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Conserved domains on  [gi|1844122053|ref|NP_002823|]
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tyrosine-protein phosphatase non-receptor type 7 isoform 1 [Homo sapiens]

Protein Classification

PTPc-N7 domain-containing protein( domain architecture ID 12998695)

PTPc-N7 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 105-350 0e+00

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: 523.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 105 PSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQ-EDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMV 183
Cdd:cd14612     1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 184 WQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPES 263
Cdd:cd14612    81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 264 AGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 343
Cdd:cd14612   161 AGPLLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                  ....*..
gi 1844122053 344 HHTLALY 350
Cdd:cd14612   241 HHTLALY 247
 
Name Accession Description Interval E-value
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 105-350 0e+00

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: 523.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 105 PSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQ-EDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMV 183
Cdd:cd14612     1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 184 WQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPES 263
Cdd:cd14612    81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 264 AGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 343
Cdd:cd14612   161 AGPLLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                  ....*..
gi 1844122053 344 HHTLALY 350
Cdd:cd14612   241 HHTLALY 247
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
96-348 8.62e-111

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 323.84  E-value: 8.62e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053   96 QLEEEFLKIPSNFVSPEDLDI---PGHASKDRYKTILPNPQSRVCLGRAQSqEDGDYINANYIRGYDGKeKVYIATQGPM 172
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGP-KAYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053  173 PNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEE---ETYGPFQIRIQDMKECPEYTVRQLTIQY--QEERRS 246
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEkGREKCAQYWPDEEgepLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSETRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053  247 VKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQL 326
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTST--GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKEL 236

                          250       260
                   ....*....|....*....|..
gi 1844122053  327 RLDRGGMIQTAEQYQFLHHTLA 348
Cdd:smart00194 237 RSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
119-348 2.13e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 311.48  E-value: 2.13e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 119 HASKDRYKTILPNPQSRVCLGRaqSQEDGDYINANYIRGYdGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLR 198
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTG--DPGPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 199 E-GKEKCVHYWPTEEE---TYGPFQIRIQDMKE-CPEYTVRQLTIQY--QEERRSVKHILFSAWPDHQTPESAGPLLRLV 271
Cdd:pfam00102  78 EkGREKCAQYWPEEEGeslEYGDFTVTLKKEKEdEKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844122053 272 AEVEESPETAAHpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLA 348
Cdd:pfam00102 158 RKVRKSSLDGRS-GPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PHA02738 PHA02738
hypothetical protein; Provisional
 123-350 1.01e-44

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 156.24  E-value: 1.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 123 DRYKTILPNPQSRVCLGRAQSQedGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GK 201
Cdd:PHA02738   53 NRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKK-FICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEnGR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 202 EKCVHYWPTEEET---YGPFQIRIQDMKECPEYTVRQLTI-QYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEES 277
Cdd:PHA02738  130 EKCFPYWSDVEQGsirFGKFKITTTQVETHPHYVKSTLLLtDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQC 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 278 PETAA-----------HPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHT 346
Cdd:PHA02738  210 QKELAqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRA 289


                  ....
gi 1844122053 347 LALY 350
Cdd:PHA02738  290 VKRY 293
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
95-343 2.86e-44

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 153.71  E-value: 2.86e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053  95 KQLEEEFLKIPSNFVSPEDLDIPGHASKDRYKTILPNPQSRVclgraqsQEDGDYINANYIRGYDGKekVYIATQGPMPN 174
Cdd:COG5599    18 SRLSTLTNELAPSHNDPQYLQNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIGNH--RYIATQYPLEE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 175 TVSDFWEMVWQEEVSLIVMLTQLREGKE---KCVHYWPTEEEtYGPFQIR--------IQDMKECPEYTVRQLtiQYQEE 243
Cdd:COG5599    89 QLEDFFQMLFDNNTPVLVVLASDDEISKpkvKMPVYFRQDGE-YGKYEVSseltesiqLRDGIEARTYVLTIK--GTGQK 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 244 RRSVKHILFSAWPDHQTPeSAGPLLRLVAEVEESPETAAHP-GPIVVHCSAGIGRTGCFIATRIGCQQLKARGE--VDIL 320
Cdd:COG5599   166 KIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKEKIKDPDkLLPVVHCRAGVGRTGTLIACLALSKSINALVQitLSVE 244

                         250       260
                  ....*....|....*....|....
gi 1844122053 321 GIVCQLRLDRG-GMIQTAEQYQFL 343
Cdd:COG5599   245 EIVIDMRTSRNgGMVQTSEQLDVL 268
 
Name Accession Description Interval E-value
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 105-350 0e+00

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: 523.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 105 PSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQ-EDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMV 183
Cdd:cd14612     1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 184 WQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPES 263
Cdd:cd14612    81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 264 AGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 343
Cdd:cd14612   161 AGPLLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                  ....*..
gi 1844122053 344 HHTLALY 350
Cdd:cd14612   241 HHTLALY 247
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 123-345 1.61e-161

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: 451.08  E-value: 1.61e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 123 DRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKE 202
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 203 KCVHYWPTEE-ETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETA 281
Cdd:cd14547    81 KCAQYWPEEEnETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEARQTE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844122053 282 AHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHH 345
Cdd:cd14547   161 PHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 97-350 1.52e-124

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: 358.79  E-value: 1.52e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053  97 LEEEFLKIPSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLgRAQSQED--GDYINANYIRGYDGKEKVYIATQGPMPN 174
Cdd:cd14613     3 LQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCL-TSPDQDDplSSYINANYIRGYGGEEKVYIATQGPTVN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 175 TVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSA 254
Cdd:cd14613    82 TVGDFWRMVWQERSPIIVMITNIEEMNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 255 WPDHQTPESAGPLLRLVAEVEESPETA-AHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGM 333
Cdd:cd14613   162 WPDQKTPDNAPPLLQLVQEVEEARQQAePNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGM 241

                         250
                  ....*....|....*..
gi 1844122053 334 IQTAEQYQFLHHTLALY 350
Cdd:cd14613   242 IQTCEQYQFVHHVLSLY 258
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 121-345 5.05e-119

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: 343.44  E-value: 5.05e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 121 SKDRYKTILPNPQSRVCLGRAQSQED-GDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE 199
Cdd:cd14611     1 TKNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 200 GKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPE 279
Cdd:cd14611    81 KNEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844122053 280 TAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHH 345
Cdd:cd14611   161 ASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
96-348 8.62e-111

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 323.84  E-value: 8.62e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053   96 QLEEEFLKIPSNFVSPEDLDI---PGHASKDRYKTILPNPQSRVCLGRAQSqEDGDYINANYIRGYDGKeKVYIATQGPM 172
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGP-KAYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053  173 PNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEE---ETYGPFQIRIQDMKECPEYTVRQLTIQY--QEERRS 246
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEkGREKCAQYWPDEEgepLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSETRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053  247 VKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQL 326
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTST--GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKEL 236

                          250       260
                   ....*....|....*....|..
gi 1844122053  327 RLDRGGMIQTAEQYQFLHHTLA 348
Cdd:smart00194 237 RSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
119-348 2.13e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 311.48  E-value: 2.13e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 119 HASKDRYKTILPNPQSRVCLGRaqSQEDGDYINANYIRGYdGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLR 198
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTG--DPGPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 199 E-GKEKCVHYWPTEEE---TYGPFQIRIQDMKE-CPEYTVRQLTIQY--QEERRSVKHILFSAWPDHQTPESAGPLLRLV 271
Cdd:pfam00102  78 EkGREKCAQYWPEEEGeslEYGDFTVTLKKEKEdEKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844122053 272 AEVEESPETAAHpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLA 348
Cdd:pfam00102 158 RKVRKSSLDGRS-GPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 149-345 3.26e-93

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: 276.86  E-value: 3.26e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEE---TYGPFQIRIQD 224
Cdd:cd00047     1 YINASYIDGYRGPKE-YIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEkGREKCERYWPEEGGkplEYGDITVTLVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 225 MKECPEYTVRQLTIQYQ--EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPEtaAHPGPIVVHCSAGIGRTGCFI 302
Cdd:cd00047    80 EEELSDYTIRTLELSPKgcSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEAR--KPNGPIVVHCSAGVGRTGTFI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1844122053 303 ATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHH 345
Cdd:cd00047   158 AIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 122-347 1.00e-78

