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Conserved domains on  [gi|1524085|emb|CAB01957|]
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protein-tyrosine phosphatase NC-PTPCOM1 [Homo sapiens]

Protein Classification

receptor-type tyrosine-protein phosphatase R( domain architecture ID 12998692)

receptor-type tyrosine-protein phosphatase R is a mitogen-activated protein kinase (MAPK)-specific protein tyrosine phosphatase which sequesters MAPKs such as MAPK1, MAPK3 and MAPK14 in the cytoplasm in an inactive form; similar to Mus musculus PTPRR

EC:  3.1.3.48
Gene Ontology:  GO:0004721|GO:0004725
PubMed:  27514797

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 417-642 1.98e-178

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: 505.99  E-value: 1.98e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  417 TKNRYKTILPNPLSRVCLRPKNVTDSLSTYINANYIRGYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKE 496
Cdd:cd14611   1 TKNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  497 KNEKCVLYWPEKRGIYGKVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRL 576
Cdd:cd14611  81 KNEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRL 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524085  577 ASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHH 642
Cdd:cd14611 161 ASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
 
Name Accession Description Interval E-value
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 417-642 1.98e-178

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: 505.99  E-value: 1.98e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  417 TKNRYKTILPNPLSRVCLRPKNVTDSLSTYINANYIRGYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKE 496
Cdd:cd14611   1 TKNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  497 KNEKCVLYWPEKRGIYGKVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRL 576
Cdd:cd14611  81 KNEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRL 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524085  577 ASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHH 642
Cdd:cd14611 161 ASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
392-644 1.17e-104

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 318.45  E-value: 1.17e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085     392 LLQSEFMEIPMNFVDPKEIDI---PRHGTKNRYKTILPNPLSRVCLRPKNvtDSLSTYINANYIRGYSGKeKAFIATQGP 468
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKLKPPP--GEGSDYINASYIDGPNGP-KAYIATQGP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085     469 MINTVDDFWQMVWQEDSPVIVMITKLKEKN-EKCVLYWPEKRG---IYGKVEVLVISVNECDNYTIRNLVLK--QGSHTQ 542
Cdd:smart00194  78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGrEKCAQYWPDEEGeplTYGDITVTLKSVEKVDDYTIRTLEVTntGCSETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085     543 HVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRlaSQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQ 622
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQ--STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                          250       260
                   ....*....|....*....|..
gi 1524085     623 LRMDRGGMVQTSEQYEFVHHAL 644
Cdd:smart00194 236 LRSQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
417-644 2.35e-96

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 296.08  E-value: 2.35e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085    417 TKNRYKTILPNPLSRVCLRPknvTDSLSTYINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKE 496
Cdd:pfam00102   3 EKNRYKDVLPYDHTRVKLTG---DPGPSDYINASYIDGYK-KPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085    497 KN-EKCVLYWPEKRG---IYGKVEV-LVISVNECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLML 569
Cdd:pfam00102  79 KGrEKCAQYWPEEEGeslEYGDFTVtLKKEKEDEKDYTVRTLEVSngGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524085    570 DVEEDRLASQgRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:pfam00102 159 KVRKSSLDGR-SGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 394-644 9.96e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 154.42  E-value: 9.96e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085   394 QSEFMEIPMNFVDPKEIDiPRHGTKNRYKTILPNPLSRVCLRPKN----------------VT--DSLSTYINANYIRGY 455
Cdd:PHA02746  31 HAEVMDIPIRGTTNHFLK-KENLKKNRFHDIPCWDHSRVVINAHEslkmfdvgdsdgkkieVTseDNAENYIHANFVDGF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085   456 SGKEKaFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPEKRG---IYGKVEVLVISVNECDNYTIRN 532
Cdd:PHA02746 110 KEANK-FICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKEEDselAFGRFVAKILDIIEELSFTKTR 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085   533 LVL--KQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLA--------SQGRGPVVVHCSAGIGRTGCFIATS 602
Cdd:PHA02746 189 LMItdKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAElikqadndPQTLGPIVVHCSAGIGRAGTFCAID 268

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 1524085   603 IGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:PHA02746 269 NALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
403-639 3.76e-37

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 140.23  E-value: 3.76e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  403 NFVDPKEIDIPRHGTKNRYKTILPNPLSRVclRPKNVtdslstYINANYIRGysGKEKAFIATQGPMINTVDDFWQMVWQ 482
Cdd:COG5599  30 SHNDPQYLQNINGSPLNRFRDIQPYKETAL--RANLG------YLNANYIQV--IGNHRYIATQYPLEEQLEDFFQMLFD 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  483 EDSPVIVMIT---KLKEKNEKCVLYWPEKrGIYGK--VEVLVISVNEC-DNYTIRNLVLKQ---GSHTQHVKHYWYTSWP 553
Cdd:COG5599 100 NNTPVLVVLAsddEISKPKVKMPVYFRQD-GEYGKyeVSSELTESIQLrDGIEARTYVLTIkgtGQKKIEIPVLHVKNWP 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  554 DHKTPDSAQpLLQLMLDV-EEDRLASQGRGPVVVHCSAGIGRTGCFIAtsigCQQLKEEG------VVDALSIVCQLRMD 626
Cdd:COG5599 179 DHGAISAEA-LKNLADLIdKKEKIKDPDKLLPVVHCRAGVGRTGTLIA----CLALSKSInalvqiTLSVEEIVIDMRTS 253

                       250
                ....*....|....
gi 1524085  627 RG-GMVQTSEQYEF 639
Cdd:COG5599 254 RNgGMVQTSEQLDV 267
 
Name Accession Description Interval E-value
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 417-642 1.98e-178

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: 505.99  E-value: 1.98e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  417 TKNRYKTILPNPLSRVCLRPKNVTDSLSTYINANYIRGYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKE 496
Cdd:cd14611   1 TKNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  497 KNEKCVLYWPEKRGIYGKVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRL 576
Cdd:cd14611  81 KNEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRL 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524085  577 ASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHH 642
Cdd:cd14611 161 ASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 419-642 8.92e-162

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: 463.41  E-value: 8.92e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  419 NRYKTILPNPLSRVCLrPKNVTDSLSTYINANYIRGYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKN 498
Cdd:cd14547   1 NRYKTILPNEHSRVCL-PSVDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  499 EKCVLYWPEKRG-IYGKVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLA 577
Cdd:cd14547  80 EKCAQYWPEEENeTYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEARQT 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524085  578 SQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHH 642
Cdd:cd14547 160 EPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 401-647 4.16e-156

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: 450.06  E-value: 4.16e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  401 PMNFVDPKEIDIPRHGTKNRYKTILPNPLSRVCLRPKNVTDSLSTYINANYIRGYSGKEKAFIATQGPMINTVDDFWQMV 480
Cdd:cd14612   1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQEEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  481 WQEDSPVIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDS 560
Cdd:cd14612  81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  561 AQPLLQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFV 640
Cdd:cd14612 161 AGPLLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                ....*..
gi 1524085  641 HHALCLY 647
Cdd:cd14612 241 HHTLALY 247
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 392-647 1.05e-145

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: 423.89  E-value: 1.05e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  392 LLQSEFMEIPMNFVDPKEIDIPRHGTKNRYKTILPNPLSRVCLRPKNVTDSLSTYINANYIRGYSGKEKAFIATQGPMIN 471
Cdd:cd14613   2 LLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYGGEEKVYIATQGPTVN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  472 TVDDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTS 551
Cdd:cd14613  82 TVGDFWRMVWQERSPIIVMITNIEEMNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTS 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  552 WPDHKTPDSAQPLLQLMLDVEEDR-LASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGM 630
Cdd:cd14613 162 WPDQKTPDNAPPLLQLVQEVEEARqQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGM 241

                       250
                ....*....|....*..
gi 1524085  631 VQTSEQYEFVHHALCLY 647
Cdd:cd14613 242 IQTCEQYQFVHHVLSLY 258
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
392-644 1.17e-104

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 318.45  E-value: 1.17e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085     392 LLQSEFMEIPMNFVDPKEIDI---PRHGTKNRYKTILPNPLSRVCLRPKNvtDSLSTYINANYIRGYSGKeKAFIATQGP 468
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKLKPPP--GEGSDYINASYIDGPNGP-KAYIATQGP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085     469 MINTVDDFWQMVWQEDSPVIVMITKLKEKN-EKCVLYWPEKRG---IYGKVEVLVISVNECDNYTIRNLVLK--QGSHTQ 542
Cdd:smart00194  78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGrEKCAQYWPDEEGeplTYGDITVTLKSVEKVDDYTIRTLEVTntGCSETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085     543 HVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRlaSQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQ 622
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQ--STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                          250       260
                   ....*....|....*....|..
gi 1524085     623 LRMDRGGMVQTSEQYEFVHHAL 644
Cdd:smart00194 236 LRSQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
417-644 2.35e-96

