD-YTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564388256 343 K---SHI-TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVL 414
Cdd:cd14619  158 QwldQTMsGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 184-416 1.97e-60

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: 196.53  E-value: 1.97e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 184 NRDKNRYRDILPYDSTRVPLG------KNKDYINASYIRIVNHEEEYF-----YIATQGPLPDTIEDFWQMVLENNCNVI 252
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKdrdpnvPGSDYINANYIRNENEGPTTDenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 253 AMITREIEGGVIKCCSYWP--VSLKeplEFKHFHV--LLENfqITQYFVIRIFQIVKKSTGKS-HSVKHLQFIKWPDHGT 327
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPdeGMQK---QYGPYRVqnVSEH--DTTDYTLRELQVSKLDQGDPiREIWHYQYLSWPDHGV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 328 PASADFFIKYVRYV--RKSHI--TGPLLVHCSAGVGRTGVFICVDVVFCTIEKN---YSFNIMNIVTQMRKQRFGMIQTK 400
Cdd:cd14544  156 PSDPGGVLNFLEDVnqRQESLphAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKgldCDIDIQKTIQMVRSQRSGMVQTE 235

                        250
                 ....*....|....*.
gi 564388256 401 EQYQFCYEIVLEVLQN 416
Cdd:cd14544  236 AQYKFIYVAVAQYIET 251
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 188-408 1.43e-59

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: 193.60  E-value: 1.43e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 188 NRYRDILPYDSTRVPLGKNK-----DYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGG 262
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDddpcsDYINASYIPGNNFRREY--IATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 263 VIKCCSYWPVSlKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHS-VKHLQFIKWPDHGTPASADFFIKYVR-- 339
Cdd:cd14617   79 RVKCDHYWPAD-QDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRlVRHFHYTVWPDHGVPETTQSLIQFVRtv 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388256 340 --YVRKSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 408
Cdd:cd14617  158 rdYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 164-410 1.74e-58

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


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 192.10  E-value: 1.74e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 164 FLELEEMIPPDDFKSGYELQNRDKNRYRDILPYDSTRVPL-GKNKDYINASYIRIvnHEEEYFYIATQGPLPDTIEDFWQ 242
Cdd:cd14607    4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLqNTENDYINASLVVI--EEAQRSYILTQGPLPNTCCHFWL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 243 MVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKH--FHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFI 320
Cdd:cd14607   82 MVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 321 KWPDHGTPASADFFIKYVRYVRKSHI----TGPLLVHCSAGVGRTGVFICVDVVFCTIEKN--YSFNIMNIVTQMRKQRF 394
Cdd:cd14607  162 TWPDFGVPESPASFLNFLFKVRESGSlspeHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKdpDSVDIKQVLLDMRKYRM 241

                        250
                 ....*....|....*.
gi 564388256 395 GMIQTKEQYQFCYEIV 410
Cdd:cd14607  242 GLIQTPDQLRFSYMAV 257
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 184-414 2.62e-58

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: 192.64  E-value: 2.62e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 184 NRDKNRYRDILPYDSTRVPLG-----KNKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITRE 258
Cdd:cd14627   53 NKFKNRLVNIMPYETTRVCLQpirgvEGSDYINASFID--GYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKL 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 259 IEGGVIKCCSYWPVslKEPLEFKHFHV-LLENFQITQYfVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY 337
Cdd:cd14627  131 REMGREKCHQYWPA--ERSARYQYFVVdPMAEYNMPQY-ILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 338 VRYVRKSH----ITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEV 413
Cdd:cd14627  208 IGQVHKTKeqfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEY 287


                 .
gi 564388256 414 L 414
Cdd:cd14627  288 L 288
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 183-412 2.99e-58

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: 192.16  E-value: 2.99e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 183 QNRDKNRYRDILPYDSTRVPLGK-NKDYINASYIRIvnHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEG 261
Cdd:cd14608   24 KNKNRNRYRDVSPFDHSRIKLHQeDNDYINASLIKM--EEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 262 GVIKCCSYWPVSLKEPLEFK--HFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVR 339
Cdd:cd14608  102 GSLKCAQYWPQKEEKEMIFEdtNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLF 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 340 YVRKSHIT----GPLLVHCSAGVGRTGVFICVDVVFCTIEKN---YSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:cd14608  182 KVRESGSLspehGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 261
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 173-407 3.46e-58

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: 190.82  E-value: 3.46e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 173 PDDFKSGYELQ---NRDKNRYRDILPYDSTRVPLGKNK------DYINASYIRIVNHEEEYfYIATQGPLPDTIEDFWQM 243
Cdd:cd14612    1 PPNFVSPEELDipgHASKDRYKTILPNPQSRVCLRRAGsqeeegSYINANYIRGYDGKEKA-YIATQGPMLNTVSDFWEM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 244 VLENNCNVIAMITREIEGGViKCCSYWPvslKEPLEFKHFHVLLENFQITQYFVIRifQIVKKSTGKSHSVKHLQFIKWP 323
Cdd:cd14612   80 VWQEECPIIVMITKLKEKKE-KCVHYWP---EKEGTYGRFEIRVQDMKECDGYTIR--DLTIQLEEESRSVKHYWFSSWP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 324 DHGTPASADFFIKYVRYVRKSHIT----GPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQT 399
Cdd:cd14612  154 DHQTPESAGPLLRLVAEVEESRQTaaspGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQT 233


                 ....*...
gi 564388256 400 KEQYQFCY 407
Cdd:cd14612  234 SEQYQFLH 241
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 184-411 4.15e-58

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 190.48  E-value: 4.15e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 184 NRDKNRYRDILPYDSTRVPL-----GKNKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITRE 258
Cdd:cd14614   12 NRCKNRYTNILPYDFSRVKLvsmheEEGSDYINANYIPGYNSPQEY--IATQGPLPETRNDFWKMVLQQKSQIIVMLTQC 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 259 IEGGVIKCCSYWPVSlKEPLEFKHFHVLLENFQITQYFVIRIFQIvkKSTGKSHSVKHLQFIKWPDHGTPA--SADFFIK 336
Cdd:cd14614   90 NEKRRVKCDHYWPFT-EEPVAYGDITVEMLSEEEQPDWAIREFRV--SYADEVQDVMHFNYTAWPDHGVPTanAAESILQ 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388256 337 YVRYVRKSHIT--GPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVL 411
Cdd:cd14614  167 FVQMVRQQAVKskGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 243
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 169-418 5.69e-58

