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Conserved domains on  [gi|1958683650|ref|XP_038950399|]
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tyrosine-protein phosphatase non-receptor type 20 isoform X2 [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 ...
 40-246 9.08e-124

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: 350.20  E-value: 9.08e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLE 119
Cdd:cd14596     1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 120 NFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHITGPLLVHCSAGVGRTGVFICVD 199
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICVD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958683650 200 VVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVLQ 246
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 ...
 40-246 9.08e-124

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: 350.20  E-value: 9.08e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLE 119
Cdd:cd14596     1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 120 NFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHITGPLLVHCSAGVGRTGVFICVD 199
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICVD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958683650 200 VVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVLQ 246
Cdd:cd14596   161 VLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
2-243 2.62e-110

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 318.06  E-value: 2.62e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650    2 IPPDDFKSGYELQNRDKNRYRDILPYDSTRVPL----GKNKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLE 77
Cdd:smart00194  14 PDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLkpppGEGSDYINASYIDGPNGPKAY--IATQGPLPSTVEDFWRMVWE 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650   78 NNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHG 157
Cdd:smart00194  92 QKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHYTNWPDHG 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  158 TPASADFFIKYVRYVRKSHI--TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQ 235
Cdd:smart00194 172 VPESPESILDLIRAVRKSQStsTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYI 251


                   ....*...
gi 1958683650  236 FCYEIVLE 243
Cdd:smart00194 252 FLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
15-243 9.11e-109

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 313.02  E-value: 9.11e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  15 NRDKNRYRDILPYDSTRVPLGK---NKDYINASYIRIvnHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIE 91
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGdpgPSDYINASYIDG--YKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  92 GGVIKCCSYWPVSLKEPLEFKHFHV-LLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVR 170
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVtLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958683650 171 YVRKSHI---TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:pfam00102 159 KVRKSSLdgrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
18-236 9.21e-54

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 174.89  E-value: 9.21e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  18 KNRYRDILPYDSTRVplGKNKDYINASYIRIVNheeEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGV--I 95
Cdd:COG5599    45 LNRFRDIQPYKETAL--RANLGYLNANYIQVIG---NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKpkV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  96 KCCSYWPVS---LKEPLEFKhfhvLLENFQITQYFVIRIFQIVKKSTG-KSHSVKHLQFIKWPDHGTPaSADFFIKYVRY 171
Cdd:COG5599   120 KMPVYFRQDgeyGKYEVSSE----LTESIQLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAI-SAEALKNLADL 194

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683650 172 VRKSHIT-----GPLLVHCSAGVGRTGVFICVDVVFCTI--EKNYSFNIMNIVTQMRKQR-FGMIQTKEQYQF 236
Cdd:COG5599   195 IDKKEKIkdpdkLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRnGGMVQTSEQLDV 267
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 12-243 3.16e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 153.62  E-value: 3.16e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  12 ELQNRDKNRYRDILPYDSTRVPLGKNK---DYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITR 88
Cdd:PHA02742   49 ELKNMKKCRYPDAPCFDRNRVILKIEDggdDFINASYVD--GHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITK 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  89 EIEGGVIKCCSYWPVSLKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY 168
Cdd:PHA02742  127 IMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDF 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 169 VRYVRKSHITG-------------PLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQ 235
Cdd:PHA02742  207 VLAVREADLKAdvdikgenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYI 286


                  ....*...
gi 1958683650 236 FCYEIVLE 243
Cdd:PHA02742  287 FCYFIVLI 294
 
Name Accession Description Interval E-value
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 40-246 9.08e-124

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: 350.20  E-value: 9.08e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLE 119
Cdd:cd14596     1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 120 NFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHITGPLLVHCSAGVGRTGVFICVD 199
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICVD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958683650 200 VVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVLQ 246
Cdd:cd14596   161 VLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 40-245 5.38e-119

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: 338.19  E-value: 5.38e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPL-EFKHFHVLL 118
Cdd:cd14538     1 YINASHIRIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLiCGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 119 ENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHITGPLLVHCSAGVGRTGVFICV 198
Cdd:cd14538    81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNSGPIVVHCSAGIGRTGVLITI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958683650 199 DVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVL 245
Cdd:cd14538   161 DVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
2-243 2.62e-110

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 318.06  E-value: 2.62e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650    2 IPPDDFKSGYELQNRDKNRYRDILPYDSTRVPL----GKNKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLE 77
Cdd:smart00194  14 PDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLkpppGEGSDYINASYIDGPNGPKAY--IATQGPLPSTVEDFWRMVWE 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650   78 NNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHG 157
Cdd:smart00194  92 QKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHYTNWPDHG 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  158 TPASADFFIKYVRYVRKSHI--TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQ 235
Cdd:smart00194 172 VPESPESILDLIRAVRKSQStsTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYI 251


                   ....*...
gi 1958683650  236 FCYEIVLE 243
Cdd:smart00194 252 FLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
15-243 9.11e-109

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 313.02  E-value: 9.11e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  15 NRDKNRYRDILPYDSTRVPLGK---NKDYINASYIRIvnHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIE 91
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGdpgPSDYINASYIDG--YKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  92 GGVIKCCSYWPVSLKEPLEFKHFHV-LLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVR 170
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVtLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958683650 171 YVRKSHI---TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:pfam00102 159 KVRKSSLdgrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 14-245 2.21e-98

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: 287.11  E-value: 2.21e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  14 QNRDKNRYRDILPYDSTRVPLGKNKDYINASYIRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGG 93
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPLGDEGGYINASFIKMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  94 VIKCCSYWPVSLKEPLEF-KHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYV 172
Cdd:cd14597    82 KIKCQRYWPEILGKTTMVdNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFISYM 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683650 173 RKSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVL 245
Cdd:cd14597   162 RHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILYVL 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 40-239 5.52e-86

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 254.13  E-value: 5.52e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLE 119
Cdd:cd00047     1 YINASYIDGYRGPKEY--IATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 120 NFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHI--TGPLLVHCSAGVGRTGVFIC 197
Cdd:cd00047    79 SEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARkpNGPIVVHCSAGVGRTGTFIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958683650 198 VDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 239
Cdd:cd00047   159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 14-244 4.46e-77

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: 234.36  E-value: 4.46e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  14 QNRDKNRYRDILPYDSTRVPLGKNKDYINASYIR-------IVNHeeeyfYIATQGPLPDTIEDFWQMVLENNCNVIAMI 86
Cdd:cd14600    39 QNMDKNRYKDVLPYDATRVVLQGNEDYINASYVNmeipsanIVNK-----YIATQGPLPHTCAQFWQVVWEQKLSLIVML 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  87 TREIEGGVIKCCSYWPvSLKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFI 166
Cdd:cd14600   114 TTLTERGRTKCHQYWP-DPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFL 192

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683650 167 KYVRYVRKSHITG-PLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEV 244
Cdd:cd14600   193 EFVNYVRSKRVENePVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRV 271
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1-238 4.95e-77

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: 234.18  E-value: 4.95e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650   1 MIPPDDFKSGYELQNRDKNRYRDILPYDSTRVPLGK-----NKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMV 75
Cdd:cd14543    15 EPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKrngdeRTDYINANFMD--GYKQKNAYIATQGPLPKTYSDFWRMV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  76 LENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPD 155
Cdd:cd14543    93 WEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTSWPD 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 156 HGTPASADFFIKYVRYVR--------------KSHITG-PLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQM 220
Cdd:cd14543   173 FGVPSSAAALLDFLGEVRqqqalavkamgdrwKGHPPGpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRM 252