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 296.08  E-value: 2.35e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085    417 TKNRYKTILPNPLSRVCLRPknvTDSLSTYINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKE 496
Cdd:pfam00102   3 EKNRYKDVLPYDHTRVKLTG---DPGPSDYINASYIDGYK-KPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085    497 KN-EKCVLYWPEKRG---IYGKVEV-LVISVNECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLML 569
Cdd:pfam00102  79 KGrEKCAQYWPEEEGeslEYGDFTVtLKKEKEDEKDYTVRTLEVSngGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524085    570 DVEEDRLASQgRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:pfam00102 159 KVRKSSLDGR-SGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 446-642 2.84e-89

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: 276.47  E-value: 2.84e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSGKeKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKN-EKCVLYWPEKRG---IYGKVEVLVIS 521
Cdd:cd00047   1 YINASYIDGYRGP-KEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGrEKCERYWPEEGGkplEYGDITVTLVS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  522 VNECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRlaSQGRGPVVVHCSAGIGRTGCFI 599
Cdd:cd00047  80 EEELSDYTIRTLELSpkGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEA--RKPNGPIVVHCSAGVGRTGTFI 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 1524085  600 ATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHH 642
Cdd:cd00047 158 AIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 420-641 1.95e-72

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


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 233.40  E-value: 1.95e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  420 RYKTILPNPLSRVCLRPKNvTDSLSTYINANYIRGYSGKEKaFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEK-N 498
Cdd:cd14548   1 RYTNILPYDHSRVKLIPIN-EEEGSDYINANYIPGYNSPRE-FIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKgR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  499 EKCVLYWPEKR--GIYGKVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRl 576
Cdd:cd14548  79 VKCDHYWPFDQdpVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYI- 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524085  577 aSQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVH 641
Cdd:cd14548 158 -KQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 418-644 3.39e-70

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: 228.05  E-value: 3.39e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  418 KNRYKTILPNPLSRVCLRPKNVTDSlSTYINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEK 497
Cdd:cd14553   6 KNRYANVIAYDHSRVILQPIEGVPG-SDYINANYCDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEER 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  498 NE-KCVLYWPeKRG--IYGKVEVLVISVNECDNYTIRNLVL-KQGS-HTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 572
Cdd:cd14553  84 SRvKCDQYWP-TRGteTYGLIQVTLLDTVELATYTVRTFALhKNGSsEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524085  573 EdrLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd14553 163 A--CNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 446-641 3.81e-69

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: 224.15  E-value: 3.81e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEK-NEKCVLYWPeKRGI--YGKVEVLVISV 522
Cdd:cd14549   1 YINANYVDGYN-KARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERgRRKCDQYWP-KEGTetYGNIQVTLLST 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  523 NECDNYTIRNLVLK--------QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMldveedRLASQ----GRGPVVVHCSA 590
Cdd:cd14549  79 EVLATYTVRTFSLKnlklkkvkGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFV------RKSSAanppGAGPIVVHCSA 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 1524085  591 GIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVH 641
Cdd:cd14549 153 GVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 417-647 4.36e-69

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: 225.80  E-value: 4.36e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  417 TKNRYKTILPNPLSRVCLRPKNVTDSLSTYINANYIR------GYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVM 490
Cdd:cd14544   3 GKNRYKNILPFDHTRVILKDRDPNVPGSDYINANYIRnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVIVM 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  491 ITKLKEK-NEKCVLYWPEKRGI--YGKVEVLVISVNECDNYTIRNLVLK---QGSHTQHVKHYWYTSWPDHKTPDSAQPL 564
Cdd:cd14544  83 TTKEVERgKNKCVRYWPDEGMQkqYGPYRVQNVSEHDTTDYTLRELQVSkldQGDPIREIWHYQYLSWPDHGVPSDPGGV 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  565 LQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGV---VDALSIVCQLRMDRGGMVQTSEQYEFVH 641
Cdd:cd14544 163 LNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKFIY 242


                ....*.
gi 1524085  642 HALCLY 647
Cdd:cd14544 243 VAVAQY 248
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 417-641 3.16e-67

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: 221.47  E-value: 3.16e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  417 TKNRYKTILPNPLSRVCLRPKNvTDSLSTYINANYIRGYSGKeKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKE 496
Cdd:cd14543  31 EKNRYGDVLCLDQSRVKLPKRN-GDERTDYINANFMDGYKQK-NAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTRVVE 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  497 KNE-KCVLYWP---EKRGIYGKVEVLVISVNECDNYTIRNLVL--KQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLD 570
Cdd:cd14543 109 RGRvKCGQYWPleeGSSLRYGDLTVTNLSVENKEHYKKTTLEIhnTETDESRQVTHFQFTSWPDFGVPSSAAALLDFLGE 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  571 V-EEDRLASQGRG----------PVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEF 639
Cdd:cd14543 189 VrQQQALAVKAMGdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYF 268


                ..
gi 1524085  640 VH 641
Cdd:cd14543 269 CY 270
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 411-646 1.35e-62

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: 208.20  E-value: 1.35e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  411 DIPRHGTKNRYKTILPNPLSRVCLRPKNvTDSLSTYINANYIRGYSGKEKaFIATQGPMINTVDDFWQMVWQEDSPVIVM 490
Cdd:cd14614   8 DLPVNRCKNRYTNILPYDFSRVKLVSMH-EEEGSDYINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSQIIVM 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  491 ITKLKEKNE-KCVLYWP--EKRGIYGKVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTP--DSAQPLL 565
Cdd:cd14614  86 LTQCNEKRRvKCDHYWPftEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPtaNAAESIL 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  566 QLMLDVEEDRLASqgRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHALC 645
Cdd:cd14614 166 QFVQMVRQQAVKS--KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 243


                .
gi 1524085  646 L 646
Cdd:cd14614 244 L 244
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 419-640 5.72e-62

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 206.21  E-value: 5.72e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  419 NRYKTILPNPLSRVCLrpKNVTDSLSTYINANYIRGYSGKeKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKN 498
Cdd:cd14615   1 NRYNNVLPYDISRVKL--SVQSHSTDDYINANYMPGYNSK-KEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  499 E-KCVLYWPEKRGI-YGKVEVLVISVNECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEED 574
Cdd:cd14615  78 RtKCEEYWPSKQKKdYGDITVTMTSEIVLPEWTIRDFTVKnaQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524085  575 RLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFV 640
Cdd:cd14615 158 MKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 411-643 7.84e-60

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 200.83  E-value: 7.84e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  411 DIPRHGTKNRYKTILPNPLSRVCLRPKNVTDSlSTYINANYIRGYSGKeKAFIATQGPMINTVDDFWQMVWQEDSPVIVM 490
Cdd:cd14554   2 NLPCNKFKNRLVNILPYESTRVCLQPIRGVEG-SDYINASFIDGYRQR-GAYIATQGPLAETTEDFWRMLWEHNSTIIVM 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  491 ITKLKEKN-EKCVLYWPEKRGI-YGKVEVLVISVNECDNYTIRNLVLKQGSHTQ--HVKHYWYTSWPDHKTPDSAQPLLQ 566
Cdd:cd14554  80 LTKLREMGrEKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARDGQsrTVRQFQFTDWPEQGVPKSGEGFID 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1524085  567 LMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHA 643
Cdd:cd14554 160 FIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 446-642 7.99e-60

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: 199.78  E-value: 7.99e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKN-EKCVLYWPEKR--GIYGKVEVLVISV 522
Cdd:cd18533   1 YINASYITLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGrEKCDQYWPSGEyeGEYGDLTVELVSE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  523 NECD--NYTIRNLVLKQGSH-TQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFI 599
Cdd:cd18533  81 EENDdgGFIVREFELSKEDGkVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGTFI 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 1524085  600 ATSIGCQQLKE--------EGVVDA-LSIVCQLRMDRGGMVQTSEQYEFVHH 642
Cdd:cd18533 161 ALDSLLDELKRglsdsqdlEDSEDPvYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 418-644 1.62e-59

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: 199.87  E-value: 1.62e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  418 KNRYKTILPNPLSRVCLRPKNvTDSLSTYINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEK 497
Cdd:cd14630   6 KNRYGNIISYDHSRVRLQLLD-GDPHSDYINANYIDGYH-RPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  498 NE-KCVLYWPEKRGIYGKVEVLVISVNECDNYTIRNL-VLKQGSH-TQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEed 574
Cdd:cd14630  84 GRvKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFtVQKKGYHeIREIRQFHFTSWPDHGVPCYATGLLGFVRQVK-- 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  575 RLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd14630 162 FLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 413-644 9.55e-59