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


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 192.07  E-value: 5.69e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 169 EMIPPDDFksGYELQNRDKNRYRDILPYDSTRVPL-----GKNKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQM 243
Cdd:cd14604   44 EKIYPTAT--GEKEENVKKNRYKDILPFDHSRVKLtlktsSQDSDYINANFIKGVYGPKAY--IATQGPLANTVIDFWRM 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 244 VLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLENFQITQYFVIRIFQIvkKSTGKSHSVKHLQFIKWP 323
Cdd:cd14604  120 IWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLL--EFQNETRRLYQFHYVNWP 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 324 DHGTPASADFFIKYVRYVRK--SHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNY---SFNIMNIVTQMRKQRFGMIQ 398
Cdd:cd14604  198 DHDVPSSFDSILDMISLMRKyqEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQ 277

                        250       260
                 ....*....|....*....|
gi 564388256 399 TKEQYQFCYEIVLEVLQNLL 418
Cdd:cd14604  278 TKEQYELVHRAIAQLFEKQL 297
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 209-408 8.03e-58

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: 188.33  E-value: 8.03e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEplEFKHFHVLLE 288
Cdd:cd14549    1 YINANYVDGYNKARAY--IATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE--TYGNIQVTLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 289 NFQITQYFVIRIFQI--VKKSTGKSHS----VKHLQFIKWPDHGTPASAdffIKYVRYVRKS-----HITGPLLVHCSAG 357
Cdd:cd14549   77 STEVLATYTVRTFSLknLKLKKVKGRSservVYQYHYTQWPDHGVPDYT---LPVLSFVRKSsaanpPGAGPIVVHCSAG 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564388256 358 VGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 408
Cdd:cd14549  154 VGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 145-412 1.33e-56

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: 187.55  E-value: 1.33e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 145 LRDCLKALQKKEELDIIREFlelEEMIPPDDF---KSGYELqNRDKNRYRDILPYDSTRVPLGK-----NKDYINASYIR 216
Cdd:cd14626    3 LADNIERLKANDGLKFSQEY---ESIDPGQQFtweNSNLEV-NKPKNRYANVIAYDHSRVILTSvdgvpGSDYINANYID 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 217 ivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFhVLLENFQITQYF 296
Cdd:cd14626   79 --GYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQV-TLLDTVELATYS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 297 ViRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHI--TGPLLVHCSAGVGRTGVFICVDVVFCTI 374
Cdd:cd14626  156 V-RTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPpdAGPMVVHCSAGVGRTGCFIVIDAMLERM 234

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564388256 375 EKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:cd14626  235 KHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 184-414 7.67e-56

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: 186.09  E-value: 7.67e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 184 NRDKNRYRDILPYDSTRVPLG-----KNKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITRE 258
Cdd:cd14628   52 NKFKNRLVNIMPYESTRVCLQpirgvEGSDYINASFID--GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKL 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 259 IEGGVIKCCSYWPVslKEPLEFKHFHV-LLENFQITQYfVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY 337
Cdd:cd14628  130 REMGREKCHQYWPA--ERSARYQYFVVdPMAEYNMPQY-ILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 338 VRYVRKSH----ITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEV 413
Cdd:cd14628  207 IGQVHKTKeqfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEY 286


                 .
gi 564388256 414 L 414
Cdd:cd14628  287 L 287
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 188-411 1.41e-55

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: 183.61  E-value: 1.41e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 188 NRYRDILPYDSTRVPLGK-----NKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGG 262
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQlggepHSDYINANFIPGYTSPQEF--IATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 263 VIKCCSYWPVSLKePLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVR 342
Cdd:cd14618   79 RVLCDHYWPSEST-PVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388256 343 KsHI-----TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVL 411
Cdd:cd14618  158 E-HVqatkgKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 209-407 2.19e-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: 181.85  E-value: 2.19e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLE 288
Cdd:cd14542    1 YINANFIKGVSGSKAY--IATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 289 NFQ-ITQYFVIRIFQIVKKSTgkSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRK--SHITGPLLVHCSAGVGRTGVFI 365
Cdd:cd14542   79 KEKrVGPDFLIRTLKVTFQKE--SRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDyqGSEDVPICVHCSAGCGRTGTIC 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 564388256 366 CVDVVFCTIEK---NYSFNIMNIVTQMRKQRFGMIQTKEQYQFCY 407
Cdd:cd14542  157 AIDYVWNLLKTgkiPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 187-413 3.22e-55

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


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 182.73  E-value: 3.22e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 187 KNRYRDILPYDSTRVPLG-----KNKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEG 261
Cdd:cd14602    1 KNRYKDILPYDHSRVELSlitsdEDSDYINANFIKGVYGPRAY--IATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 262 GVIKCCSYWPVSLKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKStgKSHSVKHLQFIKWPDHGTPASADFFIKYVRYV 341
Cdd:cd14602   79 GKKKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS--ETRTIYQFHYKNWPDHDVPSSIDPILELIWDV 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388256 342 R--KSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNY---SFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEV 413
Cdd:cd14602  157 RcyQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIipeNFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 183-412 8.71e-55

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: 181.76  E-value: 8.71e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 183 QNRDKNRYRDILPYDSTRVPL-----GKNKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITR 257
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLqlldgDPHSDYINANYID--GYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 258 EIEGGVIKCCSYWPVSLKEPLEFKHfhVLLENFQITQYfVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY 337
Cdd:cd14630   80 LVEVGRVKCVRYWPDDTEVYGDIKV--TLIETEPLAEY-VIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGF 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388256 338 VRYVR--KSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:cd14630  157 VRQVKflNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 209-408 1.96e-54

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: 179.58  E-value: 1.96e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEG-GVIKCCSYWPVSLKEPLEFKHFHVLL 287
Cdd:cd17658    1 YINASLVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNySTAKCADYFPAEENESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 288 ENFQITQY-FVIRIFQI-VKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRyvRKSHI---TGPLLVHCSAGVGRTG 362
Cdd:cd17658   81 KKLKHSQHsITLRVLEVqYIESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLK--RLYGIppsAGPIVVHCSAGIGRTG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564388256 363 VFICVDVVFCTIEKN--YSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 408
Cdd:cd17658  159 AYCTIHNTIRRILEGdmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 183-412 2.91e-54

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: 181.39  E-value: 2.91e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 183 QNRDKNRYRDILPYDSTRVPL-----GKNKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITR 257
Cdd:cd14633   39 ENRMKNRYGNIIAYDHSRVRLqpiegETSSDYINGNYID--GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTN 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 258 EIEGGVIKCCSYWPvslKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY 337
Cdd:cd14633  117 LVEVGRVKCCKYWP---DDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGF 193

