NCBI Conserved Domain Search

Conserved domains on [gi|20141721|sp|P35236|]

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RecName: Full=Tyrosine-protein phosphatase non-receptor type 7; AltName: Full=Hematopoietic protein-tyrosine phosphatase; Short=HEPTP; AltName: Full=Protein-tyrosine phosphatase LC-PTP

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 20141721 105 PSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQ-EDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMV 183
Cdd:cd14612   1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 184 WQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPES 263
Cdd:cd14612  81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 264 AGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 343
Cdd:cd14612 161 AGPLLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                ....*..
gi 20141721 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

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 20141721 105 PSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQ-EDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMV 183
Cdd:cd14612   1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 184 WQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPES 263
Cdd:cd14612  81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 264 AGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 343
Cdd:cd14612 161 AGPLLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                ....*..
gi 20141721 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 20141721     96 QLEEEFLKIPSNFVSPEDLDI---PGHASKDRYKTILPNPQSRVCLGRAQSqEDGDYINANYIRGYDGKeKVYIATQGPM 172
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGP-KAYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721    173 PNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEE---ETYGPFQIRIQDMKECPEYTVRQLTIQY--QEERRS 246
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEkGREKCAQYWPDEEgepLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSETRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721    247 VKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQL 326
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTST--GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKEL 236

                          250       260
                   ....*....|....*....|..
gi 20141721    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 20141721   119 HASKDRYKTILPNPQSRVCLGRaqSQEDGDYINANYIRGYdGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLR 198
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTG--DPGPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721   199 E-GKEKCVHYWPTEEE---TYGPFQIRIQDMKE-CPEYTVRQLTIQY--QEERRSVKHILFSAWPDHQTPESAGPLLRLV 271
Cdd:pfam00102  78 EkGREKCAQYWPEEEGeslEYGDFTVTLKKEKEdEKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20141721   272 AEVEESPETAAHpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLA 348
Cdd:pfam00102 158 RKVRKSSLDGRS-GPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233

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 20141721  123 DRYKTILPNPQSRVCLGRAQSQedGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GK 201
Cdd:PHA02738  53 NRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKK-FICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEnGR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721  202 EKCVHYWPTEEET---YGPFQIRIQDMKECPEYTVRQLTI-QYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEES 277
Cdd:PHA02738 130 EKCFPYWSDVEQGsirFGKFKITTTQVETHPHYVKSTLLLtDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQC 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721  278 PETAA-----------HPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHT 346
Cdd:PHA02738 210 QKELAqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRA 289


                 ....
gi 20141721  347 LALY 350
Cdd:PHA02738 290 VKRY 293

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 20141721  95 KQLEEEFLKIPSNFVSPEDLDIPGHASKDRYKTILPNPQSRVclgraqsQEDGDYINANYIRGYDGKekVYIATQGPMPN 174
Cdd:COG5599  18 SRLSTLTNELAPSHNDPQYLQNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIGNH--RYIATQYPLEE 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 175 TVSDFWEMVWQEEVSLIVMLTQLREGKE---KCVHYWPTEEEtYGPFQIR--------IQDMKECPEYTVRQLtiQYQEE 243
Cdd:COG5599  89 QLEDFFQMLFDNNTPVLVVLASDDEISKpkvKMPVYFRQDGE-YGKYEVSseltesiqLRDGIEARTYVLTIK--GTGQK 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 244 RRSVKHILFSAWPDHQTPeSAGPLLRLVAEVEESPETAAHP-GPIVVHCSAGIGRTGCFIATRIGCQQLKARGE--VDIL 320
Cdd:COG5599 166 KIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKEKIKDPDkLLPVVHCRAGVGRTGTLIACLALSKSINALVQitLSVE 244

                       250       260
                ....*....|....*....|....
gi 20141721 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

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 20141721 105 PSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQ-EDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMV 183
Cdd:cd14612   1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 184 WQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPES 263
Cdd:cd14612  81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 264 AGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 343
Cdd:cd14612 161 AGPLLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                ....*..
gi 20141721 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 20141721 123 DRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKE 202
Cdd:cd14547   1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 203 KCVHYWPTEE-ETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETA 281
Cdd:cd14547  81 KCAQYWPEEEnETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEARQTE 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20141721 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 20141721  97 LEEEFLKIPSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLgRAQSQED--GDYINANYIRGYDGKEKVYIATQGPMPN 174
Cdd:cd14613   3 LQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCL-TSPDQDDplSSYINANYIRGYGGEEKVYIATQGPTVN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 175 TVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSA 254
Cdd:cd14613  82 TVGDFWRMVWQERSPIIVMITNIEEMNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTS 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 255 WPDHQTPESAGPLLRLVAEVEESPETA-AHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGM 333
Cdd:cd14613 162 WPDQKTPDNAPPLLQLVQEVEEARQQAePNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGM 241

                       250
                ....*....|....*..
gi 20141721 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 20141721 121 SKDRYKTILPNPQSRVCLGRAQSQED-GDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE 199
Cdd:cd14611   1 TKNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 200 GKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPE 279
Cdd:cd14611  81 KNEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRL 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20141721 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 20141721     96 QLEEEFLKIPSNFVSPEDLDI---PGHASKDRYKTILPNPQSRVCLGRAQSqEDGDYINANYIRGYDGKeKVYIATQGPM 172
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGP-KAYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721    173 PNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEE---ETYGPFQIRIQDMKECPEYTVRQLTIQY--QEERRS 246
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEkGREKCAQYWPDEEgepLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSETRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721    247 VKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQL 326
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTST--GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKEL 236

