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Conserved domains on  [gi|1284806101|ref|NP_001345413|]
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receptor-type tyrosine-protein phosphatase R isoform d [Mus musculus]

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 ...
 295-520 1.48e-177

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: 498.67  E-value: 1.48e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 295 TKNRYKTILPNPLSRVCLRPKNITDSLSTYINANYIRGYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 374
Cdd:cd14611     1 TKNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 375 KNEKCVLYWPEKRGIYGKVEVLVTGVTECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRL 454
Cdd:cd14611    81 KNEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1284806101 455 ASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHH 520
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 ...
 295-520 1.48e-177

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: 498.67  E-value: 1.48e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 295 TKNRYKTILPNPLSRVCLRPKNITDSLSTYINANYIRGYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 374
Cdd:cd14611     1 TKNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 375 KNEKCVLYWPEKRGIYGKVEVLVTGVTECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRL 454
Cdd:cd14611    81 KNEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1284806101 455 ASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHH 520
Cdd:cd14611   161 ASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
270-522 3.59e-103

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 310.75  E-value: 3.59e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101  270 LLQSEFMEIPMNFVDPKEIDI---PRHGTKNRYKTILPNPLSRVCLrpKNITDSLSTYINANYIRGYSGKeKAFIATQGP 346
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKL--KPPPGEGSDYINASYIDGPNGP-KAYIATQGP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101  347 MINTVNDFWQMVWQEDSPVIVMITKLKEKN-EKCVLYWPEKRG---IYGKVEVLVTGVTECDNYTIRNLVLK--QGSHTQ 420
Cdd:smart00194  78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGrEKCAQYWPDEEGeplTYGDITVTLKSVEKVDDYTIRTLEVTntGCSETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101  421 HVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRlaSEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQ 500
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQ--STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                          250       260
                   ....*....|....*....|..
gi 1284806101  501 LRVDRGGMVQTSEQYEFVHHAL 522
Cdd:smart00194 236 LRSQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
295-522 2.77e-96

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 291.84  E-value: 2.77e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 295 TKNRYKTILPNPLSRVCLRPkniTDSLSTYINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 374
Cdd:pfam00102   3 EKNRYKDVLPYDHTRVKLTG---DPGPSDYINASYIDGYK-KPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 375 KN-EKCVLYWPEKRG---IYGKVEV-LVTGVTECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLML 447
Cdd:pfam00102  79 KGrEKCAQYWPEEEGeslEYGDFTVtLKKEKEDEKDYTVRTLEVSngGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1284806101 448 DVEEDRLASEgRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:pfam00102 159 KVRKSSLDGR-SGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 295-530 5.82e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 152.46  E-value: 5.82e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 295 TKNRYKTILPNPLSRVCLRpknITDSLSTYINANYIRGYSGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 374
Cdd:PHA02742   54 KKCRYPDAPCFDRNRVILK---IEDGGDDFINASYVDGHNAKGR-FICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 375 KN-EKCVLYW-PEKRG--IYGKVEVLVTGVTECDNYTIRNLVLKQGS--HTQHVKHYWYTSWPDHKTPDSAQPLLQLMLD 448
Cdd:PHA02742  130 DGkEACYPYWmPHERGkaTHGEFKIKTKKIKSFRNYAVTNLCLTDTNtgASLDIKHFAYEDWPHGGLPRDPNKFLDFVLA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 449 VEEDRLASE---------GRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVH 519
Cdd:PHA02742  210 VREADLKADvdikgenivKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289

                         250
                  ....*....|.
gi 1284806101 520 HALCLFESRLS 530
Cdd:PHA02742  290 FIVLIFAKLMA 300
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
281-517 1.11e-38

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 142.92  E-value: 1.11e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 281 NFVDPKEIDIPRHGTKNRYKTILPNPLSRVclrPKNITdslstYINANYIRGysGKEKAFIATQGPMINTVNDFWQMVWQ 360
Cdd:COG5599    30 SHNDPQYLQNINGSPLNRFRDIQPYKETAL---RANLG-----YLNANYIQV--IGNHRYIATQYPLEEQLEDFFQMLFD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 361 EDSPVIVMIT---KLKEKNEKCVLYWPEKrGIYGK--VEVLVTGVTEC-DNYTIRNLVLKQ---GSHTQHVKHYWYTSWP 431
Cdd:COG5599   100 NNTPVLVVLAsddEISKPKVKMPVYFRQD-GEYGKyeVSSELTESIQLrDGIEARTYVLTIkgtGQKKIEIPVLHVKNWP 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 432 DHKTPDSAQpLLQLMLDV-EEDRLASEGRGPVVVHCSAGIGRTGCFIAtsigCQQLKEEG------VVDALSIVCQLRVD 504
Cdd:COG5599   179 DHGAISAEA-LKNLADLIdKKEKIKDPDKLLPVVHCRAGVGRTGTLIA----CLALSKSInalvqiTLSVEEIVIDMRTS 253

                         250
                  ....*....|....
gi 1284806101 505 RG-GMVQTSEQYEF 517
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 ...
 295-520 1.48e-177

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: 498.67  E-value: 1.48e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 295 TKNRYKTILPNPLSRVCLRPKNITDSLSTYINANYIRGYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 374
Cdd:cd14611     1 TKNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 375 KNEKCVLYWPEKRGIYGKVEVLVTGVTECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRL 454
Cdd:cd14611    81 KNEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1284806101 455 ASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHH 520
Cdd:cd14611   161 ASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 297-520 9.12e-159

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 451.08  E-value: 9.12e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 297 NRYKTILPNPLSRVCLrPKNITDSLSTYINANYIRGYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKN 376
Cdd:cd14547     1 NRYKTILPNEHSRVCL-PSVDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 377 EKCVLYWPEKRG-IYGKVEVLVTGVTECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLA 455
Cdd:cd14547    80 EKCAQYWPEEENeTYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEARQT 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1284806101 456 SEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHH 520
Cdd:cd14547   160 EPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 279-525 3.42e-157

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: 447.75  E-value: 3.42e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 279 PMNFVDPKEIDIPRHGTKNRYKTILPNPLSRVCLRPKNITDSLSTYINANYIRGYSGKEKAFIATQGPMINTVNDFWQMV 358
Cdd:cd14612     1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQEEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 359 WQEDSPVIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVTGVTECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDS 438
Cdd:cd14612    81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 439 AQPLLQLMLDVEEDRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFV 518
Cdd:cd14612   161 AGPLLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                  ....*..
gi 1284806101 519 HHALCLF 525
Cdd:cd14612   241 HHTLALY 247
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 270-525 1.21e-146

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: 421.58  E-value: 1.21e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 270 LLQSEFMEIPMNFVDPKEIDIPRHGTKNRYKTILPNPLSRVCLRPKNITDSLSTYINANYIRGYSGKEKAFIATQGPMIN 349
Cdd:cd14613     2 LLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYGGEEKVYIATQGPTVN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 350 TVNDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVTGVTECDNYTIRNLVLKQGSHTQHVKHYWYTS 429
Cdd:cd14613    82 TVGDFWRMVWQERSPIIVMITNIEEMNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 430 WPDHKTPDSAQPLLQLMLDVEEDR-LASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGM 508
Cdd:cd14613   162 WPDQKTPDNAPPLLQLVQEVEEARqQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGM 241

                         250
                  ....*....|....*..
gi 1284806101 509 VQTSEQYEFVHHALCLF 525
Cdd:cd14613   242 IQTCEQYQFVHHVLSLY 258
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
270-522 3.59e-103

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 310.75  E-value: 3.59e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101  270 LLQSEFMEIPMNFVDPKEIDI---PRHGTKNRYKTILPNPLSRVCLrpKNITDSLSTYINANYIRGYSGKeKAFIATQGP 346
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKL--KPPPGEGSDYINASYIDGPNGP-KAYIATQGP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101  347 MINTVNDFWQMVWQEDSPVIVMITKLKEKN-EKCVLYWPEKRG---IYGKVEVLVTGVTECDNYTIRNLVLK--QGSHTQ 420
Cdd:smart00194  78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGrEKCAQYWPDEEGeplTYGDITVTLKSVEKVDDYTIRTLEVTntGCSETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101  421 HVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRlaSEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQ 500
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQ--STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                          250       260
                   ....*....|....*....|..
gi 1284806101  501 LRVDRGGMVQTSEQYEFVHHAL 522
Cdd:smart00194 236 LRSQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
295-522 2.77e-96