                         250
                  ....*....|....*...
gi 1958683650 221 RKQRFGMIQTKEQYQFCY 238
Cdd:cd14543   253 RTQRAFSIQTPDQYYFCY 270
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 40-239 1.61e-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: 222.89  E-value: 1.61e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRIVNHEEEYfYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPvSLKEPLEFKHFHV-LL 118
Cdd:cd18533     1 YINASYITLPGTSSKR-YIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWP-SGEYEGEYGDLTVeLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 119 ENFQITQY-FVIRIFQiVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRK----SHITGPLLVHCSAGVGRTG 193
Cdd:cd18533    79 SEEENDDGgFIVREFE-LSKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElndsASLDPPIIVHCSAGVGRTG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958683650 194 VFICVDVVFCTIEKNYSFN---------IMNIVTQMRKQRFGMIQTKEQYQFCYE 239
Cdd:cd18533   158 TFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 20-236 1.05e-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: 221.46  E-value: 1.05e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  20 RYRDILPYDSTRVPL-----GKNKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGV 94
Cdd:cd14548     1 RYTNILPYDHSRVKLipineEEGSDYINANYIPGYNSPREF--IATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  95 IKCCSYWPVSlKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKstGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRK 174
Cdd:cd14548    79 VKCDHYWPFD-QDPVYYGDITVTMLSESVLPDWTIREFKLERG--DEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958683650 175 S--HITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQF 236
Cdd:cd14548   156 YikQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 18-238 8.40e-71

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: 216.87  E-value: 8.40e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  18 KNRYRDILPYDSTRVPLGKNK---DYINASyiRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGV 94
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQgdnDYINAS--LVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  95 IKCCSYWPVSLKEPLEFKH--FHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYV 172
Cdd:cd14545    79 IKCAQYWPQGEGNAMIFEDtgLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958683650 173 RKSHI----TGPLLVHCSAGVGRTGVFICVDVVFCTIEK-NYS-FNIMNIVTQMRKQRFGMIQTKEQYQFCY 238
Cdd:cd14545   159 RESGSlssdVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKgNPSsVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 19-236 1.73e-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: 215.72  E-value: 1.73e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  19 NRYRDILPYDSTRVPLGKNKD-----YINASYIRIVNHEEEYfYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGG 93
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDdplssYINANYIRGYDGEEKA-YIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  94 ViKCCSYWPVslKEPLEFKHFHVLLENFQITQYFVIRifQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYV- 172
Cdd:cd14547    80 E-KCAQYWPE--EENETYGDFEVTVQSVKETDGYTVR--KLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVe 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683650 173 ---RKSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQF 236
Cdd:cd14547   155 earQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 15-243 1.27e-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: 211.49  E-value: 1.27e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  15 NRDKNRYRDILPYDSTRVPLGK-----NKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITRE 89
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPiegvpGSDYINANYCD--GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  90 IEGGVIKCCSYWPVSLKEPLEFkhFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYV 169
Cdd:cd14553    81 EERSRVKCDQYWPTRGTETYGL--IQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958683650 170 RYVRKSHI--TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:cd14553   159 RRVKACNPpdAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 39-244 1.69e-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: 210.26  E-value: 1.69e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  39 DYINASYIR-------IVNHeeeyfYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVsLKEPLEF 111
Cdd:cd14541     1 DYINANYVNmeipgsgIVNR-----YIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPD-LGETMQF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 112 KHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHITG--PLLVHCSAGV 189
Cdd:cd14541    75 GNLQITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMvePTVVHCSAGI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958683650 190 GRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEV 244
Cdd:cd14541   155 GRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 15-242 1.72e-68

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: 211.23  E-value: 1.72e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  15 NRDKNRYRDILPYDSTRVPLG-----KNKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITRE 89
Cdd:cd14554     6 NKFKNRLVNILPYESTRVCLQpirgvEGSDYINASFID--GYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  90 IEGGVIKCCSYWPvsLKEPLEFKHFHV-LLENFQITQYfVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY 168
Cdd:cd14554    84 REMGREKCHQYWP--AERSARYQYFVVdPMAEYNMPQY-ILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683650 169 VRYVRKSH----ITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVL 242
Cdd:cd14554   161 IGQVHKTKeqfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 14-244 1.02e-67

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


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 210.07  E-value: 1.02e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  14 QNRDKNRYRDILPYDSTRVPLG-----KNKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITR 88
Cdd:cd14603    29 ENVKKNRYKDILPYDQTRVILSllqeeGHSDYINANFIKGVDGSRAY--IATQGPLSHTVLDFWRMIWQYGVKVILMACR 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  89 EIEGGVIKCCSYWPvSLKEPLEFKHFHV-LLENFQITQYFVIRIFQIVKKStgKSHSVKHLQFIKWPDHGTPASADFFIK 167
Cdd:cd14603   107 EIEMGKKKCERYWA-QEQEPLQTGPFTItLVKEKRLNEEVILRTLKVTFQK--ESRSVSHFQYMAWPDHGIPDSPDCMLA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 168 YVRYVRKSHITG--PLLVHCSAGVGRTGVFICVDVV---FCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVL 242
Cdd:cd14603   184 MIELARRLQGSGpePLCVHCSAGCGRTGVICTVDYVrqlLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVA 263


                  ..
gi 1958683650 243 EV 244
Cdd:cd14603   264 QM 265
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 40-245 5.72e-67

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: 206.54  E-value: 5.72e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKE--PLEFKHFHVL 117
Cdd:cd14540     1 YINASHITATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEhdALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 118 LENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY---VRYVRKsHITG---------PLLVHC 185
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeINSVRR-HTNQdvaghnrnpPTLVHC 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 186 SAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVL 245
Cdd:cd14540   160 SAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 19-245 1.74e-64

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 200.89  E-value: 1.74e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  19 NRYRDILPYDSTRVPLGKNK-----DYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGG 93
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHeepgsDYINANYMPGYWSSQEF--IATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  94 VIKCCSYWPVSlKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVR 173
Cdd:cd14619    79 RVKCEHYWPLD-YTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958683650 174 K---SHI-TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVL 245
Cdd:cd14619   158 QwldQTMsGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 19-243 5.10e-64

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: 199.27  E-value: 5.10e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  19 NRYRDILPYDSTRVPLG----KNKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGV 94
Cdd:cd14615     1 NRYNNVLPYDISRVKLSvqshSTDDYINANYMPGYNSKKEF--IAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  95 IKCCSYWPVslKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY---VR- 170
Cdd:cd14615    79 TKCEEYWPS--KQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFrhlVRe 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683650 171 YVRKSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:cd14615   157 YMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 14-246 5.92e-64

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: 201.38  E-value: 5.92e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  14 QNRDKNRYRDILPYDSTRVPLGKNKD----YINASYIRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITRE 89
Cdd:cd14599    37 ENAERNRIREVVPYEENRVELVPTKEnntgYINASHIKVTVGGEEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  90 IEGGVIKCCSYWPvslkePLEFKHFHVLLENFQITQYF-------VIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASA 162
Cdd:cd14599   117 EEGGRSKSHRYWP-----KLGSKHSSATYGKFKVTTKFrtdsgcyATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEV 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 163 DFFIKY---VRYVRK---------SHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQT 230
Cdd:cd14599   192 QGFLSYleeIQSVRRhtnsmldstKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQT 271

                         250
                  ....*....|....*.
gi 1958683650 231 KEQYQFCYEIVLEVLQ 246
Cdd:cd14599   272 IAQYKFVYQVLIQFLK 287
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 15-247 1.78e-61

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: 193.83  E-value: 1.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  15 NRDKNRYRDILPYDSTRVPLG------KNKDYINASYIRIVNHEEEYF-----YIATQGPLPDTIEDFWQMVLENNCNVI 83
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKdrdpnvPGSDYINANYIRNENEGPTTDenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  84 AMITREIEGGVIKCCSYWPvSLKEPLEFKHFHV--LLENfqITQYFVIRIFQIVKKSTGKS-HSVKHLQFIKWPDHGTPA 160
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWP-DEGMQKQYGPYRVqnVSEH--DTTDYTLRELQVSKLDQGDPiREIWHYQYLSWPDHGVPS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 161 SADFFIKYVRYV--RKSHI--TGPLLVHCSAGVGRTGVFICVDVVFCTIEKN---YSFNIMNIVTQMRKQRFGMIQTKEQ 233
Cdd:cd14544   158 DPGGVLNFLEDVnqRQESLphAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKgldCDIDIQKTIQMVRSQRSGMVQTEAQ 237

                         250
                  ....*....|....
gi 1958683650 234 YQFCYEIVLEVLQN 247
Cdd:cd14544   238 YKFIYVAVAQYIET 251
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 19-239 3.96e-61