                          250       260
                   ....*....|....*....|..
gi 20141721    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 20141721   119 HASKDRYKTILPNPQSRVCLGRaqSQEDGDYINANYIRGYdGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLR 198
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTG--DPGPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721   199 E-GKEKCVHYWPTEEE---TYGPFQIRIQDMKE-CPEYTVRQLTIQY--QEERRSVKHILFSAWPDHQTPESAGPLLRLV 271
Cdd:pfam00102  78 EkGREKCAQYWPEEEGeslEYGDFTVTLKKEKEdEKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20141721   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 20141721 149 YINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEE---TYGPFQIRIQD 224
Cdd:cd00047   1 YINASYIDGYRGPKE-YIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEkGREKCERYWPEEGGkplEYGDITVTLVS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 225 MKECPEYTVRQLTIQYQ--EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPEtaAHPGPIVVHCSAGIGRTGCFI 302
Cdd:cd00047  80 EEELSDYTIRTLELSPKgcSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEAR--KPNGPIVVHCSAGVGRTGTFI 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 20141721 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 20141721 122 KDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-G 200
Cdd:cd14553   6 KNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEErS 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 201 KEKCVHYWPTE-EETYGPFQIRIQDMKECPEYTVRQLTI--QYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEes 277
Cdd:cd14553  85 RVKCDQYWPTRgTETYGLIQVTLLDTVELATYTVRTFALhkNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK-- 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20141721 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 20141721 124 RYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKE 202
Cdd:cd14548   1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPRE-FIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEkGRV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 203 KCVHYWP--TEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEEspET 280
Cdd:cd14548  80 KCDHYWPfdQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD--YI 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20141721 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 20141721 117 PGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKeKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQ 196
Cdd:cd14543  27 PANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQK-NAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTR 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 197 LRE-GKEKCVHYWPTEEET---YGPFQIRIQDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGPLLRL 270
Cdd:cd14543 106 VVErGRVKCGQYWPLEEGSslrYGDLTVTNLSVENKEHYKKTTLEIHNTEtdESRQVTHFQFTSWPDFGVPSSAAALLDF 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 271 VAEVEE---------SPETAAHPG--PIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQ 339
Cdd:cd14543 186 LGEVRQqqalavkamGDRWKGHPPgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQ 265


                ....*
gi 20141721 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 20141721 149 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMK 226
Cdd:cd14549   1 YINANYVDGYN-KARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVErGRRKCDQYWPKEgTETYGNIQVTLLSTE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 227 ECPEYTVRQLTIQY--------QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVeespeTAAHP---GPIVVHCSAGI 295
Cdd:cd14549  80 VLATYTVRTFSLKNlklkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKS-----SAANPpgaGPIVVHCSAGV 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 20141721 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 20141721 120 ASKDRYKTILPNPQSRVCLGRAQSQEDG-DYINANYIR------GYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIV 192
Cdd:cd14544   2 KGKNRYKNILPFDHTRVILKDRDPNVPGsDYINANYIRnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVIV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 193 MLT-QLREGKEKCVHYWPTEEET--YGPFQIRIQDMKECPEYTVRQLTIQYQEER---RSVKHILFSAWPDHQTPESAGP 266
Cdd:cd14544  82 MTTkEVERGKNKCVRYWPDEGMQkqYGPYRVQNVSEHDTTDYTLRELQVSKLDQGdpiREIWHYQYLSWPDHGVPSDPGG 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 267 LLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQYQFL 343
Cdd:cd14544 162 VLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQYKFI 241


                ....*..
gi 20141721 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 20141721 109 VSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEV 188
Cdd:cd14614   2 IPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 189 SLIVMLTQLREGKE-KCVHYWPTEEE--TYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTP--ES 263
Cdd:cd14614  81 QIIVMLTQCNEKRRvKCDHYWPFTEEpvAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPtaNA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 264 AGPLLRLVAEVEEspETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 343
Cdd:cd14614 161 AESILQFVQMVRQ--QAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFI 238


                ....*.
gi 20141721 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 20141721 122 KDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGkEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVM-LTQLREG 200
Cdd:cd14603  33 KNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDG-SRAYIATQGPLSHTVLDFWRMIWQYGVKVILMaCREIEMG 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 201 KEKCVHYWPTEEET--YGPFQI-RIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEEs 277
Cdd:cd14603 112 KKKCERYWAQEQEPlqTGPFTItLVKEKRLNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARR- 190

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20141721 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 20141721 149 YINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEET--YGPFQIRIQDM 225
Cdd:cd18533   1 YINASYITLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVEnGREKCDQYWPSGEYEgeYGDLTVELVSE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 226 KECPE--YTVRQLTIQY-QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFI 302
Cdd:cd18533  81 EENDDggFIVREFELSKeDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGTFI 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 20141721 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 20141721 123 DRYKTILPNPQSRVCLGRAQSQEDgDYINANYIRGYDGKeKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GK 201
Cdd:cd14615   1 NRYNNVLPYDISRVKLSVQSHSTD-DYINANYMPGYNSK-KEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEqGR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 202 EKCVHYWPTEE-ETYGPFQIRIQDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESP 278
Cdd:cd14615  79 TKCEEYWPSKQkKDYGDITVTMTSEIVLPEWTIRDFTVKNAQtnESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYM 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20141721 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 20141721 123 DRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GK 201
Cdd:cd14617   1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRRE-YIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEkGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 202 EKCVHYWPTEEET--YGPFQIRIQDMKECPEYTVRQLTIQYQEE---RRSVKHILFSAWPDHQTPESAGPLLRLVAEVEE 276
Cdd:cd14617  80 VKCDHYWPADQDSlyYGDLIVQMLSESVLPEWTIREFKICSEEQldaPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20141721 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 20141721  96 QLEEEFLKI-PSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPN 174
Cdd:cd14626  17 KFSQEYESIdPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYR-KQNAYIATQGPLPE 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 175 TVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMKECPEYTVRQLTIQYQ--EERRSVKHI 250
Cdd:cd14626  96 TLSDFWRMVWEQRTATIVMMTRLEEkSRVKCDQYWPIRgTETYGMIQVTLLDTVELATYSVRTFALYKNgsSEKREVRQF 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 251 LFSAWPDHQTPESAGPLLRLVAEVEE-SPETAahpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLD 329
Cdd:cd14626 176 QFMAWPDHGVPEYPTPILAFLRRVKAcNPPDA---GPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQ 252

                       250
                ....*....|....*...
gi 20141721 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 20141721 123 DRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYdGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GK 201
Cdd:cd14619   1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGY-WSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEaGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 202 EKCVHYWPTEEE--TYGPFQIRIQDMKECPEYTVRQLTIQY--QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEES 277
Cdd:cd14619  80 VKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQveEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQW 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20141721 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 20141721 149 YINANYIRGYDGKEK-VYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEET----YGPFQIRI 222
Cdd:cd14538   1 YINASHIRIPVGGDTyHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEgGKVKCHRYWPDSLNKplicGGRLEVSL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 223 QDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESpetaAHPGPIVVHCSAGIGRTGC 300
Cdd:cd14538  81 EKYQSLQDFVIRRISLRDKEtgEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRI----HNSGPIVVHCSAGIGRTGV 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 20141721 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 20141721 123 DRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLT-QLREGK 201
Cdd:cd14618   1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQE-FIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvGMENGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 202 EKCVHYWPTEEE--TYGPFQIRIQDMKECPEYTVRQLTIQYQEER--RSVKHILFSAWPDHQTPESAGPLLRLVAEVEES 277
Cdd:cd14618  80 VLCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRkeRRVKHLHYTAWPDHGIPESTSSLMAFRELVREH 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 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 20141721 149 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEETYGPFQIRIQDMKE 227
Cdd:cd14555   1 YINANYIDGYH-RPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEvGRVKCSRYWPDDTEVYGDIKVTLVETEP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 228 CPEYTVRQLTIQYQ--EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhpGPIVVHCSAGIGRTGCFIATR 305
Cdd:cd14555  80 LAEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSA--GPIVVHCSAGAGRTGCYIVID 157