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 291.84  E-value: 2.77e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 295 TKNRYKTILPNPLSRVCLRPkniTDSLSTYINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 374
Cdd:pfam00102   3 EKNRYKDVLPYDHTRVKLTG---DPGPSDYINASYIDGYK-KPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 375 KN-EKCVLYWPEKRG---IYGKVEV-LVTGVTECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLML 447
Cdd:pfam00102  79 KGrEKCAQYWPEEEGeslEYGDFTVtLKKEKEDEKDYTVRTLEVSngGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1284806101 448 DVEEDRLASEgRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:pfam00102 159 KVRKSSLDGR-SGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 324-520 2.25e-88

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: 270.31  E-value: 2.25e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSGKeKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKN-EKCVLYWPEKRG---IYGKVEVLVTG 399
Cdd:cd00047     1 YINASYIDGYRGP-KEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGrEKCERYWPEEGGkplEYGDITVTLVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 400 VTECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRlaSEGRGPVVVHCSAGIGRTGCFI 477
Cdd:cd00047    80 EEELSDYTIRTLELSpkGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEA--RKPNGPIVVHCSAGVGRTGTFI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1284806101 478 ATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHH 520
Cdd:cd00047   158 AIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 296-522 9.57e-72

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: 228.82  E-value: 9.57e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 296 KNRYKTILPNPLSRVCLRPkniTDSL--STYINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLK 373
Cdd:cd14553     6 KNRYANVIAYDHSRVILQP---IEGVpgSDYINANYCDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 374 EKNE-KCVLYWPeKRG--IYGKVEVLVTGVTECDNYTIRNLVL-KQGS-HTQHVKHYWYTSWPDHKTPDSAQPLLQLMLD 448
Cdd:cd14553    82 ERSRvKCDQYWP-TRGteTYGLIQVTLLDTVELATYTVRTFALhKNGSsEKREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1284806101 449 VEEdrLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd14553   161 VKA--CNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 298-519 2.68e-71

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: 227.24  E-value: 2.68e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 298 RYKTILPNPLSRVCLRPKNiTDSLSTYINANYIRGYSGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK-N 376
Cdd:cd14548     1 RYTNILPYDHSRVKLIPIN-EEEGSDYINANYIPGYNSPRE-FIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKgR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 377 EKCVLYWPEKR--GIYGKVEVLVTGVTECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRL 454
Cdd:cd14548    79 VKCDHYWPFDQdpVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1284806101 455 ASEGrgPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVH 519
Cdd:cd14548   159 QEKG--PTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 295-522 7.17e-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: 221.95  E-value: 7.17e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 295 TKNRYKTILPNPLSRVCLRPKNITDSLSTYINANYIR------GYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVM 368
Cdd:cd14544     3 GKNRYKNILPFDHTRVILKDRDPNVPGSDYINANYIRnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVIVM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 369 ITKLKEK-NEKCVLYWPEKRGI--YGKVEVLVTGVTECDNYTIRNLVLK---QGSHTQHVKHYWYTSWPDHKTPDSAQPL 442
Cdd:cd14544    83 TTKEVERgKNKCVRYWPDEGMQkqYGPYRVQNVSEHDTTDYTLRELQVSkldQGDPIREIWHYQYLSWPDHGVPSDPGGV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 443 LQLMLDVEEDRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGV---VDALSIVCQLRVDRGGMVQTSEQYEFVH 519
Cdd:cd14544   163 LNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKFIY 242


                  ...
gi 1284806101 520 HAL 522
Cdd:cd14544   243 VAV 245
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 295-519 2.32e-68

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: 221.08  E-value: 2.32e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 295 TKNRYKTILPNPLSRVCLrPKNITDSLSTYINANYIRGYSGKeKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 374
Cdd:cd14543    31 EKNRYGDVLCLDQSRVKL-PKRNGDERTDYINANFMDGYKQK-NAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTRVVE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 375 KNE-KCVLYWP---EKRGIYGKVEVLVTGVTECDNYTIRNLVL--KQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLD 448
Cdd:cd14543   109 RGRvKCGQYWPleeGSSLRYGDLTVTNLSVENKEHYKKTTLEIhnTETDESRQVTHFQFTSWPDFGVPSSAAALLDFLGE 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 449 VEE----------DRLASEGRGP-VVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEF 517
Cdd:cd14543   189 VRQqqalavkamgDRWKGHPPGPpIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYF 268


                  ..
gi 1284806101 518 VH 519
Cdd:cd14543   269 CY 270
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 324-519 2.89e-68

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: 218.37  E-value: 2.89e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK-NEKCVLYWPeKRGI--YGKVEVLVTGV 400
Cdd:cd14549     1 YINANYVDGYN-KARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERgRRKCDQYWP-KEGTetYGNIQVTLLST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 401 TECDNYTIRNLVLK--------QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMldveedRLAS----EGRGPVVVHCSA 468
Cdd:cd14549    79 EVLATYTVRTFSLKnlklkkvkGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFV------RKSSaanpPGAGPIVVHCSA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1284806101 469 GIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVH 519
Cdd:cd14549   153 GVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 289-524 1.20e-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: 205.51  E-value: 1.20e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 289 DIPRHGTKNRYKTILPNPLSRVCLRPKNiTDSLSTYINANYIRGYSGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVM 368
Cdd:cd14614     8 DLPVNRCKNRYTNILPYDFSRVKLVSMH-EEEGSDYINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSQIIVM 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 369 ITKLKEKNE-KCVLYWP--EKRGIYGKVEVLVTGVTECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTP--DSAQPLL 443
Cdd:cd14614    86 LTQCNEKRRvKCDHYWPftEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPtaNAAESIL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 444 QLMLDVEEDRLASegRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHALC 523
Cdd:cd14614   166 QFVQMVRQQAVKS--KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 243


                  .
gi 1284806101 524 L 524
Cdd:cd14614   244 L 244
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 297-518 9.95e-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: 202.35  E-value: 9.95e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 297 NRYKTILPNPLSRVCLrpKNITDSLSTYINANYIRGYSGKeKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKN 376
Cdd:cd14615     1 NRYNNVLPYDISRVKL--SVQSHSTDDYINANYMPGYNSK-KEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 377 E-KCVLYWPEKRGI-YGKVEVLVTGVTECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEED 452
Cdd:cd14615    78 RtKCEEYWPSKQKKdYGDITVTMTSEIVLPEWTIRDFTVKnaQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1284806101 453 RLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFV 518
Cdd:cd14615   158 MKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 291-522 1.49e-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: 198.34  E-value: 1.49e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 291 PRHGTKNRYKTILPNPLSRVCLRPKNITDSL-STYINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMI 369
Cdd:cd17667    25 PDNKHKNRYINILAYDHSRVKLRPLPGKDSKhSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMI 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 370 TKLKEKNE-KCVLYWP-EKRGIYGKVEVLV--TGVTEC---DNYTIRNLVLKQGS--------HTQHVKHYWYTSWPDHK 434
Cdd:cd17667   104 TNLVEKGRrKCDQYWPtENSEEYGNIIVTLksTKIHACytvRRFSIRNTKVKKGQkgnpkgrqNERTVIQYHYTQWPDMG 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 435 TPDSAQPLLQLMldveedRLASEGR----GPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQ 510
Cdd:cd17667   184 VPEYALPVLTFV------RRSSAARtpemGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQ 257

                         250
                  ....*....|..
gi 1284806101 511 TSEQYEFVHHAL 522
Cdd:cd17667   258 TEEQYIFIHDAL 269
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 324-520 3.72e-59