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 192.06  E-value: 3.96e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  19 NRYRDILPYDSTRVPLGKNK-----DYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGG 93
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDddpcsDYINASYIPGNNFRREY--IATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  94 VIKCCSYWPVSlKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHS-VKHLQFIKWPDHGTPASADFFIKYVR-- 170
Cdd:cd14617    79 RVKCDHYWPAD-QDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRlVRHFHYTVWPDHGVPETTQSLIQFVRtv 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958683650 171 --YVRKSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 239
Cdd:cd14617   158 rdYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 14-241 6.99e-61

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


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 192.49  E-value: 6.99e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  14 QNRDKNRYRDILPYDSTRVPL-GKNKDYINASYIRIvnHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEG 92
Cdd:cd14607    23 ENRNRNRYRDVSPYDHSRVKLqNTENDYINASLVVI--EEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  93 GVIKCCSYWPVSLKEPLEFKH--FHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVR 170
Cdd:cd14607   101 DSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPASFLNFLF 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683650 171 YVRKSHI----TGPLLVHCSAGVGRTGVFICVDVVFCTIEKN--YSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIV 241
Cdd:cd14607   181 KVRESGSlspeHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKdpDSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 15-245 1.34e-60

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: 1.34e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  15 NRDKNRYRDILPYDSTRVPLG-----KNKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITRE 89
Cdd:cd14627    53 NKFKNRLVNIMPYETTRVCLQpirgvEGSDYINASFID--GYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  90 IEGGVIKCCSYWPVslKEPLEFKHFHV-LLENFQITQYfVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY 168
Cdd:cd14627   131 REMGREKCHQYWPA--ERSARYQYFVVdPMAEYNMPQY-ILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 169 VRYVRKSH----ITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEV 244
Cdd:cd14627   208 IGQVHKTKeqfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEY 287


                  .
gi 1958683650 245 L 245
Cdd:cd14627   288 L 288
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 14-243 1.87e-60

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: 1.87e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  14 QNRDKNRYRDILPYDSTRVPLGK-NKDYINASYIRIvnHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEG 92
Cdd:cd14608    24 KNKNRNRYRDVSPFDHSRIKLHQeDNDYINASLIKM--EEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  93 GVIKCCSYWPVSLKEPLEFK--HFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVR 170
Cdd:cd14608   102 GSLKCAQYWPQKEEKEMIFEdtNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLF 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 171 YVRKSHIT----GPLLVHCSAGVGRTGVFICVDVVFCTIEKN---YSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:cd14608   182 KVRESGSLspehGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 261
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 4-238 3.04e-60

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: 190.43  E-value: 3.04e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650   4 PDDFKSGYELQ---NRDKNRYRDILPYDSTRVPLGKNK------DYINASYIRIVNHEEEYfYIATQGPLPDTIEDFWQM 74
Cdd:cd14612     1 PPNFVSPEELDipgHASKDRYKTILPNPQSRVCLRRAGsqeeegSYINANYIRGYDGKEKA-YIATQGPMLNTVSDFWEM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  75 VLENNCNVIAMITREIEGGViKCCSYWPvslKEPLEFKHFHVLLENFQITQYFVIRifQIVKKSTGKSHSVKHLQFIKWP 154
Cdd:cd14612    80 VWQEECPIIVMITKLKEKKE-KCVHYWP---EKEGTYGRFEIRVQDMKECDGYTIR--DLTIQLEEESRSVKHYWFSSWP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 155 DHGTPASADFFIKYVRYVRKSHIT----GPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQT 230
Cdd:cd14612   154 DHQTPESAGPLLRLVAEVEESRQTaaspGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQT 233


                  ....*...
gi 1958683650 231 KEQYQFCY 238
Cdd:cd14612   234 SEQYQFLH 241
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 15-242 9.40e-60

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: 188.94  E-value: 9.40e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  15 NRDKNRYRDILPYDSTRVPL-----GKNKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITRE 89
Cdd:cd14614    12 NRCKNRYTNILPYDFSRVKLvsmheEEGSDYINANYIPGYNSPQEY--IATQGPLPETRNDFWKMVLQQKSQIIVMLTQC 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  90 IEGGVIKCCSYWPVSlKEPLEFKHFHVLLENFQITQYFVIRIFQIvkKSTGKSHSVKHLQFIKWPDHGTPA--SADFFIK 167
Cdd:cd14614    90 NEKRRVKCDHYWPFT-EEPVAYGDITVEMLSEEEQPDWAIREFRV--SYADEVQDVMHFNYTAWPDHGVPTanAAESILQ 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683650 168 YVRYVRKSHIT--GPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVL 242
Cdd:cd14614   167 FVQMVRQQAVKskGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 243
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 2-249 3.16e-59

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: 189.37  E-value: 3.16e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650   2 IPPDDFksGYELQNRDKNRYRDILPYDSTRVPL-----GKNKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVL 76
Cdd:cd14604    46 IYPTAT--GEKEENVKKNRYKDILPFDHSRVKLtlktsSQDSDYINANFIKGVYGPKAY--IATQGPLANTVIDFWRMIW 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  77 ENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLENFQITQYFVIRIFQIvkKSTGKSHSVKHLQFIKWPDH 156
Cdd:cd14604   122 EYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLL--EFQNETRRLYQFHYVNWPDH 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 157 GTPASADFFIKYVRYVRK--SHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNY---SFNIMNIVTQMRKQRFGMIQTK 231
Cdd:cd14604   200 DVPSSFDSILDMISLMRKyqEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTK 279

                         250
                  ....*....|....*...
gi 1958683650 232 EQYQFCYEIVLEVLQNLL 249
Cdd:cd14604   280 EQYELVHRAIAQLFEKQL 297
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 15-245 2.54e-58

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: 186.86  E-value: 2.54e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  15 NRDKNRYRDILPYDSTRVPLG-----KNKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITRE 89
Cdd:cd14628    52 NKFKNRLVNIMPYESTRVCLQpirgvEGSDYINASFID--GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  90 IEGGVIKCCSYWPVslKEPLEFKHFHV-LLENFQITQYfVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY 168
Cdd:cd14628   130 REMGREKCHQYWPA--ERSARYQYFVVdPMAEYNMPQY-ILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 169 VRYVRKSH----ITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEV 244
Cdd:cd14628   207 IGQVHKTKeqfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEY 286


                  .
gi 1958683650 245 L 245
Cdd:cd14628   287 L 287
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 19-242 4.80e-58

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: 184.38  E-value: 4.80e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  19 NRYRDILPYDSTRVPLGK-----NKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGG 93
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQlggepHSDYINANFIPGYTSPQEF--IATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  94 VIKCCSYWPVSLKePLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVR 173
Cdd:cd14618    79 RVLCDHYWPSEST-PVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958683650 174 KsHI-----TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVL 242
Cdd:cd14618   158 E-HVqatkgKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 15-243 5.83e-58

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: 185.62  E-value: 5.83e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  15 NRDKNRYRDILPYDSTRVPLGK-----NKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITRE 89
Cdd:cd14626    41 NKPKNRYANVIAYDHSRVILTSvdgvpGSDYINANYID--GYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  90 IEGGVIKCCSYWPVSLKEPLEFKHFhVLLENFQITQYFViRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYV 169
Cdd:cd14626   119 EEKSRVKCDQYWPIRGTETYGMIQV-TLLDTVELATYSV-RTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFL 196

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958683650 170 RYVRKSHI--TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:cd14626   197 RRVKACNPpdAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 40-239 6.76e-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: 182.94  E-value: 6.76e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEplEFKHFHVLLE 119
Cdd:cd14549     1 YINANYVDGYNKARAY--IATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE--TYGNIQVTLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 120 NFQITQYFVIRIFQI--VKKSTGKSHS----VKHLQFIKWPDHGTPASAdffIKYVRYVRKS-----HITGPLLVHCSAG 188
Cdd:cd14549    77 STEVLATYTVRTFSLknLKLKKVKGRSservVYQYHYTQWPDHGVPDYT---LPVLSFVRKSsaanpPGAGPIVVHCSAG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958683650 189 VGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 239
Cdd:cd14549   154 VGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 15-245 2.53e-56