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: 241.15  E-value: 1.00e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 122 KDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-G 200
Cdd:cd14553     6 KNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEErS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 201 KEKCVHYWPTE-EETYGPFQIRIQDMKECPEYTVRQLTI--QYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEes 277
Cdd:cd14553    85 RVKCDQYWPTRgTETYGLIQVTLLDTVELATYTVRTFALhkNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK-- 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844122053 278 petAAHP---GPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 347
Cdd:cd14553   163 ---ACNPpdaGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 124-344 1.84e-78

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: 239.95  E-value: 1.84e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 124 RYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKE 202
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPRE-FIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEkGRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 203 KCVHYWP--TEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEEspET 280
Cdd:cd14548    80 KCDHYWPfdQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD--YI 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844122053 281 AAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14548   158 KQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 117-344 1.23e-74

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 231.87  E-value: 1.23e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 117 PGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKeKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQ 196
Cdd:cd14543    27 PANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQK-NAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTR 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 197 LRE-GKEKCVHYWPTEEET---YGPFQIRIQDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGPLLRL 270
Cdd:cd14543   106 VVErGRVKCGQYWPLEEGSslrYGDLTVTNLSVENKEHYKKTTLEIHNTEtdESRQVTHFQFTSWPDFGVPSSAAALLDF 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 271 VAEVEE---------SPETAAHPG--PIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQ 339
Cdd:cd14543   186 LGEVRQqqalavkamGDRWKGHPPgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQ 265


                  ....*
gi 1844122053 340 YQFLH 344
Cdd:cd14543   266 YYFCY 270
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 149-344 3.72e-74

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: 228.39  E-value: 3.72e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMK 226
Cdd:cd14549     1 YINANYVDGYN-KARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVErGRRKCDQYWPKEgTETYGNIQVTLLSTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 227 ECPEYTVRQLTIQY--------QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVeespeTAAHP---GPIVVHCSAGI 295
Cdd:cd14549    80 VLATYTVRTFSLKNlklkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKS-----SAANPpgaGPIVVHCSAGV 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1844122053 296 GRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14549   155 GRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 120-350 5.85e-73

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: 226.96  E-value: 5.85e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 120 ASKDRYKTILPNPQSRVCLGRAQSQEDG-DYINANYIR------GYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIV 192
Cdd:cd14544     2 KGKNRYKNILPFDHTRVILKDRDPNVPGsDYINANYIRnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 193 MLT-QLREGKEKCVHYWPTEEET--YGPFQIRIQDMKECPEYTVRQLTIQYQEER---RSVKHILFSAWPDHQTPESAGP 266
Cdd:cd14544    82 MTTkEVERGKNKCVRYWPDEGMQkqYGPYRVQNVSEHDTTDYTLRELQVSKLDQGdpiREIWHYQYLSWPDHGVPSDPGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 267 LLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQYQFL 343
Cdd:cd14544   162 VLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQYKFI 241


                  ....*..
gi 1844122053 344 HHTLALY 350
Cdd:cd14544   242 YVAVAQY 248
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 109-349 7.05e-69

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: 216.29  E-value: 7.05e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 109 VSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEV 188
Cdd:cd14614     2 IPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 189 SLIVMLTQLREGKE-KCVHYWPTEEE--TYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTP--ES 263
Cdd:cd14614    81 QIIVMLTQCNEKRRvKCDHYWPFTEEpvAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPtaNA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 264 AGPLLRLVAEVEEspETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 343
Cdd:cd14614   161 AESILQFVQMVRQ--QAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFI 238


                  ....*.
gi 1844122053 344 HHTLAL 349
Cdd:cd14614   239 HQCVQL 244
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 122-348 5.97e-68

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: 214.69  E-value: 5.97e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 122 KDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGkEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVM-LTQLREG 200
Cdd:cd14603    33 KNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDG-SRAYIATQGPLSHTVLDFWRMIWQYGVKVILMaCREIEMG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 201 KEKCVHYWPTEEET--YGPFQI-RIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEEs 277
Cdd:cd14603   112 KKKCERYWAQEQEPlqTGPFTItLVKEKRLNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARR- 190

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844122053 278 pETAAHPGPIVVHCSAGIGRTGCfIATRIGCQQL----KARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLA 348
Cdd:cd14603   191 -LQGSGPEPLCVHCSAGCGRTGV-ICTVDYVRQLlltqRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVA 263
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 149-345 6.07e-68

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: 212.88  E-value: 6.07e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEET--YGPFQIRIQDM 225
Cdd:cd18533     1 YINASYITLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVEnGREKCDQYWPSGEYEgeYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 226 KECPE--YTVRQLTIQY-QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFI 302
Cdd:cd18533    81 EENDDggFIVREFELSKeDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGTFI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1844122053 303 A--------TRIGCQQLKARGEVD-ILGIVCQLRLDRGGMIQTAEQYQFLHH 345
Cdd:cd18533   161 AldslldelKRGLSDSQDLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 123-343 3.06e-67

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: 211.60  E-value: 3.06e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 123 DRYKTILPNPQSRVCLGRAQSQEDgDYINANYIRGYDGKeKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GK 201
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTD-DYINANYMPGYNSK-KEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEqGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 202 EKCVHYWPTEE-ETYGPFQIRIQDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESP 278
Cdd:cd14615    79 TKCEEYWPSKQkKDYGDITVTMTSEIVLPEWTIRDFTVKNAQtnESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYM 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844122053 279 ETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 343
Cdd:cd14615   159 KQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 123-344 1.95e-66

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: 209.39  E-value: 1.95e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 123 DRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GK 201
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRRE-YIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEkGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 202 EKCVHYWPTEEET--YGPFQIRIQDMKECPEYTVRQLTIQYQEE---RRSVKHILFSAWPDHQTPESAGPLLRLVAEVEE 276
Cdd:cd14617    80 VKCDHYWPADQDSlyYGDLIVQMLSESVLPEWTIREFKICSEEQldaPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844122053 277 SPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14617   160 YINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 96-347 5.78e-66

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: 209.89  E-value: 5.78e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053  96 QLEEEFLKI-PSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPN 174
Cdd:cd14626    17 KFSQEYESIdPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYR-KQNAYIATQGPLPE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 175 TVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMKECPEYTVRQLTIQYQ--EERRSVKHI 250
Cdd:cd14626    96 TLSDFWRMVWEQRTATIVMMTRLEEkSRVKCDQYWPIRgTETYGMIQVTLLDTVELATYSVRTFALYKNgsSEKREVRQF 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 251 LFSAWPDHQTPESAGPLLRLVAEVEE-SPETAahpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLD 329
Cdd:cd14626   176 QFMAWPDHGVPEYPTPILAFLRRVKAcNPPDA---GPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQ 252

                         250
                  ....*....|....*...
gi 1844122053 330 RGGMIQTAEQYQFLHHTL 347
Cdd:cd14626   253 RNYMVQTEDQYIFIHEAL 270
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 123-344 2.09e-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: 204.35  E-value: 2.09e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 123 DRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYdGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GK 201
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGY-WSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEaGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 202 EKCVHYWPTEEE--TYGPFQIRIQDMKECPEYTVRQLTIQY--QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEES 277
Cdd:cd14619    80 VKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQveEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQW 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844122053 278 PETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14619   160 LDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLH 226
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 149-342 3.40e-64

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: 202.99  E-value: 3.40e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDGKEK-VYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEET----YGPFQIRI 222
Cdd:cd14538     1 YINASHIRIPVGGDTyHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEgGKVKCHRYWPDSLNKplicGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 223 QDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESpetaAHPGPIVVHCSAGIGRTGC 300
Cdd:cd14538    81 EKYQSLQDFVIRRISLRDKEtgEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRI----HNSGPIVVHCSAGIGRTGV 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1844122053 301 FIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 342
Cdd:cd14538   157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIF 198
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 123-347 1.48e-63

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: 202.10  E-value: 1.48e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 123 DRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLT-QLREGK 201
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQE-FIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvGMENGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 202 EKCVHYWPTEEE--TYGPFQIRIQDMKECPEYTVRQLTIQYQEER--RSVKHILFSAWPDHQTPESAGPLLRLVAEVEES 277
Cdd:cd14618    80 VLCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRkeRRVKHLHYTAWPDHGIPESTSSLMAFRELVREH 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 278 PETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 347
Cdd:cd14618   160 VQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 149-344 6.92e-63