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: 195.16  E-value: 3.72e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKN-EKCVLYWPEKR--GIYGKVEVLVTGV 400
Cdd:cd18533     1 YINASYITLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGrEKCDQYWPSGEyeGEYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 401 TECD--NYTIRNLVLKQGSH-TQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASEGRGPVVVHCSAGIGRTGCFI 477
Cdd:cd18533    81 EENDdgGFIVREFELSKEDGkVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGTFI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1284806101 478 ATSIGCQQLKE--------EGVVDA-LSIVCQLRVDRGGMVQTSEQYEFVHH 520
Cdd:cd18533   161 ALDSLLDELKRglsdsqdlEDSEDPvYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 296-522 4.31e-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: 196.01  E-value: 4.31e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 296 KNRYKTILPNPLSRVCLRPKNiTDSLSTYINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 375
Cdd:cd14630     6 KNRYGNIISYDHSRVRLQLLD-GDPHSDYINANYIDGYH-RPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 376 NE-KCVLYWPEKRGIYGKVEVLVTGVTECDNYTIRNL-VLKQGSH-TQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEed 452
Cdd:cd14630    84 GRvKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFtVQKKGYHeIREIRQFHFTSWPDHGVPCYATGLLGFVRQVK-- 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 453 RLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd14630   162 FLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 289-521 5.65e-59

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: 195.44  E-value: 5.65e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 289 DIPRHGTKNRYKTILPNPLSRVCLRPKNITDSlSTYINANYIRGYSGKeKAFIATQGPMINTVNDFWQMVWQEDSPVIVM 368
Cdd:cd14554     2 NLPCNKFKNRLVNILPYESTRVCLQPIRGVEG-SDYINASFIDGYRQR-GAYIATQGPLAETTEDFWRMLWEHNSTIIVM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 369 ITKLKEKN-EKCVLYWPEKRGIYGKVEVlVTGVTECD--NYTIRNLVLKQGSHTQ--HVKHYWYTSWPDHKTPDSAQPLL 443
Cdd:cd14554    80 LTKLREMGrEKCHQYWPAERSARYQYFV-VDPMAEYNmpQYILREFKVTDARDGQsrTVRQFQFTDWPEQGVPKSGEGFI 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1284806101 444 QLMLDVEEDRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHA 521
Cdd:cd14554   159 DFIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 296-522 6.85e-59

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 196.01  E-value: 6.85e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 296 KNRYKTILPNPLSRVCLRPKNITDSLSTYINANYI-------RGYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVM 368
Cdd:cd14605     5 KNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIImpefetkCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVM 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 369 ITKLKEKNE-KCVLYWPEKRGI--YGKVEVLVTGVTECDNYTIRNLVLK---QGSHTQHVKHYWYTSWPDHKTPDSAQPL 442
Cdd:cd14605    85 TTKEVERGKsKCVKYWPDEYALkeYGVMRVRNVKESAAHDYILRELKLSkvgQGNTERTVWQYHFRTWPDHGVPSDPGGV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 443 LQLMLDVEEDRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGV---VDALSIVCQLRVDRGGMVQTSEQYEFVH 519
Cdd:cd14605   165 LDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQYRFIY 244


                  ...
gi 1284806101 520 HAL 522
Cdd:cd14605   245 MAV 247
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 297-527 1.88e-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: 193.95  E-value: 1.88e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 297 NRYKTILPNPLSRVCLRPkNITDSLSTYINANYIRGYsGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKN 376
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKP-IHEEPGSDYINANYMPGY-WSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 377 E-KCVLYWP--EKRGIYGKVEVLVTGVTECDNYTIRNLVLKQG--SHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE 451
Cdd:cd14619    79 RvKCEHYWPldYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVeeQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQ 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1284806101 452 DRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHalCLFES 527
Cdd:cd14619   159 WLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQ--CILDF 232
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 324-524 2.68e-57

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: 190.13  E-value: 2.68e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKRGIYGKVEVLVTGVTE 402
Cdd:cd14555     1 YINANYIDGYH-RPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRvKCSRYWPDDTEVYGDIKVTLVETEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 403 CDNYTIRNLVL-KQGSHTQH-VKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASEGrgPVVVHCSAGIGRTGCFIATS 480
Cdd:cd14555    80 LAEYVVRTFALeRRGYHEIReVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAG--PIVVHCSAGAGRTGCYIVID 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1284806101 481 IGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL---CL 524
Cdd:cd14555   158 IMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIleaCL 204
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 296-522 2.89e-57

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: 2.89e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 296 KNRYKTILPNPLSRVCLRPKNITDSlSTYINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 375
Cdd:cd14626    44 KNRYANVIAYDHSRVILTSVDGVPG-SDYINANYIDGYR-KQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEK 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 376 NE-KCVLYWPeKRG--IYGKVEVLVTGVTECDNYTIRNLVL-KQGS-HTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 450
Cdd:cd14626   122 SRvKCDQYWP-IRGteTYGMIQVTLLDTVELATYSVRTFALyKNGSsEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVK 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1284806101 451 EDRLASEGrgPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
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; ...
 324-522 3.96e-57

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 189.40  E-value: 3.96e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSGKEkAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKN-EKCVLYWPEKRGI-YGKVEVLVTGVT 401
Cdd:cd14552     1 YINASFIDGYRQKD-AYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSqNKCAQYWPEDGSVsSGDITVELKDQT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 402 ECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASeGRGPVVVHCSAGIGRTGCFIAT 479
Cdd:cd14552    80 DYEDYTLRDFLVTkgKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQS-GNHPITVHCSAGAGRTGTFCAL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1284806101 480 SIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd14552   159 STVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 324-522 1.74e-56

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: 187.97  E-value: 1.74e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSGKEK-AFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKRG----IYGKVEVLV 397
Cdd:cd14538     1 YINASHIRIPVGGDTyHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKvKCHRYWPDSLNkpliCGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 398 TGVTECDNYTIR--NLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMldveedRLA--SEGRGPVVVHCSAGIGRT 473
Cdd:cd14538    81 EKYQSLQDFVIRriSLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFI------RYMrrIHNSGPIVVHCSAGIGRT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1284806101 474 GCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd14538   155 GVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 297-522 4.92e-55

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 184.76  E-value: 4.92e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 297 NRYKTILPNPLSRVCLRPKNiTDSLSTYINANYIRGYSGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKN 376
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLG-GEPHSDYINANFIPGYTSPQE-FIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 377 EK-CVLYWPEKRG--IYGKVEVLVTGVTECDNYTIRNLVLKQGS--HTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE 451
Cdd:cd14618    79 RVlCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDlrKERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1284806101 452 DRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd14618   159 HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 279-525 1.54e-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: 184.70  E-value: 1.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 279 PMNFVDPKEIDIPRHGTKNRYKTILPNPLSRVCLRPKNITDSLSTYINANYIR----GYSGKEKAFIATQGPMINTVNDF 354
Cdd:cd14606     4 VKNLHQRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVKnqllGPDENAKTYIASQGCLEATVNDF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 355 WQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKRGI--YGKVEVLVTGVTECDNYTIRNL---VLKQGSHTQHVKHYWYT 428
Cdd:cd14606    84 WQMAWQENSRVIVMTTREVEKGRnKCVPYWPEVGMQraYGPYSVTNCGEHDTTEYKLRTLqvsPLDNGELIREIWHYQYL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 429 SWPDHKTPDSAQPLLQLMLDVEEDRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGV---VDALSIVCQLRVDR 505
Cdd:cd14606   164 SWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQR 243

                         250       260
                  ....*....|....*....|
gi 1284806101 506 GGMVQTSEQYEFVHHALCLF 525
Cdd:cd14606   244 SGMVQTEAQYKFIYVAIAQF 263
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 296-522 2.41e-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: 184.91  E-value: 2.41e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 296 KNRYKTILPNPLSRVCLRP-KNITDSlsTYINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 374
Cdd:cd14625    50 KNRYANVIAYDHSRVILQPiEGIMGS--DYINANYIDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 375 KNE-KCVLYWPeKRGI--YGKVEVLVTGVTECDNYTIRNLVLKQ--GSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDV 449
Cdd:cd14625   127 KSRiKCDQYWP-SRGTetYGMIQVTLLDTIELATFCVRTFSLHKngSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRV 205