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: 2.53e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  15 NRDKNRYRDILPYDSTRVPLG-----KNKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITRE 89
Cdd:cd14629    53 NKFKNRLVNIMPYELTRVCLQpirgvEGSDYINASFID--GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  90 IEGGVIKCCSYWPVslKEPLEFKHFHV-LLENFQITQYfVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY 168
Cdd:cd14629   131 REMGREKCHQYWPA--ERSARYQYFVVdPMAEYNMPQY-ILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDF 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 169 VRYVRKSH----ITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEV 244
Cdd:cd14629   208 IGQVHKTKeqfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEY 287


                  .
gi 1958683650 245 L 245
Cdd:cd14629   288 L 288
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 40-238 5.24e-56

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: 178.00  E-value: 5.24e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLE 119
Cdd:cd14542     1 YINANFIKGVSGSKAY--IATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 120 NFQ-ITQYFVIRIFQIVKKSTgkSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRK--SHITGPLLVHCSAGVGRTGVFI 196
Cdd:cd14542    79 KEKrVGPDFLIRTLKVTFQKE--SRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDyqGSEDVPICVHCSAGCGRTGTIC 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958683650 197 CVDVVFCTIEK---NYSFNIMNIVTQMRKQRFGMIQTKEQYQFCY 238
Cdd:cd14542   157 AIDYVWNLLKTgkiPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 14-243 5.55e-56

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: 179.07  E-value: 5.55e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  14 QNRDKNRYRDILPYDSTRVPL-----GKNKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITR 88
Cdd:cd14630     2 ENRNKNRYGNIISYDHSRVRLqlldgDPHSDYINANYID--GYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  89 EIEGGVIKCCSYWPVSLKEPLEFKHfhVLLENFQITQYfVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY 168
Cdd:cd14630    80 LVEVGRVKCVRYWPDDTEVYGDIKV--TLIETEPLAEY-VIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGF 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683650 169 VRYVR--KSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:cd14630   157 VRQVKflNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 14-243 1.10e-55

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: 179.47  E-value: 1.10e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  14 QNRDKNRYRDILPYDSTRVPL-----GKNKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITR 88
Cdd:cd14633    39 ENRMKNRYGNIIAYDHSRVRLqpiegETSSDYINGNYID--GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTN 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  89 EIEGGVIKCCSYWPvslKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY 168
Cdd:cd14633   117 LVEVGRVKCCKYWP---DDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGF 193

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683650 169 VRYVRKSHI--TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:cd14633   194 VRQVKSKSPpnAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 18-244 1.58e-55

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


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 178.11  E-value: 1.58e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  18 KNRYRDILPYDSTRVPLG-----KNKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEG 92
Cdd:cd14602     1 KNRYKDILPYDHSRVELSlitsdEDSDYINANFIKGVYGPRAY--IATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  93 GVIKCCSYWPVSLKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKStgKSHSVKHLQFIKWPDHGTPASADFFIKYVRYV 172
Cdd:cd14602    79 GKKKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS--ETRTIYQFHYKNWPDHDVPSSIDPILELIWDV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683650 173 R--KSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNY---SFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEV 244
Cdd:cd14602   157 RcyQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIipeNFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 40-239 1.63e-55

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: 176.89  E-value: 1.63e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEG-GVIKCCSYWPVSLKEPLEFKHFHVLL 118
Cdd:cd17658     1 YINASLVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNySTAKCADYFPAEENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 119 ENFQITQY-FVIRIFQI-VKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRyvRKSHI---TGPLLVHCSAGVGRTG 193
Cdd:cd17658    81 KKLKHSQHsITLRVLEVqYIESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLK--RLYGIppsAGPIVVHCSAGIGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958683650 194 VFICVDVVFCTIEKN--YSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 239
Cdd:cd17658   159 AYCTIHNTIRRILEGdmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 15-245 1.64e-55

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: 179.08  E-value: 1.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  15 NRDKNRYRDILPYDSTRVPL-------GKNKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMIT 87
Cdd:cd17667    27 NKHKNRYINILAYDHSRVKLrplpgkdSKHSDYINANYVDGYNKAKAY--IATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  88 REIEGGVIKCCSYWPVSLKEplEFKHFHVLLENFQITQYFVIRIFQI----VKKSTGKS-------HSVKHLQFIKWPDH 156
Cdd:cd17667   105 NLVEKGRRKCDQYWPTENSE--EYGNIIVTLKSTKIHACYTVRRFSIrntkVKKGQKGNpkgrqneRTVIQYHYTQWPDM 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 157 GTPasaDFFIKYVRYVRKSHI-----TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTK 231
Cdd:cd17667   183 GVP---EYALPVLTFVRRSSAartpeMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 259

                         250
                  ....*....|....
gi 1958683650 232 EQYQFCYEIVLEVL 245
Cdd:cd17667   260 EQYIFIHDALLEAI 273
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 15-245 2.09e-55

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: 179.13  E-value: 2.09e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  15 NRDKNRYRDILPYDSTRVPLGK-----NKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITRE 89
Cdd:cd14625    47 NKPKNRYANVIAYDHSRVILQPiegimGSDYINANYID--GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  90 IEGGVIKCCSYWPVSLKEPLEFKHFhVLLENFQITQyFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYV 169
Cdd:cd14625   125 EEKSRIKCDQYWPSRGTETYGMIQV-TLLDTIELAT-FCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFL 202

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683650 170 RYVRKSHI--TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVL 245
Cdd:cd14625   203 RRVKTCNPpdAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 14-241 1.57e-54

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: 1.57e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  14 QNRDKNRYRDILPYDSTRVPLGKN------KDYINASYI------RIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCN 81
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLHDGdpnepvSDYINANIImpefetKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  82 VIAMITREIEGGVIKCCSYWPvslkEPLEFKHFHVL-LENFQIT--QYFVIRIFQIVKKSTGKSH-SVKHLQFIKWPDHG 157
Cdd:cd14605    81 VIVMTTKEVERGKSKCVKYWP----DEYALKEYGVMrVRNVKESaaHDYILRELKLSKVGQGNTErTVWQYHFRTWPDHG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 158 TPASADFFIKYVRYV--RKSHIT--GPLLVHCSAGVGRTGVFICVDVVFCTI-EK--NYSFNIMNIVTQMRKQRFGMIQT 230
Cdd:cd14605   157 VPSDPGGVLDFLEEVhhKQESIMdaGPVVVHCSAGIGRTGTFIVIDILIDIIrEKgvDCDIDVPKTIQMVRSQRSGMVQT 236

                         250
                  ....*....|.
gi 1958683650 231 KEQYQFCYEIV 241
Cdd:cd14605   237 EAQYRFIYMAV 247
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 39-244 3.63e-54

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: 173.59  E-value: 3.63e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  39 DYINASYIR-------IVNHeeeyfYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPvslkEPL-- 109
Cdd:cd14601     1 DYINANYINmeipsssIINR-----YIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP----EPSgs 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 110 -EFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHITG--PLLVHCS 186
Cdd:cd14601    72 sSYGGFQVTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKdePVVVHCS 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683650 187 AGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEV 244
Cdd:cd14601   152 AGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKV 209
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 40-239 4.48e-54

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: 173.34  E-value: 4.48e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIR-IVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLL 118
Cdd:cd14539     1 YINASLIEdLTPYCPRF--IATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 119 ENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYV-------RKSHItgPLLVHCSAGVGR 191
Cdd:cd14539    79 QSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVhshylqqRSLQT--PIVVHCSSGVGR 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958683650 192 TGVFICVDVVFCTIEK-NYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 239
Cdd:cd14539   157 TGAFCLLYAAVQEIEAgNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 40-246 7.94e-54

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: 7.94e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPvslkePLEFKHFHVLLE 119
Cdd:cd14598     1 YINASHIKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWP-----RLGSRHNTVTYG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 120 NFQITQYF-------VIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY---VRYVRKsHITG---------P 180
Cdd:cd14598    76 RFKITTRFrtdsgcyATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeIQSVRR-HTNStidpkspnpP 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958683650 181 LLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVLQ 246
Cdd:cd14598   155 VLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
18-236 9.21e-54

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 174.89  E-value: 9.21e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  18 KNRYRDILPYDSTRVplGKNKDYINASYIRIVNheeEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGV--I 95
Cdd:COG5599    45 LNRFRDIQPYKETAL--RANLGYLNANYIQVIG---NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKpkV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  96 KCCSYWPVS---LKEPLEFKhfhvLLENFQITQYFVIRIFQIVKKSTG-KSHSVKHLQFIKWPDHGTPaSADFFIKYVRY 171
Cdd:COG5599   120 KMPVYFRQDgeyGKYEVSSE----LTESIQLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAI-SAEALKNLADL 194