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 20141721 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 20141721 115 DIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKeKVYIATQGPMPNTVSDFWEMVWQEEVSLIVML 194
Cdd:cd14554   2 NLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQR-GAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 195 TQLRE-GKEKCVHYWPTEEET-YGPFQIRIQDMKECPEYTVRQLTIQYQEER--RSVKHILFSAWPDHQTPESAGPLLRL 270
Cdd:cd14554  81 TKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARDGqsRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20141721 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 20141721 121 SKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE- 199
Cdd:cd14630   5 NKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYH-RPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEv 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 200 GKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQ--EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVE-- 275
Cdd:cd14630  84 GRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKgyHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQVKfl 163

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20141721 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 20141721 149 YINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREG-KEKCVHYWPTEEE---TYGPFQIRIQD 224
Cdd:cd14557   1 YINASYIDGFKEPRK-YIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGnRNKCAQYWPSMEEgsrAFGDVVVKINE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 225 MKECPEYTVRQLTIQYQEERRS---VKHILFSAWPDHQTPESAGPLLRLVAEVEESpeTAAHPGPIVVHCSAGIGRTGCF 301
Cdd:cd14557  80 EKICPDYIIRKLNINNKKEKGSgreVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAF--NNFFSGPIVVHCSAGVGRTGTY 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 20141721 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 20141721 109 VSPEDLDIPGHASKDRYKTILPNPQSRVCLgRAQSQEDG---DYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQ 185
Cdd:cd17667  17 ITAEHSNHPDNKHKNRYINILAYDHSRVKL-RPLPGKDSkhsDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 186 EEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMKECPEYTVRQLTIQY-------------QEERRSVKHI 250
Cdd:cd17667  95 QNTGIIVMITNLVEkGRRKCDQYWPTEnSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpkgRQNERTVIQY 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 251 LFSAWPDHQTPESAGPLLRLVAEveESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDR 330
Cdd:cd17667 175 HYTQWPDMGVPEYALPVLTFVRR--SSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQR 252

                       250
                ....*....|....*..
gi 20141721 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 20141721 148 DYINANY----IRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEET--YGPFQI 220
Cdd:cd14541   1 DYINANYvnmeIPGSGIVNR-YIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVErGRVKCHQYWPDLGETmqFGNLQI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 221 RIQDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHpgPIVVHCSAGIGRT 298
Cdd:cd14541  80 TCVSEEVTPSFAFREFILTNTNtgEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVE--PTVVHCSAGIGRT 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 20141721 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 20141721 105 PSNFVSPEDldipgHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKeKVYIATQGPMPNTVSDFWEMVW 184
Cdd:cd14604  48 PTATGEKEE-----NVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGP-KAYIATQGPLANTVIDFWRMIW 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 185 QEEVSLIVMLTQLRE-GKEKCVHYWPTEEE---TYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQT 260
Cdd:cd14604 122 EYNVAIIVMACREFEmGRKKCERYWPLYGEepmTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDV 201

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 261 PESAGPLLRLVAEVEESPETaaHPGPIVVHCSAGIGRTGCFIATRIGCQQLKA---RGEVDILGIVCQLRLDRGGMIQTA 337
Cdd:cd14604 202 PSSFDSILDMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTK 279

                       250
                ....*....|....*...
gi 20141721 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 20141721 125 YKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKE-K 203
Cdd:cd14620   1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEeK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 204 CVHYWPTEE-ETYGPFQIRIQDMKECPEYTVRQLTIQYQ-----EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEES 277
Cdd:cd14620  80 CYQYWPDQGcWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSV 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 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 20141721 149 YINANYIRGYDGkEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREG-KEKCVHYWPTEEETYGPFQIRIQDMKE 227
Cdd:cd14558   1 YINASFIDGYWG-PKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGdQEQCAQYWGDEKKTYGDIEVELKDTEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 228 CPEYTVRQLTIQY--QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEES-PETAAHPG---PIVVHCSAGIGRTGCF 301
Cdd:cd14558  80 SPTYTVRVFEITHlkRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKlPYKNSKHGrsvPIVVHCSDGSSRTGIF 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 20141721 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 20141721 149 YINANYIRGYDGkEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEE---TYGPFQIRIQD 224
Cdd:cd14542   1 YINANFIKGVSG-SKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEmGKKKCERYWPEEGEeqlQFGPFKISLEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 225 MKE-CPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESpeTAAHPGPIVVHCSAGIGRTGCFIA 303
Cdd:cd14542  80 EKRvGPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVPICVHCSAGCGRTGTICA 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 20141721 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 20141721 117 PGHASKDRYKTILPNPQSRVCLGRAQSQEDG-DYINANYIR----GYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLI 191
Cdd:cd14606  16 PENKSKNRYKNILPFDHSRVILQGRDSNIPGsDYINANYVKnqllGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 192 VMLT-QLREGKEKCVHYWPTEEET--YGPFQIRIQDMKECPEYTVRQL---TIQYQEERRSVKHILFSAWPDHQTPESAG 265
Cdd:cd14606  96 VMTTrEVEKGRNKCVPYWPEVGMQraYGPYSVTNCGEHDTTEYKLRTLqvsPLDNGELIREIWHYQYLSWPDHGVPSEPG 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 266 PLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQYQF 342
Cdd:cd14606 176 GVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSGMVQTEAQYKF 255


                ....*...
gi 20141721 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 20141721 149 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEETYGPFQIRIQDMKE 227
Cdd:cd14632   1 YINANYIDGYH-RSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEvGRVKCSKYWPDDSDTYGDIKITLLKTET 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 228 CPEYTVRQLTIQYQ--EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESpeTAAHPGPIVVHCSAGIGRTGCFIATR 305
Cdd:cd14632  80 LAEYSVRTFALERRgySARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKAS--TPPDAGPVVVHCSAGAGRTGCYIVLD 157