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1284806101 450 EEdrLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd14625   206 KT--CNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 324-517 5.64e-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: 181.05  E-value: 5.64e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSGkEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE-KNEKCVLYWPEKRGIYGKVEVLVTGVTE 402
Cdd:cd14558     1 YINASFIDGYWG-PKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEgDQEQCAQYWGDEKKTYGDIEVELKDTEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 403 CDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDV----EEDRLASEGRGPVVVHCSAGIGRTGCF 476
Cdd:cd14558    80 SPTYTVRVFEIThlKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklPYKNSKHGRSVPIVVHCSDGSSRTGIF 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1284806101 477 IATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEF 517
Cdd:cd14558   160 CALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQF 200
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 324-524 1.21e-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: 180.25  E-value: 1.21e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKRGIYGKVEVLVTGVTE 402
Cdd:cd14632     1 YINANYIDGYH-RSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRvKCSKYWPDDSDTYGDIKITLLKTET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 403 CDNYTIRNLVL-KQGSHTQH-VKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDrlASEGRGPVVVHCSAGIGRTGCFIATS 480
Cdd:cd14632    80 LAEYSVRTFALeRRGYSARHeVKQFHFTSWPEHGVPYHATGLLAFIRRVKAS--TPPDAGPVVVHCSAGAGRTGCYIVLD 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1284806101 481 IGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL---CL 524
Cdd:cd14632   158 VMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIleaCL 204
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 299-522 1.55e-53

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: 180.91  E-value: 1.55e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 299 YKTILPNPLSRVCLRPKNiTDSLSTYINANYIRGYSGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE-KNE 377
Cdd:cd14620     1 YPNILPYDHSRVILSQLD-GIPCSDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKErKEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 378 KCVLYWPEKR-GIYGKVEVLVTGVTECDNYTIRNLVLKQGSH-----TQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE 451
Cdd:cd14620    79 KCYQYWPDQGcWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPdgckaPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1284806101 452 drLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd14620   159 --VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 309-522 5.93e-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: 179.06  E-value: 5.93e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 309 RVCLRPKNiTDSLSTYINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKR 387
Cdd:cd14631     1 RVILQPVE-DDPSSDYINANYIDGYQ-RPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRvKCYKYWPDDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 388 GIYGKVEVLVTGVTECDNYTIRNLVLKQGSHTQ--HVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRlaSEGRGPVVVH 465
Cdd:cd14631    79 EVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEirEVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSN--PPSAGPIVVH 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1284806101 466 CSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd14631   157 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 324-522 5.96e-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: 178.63  E-value: 5.96e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWP-EKRGIYGKVEVL----- 396
Cdd:cd17668     1 YINANYVDGYN-KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRrKCDQYWPaDGSEEYGNFLVTqksvq 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 397 VTGVTECDNYTIRNLVLKQGSHT-----QHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASegRGPVVVHCSAGIG 471
Cdd:cd17668    80 VLAYYTVRNFTLRNTKIKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHA--VGPVVVHCSAGVG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1284806101 472 RTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd17668   158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 296-522 8.47e-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: 180.62  E-value: 8.47e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 296 KNRYKTILPNPLSRVCLRPKNiTDSLSTYINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 375
Cdd:cd14633    43 KNRYGNIIAYDHSRVRLQPIE-GETSSDYINGNYIDGYH-RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 376 NE-KCVLYWPEKRGIYGKVEVLVTGVTECDNYTIRNL-VLKQGSH-TQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEED 452
Cdd:cd14633   121 GRvKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFaVEKRGVHeIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSK 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 453 RLASEGrgPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd14633   201 SPPNAG--PLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 324-519 9.81e-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: 177.71  E-value: 9.81e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWP---EKRGIYGKVEVLVTG 399
Cdd:cd14557     1 YINASYIDGFKEPRK-YIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRnKCAQYWPsmeEGSRAFGDVVVKINE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 400 VTECDNYTIRNLVL---KQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVeeDRLASEGRGPVVVHCSAGIGRTGCF 476
Cdd:cd14557    80 EKICPDYIIRKLNInnkKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRV--NAFNNFFSGPIVVHCSAGVGRTGTY 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1284806101 477 IATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVH 519
Cdd:cd14557   158 IGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 297-519 2.10e-52

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: 177.80  E-value: 2.10e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 297 NRYKTILPNPLSRVCLRPKNiTDSLSTYINANYIRGYSGKeKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKN 376
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVD-DDPCSDYINASYIPGNNFR-REYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 377 E-KCVLYWPEKRG--IYGKVEVLVTGVTECDNYTIRNLVL---KQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 450
Cdd:cd14617    79 RvKCDHYWPADQDslYYGDLIVQMLSESVLPEWTIREFKIcseEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1284806101 451 EDRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVH 519
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; ...
 324-520 2.84e-52

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: 176.46  E-value: 2.84e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSGkEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKRG---IYGKVEV-LVT 398
Cdd:cd14542     1 YINANFIKGVSG-SKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKkKCERYWPEEGEeqlQFGPFKIsLEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 399 GVTECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEedRLASEGRGPVVVHCSAGIGRTGCFIA 478
Cdd:cd14542    80 EKRVGPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVR--DYQGSEDVPICVHCSAGCGRTGTICA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1284806101 479 TSIGCQQLKEEGVVDALS---IVCQLRVDRGGMVQTSEQYEFVHH 520
Cdd:cd14542   158 IDYVWNLLKTGKIPEEFSlfdLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 296-517 1.22e-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: 176.04  E-value: 1.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 296 KNRYKTILPNPLSRVCLRpknITDSLSTYINANYIRGYSGKeKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 375
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVK---LKQGDNDYINASLVEVEEAK-RSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 376 NE-KCVLYWPEKRG---IYGKVEVLVTGVTECD--NYTIRNLVL--KQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLML 447
Cdd:cd14545    77 GQiKCAQYWPQGEGnamIFEDTGLKVTLLSEEDksYYTVRTLELenLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1284806101 448 DVEEDRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGV--VDALSIVCQLRVDRGGMVQTSEQYEF 517
Cdd:cd14545   157 KVRESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 289-521 1.31e-51

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: 178.00  E-value: 1.31e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 289 DIPRHGTKNRYKTILPNPLSRVCLRPKNITDSlSTYINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVM 368
Cdd:cd14628    48 NLPCNKFKNRLVNIMPYESTRVCLQPIRGVEG-SDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 369 ITKLKEKN-EKCVLYWPEKRGiyGKVEVLVtgVTECDNYTIRNLVLKQ-------GSHTQHVKHYWYTSWPDHKTPDSAQ 440
Cdd:cd14628   126 LTKLREMGrEKCHQYWPAERS--ARYQYFV--VDPMAEYNMPQYILREfkvtdarDGQSRTVRQFQFTDWPEQGVPKSGE 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 441 PLLQLMLDVEEDRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHH 520
Cdd:cd14628   202 GFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYR 281


                  .
gi 1284806101 521 A 521
Cdd:cd14628   282 A 282
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 289-521 2.80e-51

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: 177.23  E-value: 2.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 289 DIPRHGTKNRYKTILPNPLSRVCLRPKNITDSlSTYINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVM 368
Cdd:cd14627    49 NLPCNKFKNRLVNIMPYETTRVCLQPIRGVEG-SDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWENNSTIVVM 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 369 ITKLKEKN-EKCVLYWPEKRGiyGKVEVLVtgVTECDNYTIRNLVLKQ-------GSHTQHVKHYWYTSWPDHKTPDSAQ 440
Cdd:cd14627   127 LTKLREMGrEKCHQYWPAERS--ARYQYFV--VDPMAEYNMPQYILREfkvtdarDGQSRTVRQFQFTDWPEQGVPKSGE 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 441 PLLQLMLDVEEDRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHH 520
Cdd:cd14627   203 GFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQ 282


                  .
gi 1284806101 521 A 521
Cdd:cd14627   283 A 283
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 296-522 5.94e-51

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 176.08  E-value: 5.94e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 296 KNRYKTILPNPLSRVCLRPKNITDSlSTYINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 375
Cdd:cd14624    50 KNRYANVIAYDHSRVLLSAIEGIPG-SDYINANYIDGYR-KQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEER 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 376 NE-KCVLYWPEkRGI--YGKVEVLVTGVTECDNYTIRNLVL-KQGS-HTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 450
Cdd:cd14624   128 SRvKCDQYWPS-RGTetYGLIQVTLLDTVELATYCVRTFALyKNGSsEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK 206