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683650 172 VRKSHIT-----GPLLVHCSAGVGRTGVFICVDVVFCTI--EKNYSFNIMNIVTQMRKQR-FGMIQTKEQYQF 236
Cdd:COG5599   195 IDKKEKIkdpdkLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRnGGMVQTSEQLDV 267
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 18-238 1.03e-53

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: 173.18  E-value: 1.03e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  18 KNRYRDILPYDSTRVPLG-KNKD-----YINASYIRIVNHEEEYFyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIE 91
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKpKNSNdslstYINANYIRGYGGKEKAF-IATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  92 GGViKCCSYWPvslKEPLEFKHFHVLLENFQITQYFVIRifQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRY 171
Cdd:cd14611    81 KNE-KCVLYWP---EKRGIYGKVEVLVNSVKECDNYTIR--NLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLD 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958683650 172 V----RKSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCY 238
Cdd:cd14611   155 VeedrLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 40-243 2.04e-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: 171.64  E-value: 2.04e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPvslKEPLEFKHFHVLLE 119
Cdd:cd14555     1 YINANYID--GYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP---DDTEVYGDIKVTLV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 120 NFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSH--ITGPLLVHCSAGVGRTGVFIC 197
Cdd:cd14555    76 ETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNppSAGPIVVHCSAGAGRTGCYIV 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958683650 198 VDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:cd14555   156 IDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 6-246 2.21e-53

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: 173.53  E-value: 2.21e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650   6 DFKSGYELQNRDKNRYRDILPYDSTRVPLG------KNKDYINASYIR---IVNHEEEYFYIATQGPLPDTIEDFWQMVL 76
Cdd:cd14606     9 QRLEGQRPENKSKNRYKNILPFDHSRVILQgrdsniPGSDYINANYVKnqlLGPDENAKTYIASQGCLEATVNDFWQMAW 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  77 ENNCNVIAMITREIEGGVIKCCSYWPVSLKEPlEFKHFHVLLENFQITQYFVIRIFQI-VKKSTGKSHSVKHLQFIKWPD 155
Cdd:cd14606    89 QENSRVIVMTTREVEKGRNKCVPYWPEVGMQR-AYGPYSVTNCGEHDTTEYKLRTLQVsPLDNGELIREIWHYQYLSWPD 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 156 HGTPASADFFIKYVRYVRKSHIT----GPLLVHCSAGVGRTGVFICVDVVFCTIEK---NYSFNIMNIVTQMRKQRFGMI 228
Cdd:cd14606   168 HGVPSEPGGVLSFLDQINQRQESlphaGPIIVHCSAGIGRTGTIIVIDMLMENISTkglDCDIDIQKTIQMVRAQRSGMV 247

                         250
                  ....*....|....*...
gi 1958683650 229 QTKEQYQFCYEIVLEVLQ 246
Cdd:cd14606   248 QTEAQYKFIYVAIAQFIE 265
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 4-243 2.38e-53

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


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 174.09  E-value: 2.38e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650   4 PDDFKSGYELQNRDKNRYRDILPYDSTRVPL-GKNK----DYINASyiRIVNHEEEY-FYIATQGPLPDTIEDFWQMVLE 77
Cdd:cd14610    33 PNATNVAQREENVQKNRSLAVLPYDHSRIILkAENShshsDYINAS--PIMDHDPRNpAYIATQGPLPATVADFWQMVWE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  78 NNCNVIAMITREIEGGVIKCCSYWPvslKEPLEFKH-FHVLLENFQI-TQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPD 155
Cdd:cd14610   111 SGCVVIVMLTPLAENGVKQCYHYWP---DEGSNLYHiYEVNLVSEHIwCEDFLVRSFYLKNLQTNETRTVTQFHFLSWND 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 156 HGTPASADFFIKYVRYVRKSH--ITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNY-SFNIMNIVTQMRKQRFGMIQTKE 232
Cdd:cd14610   188 QGVPASTRSLLDFRRKVNKCYrgRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAkEIDIAATLEHLRDQRPGMVQTKE 267

                         250
                  ....*....|.
gi 1958683650 233 QYQFCYEIVLE 243
Cdd:cd14610   268 QFEFALTAVAE 278
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 40-243 3.75e-53

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: 3.75e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRIVnHEEEYFyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPvslKEPLEFKHFHVLLE 119
Cdd:cd14632     1 YINANYIDGY-HRSNHF-IATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP---DDSDTYGDIKITLL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 120 NFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHI--TGPLLVHCSAGVGRTGVFIC 197
Cdd:cd14632    76 KTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPpdAGPVVVHCSAGAGRTGCYIV 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958683650 198 VDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:cd14632   156 LDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 15-243 7.16e-53

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: 7.16e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  15 NRDKNRYRDILPYDSTRVPLG-----KNKDYINASyiRIVNHEEEY-FYIATQGPLPDTIEDFWQMVLENNCNVIAMITR 88
Cdd:cd14609    42 NVKKNRNPDFVPYDHARIKLKaesnpSRSDYINAS--PIIEHDPRMpAYIATQGPLSHTIADFWQMVWENGCTVIVMLTP 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  89 EIEGGVIKCCSYWPvslKEPLEFKH-FHVLLENFQI-TQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFI 166
Cdd:cd14609   120 LVEDGVKQCDRYWP---DEGSSLYHiYEVNLVSEHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLL 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 167 KYVRYVRKSH--ITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNY-SFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:cd14609   197 DFRRKVNKCYrgRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVkEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 15-245 1.24e-52

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: 172.22  E-value: 1.24e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  15 NRDKNRYRDILPYDSTRVPLGK-----NKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITRE 89
Cdd:cd14624    47 NKPKNRYANVIAYDHSRVLLSAiegipGSDYINANYID--GYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  90 IEGGVIKCCSYWPVSLKEPLEFKHFhVLLENFQITQYfVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYV 169
Cdd:cd14624   125 EERSRVKCDQYWPSRGTETYGLIQV-TLLDTVELATY-CVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL 202

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683650 170 RYVRKSHI--TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLEVL 245
Cdd:cd14624   203 RRVKTCNPpdAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 19-239 2.30e-50

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: 164.31  E-value: 2.30e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  19 NRYRDILPYDSTRVPLGKN-----KDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGG 93
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADagvpgSDYINASYISGYLCPNEF--IATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  94 VIKCCSYWPVSLKEPLEFKHFHV--LLENFQITqyFVIRIFQIVKKstGKSHSVKHLQFIKWPDHGTPASADFFIKYVRY 171
Cdd:cd14616    79 RIRCHQYWPEDNKPVTVFGDIVItkLMEDVQID--WTIRDLKIERH--GDYMMVRQCNFTSWPEHGVPESSAPLIHFVKL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 172 VR--KSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 239
Cdd:cd14616   155 VRasRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 18-241 3.28e-49

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: 162.34  E-value: 3.28e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  18 KNRYRDILPYDSTRVPL-GKNKD-----YINASYIRIVNhEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITrEIE 91
Cdd:cd14613    28 KNRYKTILPNPHSRVCLtSPDQDdplssYINANYIRGYG-GEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMIT-NIE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  92 GGVIKCCSYWPvslKEPLEFKHFHVLLENFQITQYFVIRIFQIvkKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRY 171
Cdd:cd14613   106 EMNEKCTEYWP---EEQVTYEGIEITVKQVIHADDYRLRLITL--KSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQE 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958683650 172 VRKSHI-----TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIV 241
Cdd:cd14613   181 VEEARQqaepnCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 40-234 6.58e-49

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: 159.99  E-value: 6.58e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHVLLE 119
Cdd:cd14557     1 YINASYID--GFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKIN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 120 NFQITQYFVIRIFQIV-KKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVR--KSHITGPLLVHCSAGVGRTGVFI 196
Cdd:cd14557    79 EEKICPDYIIRKLNINnKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNafNNFFSGPIVVHCSAGVGRTGTYI 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958683650 197 CVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQY 234
Cdd:cd14557   159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 40-239 9.43e-49