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: 199.37  E-value: 6.92e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEETYGPFQIRIQDMKE 227
Cdd:cd14555     1 YINANYIDGYH-RPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEvGRVKCSRYWPDDTEVYGDIKVTLVETEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 228 CPEYTVRQLTIQYQ--EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhpGPIVVHCSAGIGRTGCFIATR 305
Cdd:cd14555    80 LAEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSA--GPIVVHCSAGAGRTGCYIVID 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1844122053 306 IGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14555   158 IMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIH 196
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 115-346 2.21e-62

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: 199.29  E-value: 2.21e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 115 DIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKeKVYIATQGPMPNTVSDFWEMVWQEEVSLIVML 194
Cdd:cd14554     2 NLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQR-GAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 195 TQLRE-GKEKCVHYWPTEEET-YGPFQIRIQDMKECPEYTVRQLTIQYQEER--RSVKHILFSAWPDHQTPESAGPLLRL 270
Cdd:cd14554    81 TKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARDGqsRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844122053 271 VAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHT 346
Cdd:cd14554   161 IGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 121-347 6.97e-62

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: 197.94  E-value: 6.97e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 121 SKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE- 199
Cdd:cd14630     5 NKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYH-RPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEv 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 200 GKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQ--EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVE-- 275
Cdd:cd14630    84 GRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKgyHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQVKfl 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844122053 276 ESPETaahpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 347
Cdd:cd14630   164 NPPDA----GPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 149-344 5.54e-61

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: 194.66  E-value: 5.54e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREG-KEKCVHYWPTEEE---TYGPFQIRIQD 224
Cdd:cd14557     1 YINASYIDGFKEPRK-YIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGnRNKCAQYWPSMEEgsrAFGDVVVKINE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 225 MKECPEYTVRQLTIQYQEERRS---VKHILFSAWPDHQTPESAGPLLRLVAEVEESpeTAAHPGPIVVHCSAGIGRTGCF 301
Cdd:cd14557    80 EKICPDYIIRKLNINNKKEKGSgreVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAF--NNFFSGPIVVHCSAGVGRTGTY 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1844122053 302 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14557   158 IGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 109-347 7.56e-61

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: 196.80  E-value: 7.56e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 109 VSPEDLDIPGHASKDRYKTILPNPQSRVCLgRAQSQEDG---DYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQ 185
Cdd:cd17667    17 ITAEHSNHPDNKHKNRYINILAYDHSRVKL-RPLPGKDSkhsDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 186 EEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMKECPEYTVRQLTIQY-------------QEERRSVKHI 250
Cdd:cd17667    95 QNTGIIVMITNLVEkGRRKCDQYWPTEnSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpkgRQNERTVIQY 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 251 LFSAWPDHQTPESAGPLLRLVAEveESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDR 330
Cdd:cd17667   175 HYTQWPDMGVPEYALPVLTFVRR--SSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQR 252

                         250
                  ....*....|....*..
gi 1844122053 331 GGMIQTAEQYQFLHHTL 347
Cdd:cd17667   253 NYLVQTEEQYIFIHDAL 269
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 148-342 6.43e-60

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


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 192.16  E-value: 6.43e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 148 DYINANY----IRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEET--YGPFQI 220
Cdd:cd14541     1 DYINANYvnmeIPGSGIVNR-YIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVErGRVKCHQYWPDLGETmqFGNLQI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 221 RIQDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHpgPIVVHCSAGIGRT 298
Cdd:cd14541    80 TCVSEEVTPSFAFREFILTNTNtgEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVE--PTVVHCSAGIGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1844122053 299 GCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 342
Cdd:cd14541   158 GVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRF 201
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 105-354 7.07e-60

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: 194.77  E-value: 7.07e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 105 PSNFVSPEDldipgHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKeKVYIATQGPMPNTVSDFWEMVW 184
Cdd:cd14604    48 PTATGEKEE-----NVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGP-KAYIATQGPLANTVIDFWRMIW 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 185 QEEVSLIVMLTQLRE-GKEKCVHYWPTEEE---TYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQT 260
Cdd:cd14604   122 EYNVAIIVMACREFEmGRKKCERYWPLYGEepmTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDV 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 261 PESAGPLLRLVAEVEESPETaaHPGPIVVHCSAGIGRTGCFIATRIGCQQLKA---RGEVDILGIVCQLRLDRGGMIQTA 337
Cdd:cd14604   202 PSSFDSILDMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTK 279

                         250
                  ....*....|....*...
gi 1844122053 338 EQYQFLHHTLA-LYAGQL 354
Cdd:cd14604   280 EQYELVHRAIAqLFEKQL 297
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 125-347 1.12e-59

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: 192.08  E-value: 1.12e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 125 YKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKE-K 203
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEeK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 204 CVHYWPTEE-ETYGPFQIRIQDMKECPEYTVRQLTIQYQ-----EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEES 277
Cdd:cd14620    80 CYQYWPDQGcWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSV 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 278 peTAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 347
Cdd:cd14620   160 --NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 149-344 1.17e-59

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: 191.07  E-value: 1.17e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDGkEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREG-KEKCVHYWPTEEETYGPFQIRIQDMKE 227
Cdd:cd14558     1 YINASFIDGYWG-PKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGdQEQCAQYWGDEKKTYGDIEVELKDTEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 228 CPEYTVRQLTIQY--QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEES-PETAAHPG---PIVVHCSAGIGRTGCF 301
Cdd:cd14558    80 SPTYTVRVFEITHlkRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKlPYKNSKHGrsvPIVVHCSDGSSRTGIF 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1844122053 302 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14558   160 CALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 149-345 1.29e-59

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: 191.10  E-value: 1.29e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDGkEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEE---TYGPFQIRIQD 224
Cdd:cd14542     1 YINANFIKGVSG-SKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEmGKKKCERYWPEEGEeqlQFGPFKISLEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 225 MKE-CPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESpeTAAHPGPIVVHCSAGIGRTGCFIA 303
Cdd:cd14542    80 EKRvGPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVPICVHCSAGCGRTGTICA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1844122053 304 TRIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQYQFLHH 345
Cdd:cd14542   158 IDYVWNLLKTGKipeEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 117-350 2.16e-59

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: 192.79  E-value: 2.16e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 117 PGHASKDRYKTILPNPQSRVCLGRAQSQEDG-DYINANYIR----GYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLI 191
Cdd:cd14606    16 PENKSKNRYKNILPFDHSRVILQGRDSNIPGsDYINANYVKnqllGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 192 VMLT-QLREGKEKCVHYWPTEEET--YGPFQIRIQDMKECPEYTVRQL---TIQYQEERRSVKHILFSAWPDHQTPESAG 265
Cdd:cd14606    96 VMTTrEVEKGRNKCVPYWPEVGMQraYGPYSVTNCGEHDTTEYKLRTLqvsPLDNGELIREIWHYQYLSWPDHGVPSEPG 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 266 PLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQYQF 342
Cdd:cd14606   176 GVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSGMVQTEAQYKF 255


                  ....*...
gi 1844122053 343 LHHTLALY 350
Cdd:cd14606   256 IYVAIAQF 263
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 149-344 4.15e-59

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: 189.88  E-value: 4.15e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEETYGPFQIRIQDMKE 227
Cdd:cd14632     1 YINANYIDGYH-RSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEvGRVKCSKYWPDDSDTYGDIKITLLKTET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 228 CPEYTVRQLTIQYQ--EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESpeTAAHPGPIVVHCSAGIGRTGCFIATR 305
Cdd:cd14632    80 LAEYSVRTFALERRgySARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKAS--TPPDAGPVVVHCSAGAGRTGCYIVLD 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1844122053 306 IGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14632   158 VMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIH 196
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 121-350 5.62e-59