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: 199.11  E-value: 9.55e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  413 PRHGTKNRYKTILPNPLSRVCLRPKNVTDSL-STYINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMI 491
Cdd:cd17667  25 PDNKHKNRYINILAYDHSRVKLRPLPGKDSKhSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMI 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  492 TKLKEKNE-KCVLYWP-EKRGIYGKVEVLVIS--VNEC---DNYTIRNLVLKQGS--------HTQHVKHYWYTSWPDHK 556
Cdd:cd17667 104 TNLVEKGRrKCDQYWPtENSEEYGNIIVTLKStkIHACytvRRFSIRNTKVKKGQkgnpkgrqNERTVIQYHYTQWPDMG 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  557 TPDSAQPLLQLMldveedRLASQGR----GPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQ 632
Cdd:cd17667 184 VPEYALPVLTFV------RRSSAARtpemGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQ 257

                       250
                ....*....|..
gi 1524085  633 TSEQYEFVHHAL 644
Cdd:cd17667 258 TEEQYIFIHDAL 269
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 419-644 4.44e-58

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: 195.88  E-value: 4.44e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  419 NRYKTILPNPLSRVCLRPkNVTDSLSTYINANYIRGYsGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKN 498
Cdd:cd14619   1 NRFRNVLPYDWSRVPLKP-IHEEPGSDYINANYMPGY-WSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  499 E-KCVLYWP--EKRGIYGKVEVLVISVNECDNYTIRNLVLKQG--SHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE 573
Cdd:cd14619  79 RvKCEHYWPldYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVeeQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQ 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524085  574 DRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd14619 159 WLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 418-647 6.42e-58

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: 196.01  E-value: 6.42e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  418 KNRYKTILPNPLSRVCLRPKNVTDSLSTYINANYI-------RGYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVM 490
Cdd:cd14605   5 KNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIImpefetkCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVM 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  491 ITKLKEKNE-KCVLYWPEKRGI--YGKVEVLVISVNECDNYTIRNLVLK---QGSHTQHVKHYWYTSWPDHKTPDSAQPL 564
Cdd:cd14605  85 TTKEVERGKsKCVKYWPDEYALkeYGVMRVRNVKESAAHDYILRELKLSkvgQGNTERTVWQYHFRTWPDHGVPSDPGGV 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  565 LQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGV---VDALSIVCQLRMDRGGMVQTSEQYEFVH 641
Cdd:cd14605 165 LDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQYRFIY 244


                ....*.
gi 1524085  642 HALCLY 647
Cdd:cd14605 245 MAVQHY 250
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 446-646 8.23e-58

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: 193.98  E-value: 8.23e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKRGIYGKVEVLVISVNE 524
Cdd:cd14555   1 YINANYIDGYH-RPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRvKCSRYWPDDTEVYGDIKVTLVETEP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  525 CDNYTIRNLVL-KQGSHTQH-VKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASQGrgPVVVHCSAGIGRTGCFIATS 602
Cdd:cd14555  80 LAEYVVRTFALeRRGYHEIReVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAG--PIVVHCSAGAGRTGCYIVID 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 1524085  603 IGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL---CL 646
Cdd:cd14555 158 IMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIleaCL 204
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 419-644 5.14e-57

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: 192.85  E-value: 5.14e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  419 NRYKTILPNPLSRVCLRPKNvTDSLSTYINANYIRGYSGKEKaFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKN 498
Cdd:cd14618   1 NRYPHVLPYDHSRVRLSQLG-GEPHSDYINANFIPGYTSPQE-FIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  499 EK-CVLYWPEKRG--IYGKVEVLVISVNECDNYTIRNLVLKQGS--HTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE 573
Cdd:cd14618  79 RVlCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDlrKERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524085  574 DRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd14618 159 HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 446-647 6.94e-57

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: 191.82  E-value: 6.94e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSGKEK-AFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKRG----IYGKVEVLV 519
Cdd:cd14538   1 YINASHIRIPVGGDTyHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKvKCHRYWPDSLNkpliCGGRLEVSL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  520 ISVNECDNYTIR--NLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVeedRLASQGrGPVVVHCSAGIGRTGC 597
Cdd:cd14538  81 EKYQSLQDFVIRriSLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYM---RRIHNS-GPIVVHCSAGIGRTGV 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 1524085  598 FIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAlCLY 647
Cdd:cd14538 157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKA-CLE 205
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 418-644 2.55e-56

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 192.56  E-value: 2.55e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  418 KNRYKTILPNPLSRVCLRPKNVTDSlSTYINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEK 497
Cdd:cd14626  44 KNRYANVIAYDHSRVILTSVDGVPG-SDYINANYIDGYR-KQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEK 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  498 NE-KCVLYWPeKRG--IYGKVEVLVISVNECDNYTIRNLVL-KQGS-HTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 572
Cdd:cd14626 122 SRvKCDQYWP-IRGteTYGMIQVTLLDTVELATYSVRTFALyKNGSsEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVK 200

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524085  573 EDRLASQGrgPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd14626 201 ACNPPDAG--PMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 446-644 6.76e-56

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: 189.02  E-value: 6.76e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSGKEkAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKN-EKCVLYWPEKRGI-YGKVEVLVISVN 523
Cdd:cd14552   1 YINASFIDGYRQKD-AYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSqNKCAQYWPEDGSVsSGDITVELKDQT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  524 ECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASqGRGPVVVHCSAGIGRTGCFIAT 601
Cdd:cd14552  80 DYEDYTLRDFLVTkgKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQS-GNHPITVHCSAGAGRTGTFCAL 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 1524085  602 SIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd14552 159 STVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 446-648 1.20e-54

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: 185.67  E-value: 1.20e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSGkEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKE-KNEKCVLYWPEKRGIYGKVEVLVISVNE 524
Cdd:cd14558   1 YINASFIDGYWG-PKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEgDQEQCAQYWGDEKKTYGDIEVELKDTEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  525 CDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE---DRLASQGRG-PVVVHCSAGIGRTGCF 598
Cdd:cd14558  80 SPTYTVRVFEIThlKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQklpYKNSKHGRSvPIVVHCSDGSSRTGIF 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 1524085  599 IATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFvhhalcLYE 648
Cdd:cd14558 160 CALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQF------LYD 203
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 401-647 4.12e-54

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: 186.24  E-value: 4.12e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  401 PMNFVDPKEIDIPRHGTKNRYKTILPNPLSRVCLRPKNVTDSLSTYINANYIR----GYSGKEKAFIATQGPMINTVDDF 476
Cdd:cd14606   4 VKNLHQRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVKnqllGPDENAKTYIASQGCLEATVNDF 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  477 WQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKRGI--YGKVEVLVISVNECDNYTIRNL---VLKQGSHTQHVKHYWYT 550
Cdd:cd14606  84 WQMAWQENSRVIVMTTREVEKGRnKCVPYWPEVGMQraYGPYSVTNCGEHDTTEYKLRTLqvsPLDNGELIREIWHYQYL 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  551 SWPDHKTPDSAQPLLQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGV---VDALSIVCQLRMDR 627
Cdd:cd14606 164 SWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQR 243

                       250       260
                ....*....|....*....|
gi 1524085  628 GGMVQTSEQYEFVHHALCLY 647
Cdd:cd14606 244 SGMVQTEAQYKFIYVAIAQF 263
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 418-644 9.44e-54

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: 186.07  E-value: 9.44e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  418 KNRYKTILPNPLSRVCLRPKNVTDSlSTYINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEK 497
Cdd:cd14625  50 KNRYANVIAYDHSRVILQPIEGIMG-SDYINANYIDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEK 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  498 NE-KCVLYWPeKRGI--YGKVEVLVISVNECDNYTIRNLVLKQ--GSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 572
Cdd:cd14625 128 SRiKCDQYWP-SRGTetYGMIQVTLLDTIELATFCVRTFSLHKngSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVK 206

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524085  573 EdrLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd14625 207 T--CNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 418-644 1.26e-53

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: 185.25  E-value: 1.26e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  418 KNRYKTILPNPLSRVCLRPKNvTDSLSTYINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEK 497
Cdd:cd14633  43 KNRYGNIIAYDHSRVRLQPIE-GETSSDYINGNYIDGYH-RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEV 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  498 NE-KCVLYWPEKRGIYGKVEVLVISVNECDNYTIRNL-VLKQGSH-TQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEED 574
Cdd:cd14633 121 GRvKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFaVEKRGVHeIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSK 200

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  575 RLASQGrgPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd14633 201 SPPNAG--PLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 446-644 1.27e-53

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: 182.87  E-value: 1.27e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWP-EKRGIYGKVEVL----- 518
Cdd:cd17668   1 YINANYVDGYN-KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRrKCDQYWPaDGSEEYGNFLVTqksvq 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  519 VISVNECDNYTIRNLVLKQGSHT-----QHVKHYWYTSWPDHKTPDSAQPLLQLMldveedRLASQGR----GPVVVHCS 589
Cdd:cd17668  80 VLAYYTVRNFTLRNTKIKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYTLPVLTFV------RKASYAKrhavGPVVVHCS 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 1524085  590 AGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd17668 154 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 419-641 1.51e-53