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 20141721 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 20141721 121 SKDRYKTILPNPQSRVCLGRAQSQEDG-DYINANYI-------RGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIV 192
Cdd:cd14605   4 NKNRYKNILPFDHTRVVLHDGDPNEPVsDYINANIImpefetkCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 193 MLT-QLREGKEKCVHYWPTEE--ETYGpfQIRIQDMKECP--EYTVRQLTI----QYQEERrSVKHILFSAWPDHQTPES 263
Cdd:cd14605  84 MTTkEVERGKSKCVKYWPDEYalKEYG--VMRVRNVKESAahDYILRELKLskvgQGNTER-TVWQYHFRTWPDHGVPSD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 264 AGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQY 340
Cdd:cd14605 161 PGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTEAQY 240

                       250
                ....*....|
gi 20141721 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 20141721  96 QLEEEFLKI-PSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPN 174
Cdd:cd14625  23 KLSQEYESIdPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYR-KQNAYIATQGPLPE 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 175 TVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMKECPEYTVRQLTIQYQ--EERRSVKHI 250
Cdd:cd14625 102 TFGDFWRMVWEQRSATVVMMTKLEEkSRIKCDQYWPSRgTETYGMIQVTLLDTIELATFCVRTFSLHKNgsSEKREVRQF 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 251 LFSAWPDHQTPESAGPLLRLVAEVEE-SPETAahpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLD 329
Cdd:cd14625 182 QFTAWPDHGVPEYPTPFLAFLRRVKTcNPPDA---GPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQ 258

                       250
                ....*....|....*...
gi 20141721 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 20141721 135 RVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEE 213
Cdd:cd14631   1 RVILQPVEDDPSSDYINANYIDGYQ-RPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEvGRVKCYKYWPDDTE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 214 TYGPFQIRIQDMKECPEYTVRQLTIQYQ--EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhpGPIVVHC 291
Cdd:cd14631  80 VYGDFKVTCVEMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSA--GPIVVHC 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20141721 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 20141721  97 LEEEFLKIPSN------FVSPedlDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQG 170
Cdd:cd14628  27 MELEFKRLASSkahtsrFISA---NLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYR-QQKAYIATQG 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 171 PMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEET-YGPFQIRIQDMKECPEYTVRQLTIQYQE--ERRS 246
Cdd:cd14628 103 PLAETTEDFWRMLWEHNSTIVVMLTKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRT 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 247 VKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQL 326
Cdd:cd14628 183 VRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKML 262

                       250       260
                ....*....|....*....|....*...
gi 20141721 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 20141721 106 SNFVSPedlDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQ 185
Cdd:cd14627  43 SRFISA---NLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWE 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 186 EEVSLIVMLTQLRE-GKEKCVHYWPTEEET-YGPFQIRIQDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTP 261
Cdd:cd14627 119 NNSTIVVMLTKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRTVRQFQFTDWPEQGVP 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 262 ESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQ 341
Cdd:cd14627 199 KSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQ 278

                       250
                ....*....|.
gi 20141721 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 20141721 149 YINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEE-TYGPFQIRIQDMK 226
Cdd:cd14552   1 YINASFIDGYRQKDA-YIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKErSQNKCAQYWPEDGSvSSGDITVELKDQT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 227 ECPEYTVRQ--LTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHpGPIVVHCSAGIGRTGCFIAT 304
Cdd:cd14552  80 DYEDYTLRDflVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGN-HPITVHCSAGAGRTGTFCAL 158

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 20141721 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 20141721  96 QLEEEFLKI-PSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPN 174
Cdd:cd14624  23 KFSQEYESIdPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYR-KQNAYIATQGALPE 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 175 TVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMKECPEYTVRQLTI--QYQEERRSVKHI 250
Cdd:cd14624 102 TFGDFWRMIWEQRSATVVMMTKLEErSRVKCDQYWPSRgTETYGLIQVTLLDTVELATYCVRTFALykNGSSEKREVRQF 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 251 LFSAWPDHQTPESAGPLLRLVAEVEE-SPETAahpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLD 329
Cdd:cd14624 182 QFTAWPDHGVPEHPTPFLAFLRRVKTcNPPDA---GPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQ 258

                       250
                ....*....|....*...
gi 20141721 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 20141721 122 KDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKeKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-G 200
Cdd:cd14602   1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGP-RAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEmG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 201 KEKCVHYW--PTEEE-TYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEV--- 274
Cdd:cd14602  80 KKKCERYWaePGEMQlEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVrcy 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20141721 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 20141721 149 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMK 226
Cdd:cd17668   1 YINANYVDGYN-KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEkGRRKCDQYWPADgSEEYGNFLVTQKSVQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 227 ECPEYTVRQLTIQ-------YQEER---RSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhpGPIVVHCSAGIG 296
Cdd:cd17668  80 VLAYYTVRNFTLRntkikkgSQKGRpsgRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAV--GPVVVHCSAGVG 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 20141721 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 20141721 122 KDRYKTILPNPQSRVCLGraqsqEDGDYINANYIRGYDGKEK-VYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREG 200
Cdd:cd14597   6 KNRYKNILPYDTTRVPLG-----DEGGYINASFIKMPVGDEEfVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 201 -KEKCVHYWPteeETYGP-------FQIRIQDMKECPEYTVRQLTIQ--YQEERRSVKHILFSAWPDHQTPESAGPLLRL 270
Cdd:cd14597  81 gKIKCQRYWP---EILGKttmvdnrLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTPSQPEQLLTF 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 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 20141721 122 KDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-G 200
Cdd:cd14633  43 KNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYH-RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEvG 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 201 KEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQ--EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEEsp 278
Cdd:cd14633 122 RVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS-- 199

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20141721 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 20141721 106 SNFVSPedlDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQ 185
Cdd:cd14629  43 SRFISA---NLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWE 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 186 EEVSLIVMLTQLRE-GKEKCVHYWPTEEET-YGPFQIRIQDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTP 261
Cdd:cd14629 119 HNSTIVVMLTKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRTIRQFQFTDWPEQGVP 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 262 ESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQ 341
Cdd:cd14629 199 KTGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQ 278

                       250
                ....*....|...
gi 20141721 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 20141721  88 QRQPPSPKQLEEEFLKIPSNFV--SPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvY 165
Cdd:cd14621  19 RRMADDNKLFREEFNALPACPIqaTCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNK-F 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 166 IATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKE-KCVHYWPTEE-ETYGPFQIRIQDMKECPEYTVRQLTIQY--- 240
Cdd:cd14621  98 IAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKEcKCAQYWPDQGcWTYGNIRVSVEDVTVLVDYTVRKFCIQQvgd 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 241 ---QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEE-SPETAahpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGE 316
Cdd:cd14621 178 vtnKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNcNPQYA---GAIVVHCSAGVGRTGTFIVIDAMLDMMHAERK 254