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388256 338 VRYVRKSH--ITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:cd14633  194 VRQVKSKSppNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 184-414 3.59e-54

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: 181.85  E-value: 3.59e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 184 NRDKNRYRDILPYDSTRVPLG-----KNKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITRE 258
Cdd:cd14629   53 NKFKNRLVNIMPYELTRVCLQpirgvEGSDYINASFID--GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKL 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 259 IEGGVIKCCSYWPVslKEPLEFKHFHV-LLENFQITQYfVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY 337
Cdd:cd14629  131 REMGREKCHQYWPA--ERSARYQYFVVdPMAEYNMPQY-ILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDF 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 338 VRYVRKSH----ITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEV 413
Cdd:cd14629  208 IGQVHKTKeqfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEY 287


                 .
gi 564388256 414 L 414
Cdd:cd14629  288 L 288
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 184-414 2.00e-53

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: 179.46  E-value: 2.00e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 184 NRDKNRYRDILPYDSTRVPL-------GKNKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMIT 256
Cdd:cd17667   27 NKHKNRYINILAYDHSRVKLrplpgkdSKHSDYINANYVDGYNKAKAY--IATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 257 REIEGGVIKCCSYWPVSLKEplEFKHFHVLLENFQITQYFVIRIFQI----VKKSTGKS-------HSVKHLQFIKWPDH 325
Cdd:cd17667  105 NLVEKGRRKCDQYWPTENSE--EYGNIIVTLKSTKIHACYTVRRFSIrntkVKKGQKGNpkgrqneRTVIQYHYTQWPDM 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 326 GTPasaDFFIKYVRYVRKSHI-----TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTK 400
Cdd:cd17667  183 GVP---EYALPVLTFVRRSSAartpeMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 259

                        250
                 ....*....|....
gi 564388256 401 EQYQFCYEIVLEVL 414
Cdd:cd17667  260 EQYIFIHDALLEAI 273
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 209-412 3.24e-53

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: 176.26  E-value: 3.24e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPvslKEPLEFKHFHVLLE 288
Cdd:cd14555    1 YINANYID--GYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP---DDTEVYGDIKVTLV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 289 NFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSH--ITGPLLVHCSAGVGRTGVFIC 366
Cdd:cd14555   76 ETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNppSAGPIVVHCSAGAGRTGCYIV 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564388256 367 VDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:cd14555  156 IDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 166-414 5.63e-53

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: 178.36  E-value: 5.63e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 166 ELEEMIPPDDFK---SGYELqNRDKNRYRDILPYDSTRVPLGK-----NKDYINASYIRivNHEEEYFYIATQGPLPDTI 237
Cdd:cd14625   27 EYESIDPGQQFTwehSNLEV-NKPKNRYANVIAYDHSRVILQPiegimGSDYINANYID--GYRKQNAYIATQGPLPETF 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 238 EDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFhVLLENFQITQyFVIRIFQIVKKSTGKSHSVKHL 317
Cdd:cd14625  104 GDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQV-TLLDTIELAT-FCVRTFSLHKNGSSEKREVRQF 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 318 QFIKWPDHGTPASADFFIKYVRYVRKSHI--TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFG 395
Cdd:cd14625  182 QFTAWPDHGVPEYPTPFLAFLRRVKTCNPpdAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNY 261

                        250
                 ....*....|....*....
gi 564388256 396 MIQTKEQYQFCYEIVLEVL 414
Cdd:cd14625  262 MVQTEDQYSFIHDALLEAV 280
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 209-408 8.06e-53

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: 175.26  E-value: 8.06e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIR-IVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLL 287
Cdd:cd14539    1 YINASLIEdLTPYCPRF--IATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 288 ENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYV-------RKSHItgPLLVHCSAGVGR 360
Cdd:cd14539   79 QSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVhshylqqRSLQT--PIVVHCSSGVGR 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564388256 361 TGVFICVDVVFCTIEK-NYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 408
Cdd:cd14539  157 TGAFCLLYAAVQEIEAgNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 183-410 2.01e-52

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: 175.98  E-value: 2.01e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 183 QNRDKNRYRDILPYDSTRVPLGKN------KDYINASYI------RIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCN 250
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDGdpnepvSDYINANIImpefetKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 251 VIAMITREIEGGVIKCCSYWPvslkEPLEFKHFHVL-LENFQIT--QYFVIRIFQIVKKSTGKSH-SVKHLQFIKWPDHG 326
Cdd:cd14605   81 VIVMTTKEVERGKSKCVKYWP----DEYALKEYGVMrVRNVKESaaHDYILRELKLSKVGQGNTErTVWQYHFRTWPDHG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 327 TPASADFFIKYVRYV--RKSHIT--GPLLVHCSAGVGRTGVFICVDVVFCTI-EK--NYSFNIMNIVTQMRKQRFGMIQT 399
Cdd:cd14605  157 VPSDPGGVLDFLEEVhhKQESIMdaGPVVVHCSAGIGRTGTFIVIDILIDIIrEKgvDCDIDVPKTIQMVRSQRSGMVQT 236

                        250
                 ....*....|.
gi 564388256 400 KEQYQFCYEIV 410
Cdd:cd14605  237 EAQYRFIYMAV 247
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 208-413 2.65e-52

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 174.36  E-value: 2.65e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 208 DYINASYIR-------IVNHeeeyfYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPvslkEPL-- 278
Cdd:cd14601    1 DYINANYINmeipsssIINR-----YIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP----EPSgs 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 279 -EFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHITG--PLLVHCS 355
Cdd:cd14601   72 sSYGGFQVTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKdePVVVHCS 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564388256 356 AGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEV 413
Cdd:cd14601  152 AGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKV 209
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 187-407 3.99e-52

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


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 174.34  E-value: 3.99e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 187 KNRYRDILPYDSTRVPLG-KNKD-----YINASYIRIVNHEEEYFyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIE 260
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKpKNSNdslstYINANYIRGYGGKEKAF-IATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 261 GGViKCCSYWPvslKEPLEFKHFHVLLENFQITQYFVIRifQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRY 340
Cdd:cd14611   81 KNE-KCVLYWP---EKRGIYGKVEVLVNSVKECDNYTIR--NLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLD 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388256 341 V----RKSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCY 407
Cdd:cd14611  155 VeedrLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 209-415 9.68e-52