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


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 159.76  E-value: 9.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEplEFKHFHVLLE 119
Cdd:cd17668     1 YINANYVDGYNKPKAY--IAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE--EYGNFLVTQK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 120 NFQITQYFVIRIFQI----VKKSTGKSHS----VKHLQFIKWPDHGTPasaDFFIKYVRYVRKS-----HITGPLLVHCS 186
Cdd:cd17668    77 SVQVLAYYTVRNFTLrntkIKKGSQKGRPsgrvVTQYHYTQWPDMGVP---EYTLPVLTFVRKAsyakrHAVGPVVVHCS 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958683650 187 AGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 239
Cdd:cd17668   154 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 21-243 3.02e-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: 158.95  E-value: 3.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  21 YRDILPYDSTRVPL-----GKNKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVI 95
Cdd:cd14620     1 YPNILPYDHSRVILsqldgIPCSDYINASYID--GYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  96 KCCSYWPVslKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHS---VKHLQFIKWPDHG---TPASADFFIKYV 169
Cdd:cd14620    79 KCYQYWPD--QGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAprlVTQLHFTSWPDFGvpfTPIGMLKFLKKV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958683650 170 RYVRKSHiTGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:cd14620   157 KSVNPVH-AGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 40-239 6.09e-48

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: 157.55  E-value: 6.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKeplEFKHFHVLLE 119
Cdd:cd14558     1 YINASFIDGYWGPKSL--IATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK---TYGDIEVELK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 120 NFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVR--------KSHITGPLLVHCSAGVGR 191
Cdd:cd14558    76 DTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKqklpyknsKHGRSVPIVVHCSDGSSR 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958683650 192 TGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 239
Cdd:cd14558   156 TGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 40-241 9.13e-48

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: 9.13e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRIVNHEEeyFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVslKEPLEFKHFHVLLE 119
Cdd:cd14552     1 YINASFIDGYRQKD--AYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPE--DGSVSSGDITVELK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 120 NFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHI---TGPLLVHCSAGVGRTGVFI 196
Cdd:cd14552    77 DQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQqsgNHPITVHCSAGAGRTGTFC 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958683650 197 CVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIV 241
Cdd:cd14552   157 ALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 40-243 1.82e-47

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


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 156.45  E-value: 1.82e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIrIVNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPvslKEPLEFKH-FHVLL 118
Cdd:cd14546     1 YINASTI-YDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP---EEGSEVYHiYEVHL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 119 ENFQI-TQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSH--ITGPLLVHCSAGVGRTGVF 195
Cdd:cd14546    77 VSEHIwCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYrgRSCPIVVHCSDGAGRTGTY 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958683650 196 ICVDVVFCTIEKNY-SFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:cd14546   157 ILIDMVLNRMAKGAkEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 37-243 5.41e-47

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


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 155.56  E-value: 5.41e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  37 NKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEPLEFKHFHV 116
Cdd:cd14631    12 SSDYINANYID--GYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 117 LLENFQitqYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSH--ITGPLLVHCSAGVGRTGV 194
Cdd:cd14631    90 EMEPLA---EYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNppSAGPIVVHCSAGAGRTGC 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958683650 195 FICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:cd14631   167 YIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 14-243 1.42e-46

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: 156.72  E-value: 1.42e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  14 QNRDKNRYRDILPYDSTRVPLGK-----NKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITR 88
Cdd:cd14621    51 ENKEKNRYVNILPYDHSRVHLTPvegvpDSDYINASFIN--GYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTN 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  89 EIEGGVIKCCSYWPVslKEPLEFKHFHVLLENFQITQYFVIRIF--QIVKKSTGKSHS--VKHLQFIKWPDHGTPASADF 164
Cdd:cd14621   129 LKERKECKCAQYWPD--QGCWTYGNIRVSVEDVTVLVDYTVRKFciQQVGDVTNKKPQrlITQFHFTSWPDFGVPFTPIG 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 165 FIKYVRYVRKSH--ITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVL 242
Cdd:cd14621   207 MLKFLKKVKNCNpqYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALL 286


                  .
gi 1958683650 243 E 243
Cdd:cd14621   287 E 287
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 39-241 2.53e-45

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: 150.93  E-value: 2.53e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  39 DYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVslKEPLEFKHFHVLL 118
Cdd:cd14622     1 DYINASFID--GYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPS--EGSVTHGEITIEI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 119 ENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHI-TG--PLLVHCSAGVGRTGVF 195
Cdd:cd14622    77 KNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQqTGnhPIVVHCSAGAGRTGTF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958683650 196 ICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIV 241
Cdd:cd14622   157 IALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 12-243 3.16e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 153.62  E-value: 3.16e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  12 ELQNRDKNRYRDILPYDSTRVPLGKNK---DYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITR 88
Cdd:PHA02742   49 ELKNMKKCRYPDAPCFDRNRVILKIEDggdDFINASYVD--GHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITK 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  89 EIEGGVIKCCSYWPVSLKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY 168
Cdd:PHA02742  127 IMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDF 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 169 VRYVRKSHITG-------------PLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQ 235
Cdd:PHA02742  207 VLAVREADLKAdvdikgenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYI 286


                  ....*...
gi 1958683650 236 FCYEIVLE 243
Cdd:PHA02742  287 FCYFIVLI 294
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 20-243 1.61e-42

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: 144.42  E-value: 1.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  20 RYRDILPYDSTRV--PLGK---NKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGV 94
Cdd:cd14623     1 RVLQIIPYEFNRViiPVKRgeeNTDYVNASFID--GYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  95 IKCCSYWPVSlkEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRK 174
Cdd:cd14623    79 EKCAQYWPSD--GSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQK 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958683650 175 SHITG---PLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:cd14623   157 QQQQSgnhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 14-251 2.77e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 146.30  E-value: 2.77e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  14 QNRDKNRYRDILPYDSTRVPL----GKNKDYINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMIT-R 88
Cdd:PHA02747   50 ENQPKNRYWDIPCWDHNRVILdsggGSTSDYIHANWID--GFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTpT 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  89 EIEGGVIKCCSYWPVSLKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKSTGKSHSVKHLQFIKWPDHGTPASADFFIKY 168
Cdd:PHA02747  128 KGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKF 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 169 VR------------YVRKSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQF 236
Cdd:PHA02747  208 IKiidinrkksgklFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLF 287

                         250
                  ....*....|....*...
gi 1958683650 237 ---CYEIVLEVLQNLLAL 251
Cdd:PHA02747  288 iqpGYEVLHYFLSKIKAI 305
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 40-239 7.90e-41

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: 139.08  E-value: 7.90e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITrEIEGGVIKCCSYWPVslKEPLEFKHFHVLLE 119
Cdd:cd14556     1 YINAALLD--SYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLN-QLDPKDQSCPQYWPD--EGSGTYGPIQVEFV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 120 NFQITQYFVIRIFQIV--KKSTGKSHSVKHLQFIKWPDHG-TPASADFFIKYVRYVRK---SHITGPLLVHCSAGVGRTG 193
Cdd:cd14556    76 STTIDEDVISRIFRLQntTRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKwqeQSGEGPIVVHCLNGVGRSG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958683650 194 VFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 239
Cdd:cd14556   156 VFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 40-239 1.99e-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: 138.12  E-value: 1.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWPVSLKEplEFKHFHVLLE 119
Cdd:cd14551     1 YINASYID--GYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW--TYGNLRVRVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 120 NFQITQYFVIRIFQIVKKSTG----KSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHI--TGPLLVHCSAGVGRTG 193
Cdd:cd14551    77 DTVVLVDYTTRKFCIQKVNRGigekRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPprAGPIVVHCSAGVGRTG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958683650 194 VFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 239
Cdd:cd14551   157 TFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PHA02738 PHA02738
hypothetical protein; Provisional
 12-241 2.05e-39