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: 191.00  E-value: 5.62e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 121 SKDRYKTILPNPQSRVCLGRAQSQEDG-DYINANYI-------RGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIV 192
Cdd:cd14605     4 NKNRYKNILPFDHTRVVLHDGDPNEPVsDYINANIImpefetkCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 193 MLT-QLREGKEKCVHYWPTEE--ETYGpfQIRIQDMKECP--EYTVRQLTI----QYQEERrSVKHILFSAWPDHQTPES 263
Cdd:cd14605    84 MTTkEVERGKSKCVKYWPDEYalKEYG--VMRVRNVKESAahDYILRELKLskvgQGNTER-TVWQYHFRTWPDHGVPSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 264 AGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQY 340
Cdd:cd14605   161 PGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTEAQY 240

                         250
                  ....*....|
gi 1844122053 341 QFLHHTLALY 350
Cdd:cd14605   241 RFIYMAVQHY 250
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 96-347 7.92e-59

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: 191.84  E-value: 7.92e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053  96 QLEEEFLKI-PSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPN 174
Cdd:cd14625    23 KLSQEYESIdPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYR-KQNAYIATQGPLPE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 175 TVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMKECPEYTVRQLTIQYQ--EERRSVKHI 250
Cdd:cd14625   102 TFGDFWRMVWEQRSATVVMMTKLEEkSRIKCDQYWPSRgTETYGMIQVTLLDTIELATFCVRTFSLHKNgsSEKREVRQF 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 251 LFSAWPDHQTPESAGPLLRLVAEVEE-SPETAahpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLD 329
Cdd:cd14625   182 QFTAWPDHGVPEYPTPFLAFLRRVKTcNPPDA---GPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQ 258

                         250
                  ....*....|....*...
gi 1844122053 330 RGGMIQTAEQYQFLHHTL 347
Cdd:cd14625   259 RNYMVQTEDQYSFIHDAL 276
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 135-347 1.38e-58

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: 189.08  E-value: 1.38e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 135 RVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEE 213
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQ-RPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEvGRVKCYKYWPDDTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 214 TYGPFQIRIQDMKECPEYTVRQLTIQYQ--EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhpGPIVVHC 291
Cdd:cd14631    80 VYGDFKVTCVEMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSA--GPIVVHC 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1844122053 292 SAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 347
Cdd:cd14631   158 SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 97-354 1.58e-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: 191.48  E-value: 1.58e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053  97 LEEEFLKIPSN------FVSPedlDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQG 170
Cdd:cd14628    27 MELEFKRLASSkahtsrFISA---NLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYR-QQKAYIATQG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 171 PMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEET-YGPFQIRIQDMKECPEYTVRQLTIQYQE--ERRS 246
Cdd:cd14628   103 PLAETTEDFWRMLWEHNSTIVVMLTKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRT 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 247 VKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQL 326
Cdd:cd14628   183 VRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKML 262

                         250       260
                  ....*....|....*....|....*...
gi 1844122053 327 RLDRGGMIQTAEQYQFLHHTLALYAGQL 354
Cdd:cd14628   263 RTQRPAMVQTEDQYQFCYRAALEYLGSF 290
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 106-352 5.70e-58

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 189.94  E-value: 5.70e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 106 SNFVSPedlDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQ 185
Cdd:cd14627    43 SRFISA---NLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWE 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 186 EEVSLIVMLTQLRE-GKEKCVHYWPTEEET-YGPFQIRIQDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTP 261
Cdd:cd14627   119 NNSTIVVMLTKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRTVRQFQFTDWPEQGVP 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 262 ESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQ 341
Cdd:cd14627   199 KSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQ 278

                         250
                  ....*....|.
gi 1844122053 342 FLHHTLALYAG 352
Cdd:cd14627   279 FCYQAALEYLG 289
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 149-342 1.90e-57

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: 185.55  E-value: 1.90e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEE-TYGPFQIRIQDMK 226
Cdd:cd14552     1 YINASFIDGYRQKDA-YIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKErSQNKCAQYWPEDGSvSSGDITVELKDQT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 227 ECPEYTVRQ--LTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHpGPIVVHCSAGIGRTGCFIAT 304
Cdd:cd14552    80 DYEDYTLRDflVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGN-HPITVHCSAGAGRTGTFCAL 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1844122053 305 RIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 342
Cdd:cd14552   159 STVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEF 196
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 96-347 5.59e-57

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: 187.25  E-value: 5.59e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053  96 QLEEEFLKI-PSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPN 174
Cdd:cd14624    23 KFSQEYESIdPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYR-KQNAYIATQGALPE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 175 TVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMKECPEYTVRQLTI--QYQEERRSVKHI 250
Cdd:cd14624   102 TFGDFWRMIWEQRSATVVMMTKLEErSRVKCDQYWPSRgTETYGLIQVTLLDTVELATYCVRTFALykNGSSEKREVRQF 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 251 LFSAWPDHQTPESAGPLLRLVAEVEE-SPETAahpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLD 329
Cdd:cd14624   182 QFTAWPDHGVPEHPTPFLAFLRRVKTcNPPDA---GPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQ 258

                         250
                  ....*....|....*...
gi 1844122053 330 RGGMIQTAEQYQFLHHTL 347
Cdd:cd14624   259 RNYMVQTEDQYIFIHDAL 276
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 122-344 1.46e-56

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: 184.27  E-value: 1.46e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 122 KDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKeKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-G 200
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGP-RAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEmG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 201 KEKCVHYW--PTEEE-TYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEV--- 274
Cdd:cd14602    80 KKKCERYWaePGEMQlEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVrcy 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844122053 275 --EESPetaahpgPIVVHCSAGIGRTGCFIATRIGCQQLKAR---GEVDILGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14602   160 qeDDSV-------PICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYELVY 227
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 149-347 3.06e-56

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: 182.49  E-value: 3.06e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMK 226
Cdd:cd17668     1 YINANYVDGYN-KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEkGRRKCDQYWPADgSEEYGNFLVTQKSVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 227 ECPEYTVRQLTIQ-------YQEER---RSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhpGPIVVHCSAGIG 296
Cdd:cd17668    80 VLAYYTVRNFTLRntkikkgSQKGRpsgRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAV--GPVVVHCSAGVG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1844122053 297 RTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 347
Cdd:cd17668   158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 122-350 3.55e-56

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: 183.11  E-value: 3.55e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 122 KDRYKTILPNPQSRVCLGraqsqEDGDYINANYIRGYDGKEK-VYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREG 200
Cdd:cd14597     6 KNRYKNILPYDTTRVPLG-----DEGGYINASFIKMPVGDEEfVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 201 -KEKCVHYWPteeETYGP-------FQIRIQDMKECPEYTVRQLTIQ--YQEERRSVKHILFSAWPDHQTPESAGPLLRL 270
Cdd:cd14597    81 gKIKCQRYWP---EILGKttmvdnrLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTPSQPEQLLTF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 271 VAEVEESPETaahpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLaLY 350
Cdd:cd14597   158 ISYMRHIHKS----GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI-LY 232
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 122-347 9.09e-56

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: 183.71  E-value: 9.09e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 122 KDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-G 200
Cdd:cd14633    43 KNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYH-RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEvG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 201 KEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQ--EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEEsp 278
Cdd:cd14633   122 RVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS-- 199

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844122053 279 ETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 347
Cdd:cd14633   200 KSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 106-354 5.58e-55

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: 182.23  E-value: 5.58e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 106 SNFVSPedlDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQ 185
Cdd:cd14629    43 SRFISA---NLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWE 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 186 EEVSLIVMLTQLRE-GKEKCVHYWPTEEET-YGPFQIRIQDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTP 261
Cdd:cd14629   119 HNSTIVVMLTKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRTIRQFQFTDWPEQGVP 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 262 ESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQ 341
Cdd:cd14629   199 KTGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQ 278

                         250
                  ....*....|...
gi 1844122053 342 FLHHTLALYAGQL 354
Cdd:cd14629   279 LCYRAALEYLGSF 291
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 88-347 1.28e-54

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: 181.38  E-value: 1.28e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053  88 QRQPPSPKQLEEEFLKIPSNFV--SPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvY 165
Cdd:cd14621    19 RRMADDNKLFREEFNALPACPIqaTCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNK-F 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 166 IATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKE-KCVHYWPTEE-ETYGPFQIRIQDMKECPEYTVRQLTIQY--- 240
Cdd:cd14621    98 IAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKEcKCAQYWPDQGcWTYGNIRVSVEDVTVLVDYTVRKFCIQQvgd 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 241 ---QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEE-SPETAahpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGE 316
Cdd:cd14621   178 vtnKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNcNPQYA---GAIVVHCSAGVGRTGTFIVIDAMLDMMHAERK 254