                       250       260       270
                ....*....|....*....|....*....|.
gi 20141721 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 20141721 149 YINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMK 226
Cdd:cd14551   1 YINASYIDGYQEKNK-FIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKErKEKKCSQYWPDQgCWTYGNLRVRVEDTV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 227 ECPEYTVRQLTIQYQ------EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESpeTAAHPGPIVVHCSAGIGRTGC 300
Cdd:cd14551  80 VLVDYTTRKFCIQKVnrgigeKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSA--NPPRAGPIVVHCSAGVGRTGT 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 20141721 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 20141721 116 IPGHASKDRYKTILPNPQSRVCLgraqSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLT 195
Cdd:cd14608  22 LPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRS-YILTQGPLPNTCGHFWEMVWEQKSRGVVMLN 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 196 QLRE-GKEKCVHYWPTEEETYGPFQ---IRI----QDMKEcpEYTVRQLTIQ--YQEERRSVKHILFSAWPDHQTPESAG 265
Cdd:cd14608  97 RVMEkGSLKCAQYWPQKEEKEMIFEdtnLKLtlisEDIKS--YYTVRQLELEnlTTQETREILHFHYTTWPDFGVPESPA 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 266 PLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIgC----QQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQ 341
Cdd:cd14608 175 SFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADT-ClllmDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLR 253


                .
gi 20141721 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 20141721 122 KDRYKTILPNPQSRVclgRAQS-QEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE- 199
Cdd:cd14545   1 LNRYRDRDPYDHDRS---RVKLkQGDNDYINASLVEVEEAKRS-YILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEk 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 200 GKEKCVHYWPTEEET-----YGPFQIRIQDMKECPEYTVRQLTIQ--YQEERRSVKHILFSAWPDHQTPESAGPLLRLVA 272
Cdd:cd14545  77 GQIKCAQYWPQGEGNamifeDTGLKVTLLSEEDKSYYTVRTLELEnlKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20141721 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 20141721 149 YINANYIRGYDGKEK-VYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWP-TEEETY--GPFQIRIQ 223
Cdd:cd14596   1 YINASYITMPVGEEElFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVErGKVKCHRYWPeTLQEPMelENYQLRLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 224 DMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETaahpGPIVVHCSAGIGRTGCF 301
Cdd:cd14596  81 NYQALQYFIIRIIKLVEKEtgENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT----GPIVVHCSAGIGRAGVL 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 20141721 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 20141721 123 DRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GK 201
Cdd:cd14616   1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNE-FIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEkGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 202 EKCVHYWPTEEETYGPF-QIRIQDMKE--CPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESp 278
Cdd:cd14616  80 IRCHQYWPEDNKPVTVFgDIVITKLMEdvQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRAS- 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20141721 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 20141721 148 DYINANYIRGYDGKEkVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEE-TYGPFQIRIQDM 225
Cdd:cd14622   1 DYINASFIDGYRQKD-YFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQErEQEKCVQYWPSEGSvTHGEITIEIKND 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 226 KECPEYTVRQLTIQYQEER--RSVKHILFSAWPDHQTPESAGPLLRLVAEVE-ESPETAAHPgpIVVHCSAGIGRTGCFI 302
Cdd:cd14622  80 TLLETISIRDFLVTYNQEKqtRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQkQQQQTGNHP--IVVHCSAGAGRTGTFI 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 20141721 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 20141721 124 RYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKE 202
Cdd:cd14623   1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDS-YIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEErGQE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 203 KCVHYWPTEEE-TYGPFQIRIQDMKECPEYTVRQLTIQYQEERRS--VKHILFSAWPDHQTPESAGPLLRLVAEVEESPE 279
Cdd:cd14623  80 KCAQYWPSDGSvSYGDITIELKKEEECESYTVRDLLVTNTRENKSrqIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQ 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20141721 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 20141721 149 YINANYIR-GYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-----EETYGPFQIR 221
Cdd:cd14540   1 YINASHITaTVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEgGREKCFRYWPTLggehdALTFGEYKVS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 222 IQDMKECPEYTVRQLTIQYQEER--RSVKHILFSAWPDHQTPESAGPLLRLVAEV--------EESPETAAHPgPIVVHC 291
Cdd:cd14540  81 TKFSVSSGCYTTTGLRVKHTLSGqsRTVWHLQYTDWPDHGCPEDVSGFLDFLEEInsvrrhtnQDVAGHNRNP-PTLVHC 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 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 20141721  96 QLEEEFLKIPSNFVS----PEDLDipghasKDRYKTILPNPQSRVCLgraqsQEDGDYINANY----IRGYDGKEKvYIA 167
Cdd:cd14600  19 QFEQLYRKKPGLAITcaklPQNMD------KNRYKDVLPYDATRVVL-----QGNEDYINASYvnmeIPSANIVNK-YIA 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 168 TQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEET--YGPFQIRIQDMKECPEYTVRQLTIQYQE-- 242
Cdd:cd14600  87 TQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTErGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQtg 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 243 ERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhpgPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGI 322
Cdd:cd14600 167 EERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENE---PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDI 243

                       250       260
                ....*....|....*....|.
gi 20141721 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 20141721 148 DYINANYIR---GYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVML-TQLREGKEKCVHYWP--TEEETYGPFQIR 221
Cdd:cd14601   1 DYINANYINmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLtTQVERGRVKCHQYWPepSGSSSYGGFQVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 222 IQDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEEspETAAHPGPIVVHCSAGIGRTG 299
Cdd:cd14601  81 CHSEEGNPAYVFREMTLTNLEknESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRN--KRAGKDEPVVVHCSAGIGRTG 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 20141721 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 20141721 149 YINANYIRGYDGKeKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWPTEEE-TYGPFQIRIQDMKE 227
Cdd:cd14556   1 YINAALLDSYKQP-AAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDEGSgTYGPIQVEFVSTTI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 228 CPEYTVRQLTIQ----YQEERRSVKHILFSAWPDHQ-TPESAGPLLRLVAEVEESPETAAHpGPIVVHCSAGIGRTGCFI 302
Cdd:cd14556  80 DEDVISRIFRLQnttrPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGE-GPIVVHCLNGVGRSGVFC 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 20141721 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 20141721 106 SNFVSPEDLDIPghasKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQ 185
Cdd:cd14610  35 ATNVAQREENVQ----KNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWE 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 186 EEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIR-IQDMKECPEYTVRQLTIQ--YQEERRSVKHILFSAWPDHQT 260
Cdd:cd14610 111 SGCVVIVMLTPLAEnGVKQCYHYWPDEgSNLYHIYEVNlVSEHIWCEDFLVRSFYLKnlQTNETRTVTQFHFLSWNDQGV 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 261 PESAGPLLRLVAEVEESpeTAAHPGPIVVHCSAGIGRTGCFIATRIGCQQL-KARGEVDILGIVCQLRLDRGGMIQTAEQ 339
Cdd:cd14610 191 PASTRSLLDFRRKVNKC--YRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQ 268