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 138.90  E-value: 2.05e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  12 ELQNRDKNRYRDILPYDSTRVPLGKNK---DYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITR 88
Cdd:PHA02738   46 EKKNRKLNRYLDAVCFDHSRVILPAERnrgDYINANYVDGFEYKKKF--ICGQAPTRQTCYDFYRMLWMEHVQIIVMLCK 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  89 EIEGGVIKCCSYWPvslkeplEFKHFHVLLENFQITQYFVIRIFQIVKKS------TGKSHSVKHLQFIKWPDHGTPASA 162
Cdd:PHA02738  124 KKENGREKCFPYWS-------DVEQGSIRFGKFKITTTQVETHPHYVKSTllltdgTSATQTVTHFNFTAWPDHDVPKNT 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 163 DFFIKYVRYVR---------------KSHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGM 227
Cdd:PHA02738  197 SEFLNFVLEVRqcqkelaqeslqighNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYS 276

                         250
                  ....*....|....
gi 1958683650 228 IQTKEQYQFCYEIV 241
Cdd:PHA02738  277 LFIPFQYFFCYRAV 290
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
144-243 2.49e-36

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 124.39  E-value: 2.49e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  144 SVKHLQFIKWPDHGTPASADFFIKYVRYVRKSH----ITGPLLVHCSAGVGRTGVFICVDVVFCTIEK-NYSFNIMNIVT 218
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLnqseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 1958683650  219 QMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 144-243 2.49e-36

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 124.39  E-value: 2.49e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  144 SVKHLQFIKWPDHGTPASADFFIKYVRYVRKSH----ITGPLLVHCSAGVGRTGVFICVDVVFCTIEK-NYSFNIMNIVT 218
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLnqseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 1958683650  219 QMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 14-245 4.60e-35

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 127.45  E-value: 4.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  14 QNRDKNRYRDILPYDSTRVPLG------------------------KNKDYINASYIRivNHEEEYFYIATQGPLPDTIE 69
Cdd:PHA02746   50 ENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkievtsedNAENYIHANFVD--GFKEANKFICAQGPKEDTSE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  70 DFWQMVLENNCNVIAMITrEIEGGVIKCCSYWPVSLKEPLEFKHFHV-LLENFQITQYFVIRIfQIVKKSTGKSHSVKHL 148
Cdd:PHA02746  128 DFFKLISEHESQVIVSLT-DIDDDDEKCFELWTKEEDSELAFGRFVAkILDIIEELSFTKTRL-MITDKISDTSREIHHF 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 149 QFIKWPDHGTPASADFFIKYVRYVRK------------SHITGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNI 216
Cdd:PHA02746  206 WFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadndPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285

                         250       260
                  ....*....|....*....|....*....
gi 1958683650 217 VTQMRKQRFGMIQTKEQYQFCYEIVLEVL 245
Cdd:PHA02746  286 VLKIRKQRHSSVFLPEQYAFCYKALKYAI 314
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 40-243 2.77e-33

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: 119.74  E-value: 2.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITrEIEGGVIkCCSYWPVslKEPLEFKHFHVLLE 119
Cdd:cd14634     1 YINAALMD--SHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN-EMDAAQL-CMQYWPE--KTSCCYGPIQVEFV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 120 NFQITQYFVIRIFQIVKKSTGKS--HSVKHLQFIKWPDH-GTPASADFFIKYVRYVRKSHIT-----GPLLVHCSAGVGR 191
Cdd:cd14634    75 SADIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgreGRTVVHCLNGGGR 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958683650 192 TGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:cd14634   155 SGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 40-243 6.94e-29

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: 108.24  E-value: 6.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITrEIEGGVIkCCSYWP---VSLKEPLEFKHFHV 116
Cdd:cd14635     1 YINAALMD--SYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLN-DVDPAQL-CPQYWPengVHRHGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 117 LLENFQITQYFviRIFQIVKKSTGkSHSVKHLQFIKWPDH-GTPASADFFIKYVRYVRKSHIT-----GPLLVHCSAGVG 190
Cdd:cd14635    77 DLEEDIISRIF--RIYNAARPQDG-YRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynggeGRTVVHCLNGGG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958683650 191 RTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:cd14635   154 RSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 40-239 1.05e-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: 102.40  E-value: 1.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEGGviKCCSYWPvSLKEPLEFKHF----- 114
Cdd:cd14550     1 YINASYLQGYRRSNEF--IITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWP-TKEKPLECETFkvtls 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 115 ---HVLLENFQ--ITQYFVIrifqivkKSTGKSH--SVKHLQFIKWPDHGTPASADF-FIKYVRYvRKSHITGPLLVHCS 186
Cdd:cd14550    76 gedHSCLSNEIrlIVRDFIL-------ESTQDDYvlEVRQFQCPSWPNPCSPIHTVFeLINTVQE-WAQQRDGPIVVHDR 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958683650 187 AGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 239
Cdd:cd14550   148 YGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 40-243 1.06e-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: 97.40  E-value: 1.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRivNHEEEYFYIATQGPLPDTIEDFWQMVLENNCNVIAMITrEIEGgVIKCCSYWPVslKEPLEFKHFHVLLE 119
Cdd:cd14636     1 YINAALMD--SYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN-EVDL-AQGCPQYWPE--EGMLRYGPIQVECM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 120 NFQITQYFVIRIFQIVKKSTGKSH--SVKHLQFIKWPDH-GTPASADFFIKYVRYVRK-----SHITGPLLVHCSAGVGR 191
Cdd:cd14636    75 SCSMDCDVISRIFRICNLTRPQEGylMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKwqeecDEGEGRTIIHCLNGGGR 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958683650 192 TGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:cd14636   155 SGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 40-242 6.71e-24

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: 95.06  E-value: 6.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITrEIEGGVIKCCSYWPvSLKEPLEFKHF----- 114
Cdd:cd17669     1 YINASYIMGYYQSNEF--IITQHPLLHTIKDFWRMIWDHNAQLIVMLP-DGQNMAEDEFVYWP-NKDEPINCETFkvtli 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 115 ---HVLLENFQ--ITQYFVIRIFQivkksTGKSHSVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHITGPLLVHCSAGV 189
Cdd:cd17669    77 aeeHKCLSNEEklIIQDFILEATQ-----DDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958683650 190 GRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVL 242
Cdd:cd17669   152 VTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 40-243 5.70e-23

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: 92.66  E-value: 5.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINA----SYIRIVNheeeyfYIATQGPLPDTIEDFWQMVLENNCNVIAMITR-EIEGGVIKCCSYWPVSLKE---PLEF 111
Cdd:cd14637     1 YINAaltdSYTRSAA------FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQlNQSNSAWPCLQYWPEPGLQqygPMEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 112 KHFHVLLENFQITQYFviRIFQIVKKSTGKShSVKHLQFIKW-PDHGTPASADFFIKYVRYVRK---SHITGPLLVHCSA 187
Cdd:cd14637    75 EFVSGSADEDIVTRLF--RVQNITRLQEGHL-MVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKwqrESGEGRTVVHCLN 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958683650 188 GVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVLE 243
Cdd:cd14637   152 GGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 40-242 7.57e-22

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: 89.74  E-value: 7.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  40 YINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMVLENNCNVIAMITrEIEGGVIKCCSYWPvSLKEPLEFKHFHVLL- 118
Cdd:cd17670     1 YINASYIMGYYRSNEF--IITQHPLPHTTKDFWRMIWDHNAQIIVMLP-DNQGLAEDEFVYWP-SREESMNCEAFTVTLi 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 119 --ENFQITQYFVIRIFQIVKKSTGKSH--SVKHLQFIKWPDHGTPASADFfiKYVRYVRKSHIT--GPLLVHCSAGVGRT 192
Cdd:cd17670    77 skDRLCLSNEEQIIIHDFILEATQDDYvlEVRHFQCPKWPNPDAPISSTF--ELINVIKEEALTrdGPTIVHDEFGAVSA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958683650 193 GVFICVDVVFCTIEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYEIVL 242
Cdd:cd17670   155 GTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 19-235 8.85e-22

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: 90.15  E-value: 8.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  19 NRYRDIlpydSTRVPLGKNKDyINASYIRIVNHEeeyFYIATQGPLPDTIEDFWQMVLENNCNVIAMITREIEggvIKC- 97
Cdd:cd14559     1 NRFTNI----QTRVSTPVGKN-LNANRVQIGNKN---VAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKD---IQRk 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  98 ---------CSYWPVS----------LKEPLEFKHFhvlleNFQITQyfvirifqivkksTGKSHSVKHLQFIKWPDHgT 158
Cdd:cd14559    70 glppyfrqsGTYGSVTvkskktgkdeLVDGLKADMY-----NLKITD-------------GNKTITIPVVHVTNWPDH-T 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 159 PASADFFIKYVRYVRKS---HITGPLL---------------VHCSAGVGRTGVFICvdvVFCTIEKNYSFNIMNIVTQM 220
Cdd:cd14559   131 AISSEGLKELADLVNKSaeeKRNFYKSkgssaindknkllpvIHCRAGVGRTGQLAA---AMELNKSPNNLSVEDIVSDM 207