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: 173.24  E-value: 9.68e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPvslkePLEFKHFHVLLE 288
Cdd:cd14598    1 YINASHIKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWP-----RLGSRHNTVTYG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 289 NFQITQYF-------VIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY---VRYVRKsHITG---------P 349
Cdd:cd14598   76 RFKITTRFrtdsgcyATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeIQSVRR-HTNStidpkspnpP 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564388256 350 LLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVLQ 415
Cdd:cd14598  155 VLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 175-415 2.02e-51

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: 173.91  E-value: 2.02e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 175 DFKSGYELQNRDKNRYRDILPYDSTRVPLG------KNKDYINASYIR---IVNHEEEYFYIATQGPLPDTIEDFWQMVL 245
Cdd:cd14606    9 QRLEGQRPENKSKNRYKNILPFDHSRVILQgrdsniPGSDYINANYVKnqlLGPDENAKTYIASQGCLEATVNDFWQMAW 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 246 ENNCNVIAMITREIEGGVIKCCSYWPVSLKEPlEFKHFHVLLENFQITQYFVIRIFQI-VKKSTGKSHSVKHLQFIKWPD 324
Cdd:cd14606   89 QENSRVIVMTTREVEKGRNKCVPYWPEVGMQR-AYGPYSVTNCGEHDTTEYKLRTLQVsPLDNGELIREIWHYQYLSWPD 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 325 HGTPASADFFIKYVRYVRKSHIT----GPLLVHCSAGVGRTGVFICVDVVFCTIEK---NYSFNIMNIVTQMRKQRFGMI 397
Cdd:cd14606  168 HGVPSEPGGVLSFLDQINQRQESlphaGPIIVHCSAGIGRTGTIIVIDMLMENISTkglDCDIDIQKTIQMVRAQRSGMV 247

                        250
                 ....*....|....*...
gi 564388256 398 QTKEQYQFCYEIVLEVLQ 415
Cdd:cd14606  248 QTEAQYKFIYVAIAQFIE 265
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 152-412 2.40e-51

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: 174.09  E-value: 2.40e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 152 LQKKEELDIIREFLELEEMIPPDDFkSGYELQNRDKNRYRDILPYDSTRVPL-GKNK----DYINASyiRIVNHEEEY-F 225
Cdd:cd14610   13 LKNKNRLEKEWEALCAYQAEPNATN-VAQREENVQKNRSLAVLPYDHSRIILkAENShshsDYINAS--PIMDHDPRNpA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 226 YIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPvslKEPLEFKH-FHVLLENFQI-TQYFVIRIFQI 303
Cdd:cd14610   90 YIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWP---DEGSNLYHiYEVNLVSEHIwCEDFLVRSFYL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 304 VKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSH--ITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNY-SF 380
Cdd:cd14610  167 KNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYrgRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAkEI 246

                        250       260       270
                 ....*....|....*....|....*....|..
gi 564388256 381 NIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:cd14610  247 DIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 278
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 209-412 4.40e-51

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: 171.00  E-value: 4.40e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRIVnHEEEYFyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPvslKEPLEFKHFHVLLE 288
Cdd:cd14632    1 YINANYIDGY-HRSNHF-IATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP---DDSDTYGDIKITLL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 289 NFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHI--TGPLLVHCSAGVGRTGVFIC 366
Cdd:cd14632   76 KTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPpdAGPVVVHCSAGAGRTGCYIV 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564388256 367 VDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:cd14632  156 LDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
187-405 5.45e-51

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 172.97  E-value: 5.45e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 187 KNRYRDILPYDSTRVplGKNKDYINASYIRIVNheeEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGV--I 264
Cdd:COG5599   45 LNRFRDIQPYKETAL--RANLGYLNANYIQVIG---NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKpkV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 265 KCCSYWPVS---LKEPLEFKhfhvLLENFQITQYFVIRIFQIVKKSTG-KSHSVKHLQFIKWPDHGTPaSADFFIKYVRY 340
Cdd:COG5599  120 KMPVYFRQDgeyGKYEVSSE----LTESIQLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAI-SAEALKNLADL 194

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388256 341 VRKSHIT-----GPLLVHCSAGVGRTGVFICVDVVFCTI--EKNYSFNIMNIVTQMRKQR-FGMIQTKEQYQF 405
Cdd:COG5599  195 IDKKEKIkdpdkLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRnGGMVQTSEQLDV 267
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 145-414 6.98e-51

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: 172.99  E-value: 6.98e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 145 LRDCLKALQKKEELDIIREFlelEEMIPPDDFK---SGYELqNRDKNRYRDILPYDSTRVPLGK-----NKDYINASYIR 216
Cdd:cd14624    9 LADHIERLKANDNLKFSQEY---ESIDPGQQFTwehSNLEV-NKPKNRYANVIAYDHSRVLLSAiegipGSDYINANYID 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 217 ivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFhVLLENFQITQYf 296
Cdd:cd14624   85 --GYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQV-TLLDTVELATY- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 297 VIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHI--TGPLLVHCSAGVGRTGVFICVDVVFCTI 374
Cdd:cd14624  161 CVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPpdAGPMVVHCSAGVGRTGCFIVIDAMLERI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 564388256 375 EKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVL 414
Cdd:cd14624  241 KHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 184-412 8.66e-51

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: 172.53  E-value: 8.66e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 184 NRDKNRYRDILPYDSTRVPLG-----KNKDYINASyiRIVNHEEEY-FYIATQGPLPDTIEDFWQMVLENNCNVIAMITR 257
Cdd:cd14609   42 NVKKNRNPDFVPYDHARIKLKaesnpSRSDYINAS--PIIEHDPRMpAYIATQGPLSHTIADFWQMVWENGCTVIVMLTP 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 258 EIEGGVIKCCSYWPvslKEPLEFKH-FHVLLENFQI-TQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFI 335
Cdd:cd14609  120 LVEDGVKQCDRYWP---DEGSSLYHiYEVNLVSEHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLL 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 336 KYVRYVRKSH--ITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNY-SFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:cd14609  197 DFRRKVNKCYrgRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVkEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 188-408 3.03e-49