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1284806101 451 EdrLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd14624   207 T--CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 289-521 1.85e-50

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: 174.91  E-value: 1.85e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 289 DIPRHGTKNRYKTILPNPLSRVCLRPKNITDSlSTYINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVM 368
Cdd:cd14629    49 NLPCNKFKNRLVNIMPYELTRVCLQPIRGVEG-SDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 369 ITKLKEKN-EKCVLYWPEKRGiyGKVEVLVtgVTECDNYTIRNLVLKQ-------GSHTQHVKHYWYTSWPDHKTPDSAQ 440
Cdd:cd14629   127 LTKLREMGrEKCHQYWPAERS--ARYQYFV--VDPMAEYNMPQYILREfkvtdarDGQSRTIRQFQFTDWPEQGVPKTGE 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 441 PLLQLMLDVEEDRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHH 520
Cdd:cd14629   203 GFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYR 282


                  .
gi 1284806101 521 A 521
Cdd:cd14629   283 A 283
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 324-518 1.37e-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: 169.55  E-value: 1.37e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK-NEKCVLYWPEKRG-IYGKVEV-LVTGV 400
Cdd:cd14546     1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENgVKQCARYWPEEGSeVYHIYEVhLVSEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 401 TECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEdrlASEGRG-PVVVHCSAGIGRTGCFI 477
Cdd:cd14546    81 IWCDDYLVRSFYLKnlQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNK---SYRGRScPIVVHCSDGAGRTGTYI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1284806101 478 ATSIGCQQL----KEegvVDALSIVCQLRVDRGGMVQTSEQYEFV 518
Cdd:cd14546   158 LIDMVLNRMakgaKE---IDIAATLEHLRDQRPGMVKTKDQFEFV 199
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 324-519 1.79e-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: 169.42  E-value: 1.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSGKEkAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK-NEKCVLYWPEKRGI-YGKVEVLVTGVT 401
Cdd:cd14622     2 YINASFIDGYRQKD-YFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEReQEKCVQYWPSEGSVtHGEITIEIKNDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 402 ECDNYTIRNLVL--KQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASeGRGPVVVHCSAGIGRTGCFIAT 479
Cdd:cd14622    81 LLETISIRDFLVtyNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQT-GNHPIVVHCSAGAGRTGTFIAL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1284806101 480 SIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVH 519
Cdd:cd14622   160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 296-522 1.80e-49

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: 172.52  E-value: 1.80e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 296 KNRYKTILPNPLSRVCLRP-KNITDSlsTYINANYIRGYSGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 374
Cdd:cd14621    55 KNRYVNILPYDHSRVHLTPvEGVPDS--DYINASFINGYQEKNK-FIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 375 KNE-KCVLYWPEKRG-IYGKVEVLVTGVTECDNYTIRNLVLKQ-----GSHTQH-VKHYWYTSWPDHKTPDSAQPLLQLM 446
Cdd:cd14621   132 RKEcKCAQYWPDQGCwTYGNIRVSVEDVTVLVDYTVRKFCIQQvgdvtNKKPQRlITQFHFTSWPDFGVPFTPIGMLKFL 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1284806101 447 LDVEEdrLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd14621   212 KKVKN--CNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQAL 285
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 297-519 1.97e-49

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


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 170.09  E-value: 1.97e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 297 NRYKTILPNPLSRVCLRPKNITDSlSTYINANYIRGYSGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKN 376
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPG-SDYINASYISGYLCPNE-FIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 377 E-KCVLYWPEKR---GIYGkvEVLVTGVTE--CDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 450
Cdd:cd14616    79 RiRCHQYWPEDNkpvTVFG--DIVITKLMEdvQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1284806101 451 EDRlaSEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVH 519
Cdd:cd14616   157 ASR--AHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 296-522 2.35e-49

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: 171.16  E-value: 2.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 296 KNRYKTILPNPLSRVCLRPKNiTDSLSTYINANYIRGYSGkEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 375
Cdd:cd14603    33 KNRYKDILPYDQTRVILSLLQ-EEGHSDYINANFIKGVDG-SRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIEM 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 376 -NEKCVLYWPEKRGIYGKVEVLVTGVTEC---DNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEe 451
Cdd:cd14603   111 gKKKCERYWAQEQEPLQTGPFTITLVKEKrlnEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELAR- 189

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1284806101 452 dRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSI---VCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd14603   190 -RLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIfdvVLEMRKQRPAAVQTEEQYEFLYHTV 262
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 324-519 3.24e-49

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 168.35  E-value: 3.24e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSGKeKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPE-KRGIYGKVEVLVTGVTE 402
Cdd:cd14556     1 YINAALLDSYKQP-AAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDeGSGTYGPIQVEFVSTTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 403 CDNYTIRNLVLKQGSHTQH----VKHYWYTSWPDH-KTPDSAQPLLQLMLDVEEDRLASeGRGPVVVHCSAGIGRTGCFI 477
Cdd:cd14556    80 DEDVISRIFRLQNTTRPQEgyrmVQQFQFLGWPRDrDTPPSKRALLKLLSEVEKWQEQS-GEGPIVVHCLNGVGRSGVFC 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1284806101 478 ATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVH 519
Cdd:cd14556   159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 324-519 3.82e-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: 168.55  E-value: 3.82e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE-KNEKCVLYWPEK-RGIYGKVEVLVTGVT 401
Cdd:cd14551     1 YINASYIDGYQEKNK-FIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKErKEKKCSQYWPDQgCWTYGNLRVRVEDTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 402 ECDNYTIRNLVLKQ-----GSHTQH-VKHYWYTSWPDHKTPDSAQPLLQLMLDVEEdrLASEGRGPVVVHCSAGIGRTGC 475
Cdd:cd14551    80 VLVDYTTRKFCIQKvnrgiGEKRVRlVTQFHFTSWPDFGVPFTPIGMLKFLKKVKS--ANPPRAGPIVVHCSAGVGRTGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1284806101 476 FIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVH 519
Cdd:cd14551   158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 324-523 2.01e-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: 166.74  E-value: 2.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANY----IRGySGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPE--KRGIYGKVEVL 396
Cdd:cd14541     2 YINANYvnmeIPG-SGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRvKCHQYWPDlgETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 397 VTGVTECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASEgrGPVVVHCSAGIGRTG 474
Cdd:cd14541    81 CVSEEVTPSFAFREFILTntNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMV--EPTVVHCSAGIGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1284806101 475 CFIA--TSIGCQQLKEEgvVDALSIVCQLRVDRGGMVQTSEQYEFVHHALC 523
Cdd:cd14541   159 VLITmeTAMCLIEANEP--VYPLDIVRTMRDQRAMLIQTPSQYRFVCEAIL 207
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 296-522 3.67e-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: 166.93  E-value: 3.67e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 296 KNRYKTILPNPLSRVCLRPKNitdslsTYINANYIRGYSGKEK-AFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 374
Cdd:cd14597     6 KNRYKNILPYDTTRVPLGDEG------GYINASFIKMPVGDEEfVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 375 KNE-KCVLYWPEKRG----IYGKVEVLVTGVTECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLML 447
Cdd:cd14597    80 GGKiKCQRYWPEILGkttmVDNRLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTPSQPEQLLTFIS 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1284806101 448 DVEEDRLAsegrGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd14597   160 YMRHIHKS----GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 324-522 1.23e-47

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: 164.94  E-value: 1.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIR-GYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKN-EKCVLYWPEKRG-----IYGKVEVL 396
Cdd:cd14540     1 YINASHITaTVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGrEKCFRYWPTLGGehdalTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 397 VTGVTECDNYTIRNLVLKQGSHTQH--VKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLA--SEGRG-----PVVVHCS 467
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQSrtVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHtnQDVAGhnrnpPTLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1284806101 468 AGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd14540   161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVL 215
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 298-519 5.37e-47