                ...
gi 20141721 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 20141721 149 YINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVML-TQLREGKEKCVHYWPTE---EETYGPFQIRIQD 224
Cdd:cd14539   1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLvSEQENEKQKVHRYWPTErgqALVYGAITVSLQS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 225 MKECPEYTVRQLTIQYQEER--RSVKHILFSAWPDHQTPESAGPLLRLVAEVEE-----SPETAahpgPIVVHCSAGIGR 297
Cdd:cd14539  81 VRTTPTHVERIISIQHKDTRlsRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShylqqRSLQT----PIVVHCSSGVGR 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 20141721 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 20141721 149 YINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIR-IQDM 225
Cdd:cd14546   1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQEnGVKQCARYWPEEgSEVYHIYEVHlVSEH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 226 KECPEYTVRQL---TIQYQEErRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPEtaAHPGPIVVHCSAGIGRTGCFI 302
Cdd:cd14546  81 IWCDDYLVRSFylkNLQTSET-RTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYR--GRSCPIVVHCSDGAGRTGTYI 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 20141721 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 20141721 149 YINANYIRGYD-GKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREG--KEKCVHYWPTEE---ETYGPFQIRI 222
Cdd:cd17658   1 YINASLVETPAsESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNysTAKCADYFPAEEnesREFGRISVTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 223 QDMKeCPEY--TVRQLTIQY---QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAahpGPIVVHCSAGIGR 297
Cdd:cd17658  81 KKLK-HSQHsiTLRVLEVQYiesEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSA---GPIVVHCSAGIGR 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 20141721 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 20141721 117 PGHASKDRYKTILPNPQSRVCLGRAqsqeDGDYINANYIRgYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQ 196
Cdd:cd14607  22 PENRNRNRYRDVSPYDHSRVKLQNT----ENDYINASLVV-IEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNR 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 197 LRE-GKEKCVHYWPTEEETYGPFQ-----IRI--QDMKEcpEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGP 266
Cdd:cd14607  97 IVEkDSVKCAQYWPTDEEEVLSFKetgfsVKLlsEDVKS--YYTVHLLQLENINsgETRTISHFHYTTWPDFGVPESPAS 174

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20141721 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 20141721 116 IPGHASKDRYKTILPNPQSRVCLGRAQSQEDGdYINANYIR-GYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVML 194
Cdd:cd14599  35 LPENAERNRIREVVPYEENRVELVPTKENNTG-YINASHIKvTVGGEEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMV 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 195 TQLRE-GKEKCVHYWPT-----EEETYGPFQIRIQDMKECPEYTVRQLTIQY--QEERRSVKHILFSAWPDHQTPESAGP 266
Cdd:cd14599 114 TAEEEgGRSKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPDHGCPEEVQG 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 267 LLRLVAEVEE---------SPETAAHPgPIVVHCSAGIGRTGCFIATR--IGCqqLKARGEVDILGIVCQLRLDRGGMIQ 335
Cdd:cd14599 194 FLSYLEEIQSvrrhtnsmlDSTKNCNP-PIVVHCSAGVGRTGVVILTElmIGC--LEHNEKVEVPVMLRHLREQRMFMIQ 270

                       250
                ....*....|..
gi 20141721 336 TAEQYQFLHHTL 347
Cdd:cd14599 271 TIAQYKFVYQVL 282

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 20141721  123 DRYKTILPNPQSRVCLGRAQSQedGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GK 201
Cdd:PHA02738  53 NRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKK-FICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEnGR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721  202 EKCVHYWPTEEET---YGPFQIRIQDMKECPEYTVRQLTI-QYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEES 277
Cdd:PHA02738 130 EKCFPYWSDVEQGsirFGKFKITTTQVETHPHYVKSTLLLtDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQC 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721  278 PETAA-----------HPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHT 346
Cdd:PHA02738 210 QKELAqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRA 289


                 ....
gi 20141721  347 LALY 350
Cdd:PHA02738 290 VKRY 293

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 20141721  95 KQLEEEFLKIPSNFVSPEDLDIPGHASKDRYKTILPNPQSRVclgraqsQEDGDYINANYIRGYDGKekVYIATQGPMPN 174
Cdd:COG5599  18 SRLSTLTNELAPSHNDPQYLQNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIGNH--RYIATQYPLEE 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 175 TVSDFWEMVWQEEVSLIVMLTQLREGKE---KCVHYWPTEEEtYGPFQIR--------IQDMKECPEYTVRQLtiQYQEE 243
Cdd:COG5599  89 QLEDFFQMLFDNNTPVLVVLASDDEISKpkvKMPVYFRQDGE-YGKYEVSseltesiqLRDGIEARTYVLTIK--GTGQK 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 244 RRSVKHILFSAWPDHQTPeSAGPLLRLVAEVEESPETAAHP-GPIVVHCSAGIGRTGCFIATRIGCQQLKARGE--VDIL 320
Cdd:COG5599 166 KIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKEKIKDPDkLLPVVHCRAGVGRTGTLIACLALSKSINALVQitLSVE 244

                       250       260
                ....*....|....*....|....
gi 20141721 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 20141721 118 GHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQL 197
Cdd:cd14609  41 ANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPL 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 198 RE-GKEKCVHYWPTEEET-YGPFQIR-IQDMKECPEYTVRQL---TIQYQEErRSVKHILFSAWPDHQTPESAGPLLRLV 271
Cdd:cd14609 121 VEdGVKQCDRYWPDEGSSlYHIYEVNlVSEHIWCEDFLVRSFylkNVQTQET-RTLTQFHFLSWPAEGIPSSTRPLLDFR 199

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20141721 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 20141721 149 YINANYIR-GYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWP-----TEEETYGPFQIR 221
Cdd:cd14598   1 YINASHIKvTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEgGREKSFRYWPrlgsrHNTVTYGRFKIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 222 IQDMKECPEYTVRQLTIQY--QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVE-------ESPETAAHPGPIVVHCS 292
Cdd:cd14598  81 TRFRTDSGCYATTGLKIKHllTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQsvrrhtnSTIDPKSPNPPVLVHCS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20141721 293 AGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 347
Cdd:cd14598 161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215