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


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 183.58  E-value: 1.51e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  419 NRYKTILPNPLSRVCLRPKNvTDSLSTYINANYIRGYSGKeKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKN 498
Cdd:cd14617   1 NRYNNILPYDSTRVKLSNVD-DDPCSDYINASYIPGNNFR-REYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  499 E-KCVLYWPEKRG--IYGKVEVLVISVNECDNYTIRNLVL---KQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 572
Cdd:cd14617  79 RvKCDHYWPADQDslYYGDLIVQMLSESVLPEWTIREFKIcseEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524085  573 EDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVH 641
Cdd:cd14617 159 DYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 446-642 2.02e-53

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: 182.24  E-value: 2.02e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSGkEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKRG---IYGKVEVLVIS 521
Cdd:cd14542   1 YINANFIKGVSG-SKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKkKCERYWPEEGEeqlQFGPFKISLEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  522 V-NECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEedRLASQGRGPVVVHCSAGIGRTGCFIA 600
Cdd:cd14542  80 EkRVGPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVR--DYQGSEDVPICVHCSAGCGRTGTICA 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 1524085  601 TSIGCQQLKEEGVVDALS---IVCQLRMDRGGMVQTSEQYEFVHH 642
Cdd:cd14542 158 IDYVWNLLKTGKIPEEFSlfdLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 446-641 2.32e-53

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: 181.95  E-value: 2.32e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSGKEKaFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWP---EKRGIYGKVEVLVIS 521
Cdd:cd14557   1 YINASYIDGFKEPRK-YIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRnKCAQYWPsmeEGSRAFGDVVVKINE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  522 VNECDNYTIRNLVL---KQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVeeDRLASQGRGPVVVHCSAGIGRTGCF 598
Cdd:cd14557  80 EKICPDYIIRKLNInnkKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRV--NAFNNFFSGPIVVHCSAGVGRTGTY 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 1524085  599 IATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVH 641
Cdd:cd14557 158 IGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 446-646 2.67e-53

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 182.17  E-value: 2.67e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKRGIYGKVEVLVISVNE 524
Cdd:cd14632   1 YINANYIDGYH-RSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRvKCSKYWPDDSDTYGDIKITLLKTET 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  525 CDNYTIRNLVL-KQGSHTQH-VKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDrlASQGRGPVVVHCSAGIGRTGCFIATS 602
Cdd:cd14632  80 LAEYSVRTFALeRRGYSARHeVKQFHFTSWPEHGVPYHATGLLAFIRRVKAS--TPPDAGPVVVHCSAGAGRTGCYIVLD 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 1524085  603 IGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL---CL 646
Cdd:cd14632 158 VMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIleaCL 204
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 431-644 3.84e-53

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: 182.14  E-value: 3.84e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  431 RVCLRPKNvTDSLSTYINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKR 509
Cdd:cd14631   1 RVILQPVE-DDPSSDYINANYIDGYQ-RPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRvKCYKYWPDDT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  510 GIYGKVEVLVISVNECDNYTIRNLVLKQGSHTQ--HVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRlaSQGRGPVVVH 587
Cdd:cd14631  79 EVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEirEVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSN--PPSAGPIVVH 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524085  588 CSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd14631 157 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 411-647 2.69e-52

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: 182.24  E-value: 2.69e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  411 DIPRHGTKNRYKTILPNPLSRVCLRPKNVTDSlSTYINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVM 490
Cdd:cd14628  48 NLPCNKFKNRLVNIMPYESTRVCLQPIRGVEG-SDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  491 ITKLKEKN-EKCVLYWPEKRGiyGKVEVLVisVNECDNYTIRNLVLKQ-------GSHTQHVKHYWYTSWPDHKTPDSAQ 562
Cdd:cd14628 126 LTKLREMGrEKCHQYWPAERS--ARYQYFV--VDPMAEYNMPQYILREfkvtdarDGQSRTVRQFQFTDWPEQGVPKSGE 201

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  563 PLLQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHH 642
Cdd:cd14628 202 GFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYR 281


                ....*
gi 1524085  643 ALCLY 647
Cdd:cd14628 282 AALEY 286
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 411-647 5.42e-52

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


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 181.47  E-value: 5.42e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  411 DIPRHGTKNRYKTILPNPLSRVCLRPKNVTDSlSTYINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVM 490
Cdd:cd14627  49 NLPCNKFKNRLVNIMPYETTRVCLQPIRGVEG-SDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWENNSTIVVM 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  491 ITKLKEKN-EKCVLYWPEKRGiyGKVEVLVisVNECDNYTIRNLVLKQ-------GSHTQHVKHYWYTSWPDHKTPDSAQ 562
Cdd:cd14627 127 LTKLREMGrEKCHQYWPAERS--ARYQYFV--VDPMAEYNMPQYILREfkvtdarDGQSRTVRQFQFTDWPEQGVPKSGE 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  563 PLLQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHH 642
Cdd:cd14627 203 GFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQ 282


                ....*
gi 1524085  643 ALCLY 647
Cdd:cd14627 283 AALEY 287
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 421-644 2.03e-51

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: 177.83  E-value: 2.03e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  421 YKTILPNPLSRVCLRPKNvTDSLSTYINANYIRGYSGKEKaFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKE-KNE 499
Cdd:cd14620   1 YPNILPYDHSRVILSQLD-GIPCSDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKErKEE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  500 KCVLYWPEKRG-IYGKVEVLVISVNECDNYTIRNLVLKQGSH-----TQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE 573
Cdd:cd14620  79 KCYQYWPDQGCwTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPdgckaPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524085  574 drLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd14620 159 --VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 411-647 3.15e-51

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: 179.54  E-value: 3.15e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  411 DIPRHGTKNRYKTILPNPLSRVCLRPKNVTDSlSTYINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVM 490
Cdd:cd14629  49 NLPCNKFKNRLVNIMPYELTRVCLQPIRGVEG-SDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  491 ITKLKEKN-EKCVLYWPEKRGiyGKVEVLVisVNECDNYTIRNLVLKQ-------GSHTQHVKHYWYTSWPDHKTPDSAQ 562
Cdd:cd14629 127 LTKLREMGrEKCHQYWPAERS--ARYQYFV--VDPMAEYNMPQYILREfkvtdarDGQSRTIRQFQFTDWPEQGVPKTGE 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  563 PLLQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHH 642
Cdd:cd14629 203 GFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYR 282


                ....*
gi 1524085  643 ALCLY 647
Cdd:cd14629 283 AALEY 287
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 418-639 7.03e-51

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: 176.43  E-value: 7.03e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  418 KNRYKTILPNPLSRVCLRPKNvtdSLSTYINANYIRGYSGKeKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEK 497
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVKLKQ---GDNDYINASLVEVEEAK-RSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  498 NE-KCVLYWPEKRGIYGKVE-----VLVISVNECDNYTIRNLVL--KQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLML 569
Cdd:cd14545  77 GQiKCAQYWPQGEGNAMIFEdtglkVTLLSEEDKSYYTVRTLELenLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524085  570 DVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGV--VDALSIVCQLRMDRGGMVQTSEQYEF 639
Cdd:cd14545 157 KVRESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 418-644 1.80e-50

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: 176.55  E-value: 1.80e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  418 KNRYKTILPNPLSRVCLRPKnVTDSLSTYINANYIRGYSGkEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEK 497
Cdd:cd14603  33 KNRYKDILPYDQTRVILSLL-QEEGHSDYINANFIKGVDG-SRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIEM 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  498 -NEKCVLYWPEKRGI--YGKVEVLVISVNECDNYTI-RNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEe 573
Cdd:cd14603 111 gKKKCERYWAQEQEPlqTGPFTITLVKEKRLNEEVIlRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELAR- 189

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524085  574 dRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSI---VCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd14603 190 -RLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIfdvVLEMRKQRPAAVQTEEQYEFLYHTV 262
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 418-644 2.13e-50

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: 176.85  E-value: 2.13e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  418 KNRYKTILPNPLSRVCLRPKNVTDSlSTYINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEK 497
Cdd:cd14624  50 KNRYANVIAYDHSRVLLSAIEGIPG-SDYINANYIDGYR-KQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEER 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  498 NE-KCVLYWPEkRGI--YGKVEVLVISVNECDNYTIRNLVL-KQGS-HTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 572
Cdd:cd14624 128 SRvKCDQYWPS-RGTetYGLIQVTLLDTVELATYCVRTFALyKNGSsEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK 206

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524085  573 EdrLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd14624 207 T--CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 446-641 1.58e-49