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 166.62  E-value: 3.03e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 188 NRYRDILPYDSTRVPLGKN-----KDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGG 262
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADagvpgSDYINASYISGYLCPNEF--IATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 263 VIKCCSYWPVSLKEPLEFKHFHV--LLENFQITqyFVIRIFQIVKKstGKSHSVKHLQFIKWPDHGTPASADFFIKYVRY 340
Cdd:cd14616   79 RIRCHQYWPEDNKPVTVFGDIVItkLMEDVQID--WTIRDLKIERH--GDYMMVRQCNFTSWPEHGVPESSAPLIHFVKL 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 341 VR--KSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 408
Cdd:cd14616  155 VRasRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 209-408 4.69e-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: 163.23  E-value: 4.69e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEplEFKHFHVLLE 288
Cdd:cd17668    1 YINANYVDGYNKPKAY--IAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE--EYGNFLVTQK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 289 NFQITQYFVIRIFQI----VKKSTGKSHS----VKHLQFIKWPDHGTPasaDFFIKYVRYVRKS-----HITGPLLVHCS 355
Cdd:cd17668   77 SVQVLAYYTVRNFTLrntkIKKGSQKGRPsgrvVTQYHYTQWPDMGVP---EYTLPVLTFVRKAsyakrHAVGPVVVHCS 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564388256 356 AGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 408
Cdd:cd17668  154 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 190-412 9.07e-48

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: 163.19  E-value: 9.07e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 190 YRDILPYDSTRVPL-----GKNKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVI 264
Cdd:cd14620    1 YPNILPYDHSRVILsqldgIPCSDYINASYID--GYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 265 KCCSYWPVslKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHS---VKHLQFIKWPDHG---TPASADFFIKYV 338
Cdd:cd14620   79 KCYQYWPD--QGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAprlVTQLHFTSWPDFGvpfTPIGMLKFLKKV 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388256 339 RYVRKSHiTGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:cd14620  157 KSVNPVH-AGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 209-403 1.01e-47

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: 161.92  E-value: 1.01e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLE 288
Cdd:cd14557    1 YINASYID--GFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKIN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 289 NFQITQYFVIRIFQIV-KKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVR--KSHITGPLLVHCSAGVGRTGVFI 365
Cdd:cd14557   79 EEKICPDYIIRKLNINnKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNafNNFFSGPIVVHCSAGVGRTGTYI 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564388256 366 CVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQY 403
Cdd:cd14557  159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 187-410 1.02e-47

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: 163.88  E-value: 1.02e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 187 KNRYRDILPYDSTRVPL-GKNKD-----YINASYIRIVNhEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITrEIE 260
Cdd:cd14613   28 KNRYKTILPNPHSRVCLtSPDQDdplssYINANYIRGYG-GEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMIT-NIE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 261 GGVIKCCSYWPvslKEPLEFKHFHVLLENFQITQYFVIRIFQIvkKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRY 340
Cdd:cd14613  106 EMNEKCTEYWP---EEQVTYEGIEITVKQVIHADDYRLRLITL--KSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQE 180

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564388256 341 VRKSHI-----TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIV 410
Cdd:cd14613  181 VEEARQqaepnCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 209-408 1.79e-46

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


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 158.71  E-value: 1.79e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKeplEFKHFHVLLE 288
Cdd:cd14558    1 YINASFIDGYWGPKSL--IATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK---TYGDIEVELK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 289 NFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVR--------KSHITGPLLVHCSAGVGR 360
Cdd:cd14558   76 DTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKqklpyknsKHGRSVPIVVHCSDGSSR 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564388256 361 TGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 408
Cdd:cd14558  156 TGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 206-412 3.09e-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: 158.65  E-value: 3.09e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 206 NKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHV 285
Cdd:cd14631   12 SSDYINANYID--GYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 286 LLENFQitqYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSH--ITGPLLVHCSAGVGRTGV 363
Cdd:cd14631   90 EMEPLA---EYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNppSAGPIVVHCSAGAGRTGC 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564388256 364 FICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:cd14631  167 YIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 209-412 5.46e-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: 157.61  E-value: 5.46e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIrIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPvslKEPLEFKH-FHVLL 287
Cdd:cd14546    1 YINASTI-YDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP---EEGSEVYHiYEVHL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 288 ENFQI-TQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSH--ITGPLLVHCSAGVGRTGVF 364
Cdd:cd14546   77 VSEHIwCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYrgRSCPIVVHCSDGAGRTGTY 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564388256 365 ICVDVVFCTIEKNY-SFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:cd14546  157 ILIDMVLNRMAKGAkEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 209-410 8.39e-46

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: 157.05  E-value: 8.39e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRIVNHEEeyFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVslKEPLEFKHFHVLLE 288
Cdd:cd14552    1 YINASFIDGYRQKD--AYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPE--DGSVSSGDITVELK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 289 NFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHI---TGPLLVHCSAGVGRTGVFI 365
Cdd:cd14552   77 DQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQqsgNHPITVHCSAGAGRTGTFC 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 564388256 366 CVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIV 410
Cdd:cd14552  157 ALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 139-412 1.84e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 159.40  E-value: 1.84e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 139 SSSRAALRDCLKALQKKEELDIIREFLE--LEEMIPPDDFKSgYELQNRDKNRYRDILPYDSTRVPLGKNK---DYINAS 213
Cdd:PHA02742   6 SKKNSFAKNCEQLIEESNLAEILKEEHEhiMQEIVAFSCNES-LELKNMKKCRYPDAPCFDRNRVILKIEDggdDFINAS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 214 YIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLENFQIT 293
Cdd:PHA02742  85 YVD--GHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 294 QYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHITG-------------PLLVHCSAGVGR 360
Cdd:PHA02742 163 RNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVREADLKAdvdikgenivkepPILVHCSAGLDR 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564388256 361 TGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:PHA02742 243 AGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 183-412 5.16e-45

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: 157.88  E-value: 5.16e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 183 QNRDKNRYRDILPYDSTRVPLGK-----NKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITR 257
Cdd:cd14621   51 ENKEKNRYVNILPYDHSRVHLTPvegvpDSDYINASFIN--GYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTN 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 258 EIEGGVIKCCSYWPVslKEPLEFKHFHVLLENFQITQYFVIRIF--QIVKKSTGKSHS--VKHLQFIKWPDHGTPASADF 333
Cdd:cd14621  129 LKERKECKCAQYWPD--QGCWTYGNIRVSVEDVTVLVDYTVRKFciQQVGDVTNKKPQrlITQFHFTSWPDFGVPFTPIG 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 334 FIKYVRYVRKSH--ITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVL 411
Cdd:cd14621  207 MLKFLKKVKNCNpqYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALL 286


                 .
gi 564388256 412 E 412
Cdd:cd14621  287 E 287
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 208-410 8.63e-44