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 20141721   74 FLRTAGHPlTRWALQRQPPSpkqleeEFLKIP-----SNFVSPEDLdipghaSKDRYKTILPNPQSRVCLGRAQS----- 143
Cdd:PHA02746  14 FFDKTNHA-KFCEFVLLEHA------EVMDIPirgttNHFLKKENL------KKNRFHDIPCWDHSRVVINAHESlkmfd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721  144 ------------QEDGD--YINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWP 209
Cdd:PHA02746  81 vgdsdgkkievtSEDNAenYIHANFVDGFKEANK-FICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721  210 TEEE---TYGPFQIRIQDMKECPEYTVRQLTI--QYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEE-------- 276
Cdd:PHA02746 160 KEEDselAFGRFVAKILDIIEELSFTKTRLMItdKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikq 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20141721  277 SPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 347
Cdd:PHA02746 240 ADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310

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 20141721  121 SKDRYKTILPNPQSRVCLgraqSQEDG--DYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLR 198
Cdd:PHA02742  54 KKCRYPDAPCFDRNRVIL----KIEDGgdDFINASYVDGHNAKGR-FICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721  199 E-GKEKCVHYWPTEEE---TYGPFQIRIQDMKECPEYTVRQLTIQYQEERRS--VKHILFSAWPDHQTPESAGPLLRLV- 271
Cdd:PHA02742 129 EdGKEACYPYWMPHERgkaTHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASldIKHFAYEDWPHGGLPRDPNKFLDFVl 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721  272 --------AEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 343
Cdd:PHA02742 209 avreadlkADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFC 288


                 ....*...
gi 20141721  344 HHTLALYA 351
Cdd:PHA02742 289 YFIVLIFA 296

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 20141721  101 FLKIPSNFVSPEDldipghASKDRYKTILPNPQSRVCLgRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFW 180
Cdd:PHA02747  39 FDGLIANFEKPEN------QPKNRYWDIPCWDHNRVIL-DSGGGSTSDYIHANWIDGFE-DDKKFIATQGPFAETCADFW 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721  181 EMVWQEEVSLIVMLTQLR--EGKEKCVHYW-PTEEETYGPFQIRIQDMKEC--PEY--TVRQLTIQYQEERRSVKHILFS 253
Cdd:PHA02747 111 KAVWQEHCSIIVMLTPTKgtNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSvrAKYilTLIEITDKILKDSRKISHFQCS 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721  254 AWPDHQTPESAGPLLRLVAEVEESPETA--------AHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQ 325
Cdd:PHA02747 191 EWFEDETPSDHPDFIKFIKIIDINRKKSgklfnpkdALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEK 270

                        250
                 ....*....|....*....
gi 20141721  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 20141721    246 SVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKAR-GEVDILGIVC 324
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....
gi 20141721    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 20141721    246 SVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKAR-GEVDILGIVC 324
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....
gi 20141721    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 20141721 149 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLrEGKEKCVHYWPTEEE-TYGPFQIRI--QDM 225
Cdd:cd14634   1 YINAALMDSHK-QPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM-DAAQLCMQYWPEKTScCYGPIQVEFvsADI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 226 KEcpEYTVRQLTI----QYQEERRSVKHILFSAWPDHQ-TPESAGPLLRLVAEVEESPETA-AHPGPIVVHCSAGIGRTG 299
Cdd:cd14634  79 DE--DIISRIFRIcnmaRPQDGYRIVQHLQYIGWPAYRdTPPSKRSILKVVRRLEKWQEQYdGREGRTVVHCLNGGGRSG 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 20141721 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 20141721 149 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLrEGKEKCVHYWPTEEET--YGPFQIRIQDMK 226
Cdd:cd14550   1 YINASYLQGYR-RSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNEDEPIYWPTKEKPleCETFKVTLSGED 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 227 ECP-----EYTVRQLTIQYQEERR--SVKHILFSAWPDHQTP-ESAGPLLRLVAEveespETAAHPGPIVVH-----CSA 293
Cdd:cd14550  79 HSClsneiRLIVRDFILESTQDDYvlEVRQFQCPSWPNPCSPiHTVFELINTVQE-----WAQQRDGPIVVHdryggVQA 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 20141721 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 20141721 149 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEK--CVHYWPTE-EETYGPFQIRIQDM 225
Cdd:cd14637   1 YINAALTDSYT-RSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwpCLQYWPEPgLQQYGPMEVEFVSG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 226 KECPEYTVRQLTIQ----YQEERRSVKHILFSAW-PDHQTPESAGPLLRLVAEVEESPETAAHpGPIVVHCSAGIGRTGC 300
Cdd:cd14637  80 SADEDIVTRLFRVQnitrLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGE-GRTVVHCLNGGGRSGT 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 20141721 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 20141721 149 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLrEGKEKCVHYWPTEEE-TYGPFQIRIQDMKE 227
Cdd:cd14636   1 YINAALMDSYR-QPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV-DLAQGCPQYWPEEGMlRYGPIQVECMSCSM 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 228 CPEYTVRQLTI----QYQEERRSVKHILFSAWPDH-QTPESAGPLLRLVAEVEE-SPETAAHPGPIVVHCSAGIGRTGCF 301
Cdd:cd14636  79 DCDVISRIFRIcnltRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKwQEECDEGEGRTIIHCLNGGGRSGMF 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 20141721 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 20141721 149 YINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKE- 227
Cdd:cd17669   1 YINASYIMGYYQSNE-FIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEe 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 228 --CPEyTVRQLTIQ------YQEER-RSVKHILFSAWPDHQTPESAgpLLRLVAEVEEspETAAHPGPIVVHCSAGIGRT 298
Cdd:cd17669  80 hkCLS-NEEKLIIQdfileaTQDDYvLEVRHFQCPKWPNPDSPISK--TFELISIIKE--EAANRDGPMIVHDEHGGVTA 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 20141721 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 20141721 149 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLrEGKEKCVHYWPTEE-ETYGPFQIRIQDMKE 227
Cdd:cd14635   1 YINAALMDSYK-QPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV-DPAQLCPQYWPENGvHRHGPIQVEFVSADL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 228 CPEYTVRQLTI----QYQEERRSVKHILFSAWPDHQ-TPESAGPLLRLVAEVEE-SPETAAHPGPIVVHCSAGIGRTGCF 301
Cdd:cd14635  79 EEDIISRIFRIynaaRPQDGYRMVQQFQFLGWPMYRdTPVSKRSFLKLIRQVDKwQEEYNGGEGRTVVHCLNGGGRSGTF 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 20141721 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 20141721 149 YINANYIRGYdGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWPTEEETYG--PFQIR-IQDM 225
Cdd:cd17670   1 YINASYIMGY-YRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNceAFTVTlISKD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 226 KEC----PEYTVRQLTIQYQEERR--SVKHILFSAWPDHQTPESAgpLLRLVAEVEEspETAAHPGPIVVHCSAGIGRTG 299
Cdd:cd17670  80 RLClsneEQIIIHDFILEATQDDYvlEVRHFQCPKWPNPDAPISS--TFELINVIKE--EALTRDGPTIVHDEFGAVSAG 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 20141721 300 CFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 347
Cdd:cd17670 156 TLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203