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: 171.73  E-value: 1.58e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSGKEkAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEK-NEKCVLYWPEKRGI-YGKVEVLVISVN 523
Cdd:cd14622   2 YINASFIDGYRQKD-YFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEReQEKCVQYWPSEGSVtHGEITIEIKNDT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  524 ECDNYTIRNLVL--KQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASqGRGPVVVHCSAGIGRTGCFIAT 601
Cdd:cd14622  81 LLETISIRDFLVtyNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQT-GNHPIVVHCSAGAGRTGTFIAL 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 1524085  602 SIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVH 641
Cdd:cd14622 160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 446-640 2.47e-49

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: 171.47  E-value: 2.47e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEK-NEKCVLYWPEKRG-IYGKVEV-LVISV 522
Cdd:cd14546   1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENgVKQCARYWPEEGSeVYHIYEVhLVSEH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  523 NECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEdrlASQGRG-PVVVHCSAGIGRTGCFI 599
Cdd:cd14546  81 IWCDDYLVRSFYLKnlQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNK---SYRGRScPIVVHCSDGAGRTGTYI 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 1524085  600 ATSIGCQQL----KEegvVDALSIVCQLRMDRGGMVQTSEQYEFV 640
Cdd:cd14546 158 LIDMVLNRMakgaKE---IDIAATLEHLRDQRPGMVKTKDQFEFV 199
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 446-647 3.35e-49

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: 171.49  E-value: 3.35e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIR-GYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKN-EKCVLYWPEKRG-----IYGKVEVL 518
Cdd:cd14540   1 YINASHITaTVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGrEKCFRYWPTLGGehdalTFGEYKVS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  519 VISVNECDNYTIRNLVLKQGSHTQH--VKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASQGRG-------PVVVHCS 589
Cdd:cd14540  81 TKFSVSSGCYTTTGLRVKHTLSGQSrtVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDVaghnrnpPTLVHCS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 1524085  590 AGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHALCLY 647
Cdd:cd14540 161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 446-641 9.92e-49

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: 169.71  E-value: 9.92e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSGKEKaFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKE-KNEKCVLYWPeKRG--IYGKVEVLVISV 522
Cdd:cd14551   1 YINASYIDGYQEKNK-FIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKErKEKKCSQYWP-DQGcwTYGNLRVRVEDT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  523 NECDNYTIRNLVLKQ-----GSHTQH-VKHYWYTSWPDHKTPDSAQPLLQLMLDVEEdrLASQGRGPVVVHCSAGIGRTG 596
Cdd:cd14551  79 VVLVDYTTRKFCIQKvnrgiGEKRVRlVTQFHFTSWPDFGVPFTPIGMLKFLKKVKS--ANPPRAGPIVVHCSAGVGRTG 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 1524085  597 CFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVH 641
Cdd:cd14551 157 TFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 419-641 1.45e-48

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: 169.70  E-value: 1.45e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  419 NRYKTILPNPLSRVCLRPKNVTDSlSTYINANYIRGYSGKEKaFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKN 498
Cdd:cd14616   1 NRFPNIKPYNNNRVKLIADAGVPG-SDYINASYISGYLCPNE-FIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  499 E-KCVLYWPEKR---GIYGKVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEED 574
Cdd:cd14616  79 RiRCHQYWPEDNkpvTVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRAS 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1524085  575 RlaSQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVH 641
Cdd:cd14616 159 R--AHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 446-645 2.08e-48

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: 169.05  E-value: 2.08e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANY----IRGySGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPE--KRGIYGKVEVL 518
Cdd:cd14541   2 YINANYvnmeIPG-SGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRvKCHQYWPDlgETMQFGNLQIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  519 VISVNECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASQgrGPVVVHCSAGIGRTG 596
Cdd:cd14541  81 CVSEEVTPSFAFREFILTntNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMV--EPTVVHCSAGIGRTG 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 1524085  597 CFIA--TSIGCQQLKEEgvVDALSIVCQLRMDRGGMVQTSEQYEFVHHALC 645
Cdd:cd14541 159 VLITmeTAMCLIEANEP--VYPLDIVRTMRDQRAMLIQTPSQYRFVCEAIL 207
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 418-644 3.12e-48

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: 171.36  E-value: 3.12e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  418 KNRYKTILPNPLSRVCLRP-KNVTDSlsTYINANYIRGYSGKEKaFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKE 496
Cdd:cd14621  55 KNRYVNILPYDHSRVHLTPvEGVPDS--DYINASFINGYQEKNK-FIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKE 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  497 KNE-KCVLYWPEKR-GIYGKVEVLVISVNECDNYTIRNLVLKQ-----GSHTQH-VKHYWYTSWPDHKTPDSAQPLLQLM 568
Cdd:cd14621 132 RKEcKCAQYWPDQGcWTYGNIRVSVEDVTVLVDYTVRKFCIQQvgdvtNKKPQRlITQFHFTSWPDFGVPFTPIGMLKFL 211

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524085  569 LDVEEdrLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd14621 212 KKVKN--CNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQAL 285
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 418-647 3.65e-48

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: 169.24  E-value: 3.65e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  418 KNRYKTILPNPLSRVCLRPKNvtdslsTYINANYIRGYSGKEK-AFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKE 496
Cdd:cd14597   6 KNRYKNILPYDTTRVPLGDEG------GYINASFIKMPVGDEEfVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  497 KNE-KCVLYWPEKRG----IYGKVEVLVISVNECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLML 569
Cdd:cd14597  80 GGKiKCQRYWPEILGkttmVDNRLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTPSQPEQLLTFIS 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1524085  570 DVEEDRLAsqgrGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHALcLY 647
Cdd:cd14597 160 YMRHIHKS----GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI-LY 232
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 446-641 3.82e-48

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: 167.97  E-value: 3.82e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSGKeKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPE-KRGIYGKVEVLVISVNE 524
Cdd:cd14556   1 YINAALLDSYKQP-AAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDeGSGTYGPIQVEFVSTTI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  525 CDNYTIRNLVLKQGSHTQH----VKHYWYTSWPDH-KTPDSAQPLLQLMLDVEEDRLASqGRGPVVVHCSAGIGRTGCFI 599
Cdd:cd14556  80 DEDVISRIFRLQNTTRPQEgyrmVQQFQFLGWPRDrDTPPSKRALLKLLSEVEKWQEQS-GEGPIVVHCLNGVGRSGVFC 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 1524085  600 ATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVH 641
Cdd:cd14556 159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 420-641 7.50e-48

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: 167.91  E-value: 7.50e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  420 RYKTILPNPLSRVCLrPKNVTDSLSTYINANYIRGYSGKEkAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEK-N 498
Cdd:cd14623   1 RVLQIIPYEFNRVII-PVKRGEENTDYVNASFIDGYRQKD-SYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERgQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  499 EKCVLYWPEKRGI-YGKVEVLVISVNECDNYTIRNLVL--KQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDR 575
Cdd:cd14623  79 EKCAQYWPSDGSVsYGDITIELKKEEECESYTVRDLLVtnTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524085  576 LASqGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVH 641
Cdd:cd14623 159 QQS-GNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCY 223
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 446-644 1.76e-46

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: 163.38  E-value: 1.76e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSGKEKAF-IATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKRGIYGKVEVLVISVN 523
Cdd:cd14596   1 YINASYITMPVGEEELFyIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKvKCHRYWPETLQEPMELENYQLRLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  524 EC---DNYTIR--NLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEedrlASQGRGPVVVHCSAGIGRTGCF 598
Cdd:cd14596  81 NYqalQYFIIRiiKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMR----KVHNTGPIVVHCSAGIGRAGVL 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 1524085  599 IATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd14596 157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 412-644 8.33e-46

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: 163.87  E-value: 8.33e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  412 IPRHGTKNRYKTILPNPLSRVCLrpknvtDSLSTYINANYIR---GYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVI 488
Cdd:cd14600  37 LPQNMDKNRYKDVLPYDATRVVL------QGNEDYINASYVNmeiPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLI 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  489 VMITKLKEKNE-KCVLYWPEKRGI--YGKVEVLVISVNECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQP 563
Cdd:cd14600 111 VMLTTLTERGRtKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTntQTGEERTVTHLQYVAWPDHGVPDDSSD 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  564 LLQLMLDVEEDRLASQgrgPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHA 643
Cdd:cd14600 191 FLEFVNYVRSKRVENE---PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEA 267


                .
gi 1524085  644 L 644
Cdd:cd14600 268 I 268
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 404-639 8.60e-46

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


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 164.46  E-value: 8.60e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  404 FVDPKEIDIPrhgtKNRYKTILPNPLSRVCLRPKNVTDSlSTYINANYIRGYSGKEKAFIATQGPMINTVDDFWQMVWQE 483
Cdd:cd14610  37 NVAQREENVQ----KNRSLAVLPYDHSRIILKAENSHSH-SDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWES 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  484 DSPVIVMITKLKEKN-EKCVLYWP-EKRGIYGKVEVLVISVN-ECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTP 558
Cdd:cd14610 112 GCVVIVMLTPLAENGvKQCYHYWPdEGSNLYHIYEVNLVSEHiWCEDFLVRSFYLKnlQTNETRTVTQFHFLSWNDQGVP 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  559 DSAQPLLQLMLDVEEdrlASQGRG-PVVVHCSAGIGRTGCFIATSIGCQQL-KEEGVVDALSIVCQLRMDRGGMVQTSEQ 636
Cdd:cd14610 192 ASTRSLLDFRRKVNK---CYRGRScPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQ 268