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1844122053 317 VDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 347
Cdd:cd14621   255 VDVYGFVSRIRAQRCQMVQTDMQYVFIYQAL 285
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 149-344 2.46e-54

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: 177.41  E-value: 2.46e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMK 226
Cdd:cd14551     1 YINASYIDGYQEKNK-FIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKErKEKKCSQYWPDQgCWTYGNLRVRVEDTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 227 ECPEYTVRQLTIQYQ------EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESpeTAAHPGPIVVHCSAGIGRTGC 300
Cdd:cd14551    80 VLVDYTTRKFCIQKVnrgigeKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSA--NPPRAGPIVVHCSAGVGRTGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1844122053 301 FIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14551   158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 116-342 5.47e-54

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: 179.07  E-value: 5.47e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 116 IPGHASKDRYKTILPNPQSRVCLgraqSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLT 195
Cdd:cd14608    22 LPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRS-YILTQGPLPNTCGHFWEMVWEQKSRGVVMLN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 196 QLRE-GKEKCVHYWPTEEETYGPFQ---IRI----QDMKEcpEYTVRQLTIQ--YQEERRSVKHILFSAWPDHQTPESAG 265
Cdd:cd14608    97 RVMEkGSLKCAQYWPQKEEKEMIFEdtnLKLtlisEDIKS--YYTVRQLELEnlTTQETREILHFHYTTWPDFGVPESPA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 266 PLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIgC----QQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQ 341
Cdd:cd14608   175 SFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADT-ClllmDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLR 253


                  .
gi 1844122053 342 F 342
Cdd:cd14608   254 F 254
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 122-342 1.02e-53

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: 176.81  E-value: 1.02e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 122 KDRYKTILPNPQSRVclgRAQS-QEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE- 199
Cdd:cd14545     1 LNRYRDRDPYDHDRS---RVKLkQGDNDYINASLVEVEEAKRS-YILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEk 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 200 GKEKCVHYWPTEEET-----YGPFQIRIQDMKECPEYTVRQLTIQ--YQEERRSVKHILFSAWPDHQTPESAGPLLRLVA 272
Cdd:cd14545    77 GQIKCAQYWPQGEGNamifeDTGLKVTLLSEEDKSYYTVRTLELEnlKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844122053 273 EVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARG--EVDILGIVCQLRLDRGGMIQTAEQYQF 342
Cdd:cd14545   157 KVRESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 149-342 1.23e-53

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 175.71  E-value: 1.23e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDGKEK-VYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWP-TEEETY--GPFQIRIQ 223
Cdd:cd14596     1 YINASYITMPVGEEElFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVErGKVKCHRYWPeTLQEPMelENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 224 DMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETaahpGPIVVHCSAGIGRTGCF 301
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKEtgENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT----GPIVVHCSAGIGRAGVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1844122053 302 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 342
Cdd:cd14596   157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLF 197
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 123-344 3.27e-53

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: 175.48  E-value: 3.27e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 123 DRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GK 201
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNE-FIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEkGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 202 EKCVHYWPTEEETYGPF-QIRIQDMKE--CPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESp 278
Cdd:cd14616    80 IRCHQYWPEDNKPVTVFgDIVITKLMEdvQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRAS- 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844122053 279 eTAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14616   159 -RAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 148-344 1.94e-52

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: 172.50  E-value: 1.94e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 148 DYINANYIRGYDGKEkVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEE-TYGPFQIRIQDM 225
Cdd:cd14622     1 DYINASFIDGYRQKD-YFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQErEQEKCVQYWPSEGSvTHGEITIEIKND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 226 KECPEYTVRQLTIQYQEER--RSVKHILFSAWPDHQTPESAGPLLRLVAEVE-ESPETAAHPgpIVVHCSAGIGRTGCFI 302
Cdd:cd14622    80 TLLETISIRDFLVTYNQEKqtRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQkQQQQTGNHP--IVVHCSAGAGRTGTFI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1844122053 303 ATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14622   158 ALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 124-344 3.08e-52

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: 172.92  E-value: 3.08e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 124 RYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKE 202
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDS-YIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEErGQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 203 KCVHYWPTEEE-TYGPFQIRIQDMKECPEYTVRQLTIQYQEERRS--VKHILFSAWPDHQTPESAGPLLRLVAEVEESPE 279
Cdd:cd14623    80 KCAQYWPSDGSvSYGDITIELKKEEECESYTVRDLLVTNTRENKSrqIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQ 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844122053 280 TAAHpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14623   160 QSGN-HPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCY 223
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 149-351 3.12e-52

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: 172.64  E-value: 3.12e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIR-GYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-----EETYGPFQIR 221
Cdd:cd14540     1 YINASHITaTVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEgGREKCFRYWPTLggehdALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 222 IQDMKECPEYTVRQLTIQYQEER--RSVKHILFSAWPDHQTPESAGPLLRLVAEV--------EESPETAAHPgPIVVHC 291
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGqsRTVWHLQYTDWPDHGCPEDVSGFLDFLEEInsvrrhtnQDVAGHNRNP-PTLVHC 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 292 SAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLALYA 351
Cdd:cd14540   160 SAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 96-343 7.51e-52

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: 173.50  E-value: 7.51e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053  96 QLEEEFLKIPSNFVS----PEDLDipghasKDRYKTILPNPQSRVCLgraqsQEDGDYINANY----IRGYDGKEKvYIA 167
Cdd:cd14600    19 QFEQLYRKKPGLAITcaklPQNMD------KNRYKDVLPYDATRVVL-----QGNEDYINASYvnmeIPSANIVNK-YIA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 168 TQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEET--YGPFQIRIQDMKECPEYTVRQLTIQYQE-- 242
Cdd:cd14600    87 TQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTErGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQtg 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 243 ERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhpgPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGI 322
Cdd:cd14600   167 EERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENE---PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDI 243

                         250       260
                  ....*....|....*....|.
gi 1844122053 323 VCQLRLDRGGMIQTAEQYQFL 343
Cdd:cd14600   244 VRKMRDQRAMMVQTSSQYKFV 264
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 148-343 1.15e-51

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 170.90  E-value: 1.15e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 148 DYINANYIR---GYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVML-TQLREGKEKCVHYWP--TEEETYGPFQIR 221
Cdd:cd14601     1 DYINANYINmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLtTQVERGRVKCHQYWPepSGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 222 IQDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEEspETAAHPGPIVVHCSAGIGRTG 299
Cdd:cd14601    81 CHSEEGNPAYVFREMTLTNLEknESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRN--KRAGKDEPVVVHCSAGIGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1844122053 300 CFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 343
Cdd:cd14601   159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 202
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 149-344 6.10e-51

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: 168.74  E-value: 6.10e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDGKeKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWPTEEE-TYGPFQIRIQDMKE 227
Cdd:cd14556     1 YINAALLDSYKQP-AAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDEGSgTYGPIQVEFVSTTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 228 CPEYTVRQLTIQ----YQEERRSVKHILFSAWPDHQ-TPESAGPLLRLVAEVEESPETAAHpGPIVVHCSAGIGRTGCFI 302
Cdd:cd14556    80 DEDVISRIFRLQnttrPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGE-GPIVVHCLNGVGRSGVFC 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1844122053 303 ATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14556   159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 106-342 1.61e-50

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: 170.24  E-value: 1.61e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 106 SNFVSPEDLDIPghasKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQ 185
Cdd:cd14610    35 ATNVAQREENVQ----KNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 186 EEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIR-IQDMKECPEYTVRQLTIQ--YQEERRSVKHILFSAWPDHQT 260
Cdd:cd14610   111 SGCVVIVMLTPLAEnGVKQCYHYWPDEgSNLYHIYEVNlVSEHIWCEDFLVRSFYLKnlQTNETRTVTQFHFLSWNDQGV 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 261 PESAGPLLRLVAEVEESpeTAAHPGPIVVHCSAGIGRTGCFIATRIGCQQL-KARGEVDILGIVCQLRLDRGGMIQTAEQ 339
Cdd:cd14610   191 PASTRSLLDFRRKVNKC--YRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQ 268