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: 151.70  E-value: 8.63e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 208 DYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVslKEPLEFKHFHVLL 287
Cdd:cd14622    1 DYINASFID--GYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPS--EGSVTHGEITIEI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 288 ENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHI-TG--PLLVHCSAGVGRTGVF 364
Cdd:cd14622   77 KNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQqTGnhPIVVHCSAGAGRTGTF 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564388256 365 ICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIV 410
Cdd:cd14622  157 IALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 183-420 2.35e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 148.61  E-value: 2.35e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 183 QNRDKNRYRDILPYDSTRVPL----GKNKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMIT-R 257
Cdd:PHA02747  50 ENQPKNRYWDIPCWDHNRVILdsggGSTSDYIHANWID--GFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTpT 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 258 EIEGGVIKCCSYWPVSLKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY 337
Cdd:PHA02747 128 KGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKF 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 338 VR------------YVRKSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQF 405
Cdd:PHA02747 208 IKiidinrkksgklFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLF 287

                        250
                 ....*....|....*...
gi 564388256 406 ---CYEIVLEVLQNLLAL 420
Cdd:PHA02747 288 iqpGYEVLHYFLSKIKAI 305
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 189-412 1.96e-40

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


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 143.65  E-value: 1.96e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 189 RYRDILPYDSTRV--PLGK---NKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGV 263
Cdd:cd14623    1 RVLQIIPYEFNRViiPVKRgeeNTDYVNASFID--GYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 264 IKCCSYWPVSlkEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRK 343
Cdd:cd14623   79 EKCAQYWPSD--GSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQK 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564388256 344 SHITG---PLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:cd14623  157 QQQQSgnhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 209-408 5.30e-40

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: 141.59  E-value: 5.30e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEplEFKHFHVLLE 288
Cdd:cd14551    1 YINASYID--GYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW--TYGNLRVRVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 289 NFQITQYFVIRIFQIVKKSTG----KSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHI--TGPLLVHCSAGVGRTG 362
Cdd:cd14551   77 DTVVLVDYTTRKFCIQKVNRGigekRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPprAGPIVVHCSAGVGRTG 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564388256 363 VFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 408
Cdd:cd14551  157 TFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 209-408 1.28e-39

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: 140.62  E-value: 1.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITrEIEGGVIKCCSYWPVslKEPLEFKHFHVLLE 288
Cdd:cd14556    1 YINAALLD--SYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLN-QLDPKDQSCPQYWPD--EGSGTYGPIQVEFV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 289 NFQITQYFVIRIFQIV--KKSTGKSHSVKHLQFIKWPDHG-TPASADFFIKYVRYVRK---SHITGPLLVHCSAGVGRTG 362
Cdd:cd14556   76 STTIDEDVISRIFRLQntTRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKwqeQSGEGPIVVHCLNGVGRSG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564388256 363 VFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 408
Cdd:cd14556  156 VFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PHA02738 PHA02738
hypothetical protein; Provisional
 181-410 1.59e-38

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 141.22  E-value: 1.59e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 181 ELQNRDKNRYRDILPYDSTRVPLGKNK---DYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITR 257
Cdd:PHA02738  46 EKKNRKLNRYLDAVCFDHSRVILPAERnrgDYINANYVDGFEYKKKF--ICGQAPTRQTCYDFYRMLWMEHVQIIVMLCK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 258 EIEGGVIKCCSYWPvslkeplEFKHFHVLLENFQITQYFVIRIFQIVKKS------TGKSHSVKHLQFIKWPDHGTPASA 331
Cdd:PHA02738 124 KKENGREKCFPYWS-------DVEQGSIRFGKFKITTTQVETHPHYVKSTllltdgTSATQTVTHFNFTAWPDHDVPKNT 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 332 DFFIKYVRYVR---------------KSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGM 396
Cdd:PHA02738 197 SEFLNFVLEVRqcqkelaqeslqighNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYS 276

                        250
                 ....*....|....
gi 564388256 397 IQTKEQYQFCYEIV 410
Cdd:PHA02738 277 LFIPFQYFFCYRAV 290
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
313-412 9.71e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 129.79  E-value: 9.71e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256   313 SVKHLQFIKWPDHGTPASADFFIKYVRYVRKSH----ITGPLLVHCSAGVGRTGVFICVDVVFCTIEK-NYSFNIMNIVT 387
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLnqseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 564388256   388 QMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 313-412 9.71e-37

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: 129.79  E-value: 9.71e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256   313 SVKHLQFIKWPDHGTPASADFFIKYVRYVRKSH----ITGPLLVHCSAGVGRTGVFICVDVVFCTIEK-NYSFNIMNIVT 387
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLnqseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 564388256   388 QMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 183-414 3.52e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 124.37  E-value: 3.52e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 183 QNRDKNRYRDILPYDSTRVPLG------------------------KNKDYINASYIRivNHEEEYFYIATQGPLPDTIE 238
Cdd:PHA02746  50 ENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkievtsedNAENYIHANFVD--GFKEANKFICAQGPKEDTSE 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 239 DFWQMVLENNCNVIAMITrEIEGGVIKCCSYWPVSLKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQ 318
Cdd:PHA02746 128 DFFKLISEHESQVIVSLT-DIDDDDEKCFELWTKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFW 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 319 FIKWPDHGTPASADFFIKYVRYVRK------------SHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIV 386
Cdd:PHA02746 207 FPDWPDNGIPTGMAEFLELINKVNEeqaelikqadndPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIV 286

                        250       260
                 ....*....|....*....|....*...
gi 564388256 387 TQMRKQRFGMIQTKEQYQFCYEIVLEVL 414
Cdd:PHA02746 287 LKIRKQRHSSVFLPEQYAFCYKALKYAI 314
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 209-412 6.26e-32

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: 120.51  E-value: 6.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITrEIEGGVIkCCSYWPVslKEPLEFKHFHVLLE 288
Cdd:cd14634    1 YINAALMD--SHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN-EMDAAQL-CMQYWPE--KTSCCYGPIQVEFV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 289 NFQITQYFVIRIFQIVKKSTGKS--HSVKHLQFIKWPDH-GTPASADFFIKYVRYVRKSHIT-----GPLLVHCSAGVGR 360
Cdd:cd14634   75 SADIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgreGRTVVHCLNGGGR 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564388256 361 TGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:cd14634  155 SGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 209-412 7.03e-28