                         250
                  ....*....|....*.
gi 1958683650 221 RKQRFG-MIQTKEQYQ 235
Cdd:cd14559   208 RTSRNGkMVQKDEQLD 223
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 2-241 1.45e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 82.71  E-value: 1.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650   2 IPPDDFKSGYELQNRDKNRYRD------ILPYDSTRVPLGKNKDYINASYIRIVNHEEEYfyIATQGPLPDTIEDFWQMV 75
Cdd:PHA02740   34 IVPEHEDEANKACAQAENKAKDenlalhITRLLHRRIKLFNDEKVLDARFVDGYDFEQKF--ICIINLCEDACDKFLQAL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  76 LENNCNVIAMITREIEGgviKC-CSYWPVSLKEPLEFKHFHVLLENFQITQYFVIRIFQIVKKStGKSHSVKHLQFIKWP 154
Cdd:PHA02740  112 SDNKVQIIVLISRHADK---KCfNQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDKF-GQAQKISHFQYTAWP 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 155 ----DHGTPASADFFIK----YVRYVRKSHI--TGPLLVHCSAGVGRTGVFICVDVVFCTIEKNYSFNIMNIVTQMRKQR 224
Cdd:PHA02740  188 adgfSHDPDAFIDFFCNiddlCADLEKHKADgkIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKK 267

                         250
                  ....*....|....*..
gi 1958683650 225 FGMIQTKEQYQFCYEIV 241
Cdd:PHA02740  268 YGCMNCLDDYVFCYHLI 284
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
141-236 5.14e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 50.74  E-value: 5.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 141 KSHSVKHLQFiKWPDHGTPASADF--FIKYVRYVRKSHitGPLLVHCSAGVGRTG-VFICVDvvfctIEKNYSFNimNIV 217
Cdd:COG2453    44 EEAGLEYLHL-PIPDFGAPDDEQLqeAVDFIDEALREG--KKVLVHCRGGIGRTGtVAAAYL-----VLLGLSAE--EAL 113

                          90
                  ....*....|....*....
gi 1958683650 218 TQMRKQRFGMIQTKEQYQF 236
Cdd:COG2453   114 ARVRAARPGAVETPAQRAF 132
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 179-239 5.65e-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: 49.66  E-value: 5.65e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958683650 179 GPLLVHCSAGVGRTGVFICVDVVfctIEKNYSFNimNIVTQMRKQR-FGMIQTKEQYQFCYE 239
Cdd:cd14494    57 EPVLVHCKAGVGRTGTLVACYLV---LLGGMSAE--EAVRIVRLIRpGGIPQTIEQLDFLIK 113
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 116-239 7.63e-08

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: 7.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 116 VLLENFQITQYFVIRIFQIVKKSTGKSHsvkHLQFikwPDHGTPASADFFIKYVRYVRKSHITGP-LLVHCSAGVGRTGV 194
Cdd:cd14505    49 TLCTDGELEELGVPDLLEQYQQAGITWH---HLPI---PDGGVPSDIAQWQELLEELLSALENGKkVLIHCKGGLGRTGL 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958683650 195 ficvdVVFCT-IEKNYSFNIMNIVTQMRKQRFGMIQTKEQYQFCYE 239
Cdd:cd14505   123 -----IAACLlLELGDTLDPEQAIAAVRALRPGAIQTPKQENFLHQ 163
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 143-236 6.40e-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: 47.66  E-value: 6.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 143 HSVKHLqFIKWPDHGTPA--SADFFIKYVRYVRKSHitGPLLVHCSAGVGRTGVFICvdvvfCTIEKNYSFNIMNIVTQM 220
Cdd:cd14504    48 PGLRYH-HIPIEDYTPPTleQIDEFLDIVEEANAKN--EAVLVHCLAGKGRTGTMLA-----CYLVKTGKISAVDAINEI 119

                          90
                  ....*....|....*.
gi 1958683650 221 RKQRFGMIQTKEQYQF 236
Cdd:cd14504   120 RRIRPGSIETSEQEKF 135
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 153-239 1.44e-05

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 44.65  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 153 WPDHGTPaSADFFIKYVRyVRKSHI--TGPLLVHCSAGVGRTGVFICVDVVFCTiekNYSFNimNIVTQMRKQRFGMIQT 230
Cdd:cd14506    84 WKDYGVP-SLTTILDIVK-VMAFALqeGGKVAVHCHAGLGRTGVLIACYLVYAL---RMSAD--QAIRLVRSKRPNSIQT 156


                  ....*....
gi 1958683650 231 KEQYQFCYE 239
Cdd:cd14506   157 RGQVLCVRE 165
PRK15375 PRK15375
type III secretion system effector GTPase-activating protein SptP;
65-234 4.03e-04

type III secretion system effector GTPase-activating protein SptP;


Pssm-ID: 185273 [Multi-domain]  Cd Length: 535  Bit Score: 41.33  E-value: 4.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  65 PDTIEDFWQMVLENNCNVIAMITREIEGGVIKCCSYWpvslKEPLEFKHFHVLLENFQ-ITQYFVIRIFQIVKKSTGKSH 143
Cdd:PRK15375  346 PDALEAHMKMLLEKECSCLVVLTSEDQMQAKQLPPYF----RGSYTFGEVHTNSQKVSsASQGEAIDQYNMQLSCGEKRY 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650 144 SVKHLQFIKWPDHGTPASADFFIKYVRYVRKSHITGPL----------LVHCSAGVGRTGVFICVDVvfctIEKNYSFNI 213
Cdd:PRK15375  422 TIPVLHVKNWPDHQPLPSTDQLEYLADRVKNSNQNGAPgrsssdkhlpMIHCLGGVGRTGTMAAALV----LKDNPHSNL 497

                         170       180
                  ....*....|....*....|..
gi 1958683650 214 MNIVTQMRKQRFG-MIQTKEQY 234
Cdd:PRK15375  498 EQVRADFRNSRNNrMLEDASQF 519
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 154-192 6.58e-04

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: 6.58e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1958683650 154 PDHGTPASADFFiKYVRYVRKSHITGPLLVHCSAGVGRT 192
Cdd:pfam14566 109 TDEKAPLEEDFD-ALISIVKDAPEDTALVFNCQMGRGRT 146
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 154-195 4.26e-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: 4.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958683650 154 PDHGTPASADFFikyvRYVRKShiTGPLLVHCSAGVGRTGVF 195
Cdd:pfam13350 111 VTSARAAYRALF----EALADN--DGPVLFHCTAGKDRTGVA 146
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 176-211 6.24e-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: 36.66  E-value: 6.24e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958683650 176 HITGPLLVHCSAGVGRTGVFICvdvvfCTIEKNYSF 211
Cdd:cd14499   107 NEKGAIAVHCKAGLGRTGTLIA-----CYLMKHYGF 137
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 146-197 7.28e-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: 35.70  E-value: 7.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683650 146 KHLQFIKWP---DHGTPASADFF--IKYVRYVRKSHitGPLLVHCSAGVGRTGVFIC 197
Cdd:pfam00782  34 SGILYLRIPvedNHETNISKYLEeaVEFIDDARQKG--GKVLVHCQAGISRSATLII 88
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
117-197 7.49e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 35.72  E-value: 7.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683650  117 LLENFQITqyFVIRIFQIVKKSTGKSHSVKHLQfIKWpDHGTPASADFF--IKYVRYVRKSHitGPLLVHCSAGVGRTGV 194
Cdd:smart00195  21 LLKKLGIT--HVINVTNEVPNYNGSDFTYLGVP-IDD-NTETKISPYFPeaVEFIEDAESKG--GKVLVHCQAGVSRSAT 94


                   ...
gi 1958683650  195 FIC 197
Cdd:smart00195  95 LII 97
 
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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