                  ...
gi 1844122053 340 YQF 342
Cdd:cd14610   269 FEF 271
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 149-344 6.44e-50

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 166.02  E-value: 6.44e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVML-TQLREGKEKCVHYWPTE---EETYGPFQIRIQD 224
Cdd:cd14539     1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLvSEQENEKQKVHRYWPTErgqALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 225 MKECPEYTVRQLTIQYQEER--RSVKHILFSAWPDHQTPESAGPLLRLVAEVEE-----SPETAahpgPIVVHCSAGIGR 297
Cdd:cd14539    81 VRTTPTHVERIISIQHKDTRlsRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShylqqRSLQT----PIVVHCSSGVGR 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1844122053 298 TGCFIATRIGCQQLKA-RGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14539   157 TGAFCLLYAAVQEIEAgNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 149-342 1.02e-48

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: 163.00  E-value: 1.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIR-IQDM 225
Cdd:cd14546     1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQEnGVKQCARYWPEEgSEVYHIYEVHlVSEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 226 KECPEYTVRQL---TIQYQEErRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPEtaAHPGPIVVHCSAGIGRTGCFI 302
Cdd:cd14546    81 IWCDDYLVRSFylkNLQTSET-RTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYR--GRSCPIVVHCSDGAGRTGTYI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1844122053 303 ATRIGCQQL-KARGEVDILGIVCQLRLDRGGMIQTAEQYQF 342
Cdd:cd14546   158 LIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEF 198
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 149-342 1.37e-46

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: 157.63  E-value: 1.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYD-GKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREG--KEKCVHYWPTEE---ETYGPFQIRI 222
Cdd:cd17658     1 YINASLVETPAsESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNysTAKCADYFPAEEnesREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 223 QDMKeCPEY--TVRQLTIQY---QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAahpGPIVVHCSAGIGR 297
Cdd:cd17658    81 KKLK-HSQHsiTLRVLEVQYiesEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSA---GPIVVHCSAGIGR 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1844122053 298 TGCFIAT-----RIGCQQLKArgeVDILGIVCQLRLDRGGMIQTAEQYQF 342
Cdd:cd17658   157 TGAYCTIhntirRILEGDMSA---VDLSKTVRKFRSQRIGMVQTQDQYIF 203
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 117-342 4.26e-46

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: 157.82  E-value: 4.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 117 PGHASKDRYKTILPNPQSRVCLGRAqsqeDGDYINANYIRgYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQ 196
Cdd:cd14607    22 PENRNRNRYRDVSPYDHSRVKLQNT----ENDYINASLVV-IEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 197 LRE-GKEKCVHYWPTEEETYGPFQ-----IRI--QDMKEcpEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGP 266
Cdd:cd14607    97 IVEkDSVKCAQYWPTDEEEVLSFKetgfsVKLlsEDVKS--YYTVHLLQLENINsgETRTISHFHYTTWPDFGVPESPAS 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844122053 267 LLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCF--IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 342
Cdd:cd14607   175 FLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFslVDTCLVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLRF 252
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 116-347 7.46e-45

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: 155.54  E-value: 7.46e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 116 IPGHASKDRYKTILPNPQSRVCLGRAQSQEDGdYINANYIR-GYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVML 194
Cdd:cd14599    35 LPENAERNRIREVVPYEENRVELVPTKENNTG-YINASHIKvTVGGEEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 195 TQLRE-GKEKCVHYWPT-----EEETYGPFQIRIQDMKECPEYTVRQLTIQY--QEERRSVKHILFSAWPDHQTPESAGP 266
Cdd:cd14599   114 TAEEEgGRSKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPDHGCPEEVQG 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 267 LLRLVAEVEE---------SPETAAHPgPIVVHCSAGIGRTGCFIATR--IGCqqLKARGEVDILGIVCQLRLDRGGMIQ 335
Cdd:cd14599   194 FLSYLEEIQSvrrhtnsmlDSTKNCNP-PIVVHCSAGVGRTGVVILTElmIGC--LEHNEKVEVPVMLRHLREQRMFMIQ 270

                         250
                  ....*....|..
gi 1844122053 336 TAEQYQFLHHTL 347
Cdd:cd14599   271 TIAQYKFVYQVL 282
PHA02738 PHA02738
hypothetical protein; Provisional
 123-350 1.01e-44

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 156.24  E-value: 1.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 123 DRYKTILPNPQSRVCLGRAQSQedGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GK 201
Cdd:PHA02738   53 NRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKK-FICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEnGR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 202 EKCVHYWPTEEET---YGPFQIRIQDMKECPEYTVRQLTI-QYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEES 277
Cdd:PHA02738  130 EKCFPYWSDVEQGsirFGKFKITTTQVETHPHYVKSTLLLtDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQC 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 278 PETAA-----------HPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHT 346
Cdd:PHA02738  210 QKELAqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRA 289


                  ....
gi 1844122053 347 LALY 350
Cdd:PHA02738  290 VKRY 293
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
95-343 2.86e-44

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 153.71  E-value: 2.86e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053  95 KQLEEEFLKIPSNFVSPEDLDIPGHASKDRYKTILPNPQSRVclgraqsQEDGDYINANYIRGYDGKekVYIATQGPMPN 174
Cdd:COG5599    18 SRLSTLTNELAPSHNDPQYLQNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIGNH--RYIATQYPLEE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 175 TVSDFWEMVWQEEVSLIVMLTQLREGKE---KCVHYWPTEEEtYGPFQIR--------IQDMKECPEYTVRQLtiQYQEE 243
Cdd:COG5599    89 QLEDFFQMLFDNNTPVLVVLASDDEISKpkvKMPVYFRQDGE-YGKYEVSseltesiqLRDGIEARTYVLTIK--GTGQK 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 244 RRSVKHILFSAWPDHQTPeSAGPLLRLVAEVEESPETAAHP-GPIVVHCSAGIGRTGCFIATRIGCQQLKARGE--VDIL 320
Cdd:COG5599   166 KIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKEKIKDPDkLLPVVHCRAGVGRTGTLIACLALSKSINALVQitLSVE 244

                         250       260
                  ....*....|....*....|....
gi 1844122053 321 GIVCQLRLDRG-GMIQTAEQYQFL 343
Cdd:COG5599   245 EIVIDMRTSRNgGMVQTSEQLDVL 268
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 118-342 4.17e-44

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: 153.65  E-value: 4.17e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 118 GHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQL 197
Cdd:cd14609    41 ANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 198 RE-GKEKCVHYWPTEEET-YGPFQIR-IQDMKECPEYTVRQL---TIQYQEErRSVKHILFSAWPDHQTPESAGPLLRLV 271
Cdd:cd14609   121 VEdGVKQCDRYWPDEGSSlYHIYEVNlVSEHIWCEDFLVRSFylkNVQTQET-RTLTQFHFLSWPAEGIPSSTRPLLDFR 199

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844122053 272 AEVEESpeTAAHPGPIVVHCSAGIGRTGCFIATRIGCQQL-KARGEVDILGIVCQLRLDRGGMIQTAEQYQF 342
Cdd:cd14609   200 RKVNKC--YRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGMVRTKDQFEF 269
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 149-347 3.77e-42

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: 146.66  E-value: 3.77e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIR-GYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWP-----TEEETYGPFQIR 221
Cdd:cd14598     1 YINASHIKvTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEgGREKSFRYWPrlgsrHNTVTYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 222 IQDMKECPEYTVRQLTIQY--QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVE-------ESPETAAHPGPIVVHCS 292
Cdd:cd14598    81 TRFRTDSGCYATTGLKIKHllTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQsvrrhtnSTIDPKSPNPPVLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1844122053 293 AGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 347
Cdd:cd14598   161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 74-347 1.76e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 145.17  E-value: 1.76e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053  74 FLRTAGHPlTRWALQRQPPSpkqleeEFLKIP-----SNFVSPEDLdipghaSKDRYKTILPNPQSRVCLGRAQS----- 143
Cdd:PHA02746   14 FFDKTNHA-KFCEFVLLEHA------EVMDIPirgttNHFLKKENL------KKNRFHDIPCWDHSRVVINAHESlkmfd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 144 ------------QEDGD--YINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWP 209
Cdd:PHA02746   81 vgdsdgkkievtSEDNAenYIHANFVDGFKEANK-FICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 210 TEEE---TYGPFQIRIQDMKECPEYTVRQLTI--QYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEE-------- 276
Cdd:PHA02746  160 KEEDselAFGRFVAKILDIIEELSFTKTRLMItdKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikq 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844122053 277 SPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 347
Cdd:PHA02746  240 ADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 121-351 1.82e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 144.37  E-value: 1.82e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 121 SKDRYKTILPNPQSRVCLgraqSQEDG--DYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLR 198
Cdd:PHA02742   54 KKCRYPDAPCFDRNRVIL----KIEDGgdDFINASYVDGHNAKGR-FICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 199 E-GKEKCVHYWPTEEE---TYGPFQIRIQDMKECPEYTVRQLTIQYQEERRS--VKHILFSAWPDHQTPESAGPLLRLV- 271
Cdd:PHA02742  129 EdGKEACYPYWMPHERgkaTHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASldIKHFAYEDWPHGGLPRDPNKFLDFVl 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 272 --------AEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 343
Cdd:PHA02742  209 avreadlkADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFC 288