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: 109.39  E-value: 7.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITrEIEGGVIkCCSYWP---VSLKEPLEFKHFHV 285
Cdd:cd14635    1 YINAALMD--SYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLN-DVDPAQL-CPQYWPengVHRHGPIQVEFVSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 286 LLENFQITQYFviRIFQIVKKSTGkSHSVKHLQFIKWPDH-GTPASADFFIKYVRYVRKSHIT-----GPLLVHCSAGVG 359
Cdd:cd14635   77 DLEEDIISRIF--RIYNAARPQDG-YRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynggeGRTVVHCLNGGG 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564388256 360 RTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:cd14635  154 RSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 209-408 5.97e-26

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: 103.94  E-value: 5.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGviKCCSYWPvSLKEPLEFKHF----- 283
Cdd:cd14550    1 YINASYLQGYRRSNEF--IITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWP-TKEKPLECETFkvtls 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 284 ---HVLLENFQ--ITQYFVIrifqivkKSTGKSH--SVKHLQFIKWPDHGTPASADF-FIKYVRYvRKSHITGPLLVHCS 355
Cdd:cd14550   76 gedHSCLSNEIrlIVRDFIL-------ESTQDDYvlEVRQFQCPSWPNPCSPIHTVFeLINTVQE-WAQQRDGPIVVHDR 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564388256 356 AGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 408
Cdd:cd14550  148 YGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 209-412 3.24e-24

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: 99.33  E-value: 3.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITrEIEGgVIKCCSYWPVslKEPLEFKHFHVLLE 288
Cdd:cd14636    1 YINAALMD--SYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN-EVDL-AQGCPQYWPE--EGMLRYGPIQVECM 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 289 NFQITQYFVIRIFQIVKKSTGKSH--SVKHLQFIKWPDH-GTPASADFFIKYVRYVRK-----SHITGPLLVHCSAGVGR 360
Cdd:cd14636   75 SCSMDCDVISRIFRICNLTRPQEGylMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKwqeecDEGEGRTIIHCLNGGGR 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564388256 361 TGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:cd14636  155 SGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 209-411 4.14e-23

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: 96.22  E-value: 4.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITrEIEGGVIKCCSYWPvSLKEPLEFKHF----- 283
Cdd:cd17669    1 YINASYIMGYYQSNEF--IITQHPLLHTIKDFWRMIWDHNAQLIVMLP-DGQNMAEDEFVYWP-NKDEPINCETFkvtli 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 284 ---HVLLENFQ--ITQYFVIRIFQivkksTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHITGPLLVHCSAGV 358
Cdd:cd17669   77 aeeHKCLSNEEklIIQDFILEATQ-----DDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGG 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564388256 359 GRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVL 411
Cdd:cd17669  152 VTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 209-412 2.39e-22

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: 94.20  E-value: 2.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINA----SYIRIVNheeeyfYIATQGPLPDTIEDFWQMVLENNCNVIAMITR-EIEGGVIKCCSYWPVSLKE---PLEF 280
Cdd:cd14637    1 YINAaltdSYTRSAA------FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQlNQSNSAWPCLQYWPEPGLQqygPMEV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 281 KHFHVLLENFQITQYFviRIFQIVKKSTGKShSVKHLQFIKW-PDHGTPASADFFIKYVRYVRK---SHITGPLLVHCSA 356
Cdd:cd14637   75 EFVSGSADEDIVTRLF--RVQNITRLQEGHL-MVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKwqrESGEGRTVVHCLN 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564388256 357 GVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 412
Cdd:cd14637  152 GGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 209-411 6.83e-21

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: 90.12  E-value: 6.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 209 YINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITrEIEGGVIKCCSYWPvSLKEPLEFKHFHVLL- 287
Cdd:cd17670    1 YINASYIMGYYRSNEF--IITQHPLPHTTKDFWRMIWDHNAQIIVMLP-DNQGLAEDEFVYWP-SREESMNCEAFTVTLi 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 288 --ENFQITQYFVIRIFQIVKKSTGKSH--SVKHLQFIKWPDHGTPASADFfiKYVRYVRKSHIT--GPLLVHCSAGVGRT 361
Cdd:cd17670   77 skDRLCLSNEEQIIIHDFILEATQDDYvlEVRHFQCPKWPNPDAPISSTF--ELINVIKEEALTrdGPTIVHDEFGAVSA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 564388256 362 GVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVL 411
Cdd:cd17670  155 GTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 188-404 3.36e-20

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 88.61  E-value: 3.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 188 NRYRDIlpydSTRVPLGKNKDyINASYIRIVNHEeeyFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEggvIKC- 266
Cdd:cd14559    1 NRFTNI----QTRVSTPVGKN-LNANRVQIGNKN---VAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKD---IQRk 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 267 ---------CSYWPVSLKEPLEFKHFHVLLENFQitQYfVIRIfqivkKSTGKSHSVKHLQFIKWPDHgTPASADFFIKY 337
Cdd:cd14559   70 glppyfrqsGTYGSVTVKSKKTGKDELVDGLKAD--MY-NLKI-----TDGNKTITIPVVHVTNWPDH-TAISSEGLKEL 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 338 VRYVRKS---HITGPLL---------------VHCSAGVGRTGVFICvdvVFCTIEKNYSFNIMNIVTQMRKQRFG-MIQ 398
Cdd:cd14559  141 ADLVNKSaeeKRNFYKSkgssaindknkllpvIHCRAGVGRTGQLAA---AMELNKSPNNLSVEDIVSDMRTSRNGkMVQ 217


                 ....*.
gi 564388256 399 TKEQYQ 404
Cdd:cd14559  218 KDEQLD 223
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 138-410 1.74e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 88.10  E-value: 1.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 138 NSSSRAALRDCLKALQKKEELD-IIREFleleEMIPPDDFKSGYELQNRDKNRYRD------ILPYDSTRVPLGKNKDYI 210
Cdd:PHA02740   4 EDAVDINGMDFINFINKPDLLScIIKEY----RAIVPEHEDEANKACAQAENKAKDenlalhITRLLHRRIKLFNDEKVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 211 NASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGgviKC-CSYWPVSLKEPLEFKHFHVLLEN 289
Cdd:PHA02740  80 DARFVDGYDFEQKF--ICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCfNQFWSLKEGCVITSDKFQIETLE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 290 FQITQYFVIRIFQIVKKStGKSHSVKHLQFIKWP----DHGTPASADFFIK----YVRYVRKSHI--TGPLLVHCSAGVG 359
Cdd:PHA02740 155 IIIKPHFNLTLLSLTDKF-GQAQKISHFQYTAWPadgfSHDPDAFIDFFCNiddlCADLEKHKADgkIAPIIIDCIDGIS 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564388256 360 RTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIV 410
Cdd:PHA02740 234 SSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 348-408 1.15e-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: 1.15e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564388256 348 GPLLVHCSAGVGRTGVFICVDVVfctIEKNYSFNimNIVTQMRKQR-FGMIQTKEQYQFCYE 408
Cdd:cd14494   57 EPVLVHCKAGVGRTGTLVACYLV---LLGGMSAE--EAVRIVRLIRpGGIPQTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
310-405 1.15e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 50.74  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 310 KSHSVKHLQFiKWPDHGTPASADF--FIKYVRYVRKSHitGPLLVHCSAGVGRTG-VFICVDvvfctIEKNYSFNimNIV 386
Cdd:COG2453   44 EEAGLEYLHL-PIPDFGAPDDEQLqeAVDFIDEALREG--KKVLVHCRGGIGRTGtVAAAYL-----VLLGLSAE--EAL 113