                ...
gi 1524085  637 YEF 639
Cdd:cd14610 269 FEF 271
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 418-651 1.31e-44

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: 161.64  E-value: 1.31e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  418 KNRYKTILPNPLSRVCLRPKnVTDSLSTYINANYIRGYSGKeKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEK 497
Cdd:cd14604  60 KNRYKDILPFDHSRVKLTLK-TSSQDSDYINANFIKGVYGP-KAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEM 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  498 N-EKCVLYWP---EKRGIYGKVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTP---DSAQPLLQLMLD 570
Cdd:cd14604 138 GrKKCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPssfDSILDMISLMRK 217

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  571 VEEdrlasQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGV---VDALSIVCQLRMDRGGMVQTSEQYEFVHHALC-L 646
Cdd:cd14604 218 YQE-----HEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAqL 292


                ....*
gi 1524085  647 YESRL 651
Cdd:cd14604 293 FEKQL 297
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 418-644 2.30e-44

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


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 158.85  E-value: 2.30e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  418 KNRYKTILPNPLSRVCLRPKnVTDSLSTYINANYIRGYSGKeKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEK 497
Cdd:cd14602   1 KNRYKDILPYDHSRVELSLI-TSDEDSDYINANFIKGVYGP-RAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  498 -NEKCVLYWP---EKRGIYGKVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE 573
Cdd:cd14602  79 gKKKCERYWAepgEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524085  574 drLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKeEGVV----DALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd14602 159 --YQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 412-644 2.74e-44

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: 159.81  E-value: 2.74e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  412 IPRHGTKNRYKTILPNPLSRVCLRPKNvtdslSTYINANYIRgYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMI 491
Cdd:cd14608  22 LPKNKNRNRYRDVSPFDHSRIKLHQED-----NDYINASLIK-MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVML 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  492 TKLKEKNE-KCVLYWP---EKRGIY--GKVEVLVISVNECDNYTIRNLVLKQGS--HTQHVKHYWYTSWPDHKTPDSAQP 563
Cdd:cd14608  96 NRVMEKGSlKCAQYWPqkeEKEMIFedTNLKLTLISEDIKSYYTVRQLELENLTtqETREILHFHYTTWPDFGVPESPAS 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  564 LLQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIgC----QQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEF 639
Cdd:cd14608 176 FLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADT-ClllmDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 254


                ....*
gi 1524085  640 VHHAL 644
Cdd:cd14608 255 SYLAV 259
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 394-644 9.96e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 154.42  E-value: 9.96e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085   394 QSEFMEIPMNFVDPKEIDiPRHGTKNRYKTILPNPLSRVCLRPKN----------------VT--DSLSTYINANYIRGY 455
Cdd:PHA02746  31 HAEVMDIPIRGTTNHFLK-KENLKKNRFHDIPCWDHSRVVINAHEslkmfdvgdsdgkkieVTseDNAENYIHANFVDGF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085   456 SGKEKaFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPEKRG---IYGKVEVLVISVNECDNYTIRN 532
Cdd:PHA02746 110 KEANK-FICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKEEDselAFGRFVAKILDIIEELSFTKTR 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085   533 LVL--KQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLA--------SQGRGPVVVHCSAGIGRTGCFIATS 602
Cdd:PHA02746 189 LMItdKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAElikqadndPQTLGPIVVHCSAGIGRAGTFCAID 268

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 1524085   603 IGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:PHA02746 269 NALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 418-639 1.03e-41

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: 152.88  E-value: 1.03e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  418 KNRYKTILPNPLSRVCLRPKnVTDSLSTYINANYIRGYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEK 497
Cdd:cd14609  45 KNRNPDFVPYDHARIKLKAE-SNPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVED 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  498 NEK-CVLYWP-EKRGIYGKVEVLVISVN-ECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 572
Cdd:cd14609 124 GVKqCDRYWPdEGSSLYHIYEVNLVSEHiWCEDFLVRSFYLKnvQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVN 203

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  573 EdrlASQGRG-PVVVHCSAGIGRTGCFIATSIGCQQLKeEGV--VDALSIVCQLRMDRGGMVQTSEQYEF 639
Cdd:cd14609 204 K---CYRGRScPIIVHCSDGAGRTGTYILIDMVLNRMA-KGVkeIDIAATLEHVRDQRPGMVRTKDQFEF 269
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 446-639 6.75e-41

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: 148.00  E-value: 6.75e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIR-GYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNE--KCVLYWPEKRG---IYGKVEVLV 519
Cdd:cd17658   1 YINASLVEtPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStaKCADYFPAEENesrEFGRISVTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  520 ISVNECDN-YTIRNLVLKQGSHTQ---HVKHYWYTSWPDHKTPDSAQPLLQLmldVEEDRLASQGRGPVVVHCSAGIGRT 595
Cdd:cd17658  81 KKLKHSQHsITLRVLEVQYIESEEpplSVLHIQYPEWPDHGVPKDTRSVREL---LKRLYGIPPSAGPIVVHCSAGIGRT 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 1524085  596 GCFIATSIGCQQLKeEGVVDALSI---VCQLRMDRGGMVQTSEQYEF 639
Cdd:cd17658 158 GAYCTIHNTIRRIL-EGDMSAVDLsktVRKFRSQRIGMVQTQDQYIF 203
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 395-644 1.12e-40

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: 150.15  E-value: 1.12e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  395 SEFMEIPMNFVDP--KEIDIPRHGTKNRYKTILPNPLSRVCLRPKNvtDSLSTYINANYIR-GYSGKEKAFIATQGPMIN 471
Cdd:cd14599  16 TEYEQIPKKKADGvfTTATLPENAERNRIREVVPYEENRVELVPTK--ENNTGYINASHIKvTVGGEEWHYIATQGPLPH 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  472 TVDDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPE-----KRGIYGKVEVLVISVNECDNYTIRNLVLKQ--GSHTQH 543
Cdd:cd14599  94 TCHDFWQMVWEQGVNVIAMVTAEEEGGRsKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERT 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  544 VKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASQG--------RGPVVVHCSAGIGRTGCFIATS--IGCQQLKEEgv 613
Cdd:cd14599 174 VWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSmldstkncNPPIVVHCSAGVGRTGVVILTElmIGCLEHNEK-- 251

                       250       260       270
                ....*....|....*....|....*....|.
gi 1524085  614 VDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd14599 252 VEVPVMLRHLREQRMFMIQTIAQYKFVYQVL 282
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 446-641 1.29e-40

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: 147.15  E-value: 1.29e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVM-ITKLKEKNEKCVLYWPEKRG---IYGKVEVLVIS 521
Cdd:cd14539   1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMlVSEQENEKQKVHRYWPTERGqalVYGAITVSLQS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  522 VNECDNYTIR--NLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASQG-RGPVVVHCSAGIGRTGCF 598
Cdd:cd14539  81 VRTTPTHVERiiSIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSlQTPIVVHCSSGVGRTGAF 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 1524085  599 IATSIGCQQLKEE-GVVDALSIVCQLRMDRGGMVQTSEQYEFVH 641
Cdd:cd14539 161 CLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 446-648 1.88e-40

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: 147.01  E-value: 1.88e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIR---GYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKRG--IYGKVEVLV 519
Cdd:cd14601   2 YINANYINmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRvKCHQYWPEPSGssSYGGFQVTC 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  520 ISVNECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRlaSQGRGPVVVHCSAGIGRTGC 597
Cdd:cd14601  82 HSEEGNPAYVFREMTLTnlEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKR--AGKDEPVVVHCSAGIGRTGV 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 1524085  598 FIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHA-LCLYE 648
Cdd:cd14601 160 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAiLKVYE 211
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 417-647 5.40e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 149.00  E-value: 5.40e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085   417 TKNRYKTILPNPLSRVCLRpknVTDSLSTYINANYIRGYSGKEKaFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKE 496
Cdd:PHA02742  54 KKCRYPDAPCFDRNRVILK---IEDGGDDFINASYVDGHNAKGR-FICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085   497 KN-EKCVLYW-PEKRG--IYGKVEVLVISVNECDNYTIRNLVLKQGS--HTQHVKHYWYTSWPDHKTPDSAQPLLQLMLD 570
Cdd:PHA02742 130 DGkEACYPYWmPHERGkaTHGEFKIKTKKIKSFRNYAVTNLCLTDTNtgASLDIKHFAYEDWPHGGLPRDPNKFLDFVLA 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085   571 VEEDRLASQ---------GRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVH 641
Cdd:PHA02742 210 VREADLKADvdikgenivKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289