                  ....*...
gi 1844122053 344 HHTLALYA 351
Cdd:PHA02742  289 YFIVLIFA 296
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 101-344 4.23e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 143.99  E-value: 4.23e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 101 FLKIPSNFVSPEDldipghASKDRYKTILPNPQSRVCLgRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFW 180
Cdd:PHA02747   39 FDGLIANFEKPEN------QPKNRYWDIPCWDHNRVIL-DSGGGSTSDYIHANWIDGFE-DDKKFIATQGPFAETCADFW 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 181 EMVWQEEVSLIVMLTQLR--EGKEKCVHYW-PTEEETYGPFQIRIQDMKEC--PEY--TVRQLTIQYQEERRSVKHILFS 253
Cdd:PHA02747  111 KAVWQEHCSIIVMLTPTKgtNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSvrAKYilTLIEITDKILKDSRKISHFQCS 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 254 AWPDHQTPESAGPLLRLVAEVEESPETA--------AHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQ 325
Cdd:PHA02747  191 EWFEDETPSDHPDFIKFIKIIDINRKKSgklfnpkdALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEK 270

                         250
                  ....*....|....*....
gi 1844122053 326 LRLDRGGMIQTAEQYQFLH 344
Cdd:PHA02747  271 IREQRHAGIMNFDDYLFIQ 289
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
246-348 3.95e-38

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 132.10  E-value: 3.95e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053  246 SVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKAR-GEVDILGIVC 324
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....
gi 1844122053  325 QLRLDRGGMIQTAEQYQFLHHTLA 348
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALL 104
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 246-348 3.95e-38

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: 132.10  E-value: 3.95e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053  246 SVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKAR-GEVDILGIVC 324
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....
gi 1844122053  325 QLRLDRGGMIQTAEQYQFLHHTLA 348
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALL 104
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 149-344 9.77e-32

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 118.59  E-value: 9.77e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLrEGKEKCVHYWPTEEE-TYGPFQIRI--QDM 225
Cdd:cd14634     1 YINAALMDSHK-QPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM-DAAQLCMQYWPEKTScCYGPIQVEFvsADI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 226 KEcpEYTVRQLTI----QYQEERRSVKHILFSAWPDHQ-TPESAGPLLRLVAEVEESPETA-AHPGPIVVHCSAGIGRTG 299
Cdd:cd14634    79 DE--DIISRIFRIcnmaRPQDGYRIVQHLQYIGWPAYRdTPPSKRSILKVVRRLEKWQEQYdGREGRTVVHCLNGGGRSG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1844122053 300 CFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14634   157 TFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVY 201
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 149-343 1.56e-31

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: 117.81  E-value: 1.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLrEGKEKCVHYWPTEEET--YGPFQIRIQDMK 226
Cdd:cd14550     1 YINASYLQGYR-RSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNEDEPIYWPTKEKPleCETFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 227 ECP-----EYTVRQLTIQYQEERR--SVKHILFSAWPDHQTP-ESAGPLLRLVAEveespETAAHPGPIVVH-----CSA 293
Cdd:cd14550    79 HSClsneiRLIVRDFILESTQDDYvlEVRQFQCPSWPNPCSPiHTVFELINTVQE-----WAQQRDGPIVVHdryggVQA 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1844122053 294 GigrTGCFIATRigCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 343
Cdd:cd14550   154 A---TFCALTTL--HQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 149-342 9.93e-28

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: 108.07  E-value: 9.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEK--CVHYWPTE-EETYGPFQIRIQDM 225
Cdd:cd14637     1 YINAALTDSYT-RSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwpCLQYWPEPgLQQYGPMEVEFVSG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 226 KECPEYTVRQLTIQ----YQEERRSVKHILFSAW-PDHQTPESAGPLLRLVAEVEESPETAAHpGPIVVHCSAGIGRTGC 300
Cdd:cd14637    80 SADEDIVTRLFRVQnitrLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGE-GRTVVHCLNGGGRSGT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1844122053 301 FIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 342
Cdd:cd14637   159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRF 200
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 149-344 6.03e-27

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: 105.88  E-value: 6.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLrEGKEKCVHYWPTEEE-TYGPFQIRIQDMKE 227
Cdd:cd14636     1 YINAALMDSYR-QPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV-DLAQGCPQYWPEEGMlRYGPIQVECMSCSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 228 CPEYTVRQLTI----QYQEERRSVKHILFSAWPDH-QTPESAGPLLRLVAEVEE-SPETAAHPGPIVVHCSAGIGRTGCF 301
Cdd:cd14636    79 DCDVISRIFRIcnltRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKwQEECDEGEGRTIIHCLNGGGRSGMF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1844122053 302 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14636   159 CAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 149-347 7.20e-25

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: 100.07  E-value: 7.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKE- 227
Cdd:cd17669     1 YINASYIMGYYQSNE-FIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEe 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 228 --CPEyTVRQLTIQ------YQEER-RSVKHILFSAWPDHQTPESAgpLLRLVAEVEEspETAAHPGPIVVHCSAGIGRT 298
Cdd:cd17669    80 hkCLS-NEEKLIIQdfileaTQDDYvLEVRHFQCPKWPNPDSPISK--TFELISIIKE--EAANRDGPMIVHDEHGGVTA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1844122053 299 GCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 347
Cdd:cd17669   155 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 149-344 7.61e-25

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: 100.15  E-value: 7.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLrEGKEKCVHYWPTEE-ETYGPFQIRIQDMKE 227
Cdd:cd14635     1 YINAALMDSYK-QPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV-DPAQLCPQYWPENGvHRHGPIQVEFVSADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 228 CPEYTVRQLTI----QYQEERRSVKHILFSAWPDHQ-TPESAGPLLRLVAEVEE-SPETAAHPGPIVVHCSAGIGRTGCF 301
Cdd:cd14635    79 EEDIISRIFRIynaaRPQDGYRMVQQFQFLGWPMYRdTPVSKRSFLKLIRQVDKwQEEYNGGEGRTVVHCLNGGGRSGTF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1844122053 302 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14635   159 CAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 149-347 1.20e-24

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: 99.75  E-value: 1.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 149 YINANYIRGYdGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWPTEEETYG--PFQIR-IQDM 225
Cdd:cd17670     1 YINASYIMGY-YRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNceAFTVTlISKD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 226 KEC----PEYTVRQLTIQYQEERR--SVKHILFSAWPDHQTPESAgpLLRLVAEVEEspETAAHPGPIVVHCSAGIGRTG 299
Cdd:cd17670    80 RLClsneEQIIIHDFILEATQDDYvlEVRHFQCPKWPNPDAPISS--TFELINVIKE--EALTRDGPTIVHDEFGAVSAG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1844122053 300 CFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 347
Cdd:cd17670   156 TLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 132-350 4.98e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 86.17  E-value: 4.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 132 PQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREgKEKCVHYWPTE 211
Cdd:PHA02740   61 HITRLLHRRIKLFNDEKVLDARFVDGYDFEQK-FICIINLCEDACDKFLQALSDNKVQIIVLISRHAD-KKCFNQFWSLK 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 212 E---ETYGPFQIRIQDMKECPEY--TVRQLTIQYQEERRsVKHILFSAWPDHQTPESAGPLLRLVAEVE------ESPET 280
Cdd:PHA02740  139 EgcvITSDKFQIETLEIIIKPHFnlTLLSLTDKFGQAQK-ISHFQYTAWPADGFSHDPDAFIDFFCNIDdlcadlEKHKA 217