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: 163.68  E-value: 5.37e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 298 RYKTILPNPLSRVCLrPKNITDSLSTYINANYIRGYSGKEkAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK-N 376
Cdd:cd14623     1 RVLQIIPYEFNRVII-PVKRGEENTDYVNASFIDGYRQKD-SYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERgQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 377 EKCVLYWPEKRGI-YGKVEVLVTGVTECDNYTIRNLVL--KQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDR 453
Cdd:cd14623    79 EKCAQYWPSDGSVsYGDITIELKKEEECESYTVRDLLVtnTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1284806101 454 LASeGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVH 519
Cdd:cd14623   159 QQS-GNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCY 223
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 282-517 1.37e-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: 1.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 282 FVDPKEIDIPrhgtKNRYKTILPNPLSRVCLRPKNITDSlSTYINANYIRGYSGKEKAFIATQGPMINTVNDFWQMVWQE 361
Cdd:cd14610    37 NVAQREENVQ----KNRSLAVLPYDHSRIILKAENSHSH-SDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWES 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 362 DSPVIVMITKLKEKN-EKCVLYWP-EKRGIYGKVEV-LVTGVTECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTP 436
Cdd:cd14610   112 GCVVIVMLTPLAENGvKQCYHYWPdEGSNLYHIYEVnLVSEHIWCEDFLVRSFYLKnlQTNETRTVTQFHFLSWNDQGVP 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 437 DSAQPLLQLMLDVEEdrlASEGRG-PVVVHCSAGIGRTGCFIATSIGCQQL-KEEGVVDALSIVCQLRVDRGGMVQTSEQ 514
Cdd:cd14610   192 ASTRSLLDFRRKVNK---CYRGRScPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQ 268


                  ...
gi 1284806101 515 YEF 517
Cdd:cd14610   269 FEF 271
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 296-522 5.53e-46

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: 161.16  E-value: 5.53e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 296 KNRYKTILPNPLSRVCLRPKnITDSLSTYINANYIRGYSGKeKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 375
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLI-TSDEDSDYINANFIKGVYGP-RAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 376 -NEKCVLYWP---EKRGIYGKVEVLVTGVTECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE 451
Cdd:cd14602    79 gKKKCERYWAepgEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1284806101 452 drLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKeEGVV----DALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd14602   159 --YQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 324-522 9.78e-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: 159.53  E-value: 9.78e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSGKEKAF-IATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKRGIYGKVEVLVTGVT 401
Cdd:cd14596     1 YINASYITMPVGEEELFyIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKvKCHRYWPETLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 402 EC---DNYTIR--NLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEedrlASEGRGPVVVHCSAGIGRTGCF 476
Cdd:cd14596    81 NYqalQYFIIRiiKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMR----KVHNTGPIVVHCSAGIGRAGVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1284806101 477 IATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd14596   157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 296-529 1.18e-45

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: 162.02  E-value: 1.18e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 296 KNRYKTILPNPLSRVCLRPKnITDSLSTYINANYIRGYSGKeKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 375
Cdd:cd14604    60 KNRYKDILPFDHSRVKLTLK-TSSQDSDYINANFIKGVYGP-KAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEM 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 376 N-EKCVLYWP---EKRGIYGKVEVLVTGVTECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTP---DSAQPLLQLMLD 448
Cdd:cd14604   138 GrKKCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPssfDSILDMISLMRK 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 449 VEEDRLAsegrgPVVVHCSAGIGRTGCFIATSIGCQQLKEEGV---VDALSIVCQLRVDRGGMVQTSEQYEFVHHALC-L 524
Cdd:cd14604   218 YQEHEDV-----PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAqL 292


                  ....*
gi 1284806101 525 FESRL 529
Cdd:cd14604   293 FEKQL 297
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 290-522 2.07e-45

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: 160.96  E-value: 2.07e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 290 IPRHGTKNRYKTILPNPLSRVCLRPKNitdslSTYINANYIRgYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMI 369
Cdd:cd14608    22 LPKNKNRNRYRDVSPFDHSRIKLHQED-----NDYINASLIK-MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVML 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 370 TKLKEKNE-KCVLYWP---EKRGIYGKVEVLVTGVTE--CDNYTIRNLVLKQGS--HTQHVKHYWYTSWPDHKTPDSAQP 441
Cdd:cd14608    96 NRVMEKGSlKCAQYWPqkeEKEMIFEDTNLKLTLISEdiKSYYTVRQLELENLTtqETREILHFHYTTWPDFGVPESPAS 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 442 LLQLMLDVEEDRLASEGRGPVVVHCSAGIGRTGCFIATSIgC----QQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEF 517
Cdd:cd14608   176 FLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADT-ClllmDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 254


                  ....*
gi 1284806101 518 VHHAL 522
Cdd:cd14608   255 SYLAV 259
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 290-522 3.73e-45

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: 160.02  E-value: 3.73e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 290 IPRHGTKNRYKTILPNPLSRVCLrpknitDSLSTYINANYIR---GYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVI 366
Cdd:cd14600    37 LPQNMDKNRYKDVLPYDATRVVL------QGNEDYINASYVNmeiPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 367 VMITKLKEKNE-KCVLYWPEKRGI--YGKVEVLVTGvTECD-NYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQ 440
Cdd:cd14600   111 VMLTTLTERGRtKCHQYWPDPPDVmeYGGFRVQCHS-EDCTiAYVFREMLLTntQTGEERTVTHLQYVAWPDHGVPDDSS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 441 PLLQLMLDVEEDRLASEgrgPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHH 520
Cdd:cd14600   190 DFLEFVNYVRSKRVENE---PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCE 266


                  ..
gi 1284806101 521 AL 522
Cdd:cd14600   267 AI 268
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 296-517 1.66e-42

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 153.27  E-value: 1.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 296 KNRYKTILPNPLSRVCLRPKnITDSLSTYINANYIRGYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 375
Cdd:cd14609    45 KNRNPDFVPYDHARIKLKAE-SNPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVED 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 376 NEK-CVLYWP-EKRGIYGKVEV-LVTGVTECDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 450
Cdd:cd14609   124 GVKqCDRYWPdEGSSLYHIYEVnLVSEHIWCEDFLVRSFYLKnvQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVN 203

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 451 EdrlASEGRG-PVVVHCSAGIGRTGCFIATSIGCQQLKeEGV--VDALSIVCQLRVDRGGMVQTSEQYEF 517
Cdd:cd14609   204 K---CYRGRScPIIVHCSDGAGRTGTYILIDMVLNRMA-KGVkeIDIAATLEHVRDQRPGMVRTKDQFEF 269
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 273-525 4.09e-42

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: 152.46  E-value: 4.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 273 SEFMEIPMNFVDP--KEIDIPRHGTKNRYKTILPNPLSRVCLRPKNitDSLSTYINANYIR-GYSGKEKAFIATQGPMIN 349
Cdd:cd14599    16 TEYEQIPKKKADGvfTTATLPENAERNRIREVVPYEENRVELVPTK--ENNTGYINASHIKvTVGGEEWHYIATQGPLPH 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 350 TVNDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPE-----KRGIYGKVEVLVTGVTECDNYTIRNLVLKQ--GSHTQH 421
Cdd:cd14599    94 TCHDFWQMVWEQGVNVIAMVTAEEEGGRsKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERT 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 422 VKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASEG--------RGPVVVHCSAGIGRTGCFIATS--IGCQQLKEEgv 491
Cdd:cd14599   174 VWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSmldstkncNPPIVVHCSAGVGRTGVVILTElmIGCLEHNEK-- 251

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1284806101 492 VDALSIVCQLRVDRGGMVQTSEQYEFVHHALCLF 525
Cdd:cd14599   252 VEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQF 285
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 295-530 5.82e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 152.46  E-value: 5.82e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 295 TKNRYKTILPNPLSRVCLRpknITDSLSTYINANYIRGYSGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 374
Cdd:PHA02742   54 KKCRYPDAPCFDRNRVILK---IEDGGDDFINASYVDGHNAKGR-FICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 375 KN-EKCVLYW-PEKRG--IYGKVEVLVTGVTECDNYTIRNLVLKQGS--HTQHVKHYWYTSWPDHKTPDSAQPLLQLMLD 448
Cdd:PHA02742  130 DGkEACYPYWmPHERGkaTHGEFKIKTKKIKSFRNYAVTNLCLTDTNtgASLDIKHFAYEDWPHGGLPRDPNKFLDFVLA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 449 VEEDRLASE---------GRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVH 519
Cdd:PHA02742  210 VREADLKADvdikgenivKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289