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 20141721  132 PQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREgKEKCVHYWPTE 211
Cdd:PHA02740  61 HITRLLHRRIKLFNDEKVLDARFVDGYDFEQK-FICIINLCEDACDKFLQALSDNKVQIIVLISRHAD-KKCFNQFWSLK 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721  212 E---ETYGPFQIRIQDMKECPEY--TVRQLTIQYQEERRsVKHILFSAWPDHQTPESAGPLLRLVAEVE------ESPET 280
Cdd:PHA02740 139 EgcvITSDKFQIETLEIIIKPHFnlTLLSLTDKFGQAQK-ISHFQYTAWPADGFSHDPDAFIDFFCNIDdlcadlEKHKA 217

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721  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 20141721 128 ILPNPQSRVclgraqSQEDGDYINANYIRgyDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHY 207
Cdd:cd14559   2 RFTNIQTRV------STPVGKNLNANRVQ--IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 208 WPTEEETYGpfQIRIQDMKECPEYTVR-------QLTIQYQEERRSVKHILFSAWPDHqTPESAGPLLRLVAEVEESPET 280
Cdd:cd14559  74 YFRQSGTYG--SVTVKSKKTGKDELVDglkadmyNLKITDGNKTITIPVVHVTNWPDH-TAISSEGLKELADLVNKSAEE 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20141721 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 20141721 152 ANYIRGydgkeKVYIATQGPMPNtVSDFWEMVWQEEVSLIVMLTqlregkekcvhywpteeetygpfqiriqdmkecpey 231
Cdd:cd14494   1 FNWIDP-----LRLIAGALPLSP-LEADSRFLKQLGVTTIVDLT------------------------------------ 38

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721 232 tvrqltiqyqeerrsvkhilfsawpdhqtpesaGPLLRLVAEVEESPETaaHPGPIVVHCSAGIGRTGCFIATRIGCQQL 311
Cdd:cd14494  39 ---------------------------------LAMVDRFLEVLDQAEK--PGEPVLVHCKAGVGRTGTLVACYLVLLGG 83

                       170       180       190
                ....*....|....*....|....*....|....*
gi 20141721 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 20141721 230 EYTVRQLTIQYQEERRSVKHILFsawPDHQTPESAGPLLRLVAEVEESPETAAHpgpIVVHCSAGIGRTGcFIATRIgCQ 309
Cdd:cd14505  58 ELGVPDLLEQYQQAGITWHHLPI---PDGGVPSDIAQWQELLEELLSALENGKK---VLIHCKGGLGRTG-LIAACL-LL 129

                        90       100       110
                ....*....|....*....|....*....|....*
gi 20141721 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 20141721 255 WPDHQTPESAgPLLRLVAEVEESpetAAHPGPIVVHCSAGIGRTGCFIAtrigcQQLKARGeVDILGIVCQLRLDRGGMI 334
Cdd:COG2453  55 IPDFGAPDDE-QLQEAVDFIDEA---LREGKKVLVHCRGGIGRTGTVAA-----AYLVLLG-LSAEEALARVRAARPGAV 124

                        90
                ....*....|.
gi 20141721 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 20141721 260 TPESAGPLLRLVAEVEESPetaAHPGPIVVHCSAGIGRTGCFIAtrigCQQLKARGEVDILGIVcQLRLDRGGMIQTAEQ 339
Cdd:cd14504  61 TPPTLEQIDEFLDIVEEAN---AKNEAVLVHCLAGKGRTGTMLA----CYLVKTGKISAVDAIN-EIRRIRPGSIETSEQ 132


                ....
gi 20141721 340 YQFL 343
Cdd:cd14504 133 EKFV 136

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 20141721   95 KQLEEEFLKIPSNFVSPEDLDIPGHA-SKDRYKTILPNPQSRVCLgraqsqEDGDYINANYIRgYDGKEkvyIATQGPMP 173
Cdd:PRK15375 273 KNVTAELEKIEAGAPMPQTMSGPTLGlARFAVSSIPINQQTQVKL------SDGMPVPVNTLT-FDGKP---VALAGSYP 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721  174 NTVSDFWE----MVWQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEY-TVRQLTIQYQ--EERRS 246
Cdd:PRK15375 343 KNTPDALEahmkMLLEKECSCLVVLTSEDQMQAKQLPPYFRGSYTFGEVHTNSQKVSSASQGeAIDQYNMQLScgEKRYT 422

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141721  247 VKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhPG--------PIvVHCSAGIGRTGCFIATRIgcqqLKARGEVD 318
Cdd:PRK15375 423 IPVLHVKNWPDHQPLPSTDQLEYLADRVKNSNQNGA-PGrsssdkhlPM-IHCLGGVGRTGTMAAALV----LKDNPHSN 496

                        250       260
                 ....*....|....*....|...
gi 20141721  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 20141721 244 RRSVKHILFsAWPDHQTPeSAGPLLRLVAEVEESPEtaaHPGPIVVHCSAGIGRTGCFIA------TRIGCQQLkargev 317
Cdd:cd14506  74 RAGIYFYNF-GWKDYGVP-SLTTILDIVKVMAFALQ---EGGKVAVHCHAGLGRTGVLIAcylvyaLRMSADQA------ 142

                        90       100
                ....*....|....*....|....*..
gi 20141721 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 20141721 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 20141721 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 20141721   197 LREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAwPDHQTPEsAGPLLRLVAEVEE 276
Cdd:pfam14566  51 LAEAKKNGGRVLVHDETEDGIGVLTVVDVWESDVQTPEEVYERLKAEGPGVDYRRIPI-TDEKAPL-EEDFDALISIVKD 128

                          90       100
                  ....*....|....*....|..
gi 20141721   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 20141721 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