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 281 AAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLALY 350
Cdd:PHA02740  218 DGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAY 287
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 128-343 1.48e-17

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: 80.52  E-value: 1.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 128 ILPNPQSRVclgraqSQEDGDYINANYIRgyDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHY 207
Cdd:cd14559     2 RFTNIQTRV------STPVGKNLNANRVQ--IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 208 WPTEEETYGpfQIRIQDMKECPEYTVR-------QLTIQYQEERRSVKHILFSAWPDHqTPESAGPLLRLVAEVEESPET 280
Cdd:cd14559    74 YFRQSGTYG--SVTVKSKKTGKDELVDglkadmyNLKITDGNKTITIPVVHVTNWPDH-TAISSEGLKELADLVNKSAEE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844122053 281 ------AAHPGPI--------VVHCSAGIGRTGCFIATRigcQQLKARGEVDILGIVCQLRLDRGG-MIQTAEQYQFL 343
Cdd:cd14559   151 krnfykSKGSSAIndknkllpVIHCRAGVGRTGQLAAAM---ELNKSPNNLSVEDIVSDMRTSRNGkMVQKDEQLDTL 225
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 152-345 2.70e-14

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: 68.53  E-value: 2.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 152 ANYIRGydgkeKVYIATQGPMPNtVSDFWEMVWQEEVSLIVMLTqlregkekcvhywpteeetygpfqiriqdmkecpey 231
Cdd:cd14494     1 FNWIDP-----LRLIAGALPLSP-LEADSRFLKQLGVTTIVDLT------------------------------------ 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 232 tvrqltiqyqeerrsvkhilfsawpdhqtpesaGPLLRLVAEVEESPETaaHPGPIVVHCSAGIGRTGCFIATRIGCQQL 311
Cdd:cd14494    39 ---------------------------------LAMVDRFLEVLDQAEK--PGEPVLVHCKAGVGRTGTLVACYLVLLGG 83

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1844122053 312 KargevDILGIVCQLRLDRGGMI-QTAEQYQFLHH 345
Cdd:cd14494    84 M-----SAEEAVRIVRLIRPGGIpQTIEQLDFLIK 113
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 230-344 7.45e-09

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: 54.19  E-value: 7.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 230 EYTVRQLTIQYQEERRSVKHILFsawPDHQTPESAGPLLRLVAEVEESPETAAHpgpIVVHCSAGIGRTGcFIATRIgCQ 309
Cdd:cd14505    58 ELGVPDLLEQYQQAGITWHHLPI---PDGGVPSDIAQWQELLEELLSALENGKK---VLIHCKGGLGRTG-LIAACL-LL 129

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1844122053 310 QLKARGEVDilGIVCQLRLDRGGMIQTAEQYQFLH 344
Cdd:cd14505   130 ELGDTLDPE--QAIAAVRALRPGAIQTPKQENFLH 162
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
255-345 4.19e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 48.81  E-value: 4.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 255 WPDHQTPESAgPLLRLVAEVEESpetAAHPGPIVVHCSAGIGRTGCFIAtrigcQQLKARGeVDILGIVCQLRLDRGGMI 334
Cdd:COG2453    55 IPDFGAPDDE-QLQEAVDFIDEA---LREGKKVLVHCRGGIGRTGTVAA-----AYLVLLG-LSAEEALARVRAARPGAV 124

                          90
                  ....*....|.
gi 1844122053 335 QTAEQYQFLHH 345
Cdd:COG2453   125 ETPAQRAFLER 135
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 260-343 5.10e-06

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: 45.73  E-value: 5.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 260 TPESAGPLLRLVAEVEESPetaAHPGPIVVHCSAGIGRTGCFIAtrigCQQLKARGEVDILGIVcQLRLDRGGMIQTAEQ 339
Cdd:cd14504    61 TPPTLEQIDEFLDIVEEAN---AKNEAVLVHCLAGKGRTGTMLA----CYLVKTGKISAVDAIN-EIRRIRPGSIETSEQ 132


                  ....
gi 1844122053 340 YQFL 343
Cdd:cd14504   133 EKFV 136
PRK15375 PRK15375
type III secretion system effector GTPase-activating protein SptP;
95-340 1.13e-05

type III secretion system effector GTPase-activating protein SptP;


Pssm-ID: 185273 [Multi-domain]  Cd Length: 535  Bit Score: 47.10  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053  95 KQLEEEFLKIPSNFVSPEDLDIPGHA-SKDRYKTILPNPQSRVCLgraqsqEDGDYINANYIRgYDGKEkvyIATQGPMP 173
Cdd:PRK15375  273 KNVTAELEKIEAGAPMPQTMSGPTLGlARFAVSSIPINQQTQVKL------SDGMPVPVNTLT-FDGKP---VALAGSYP 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 174 NTVSDFWE----MVWQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEY-TVRQLTIQYQ--EERRS 246
Cdd:PRK15375  343 KNTPDALEahmkMLLEKECSCLVVLTSEDQMQAKQLPPYFRGSYTFGEVHTNSQKVSSASQGeAIDQYNMQLScgEKRYT 422

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 247 VKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhPG--------PIvVHCSAGIGRTGCFIATRIgcqqLKARGEVD 318
Cdd:PRK15375  423 IPVLHVKNWPDHQPLPSTDQLEYLADRVKNSNQNGA-PGrsssdkhlPM-IHCLGGVGRTGTMAAALV----LKDNPHSN 496

                         250       260
                  ....*....|....*....|...
gi 1844122053 319 ILGIVCQLRLDRGG-MIQTAEQY 340
Cdd:PRK15375  497 LEQVRADFRNSRNNrMLEDASQF 519
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 244-344 7.72e-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: 43.11  E-value: 7.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 244 RRSVKHILFsAWPDHQTPeSAGPLLRLVAEVEESPEtaaHPGPIVVHCSAGIGRTGCFIA------TRIGCQQLkargev 317
Cdd:cd14506    74 RAGIYFYNF-GWKDYGVP-SLTTILDIVKVMAFALQ---EGGKVAVHCHAGLGRTGVLIAcylvyaLRMSADQA------ 142

                          90       100
                  ....*....|....*....|....*..
gi 1844122053 318 dILGIvcqlRLDRGGMIQTAEQYQFLH 344
Cdd:cd14506   143 -IRLV----RSKRPNSIQTRGQVLCVR 164
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 282-303 1.22e-04

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: 42.05  E-value: 1.22e-04
                          10        20
                  ....*....|....*....|..
gi 1844122053 282 AHPGPIVVHCSAGIGRTGCFIA 303
Cdd:cd14499   107 NEKGAIAVHCKAGLGRTGTLIA 128
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 255-303 1.36e-03

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 39.10  E-value: 1.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1844122053 255 WPDHQTPeSAGPLLRLVAEVE----ESPETAAhpgpiVVHCSAGIGRTGCFIA 303
Cdd:cd14497    68 FPDHHPP-PLGLLLEIVDDIDswlsEDPNNVA-----VVHCKAGKGRTGTVIC 114
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 197-298 6.85e-03

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


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 36.91  E-value: 6.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844122053 197 LREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAwPDHQTPEsAGPLLRLVAEVEE 276
Cdd:pfam14566  51 LAEAKKNGGRVLVHDETEDGIGVLTVVDVWESDVQTPEEVYERLKAEGPGVDYRRIPI-TDEKAPL-EEDFDALISIVKD 128

                          90       100
                  ....*....|....*....|..
gi 1844122053 277 SPETAAhpgpIVVHCSAGIGRT 298
Cdd:pfam14566 129 APEDTA----LVFNCQMGRGRT 146
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 249-303 7.72e-03

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 36.58  E-value: 7.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1844122053 249 HILFSAW-PDHQTPESAgplLRLVAeveespeTAAHPGPIVVHCSAGIGRTGCFIA 303
Cdd:cd14529    63 NLPLSATrPTESDVQSF---LLIMD-------LKLAPGPVLIHCKHGKDRTGLVSA 108
 
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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