                         250
                  ....*....|.
gi 1284806101 520 HALCLFESRLS 530
Cdd:PHA02742  290 FIVLIFAKLMA 300
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 324-517 1.27e-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: 148.38  E-value: 1.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIR-GYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNE--KCVLYWPEKRG---IYGKVEVLV 397
Cdd:cd17658     1 YINASLVEtPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStaKCADYFPAEENesrEFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 398 TGVTECDN-YTIRNLVLKQGSHTQ---HVKHYWYTSWPDHKTPDSAQPLLQLmldVEEDRLASEGRGPVVVHCSAGIGRT 473
Cdd:cd17658    81 KKLKHSQHsITLRVLEVQYIESEEpplSVLHIQYPEWPDHGVPKDTRSVREL---LKRLYGIPPSAGPIVVHCSAGIGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1284806101 474 GCFIATSIGCQQLKeEGVVDALSI---VCQLRVDRGGMVQTSEQYEF 517
Cdd:cd17658   158 GAYCTIHNTIRRIL-EGDMSAVDLsktVRKFRSQRIGMVQTQDQYIF 203
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 272-522 2.83e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 151.33  E-value: 2.83e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 272 QSEFMEIPMNFVDPKEIDiPRHGTKNRYKTILPNPLSRVCLR--------------PKNI----TDSLSTYINANYIRGY 333
Cdd:PHA02746   31 HAEVMDIPIRGTTNHFLK-KENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdGKKIevtsEDNAENYIHANFVDGF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 334 SGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPEKRG---IYGKVEVLVTGVTECDNYTIRN 410
Cdd:PHA02746  110 KEANK-FICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKEEDselAFGRFVAKILDIIEELSFTKTR 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 411 LVL--KQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLA--------SEGRGPVVVHCSAGIGRTGCFIATS 480
Cdd:PHA02746  189 LMItdKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAElikqadndPQTLGPIVVHCSAGIGRAGTFCAID 268

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1284806101 481 IGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:PHA02746  269 NALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 324-522 3.58e-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: 144.70  E-value: 3.58e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIR---GYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKRG--IYGKVEvlV 397
Cdd:cd14601     2 YINANYINmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRvKCHQYWPEPSGssSYGGFQ--V 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 398 TGVTECDN--YTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRlaSEGRGPVVVHCSAGIGRT 473
Cdd:cd14601    80 TCHSEEGNpaYVFREMTLTnlEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKR--AGKDEPVVVHCSAGIGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1284806101 474 GCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd14601   158 GVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAI 206
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 291-522 5.26e-40

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: 145.88  E-value: 5.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 291 PRHGTKNRYKTILPNPLSRVCLRpknitDSLSTYINANYIRgYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMIT 370
Cdd:cd14607    22 PENRNRNRYRDVSPYDHSRVKLQ-----NTENDYINASLVV-IEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 371 KLKEKN-EKCVLYWP---EKRGIYGKVEVLVTGVTE--CDNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQPL 442
Cdd:cd14607    96 RIVEKDsVKCAQYWPtdeEEVLSFKETGFSVKLLSEdvKSYYTVHLLQLEniNSGETRTISHFHYTTWPDFGVPESPASF 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 443 LQLMLDVEEDRLASEGRGPVVVHCSAGIGRTGCF--IATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHH 520
Cdd:cd14607   176 LNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFslVDTCLVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLRFSYM 255


                  ..
gi 1284806101 521 AL 522
Cdd:cd14607   256 AV 257
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 324-519 6.88e-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: 143.68  E-value: 6.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVM-ITKLKEKNEKCVLYWPEKRG---IYGKVEVLVTG 399
Cdd:cd14539     1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMlVSEQENEKQKVHRYWPTERGqalVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 400 VTECDNYTIR--NLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASEG-RGPVVVHCSAGIGRTGCF 476
Cdd:cd14539    81 VRTTPTHVERiiSIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSlQTPIVVHCSSGVGRTGAF 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1284806101 477 IATSIGCQQLKEE-GVVDALSIVCQLRVDRGGMVQTSEQYEFVH 519
Cdd:cd14539   161 CLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
PHA02738 PHA02738
hypothetical protein; Provisional
 297-522 2.36e-39

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 145.84  E-value: 2.36e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 297 NRYKTILPNPLSRVCL-RPKNITDslstYINANYIRGYSGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 375
Cdd:PHA02738   53 NRYLDAVCFDHSRVILpAERNRGD----YINANYVDGFEYKKK-FICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEN 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 376 N-EKCVLYWPEKRG---IYGKVEVLVTGVTECDNYTIRNLVLKQG-SHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 450
Cdd:PHA02738  128 GrEKCFPYWSDVEQgsiRFGKFKITTTQVETHPHYVKSTLLLTDGtSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVR 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 451 --EDRLASEGRG---------PVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVH 519
Cdd:PHA02738  208 qcQKELAQESLQighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCY 287


                  ...
gi 1284806101 520 HAL 522
Cdd:PHA02738  288 RAV 290
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
281-517 1.11e-38

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 142.92  E-value: 1.11e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 281 NFVDPKEIDIPRHGTKNRYKTILPNPLSRVclrPKNITdslstYINANYIRGysGKEKAFIATQGPMINTVNDFWQMVWQ 360
Cdd:COG5599    30 SHNDPQYLQNINGSPLNRFRDIQPYKETAL---RANLG-----YLNANYIQV--IGNHRYIATQYPLEEQLEDFFQMLFD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 361 EDSPVIVMIT---KLKEKNEKCVLYWPEKrGIYGK--VEVLVTGVTEC-DNYTIRNLVLKQ---GSHTQHVKHYWYTSWP 431
Cdd:COG5599   100 NNTPVLVVLAsddEISKPKVKMPVYFRQD-GEYGKyeVSSELTESIQLrDGIEARTYVLTIkgtGQKKIEIPVLHVKNWP 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 432 DHKTPDSAQpLLQLMLDV-EEDRLASEGRGPVVVHCSAGIGRTGCFIAtsigCQQLKEEG------VVDALSIVCQLRVD 504
Cdd:COG5599   179 DHGAISAEA-LKNLADLIdKKEKIKDPDKLLPVVHCRAGVGRTGTLIA----CLALSKSInalvqiTLSVEEIVIDMRTS 253

                         250
                  ....*....|....
gi 1284806101 505 RG-GMVQTSEQYEF 517
Cdd:COG5599   254 RNgGMVQTSEQLDV 267
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 324-525 5.49e-38

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: 138.95  E-value: 5.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIR-GYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK-NEKCVLYWP-----EKRGIYGKVEVL 396
Cdd:cd14598     1 YINASHIKvTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGgREKSFRYWPrlgsrHNTVTYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 397 VTGVTECDNYTIRNLVLKQ--GSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASEG-------RGPVVVHCS 467
Cdd:cd14598    81 TRFRTDSGCYATTGLKIKHllTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNStidpkspNPPVLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1284806101 468 AGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHALCLF 525
Cdd:cd14598   161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQF 218
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 422-522 1.87e-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: 133.64  E-value: 1.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101  422 VKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQL-KEEGVVDALSIVCQ 500
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDTVKE 81

                           90       100
                   ....*....|....*....|..
gi 1284806101  501 LRVDRGGMVQTSEQYEFVHHAL 522
Cdd:smart00012  82 LRSQRPGMVQTEEQYLFLYRAL 103
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
422-522 1.87e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 133.64  E-value: 1.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101  422 VKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQL-KEEGVVDALSIVCQ 500
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDTVKE 81

                           90       100
                   ....*....|....*....|..
gi 1284806101  501 LRVDRGGMVQTSEQYEFVHHAL 522
Cdd:smart00404  82 LRSQRPGMVQTEEQYLFLYRAL 103
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 291-519 5.03e-37