                 ....*.
gi 1524085   642 HALCLY 647
Cdd:PHA02742 290 FIVLIF 295
PHA02738 PHA02738
hypothetical protein; Provisional
 419-647 3.67e-39

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 146.99  E-value: 3.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085   419 NRYKTILPNPLSRVCL-RPKNVTDslstYINANYIRGYSGKEKaFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEK 497
Cdd:PHA02738  53 NRYLDAVCFDHSRVILpAERNRGD----YINANYVDGFEYKKK-FICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEN 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085   498 N-EKCVLYWPEKRG---IYGKVEVLVISVNECDNYTIRNLVLKQG-SHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 572
Cdd:PHA02738 128 GrEKCFPYWSDVEQgsiRFGKFKITTTQVETHPHYVKSTLLLTDGtSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVR 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085   573 -------EDRLASQGRG----PVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVH 641
Cdd:PHA02738 208 qcqkelaQESLQIGHNRlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCY 287


                 ....*.
gi 1524085   642 HALCLY 647
Cdd:PHA02738 288 RAVKRY 293
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 413-644 5.46e-39

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: 144.72  E-value: 5.46e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  413 PRHGTKNRYKTILPNPLSRVCLRpknvtDSLSTYINANYIRgYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMIT 492
Cdd:cd14607  22 PENRNRNRYRDVSPYDHSRVKLQ-----NTENDYINASLVV-IEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLN 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  493 KLKEKN-EKCVLYWP---EKRGIYGKVEVLVISVNE--CDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPL 564
Cdd:cd14607  96 RIVEKDsVKCAQYWPtdeEEVLSFKETGFSVKLLSEdvKSYYTVHLLQLEniNSGETRTISHFHYTTWPDFGVPESPASF 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  565 LQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCF--IATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHH 642
Cdd:cd14607 176 LNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFslVDTCLVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLRFSYM 255


                ..
gi 1524085  643 AL 644
Cdd:cd14607 256 AV 257
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
403-639 3.76e-37

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 140.23  E-value: 3.76e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  403 NFVDPKEIDIPRHGTKNRYKTILPNPLSRVclRPKNVtdslstYINANYIRGysGKEKAFIATQGPMINTVDDFWQMVWQ 482
Cdd:COG5599  30 SHNDPQYLQNINGSPLNRFRDIQPYKETAL--RANLG------YLNANYIQV--IGNHRYIATQYPLEEQLEDFFQMLFD 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  483 EDSPVIVMIT---KLKEKNEKCVLYWPEKrGIYGK--VEVLVISVNEC-DNYTIRNLVLKQ---GSHTQHVKHYWYTSWP 553
Cdd:COG5599 100 NNTPVLVVLAsddEISKPKVKMPVYFRQD-GEYGKyeVSSELTESIQLrDGIEARTYVLTIkgtGQKKIEIPVLHVKNWP 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  554 DHKTPDSAQpLLQLMLDV-EEDRLASQGRGPVVVHCSAGIGRTGCFIAtsigCQQLKEEG------VVDALSIVCQLRMD 626
Cdd:COG5599 179 DHGAISAEA-LKNLADLIdKKEKIKDPDKLLPVVHCRAGVGRTGTLIA----CLALSKSInalvqiTLSVEEIVIDMRTS 253

                       250
                ....*....|....
gi 1524085  627 RG-GMVQTSEQYEF 639
Cdd:COG5599 254 RNgGMVQTSEQLDV 267
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 544-644 3.80e-37

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 134.02  E-value: 3.80e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085     544 VKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQL-KEEGVVDALSIVCQ 622
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDTVKE 81

                           90       100
                   ....*....|....*....|..
gi 1524085     623 LRMDRGGMVQTSEQYEFVHHAL 644
Cdd:smart00012  82 LRSQRPGMVQTEEQYLFLYRAL 103
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
544-644 3.80e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 134.02  E-value: 3.80e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085     544 VKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQL-KEEGVVDALSIVCQ 622
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDTVKE 81

                           90       100
                   ....*....|....*....|..
gi 1524085     623 LRMDRGGMVQTSEQYEFVHHAL 644
Cdd:smart00404  82 LRSQRPGMVQTEEQYLFLYRAL 103
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 413-641 6.81e-37

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 140.52  E-value: 6.81e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085   413 PRHGTKNRYKTILPNPLSRVCLRPKnvTDSLSTYINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMIT 492
Cdd:PHA02747  49 PENQPKNRYWDIPCWDHNRVILDSG--GGSTSDYIHANWIDGFE-DDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLT 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085   493 KLKEKN--EKCVLYW-PEKRGIYG----KVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLL 565
Cdd:PHA02747 126 PTKGTNgeEKCYQYWcLNEDGNIDmedfRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFI 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085   566 QLMLDVEEDRLAS--------QGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQY 637
Cdd:PHA02747 206 KFIKIIDINRKKSgklfnpkdALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285


                 ....
gi 1524085   638 EFVH 641
Cdd:PHA02747 286 LFIQ 289
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 446-644 2.98e-36

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: 135.87  E-value: 2.98e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIR-GYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEK-NEKCVLYWP-----EKRGIYGKVEVL 518
Cdd:cd14598   1 YINASHIKvTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGgREKSFRYWPrlgsrHNTVTYGRFKIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  519 VISVNECDNYTIRNLVLKQ--GSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASQG-------RGPVVVHCS 589
Cdd:cd14598  81 TRFRTDSGCYATTGLKIKHllTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNStidpkspNPPVLVHCS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 1524085  590 AGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd14598 161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 446-641 2.28e-33

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


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 127.06  E-value: 2.28e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLkEKNEKCVLYWPEK-RGIYGKVEVLVISVN- 523
Cdd:cd14634   1 YINAALMDSHK-QPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM-DAAQLCMQYWPEKtSCCYGPIQVEFVSADi 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  524 ECDN----YTIRNLVLKQGSHtQHVKHYWYTSWPDHK-TPDSAQPLLQLMLDVEEDRLASQGR-GPVVVHCSAGIGRTGC 597
Cdd:cd14634  79 DEDIisriFRICNMARPQDGY-RIVQHLQYIGWPAYRdTPPSKRSILKVVRRLEKWQEQYDGReGRTVVHCLNGGGRSGT 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 1524085  598 FIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVH 641
Cdd:cd14634 158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVY 201
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 446-639 1.33e-32

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: 124.74  E-value: 1.33e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLkEKNEKCVLYWPEKR--------GIYGKVEV 517
Cdd:cd14550   1 YINASYLQGYR-RSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNEDEPIYWPTKEkplecetfKVTLSGED 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  518 LVISVNECDnYTIRNLVL--KQGSHTQHVKHYWYTSWPDHKTPDSAQplLQLMLDVEEDrlASQGRGPVVVHCSAGIGRT 595
Cdd:cd14550  79 HSCLSNEIR-LIVRDFILesTQDDYVLEVRQFQCPSWPNPCSPIHTV--FELINTVQEW--AQQRDGPIVVHDRYGGVQA 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 1524085  596 GCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEF 639
Cdd:cd14550 154 ATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQF 197
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 446-641 4.32e-32

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: 123.60  E-value: 4.32e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLkEKNEKCVLYWPEKRGI-YGKVEVLVISVN- 523
Cdd:cd14636   1 YINAALMDSYR-QPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV-DLAQGCPQYWPEEGMLrYGPIQVECMSCSm 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  524 ECDN----YTIRNLVLKQGSHTQhVKHYWYTSWPDHK-TPDSAQPLLQLMLDVEE-DRLASQGRGPVVVHCSAGIGRTGC 597
Cdd:cd14636  79 DCDVisriFRICNLTRPQEGYLM-VQQFQYLGWASHReVPGSKRSFLKLILQVEKwQEECDEGEGRTIIHCLNGGGRSGM 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 1524085  598 FIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVH 641
Cdd:cd14636 158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 446-641 4.08e-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: 112.31  E-value: 4.08e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNEK--CVLYWPEK-RGIYGKVEVLVISV 522
Cdd:cd14637   1 YINAALTDSYT-RSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwpCLQYWPEPgLQQYGPMEVEFVSG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  523 NECDN-----YTIRNLVLKQGSHTQhVKHYWYTSWPDHK-TPDSAQPLLQLMLDVEEDRlASQGRGPVVVHCSAGIGRTG 596
Cdd:cd14637  80 SADEDivtrlFRVQNITRLQEGHLM-VRHFQFLRWSAYRdTPDSKKAFLHLLASVEKWQ-RESGEGRTVVHCLNGGGRSG 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 1524085  597 CFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVH 641
Cdd:cd14637 158 TYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCY 202
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 446-644 1.46e-27