                         90
                 ....*....|....*....
gi 564388256 387 TQMRKQRFGMIQTKEQYQF 405
Cdd:COG2453  114 ARVRAARPGAVETPAQRAF 132
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 285-408 1.77e-07

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: 50.72  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 285 VLLENFQITQYFVIRIFQIVKKSTGKSHsvkHLQFikwPDHGTPASADFFIKYVRYVRKSHITGP-LLVHCSAGVGRTGV 363
Cdd:cd14505   49 TLCTDGELEELGVPDLLEQYQQAGITWH---HLPI---PDGGVPSDIAQWQELLEELLSALENGKkVLIHCKGGLGRTGL 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 564388256 364 ficvdVVFCT-IEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 408
Cdd:cd14505  123 -----IAACLlLELGDTLDPEQAIAAVRALRPGAIQTPKQENFLHQ 163
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 312-405 6.81e-07

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: 48.43  E-value: 6.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 312 HSVKHLqFIKWPDHGTPA--SADFFIKYVRYVRKShiTGPLLVHCSAGVGRTGVFICvdvvfCTIEKNYSFNIMNIVTQM 389
Cdd:cd14504   48 PGLRYH-HIPIEDYTPPTleQIDEFLDIVEEANAK--NEAVLVHCLAGKGRTGTMLA-----CYLVKTGKISAVDAINEI 119

                         90
                 ....*....|....*.
gi 564388256 390 RKQRFGMIQTKEQYQF 405
Cdd:cd14504  120 RRIRPGSIETSEQEKF 135
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 322-408 1.65e-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: 45.42  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 322 WPDHGTPaSADFFIKYVRyVRKSHI--TGPLLVHCSAGVGRTGVFICVDVVFCTiekNYSFNimNIVTQMRKQRFGMIQT 399
Cdd:cd14506   84 WKDYGVP-SLTTILDIVK-VMAFALqeGGKVAVHCHAGLGRTGVLIACYLVYAL---RMSAD--QAIRLVRSKRPNSIQT 156


                 ....*....
gi 564388256 400 KEQYQFCYE 408
Cdd:cd14506  157 RGQVLCVRE 165
PRK15375 PRK15375
type III secretion system effector GTPase-activating protein SptP;
234-403 1.03e-03

type III secretion system effector GTPase-activating protein SptP;


Pssm-ID: 185273 [Multi-domain]  Cd Length: 535  Bit Score: 41.33  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 234 PDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWpvslKEPLEFKHFHVLLENFQ-ITQYFVIRIFQIVKKSTGKSH 312
Cdd:PRK15375 346 PDALEAHMKMLLEKECSCLVVLTSEDQMQAKQLPPYF----RGSYTFGEVHTNSQKVSsASQGEAIDQYNMQLSCGEKRY 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256 313 SVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHITGPL----------LVHCSAGVGRTGVFICVDVvfctIEKNYSFNI 382
Cdd:PRK15375 422 TIPVLHVKNWPDHQPLPSTDQLEYLADRVKNSNQNGAPgrsssdkhlpMIHCLGGVGRTGTMAAALV----LKDNPHSNL 497

                        170       180
                 ....*....|....*....|..
gi 564388256 383 MNIVTQMRKQRFG-MIQTKEQY 403
Cdd:PRK15375 498 EQVRADFRNSRNNrMLEDASQF 519
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 323-361 1.30e-03

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


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 39.22  E-value: 1.30e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 564388256  323 PDHGTPASADFFiKYVRYVRKSHITGPLLVHCSAGVGRT 361
Cdd:pfam14566 109 TDEKAPLEEDFD-ALISIVKDAPEDTALVFNCQMGRGRT 146
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 310-380 2.83e-03

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


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 38.59  E-value: 2.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564388256 310 KSHSVKH--LQFikwPDHGTPASA--DFFIKYVRyvrksHITGPLLVHCSAGVGRTGVFICvdvvfCTIEKNYSF 380
Cdd:cd14499   76 TDAGIRHydLYF---PDGSTPSDDivKKFLDICE-----NEKGAIAVHCKAGLGRTGTLIA-----CYLMKHYGF 137
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
286-366 3.08e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 37.65  E-value: 3.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388256   286 LLENFQITqyFVIRIFQIVKKSTGKSHSVKHLQfIKWpDHGTPASADFF--IKYVRYVRKSHitGPLLVHCSAGVGRTGV 363
Cdd:smart00195  21 LLKKLGIT--HVINVTNEVPNYNGSDFTYLGVP-IDD-NTETKISPYFPeaVEFIEDAESKG--GKVLVHCQAGVSRSAT 94


                   ...
gi 564388256   364 FIC 366
Cdd:smart00195  95 LII 97
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 315-366 3.93e-03

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 37.24  E-value: 3.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564388256  315 KHLQFIKWP---DHGTPASADFF--IKYVRYVRKSHitGPLLVHCSAGVGRTGVFIC 366
Cdd:pfam00782  34 SGILYLRIPvedNHETNISKYLEeaVEFIDDARQKG--GKVLVHCQAGISRSATLII 88
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 323-364 9.44e-03

Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 families.


Pssm-ID: 463853 [Multi-domain]  Cd Length: 243  Bit Score: 37.61  E-value: 9.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 564388256  323 PDHGTPASADFFikyvRYVRKShiTGPLLVHCSAGVGRTGVF 364
Cdd:pfam13350 111 VTSARAAYRALF----EALADN--DGPVLFHCTAGKDRTGVA 146
 
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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