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: 110.47  E-value: 1.46e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVISVNE- 524
Cdd:cd17669   1 YINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEe 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  525 --C----DNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQplLQLMLDVEEDrlASQGRGPVVVHCSAGIGRTG 596
Cdd:cd17669  80 hkClsneEKLIIQDFILEatQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEE--AANRDGPMIVHDEHGGVTAG 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 1524085  597 CFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd17669 156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 446-644 5.55e-25

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: 103.22  E-value: 5.55e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVISVNE- 524
Cdd:cd17670   1 YINASYIMGYY-RSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKd 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  525 --C----DNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQplLQLMLDVEEDRLASQgrGPVVVHCSAGIGRTG 596
Cdd:cd17670  80 rlClsneEQIIIHDFILEatQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRD--GPTIVHDEFGAVSAG 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 1524085  597 CFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHAL 644
Cdd:cd17670 156 TLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 446-641 3.07e-24

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: 100.92  E-value: 3.07e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  446 YINANYIRGYSgKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLkEKNEKCVLYWPEKrGIY--GKVEVLVISVN 523
Cdd:cd14635   1 YINAALMDSYK-QPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV-DPAQLCPQYWPEN-GVHrhGPIQVEFVSAD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  524 ECDNYTIRNLVLKQGSHTQH----VKHYWYTSWPDHK-TPDSAQPLLQLMLDVEE-DRLASQGRGPVVVHCSAGIGRTGC 597
Cdd:cd14635  78 LEEDIISRIFRIYNAARPQDgyrmVQQFQFLGWPMYRdTPVSKRSFLKLIRQVDKwQEEYNGGEGRTVVHCLNGGGRSGT 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 1524085  598 FIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVH 641
Cdd:cd14635 158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 430-649 3.93e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 82.71  E-value: 3.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085   430 SRVCLRPKnvtdslSTYINANYIRGYSGKEKaFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNekCVL-YWPEK 508
Cdd:PHA02740  68 RRIKLFND------EKVLDARFVDGYDFEQK-FICIINLCEDACDKFLQALSDNKVQIIVLISRHADKK--CFNqFWSLK 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085   509 RG---IYGK--VEVLVISVNECDNYTIRNLVLKQGsHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVE------EDRLA 577
Cdd:PHA02740 139 EGcviTSDKfqIETLEIIIKPHFNLTLLSLTDKFG-QAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDdlcadlEKHKA 217

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524085   578 SQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHALCLYES 649
Cdd:PHA02740 218 DGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLK 289
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 427-638 4.02e-16

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: 77.83  E-value: 4.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  427 NPLSRVCLRpknVTDSLSTYINANYIRgySGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWP 506
Cdd:cd14559   1 NRFTNIQTR---VSTPVGKNLNANRVQ--IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  507 EKRGIYGKVEVLV--ISVNE------CDNYtirNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQpLLQL--MLDVEEDR- 575
Cdd:cd14559  76 RQSGTYGSVTVKSkkTGKDElvdglkADMY---NLKITDGNKTITIPVVHVTNWPDHTAISSEG-LKELadLVNKSAEEk 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524085  576 -----------LASQGRGPVVVHCSAGIGRTGCFIATSigcQQLKEEGVVDALSIVCQLRMDRGG-MVQTSEQYE 638
Cdd:cd14559 152 rnfykskgssaINDKNKLLPVIHCRAGVGRTGQLAAAM---ELNKSPNNLSVEDIVSDMRTSRNGkMVQKDEQLD 223
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 571-642 2.92e-12

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: 63.52  E-value: 2.92e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1524085  571 VEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKeegvvDALSIVCQLRMDRGG-MVQTSEQYEFVHH 642
Cdd:cd14494  46 LEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRPGgIPQTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
552-642 1.13e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 56.90  E-value: 1.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  552 WPDHKTPDSAQplLQLMLDVEEDRLASQGRgpVVVHCSAGIGRTGCFIAtsigcQQLKEEGV--VDALSIVCQLrmdRGG 629
Cdd:COG2453  55 IPDFGAPDDEQ--LQEAVDFIDEALREGKK--VLVHCRGGIGRTGTVAA-----AYLVLLGLsaEEALARVRAA---RPG 122

                        90
                ....*....|...
gi 1524085  630 MVQTSEQYEFVHH 642
Cdd:COG2453 123 AVETPAQRAFLER 135
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 553-641 1.31e-08

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 54.58  E-value: 1.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  553 PDHKTPDSAQPLLQLMldvEEDRLA-SQGRGpVVVHCSAGIGRTGCFIAtsigCQQLKEEGVVDALSIVCQLRMDRGGMV 631
Cdd:cd14505  81 PDGGVPSDIAQWQELL---EELLSAlENGKK-VLIHCKGGLGRTGLIAA----CLLLELGDTLDPEQAIAAVRALRPGAI 152

                        90
                ....*....|
gi 1524085  632 QTSEQYEFVH 641
Cdd:cd14505 153 QTPKQENFLH 162
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 525-628 1.15e-07

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: 51.81  E-value: 1.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  525 CDNYTIRNLVLKQGSHTQHVKHYWYT-SWPDHKTPdsaqPLLQLM--LDVEEDRLASQGRGPVVVHCSAGIGRTGcFIAT 601
Cdd:cd14497  40 PDHYMIFNLSEEEYDDDSKFEGRVLHyGFPDHHPP----PLGLLLeiVDDIDSWLSEDPNNVAVVHCKAGKGRTG-TVIC 114

                        90       100
                ....*....|....*....|....*..
gi 1524085  602 SIGCQQLKEEGVVDALSIVCQLRMDRG 628
Cdd:cd14497 115 AYLLYYGQYSTADEALEYFAKKRFKEG 141
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 568-640 1.50e-07

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 51.12  E-value: 1.50e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1524085  568 MLDVEEDRLASQGrgPVVVHCSAGIGRTGCFIAtsigCqQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFV 640
Cdd:cd14504  71 FLDIVEEANAKNE--AVLVHCLAGKGRTGTMLA----C-YLVKTGKISAVDAINEIRRIRPGSIETSEQEKFV 136
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 551-641 1.59e-06

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: 49.27  E-value: 1.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  551 SWPDHKTPDsaqplLQLMLD-VEEDRLASQGRGPVVVHCSAGIGRTGCFIAtsigCQQLKEEGVV--DALSIVcqlRMDR 627
Cdd:cd14506  83 GWKDYGVPS-----LTTILDiVKVMAFALQEGGKVAVHCHAGLGRTGVLIA----CYLVYALRMSadQAIRLV---RSKR 150

                        90
                ....*....|....
gi 1524085  628 GGMVQTSEQYEFVH 641
Cdd:cd14506 151 PNSIQTRGQVLCVR 164
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
559-596 9.84e-04

Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 41.48  E-value: 9.84e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 1524085  559 DSAQPLLQLMLDVeedrLASQGRGPVVVHCSAGIGRTG 596
Cdd:COG2365 115 PDAADAYRAAFRA----LADAENGPVLFHCTAGKDRTG 148
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 581-600 1.05e-03

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


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 40.51  E-value: 1.05e-03
                        10        20
                ....*....|....*....|
gi 1524085  581 RGPVVVHCSAGIGRTGCFIA 600
Cdd:cd14499 109 KGAIAVHCKAGLGRTGTLIA 128
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 537-617 2.62e-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: 38.89  E-value: 2.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  537 QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDrlasqgrGPVVVHCSAGIGRTGCFIA-TSIGCQQLKEEGVVD 615
Cdd:cd14529  52 AAAKIDGVKYVNLPLSATRPTESDVQSFLLIMDLKLAP-------GPVLIHCKHGKDRTGLVSAlYRIVYGGSKEEANED 124


                ..
gi 1524085  616 AL 617
Cdd:cd14529 125 YR 126
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 577-648 3.37e-03

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


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 38.01  E-value: 3.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524085    577 ASQGRGPVVVHCSAGIGRTGCFIATSIgcqqLKEEG--VVDALSIVcqlRMDRGGMvqtSEQYEFVHHaLCLYE 648
Cdd:pfam00782  65 ARQKGGKVLVHCQAGISRSATLIIAYL----MKTRNlsLNEAYSFV---KERRPGI---SPNFGFKRQ-LLEYE 127
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 553-642 7.87e-03

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 37.73  E-value: 7.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524085  553 PDHKTPDsaqplLQLMLDV---EEDRLASQGRGPVVVHCSAGIGRTGCFIAT----SIGCQQLKEegvvdALSIVCQLRM 625
Cdd:cd14510  82 DDHNVPT-----LDEMLSFtaeVREWMAADPKNVVAIHCKGGKGRTGTMVCAwliySGQFESAKE-----ALEYFGERRT 151

                        90       100
                ....*....|....*....|..
gi 1524085  626 DRGGM-----VQTSEQYEFVHH 642
Cdd:cd14510 152 DKSVSskfqgVETPSQSRYVGY 173
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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