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 139.37  E-value: 5.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 291 PRHGTKNRYKTILPNPLSRVCLRPKniTDSLSTYINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMIT 370
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDSG--GGSTSDYIHANWIDGFE-DDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLT 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 371 KLKEKN--EKCVLYW-PEKRGIYG----KVEVLVTGVTECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLL 443
Cdd:PHA02747  126 PTKGTNgeEKCYQYWcLNEDGNIDmedfRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFI 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 444 QLMLDVEEDRLASEGR--------GPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQY 515
Cdd:PHA02747  206 KFIKIIDINRKKSGKLfnpkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285


                  ....
gi 1284806101 516 EFVH 519
Cdd:PHA02747  286 LFIQ 289
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 324-519 1.54e-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: 126.29  E-value: 1.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLkEKNEKCVLYWPEK-RGIYGKVEV-LVTGVT 401
Cdd:cd14634     1 YINAALMDSHK-QPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM-DAAQLCMQYWPEKtSCCYGPIQVeFVSADI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 402 ECDN----YTIRNLVLKQGSHtQHVKHYWYTSWPDHK-TPDSAQPLLQLMLDVEEDRLASEGR-GPVVVHCSAGIGRTGC 475
Cdd:cd14634    79 DEDIisriFRICNMARPQDGY-RIVQHLQYIGWPAYRdTPPSKRSILKVVRRLEKWQEQYDGReGRTVVHCLNGGGRSGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1284806101 476 FIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVH 519
Cdd:cd14634   158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVY 201
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 324-519 1.15e-31

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: 121.29  E-value: 1.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLkEKNEKCVLYWPEKRGI-YGKVEV-LVTGVT 401
Cdd:cd14636     1 YINAALMDSYR-QPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV-DLAQGCPQYWPEEGMLrYGPIQVeCMSCSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 402 ECDN----YTIRNLVLKQGSHTQhVKHYWYTSWPDHK-TPDSAQPLLQLMLDVEE-DRLASEGRGPVVVHCSAGIGRTGC 475
Cdd:cd14636    79 DCDVisriFRICNLTRPQEGYLM-VQQFQYLGWASHReVPGSKRSFLKLILQVEKwQEECDEGEGRTIIHCLNGGGRSGM 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1284806101 476 FIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVH 519
Cdd:cd14636   158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 324-517 1.10e-30

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: 118.19  E-value: 1.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLkEKNEKCVLYWPEKRGIYGKVEVLVTGVTE- 402
Cdd:cd14550     1 YINASYLQGYR-RSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNEDEPIYWPTKEKPLECETFKVTLSGEd 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 403 ------CDNYTIRNLVL--KQGSHTQHVKHYWYTSWPDHKTPDSAQplLQLMLDVEEDrlASEGRGPVVVHCSAGIGRTG 474
Cdd:cd14550    79 hsclsnEIRLIVRDFILesTQDDYVLEVRQFQCPSWPNPCSPIHTV--FELINTVQEW--AQQRDGPIVVHDRYGGVQAA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1284806101 475 CFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEF 517
Cdd:cd14550   155 TFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQF 197
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 324-519 9.17e-29

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: 113.08  E-value: 9.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNEK--CVLYWPEK-RGIYGKVEV-LVTG 399
Cdd:cd14637     1 YINAALTDSYT-RSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwpCLQYWPEPgLQQYGPMEVeFVSG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 400 VTECDNYT----IRNLVLKQGSHTQhVKHYWYTSWPDHK-TPDSAQPLLQLMLDVEEDRlASEGRGPVVVHCSAGIGRTG 474
Cdd:cd14637    80 SADEDIVTrlfrVQNITRLQEGHLM-VRHFQFLRWSAYRdTPDSKKAFLHLLASVEKWQ-RESGEGRTVVHCLNGGGRSG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1284806101 475 CFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVH 519
Cdd:cd14637   158 TYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCY 202
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 324-522 1.80e-28

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: 112.39  E-value: 1.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVTGVTE- 402
Cdd:cd17669     1 YINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEe 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 403 --C----DNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQplLQLMLDVEEDrlASEGRGPVVVHCSAGIGRTG 474
Cdd:cd17669    80 hkClsneEKLIIQDFILEatQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEE--AANRDGPMIVHDEHGGVTAG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1284806101 475 CFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd17669   156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 324-522 9.80e-26

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: 104.76  E-value: 9.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVTGVTE- 402
Cdd:cd17670     1 YINASYIMGYY-RSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 403 --C----DNYTIRNLVLK--QGSHTQHVKHYWYTSWPDHKTPDSAQplLQLMLDVEEDRLASEgrGPVVVHCSAGIGRTG 474
Cdd:cd17670    80 rlClsneEQIIIHDFILEatQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRD--GPTIVHDEFGAVSAG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1284806101 475 CFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHAL 522
Cdd:cd17670   156 TLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 324-519 1.72e-23

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: 98.22  E-value: 1.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 324 YINANYIRGYSgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLkEKNEKCVLYWPEKrGIY--GKVEV-LVTGV 400
Cdd:cd14635     1 YINAALMDSYK-QPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV-DPAQLCPQYWPEN-GVHrhGPIQVeFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 401 TECDN----YTIRNLVLKQGSHtQHVKHYWYTSWPDHK-TPDSAQPLLQLMLDVeeDRLASE---GRGPVVVHCSAGIGR 472
Cdd:cd14635    78 LEEDIisriFRIYNAARPQDGY-RMVQQFQFLGWPMYRdTPVSKRSFLKLIRQV--DKWQEEyngGEGRTVVHCLNGGGR 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1284806101 473 TGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVH 519
Cdd:cd14635   155 SGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 313-516 1.41e-17

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 81.68  E-value: 1.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 313 RPKNITDSLSTY----INANYIRgySGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPEKRG 388
Cdd:cd14559     2 RFTNIQTRVSTPvgknLNANRVQ--IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 389 IYGKVEVLVTGV--------TECDNYtirNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQpLLQL--MLDVEEDR----- 453
Cdd:cd14559    80 TYGSVTVKSKKTgkdelvdgLKADMY---NLKITDGNKTITIPVVHVTNWPDHTAISSEG-LKELadLVNKSAEEkrnfy 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1284806101 454 -------LASEGRGPVVVHCSAGIGRTGCFIATSigcQQLKEEGVVDALSIVCQLRVDRGG-MVQTSEQYE 516
Cdd:cd14559   156 kskgssaINDKNKLLPVIHCRAGVGRTGQLAAAM---ELNKSPNNLSVEDIVSDMRTSRNGkMVQKDEQLD 223
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 308-527 4.66e-15

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 75.77  E-value: 4.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 308 SRVCLRPKnitdslSTYINANYIRGYSGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNekCVL-YWPEK 386
Cdd:PHA02740   68 RRIKLFND------EKVLDARFVDGYDFEQK-FICIINLCEDACDKFLQALSDNKVQIIVLISRHADKK--CFNqFWSLK 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 387 RG---IYGKVEVLVTGVTECDNYTIRNLVLK-QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE-----DRLASE 457
Cdd:PHA02740  139 EGcviTSDKFQIETLEIIIKPHFNLTLLSLTdKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDlcadlEKHKAD 218

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1284806101 458 GR-GPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHALCLFES 527
Cdd:PHA02740  219 GKiAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLK 289
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 449-520 1.89e-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: 63.91  E-value: 1.89e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1284806101 449 VEEDRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKeegvvDALSIVCQLRVDRGG-MVQTSEQYEFVHH 520
Cdd:cd14494    46 LEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRPGgIPQTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
430-520 1.77e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 56.13  E-value: 1.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 430 WPDHKTPDSAQpLLQLMLDVEEdrLASEGRgPVVVHCSAGIGRTGCFIAtsigcQQLKEEGV--VDALSIVCQLrvdRGG 507
Cdd:COG2453    55 IPDFGAPDDEQ-LQEAVDFIDE--ALREGK-KVLVHCRGGIGRTGTVAA-----AYLVLLGLsaEEALARVRAA---RPG 122

                          90
                  ....*....|...
gi 1284806101 508 MVQTSEQYEFVHH 520
Cdd:COG2453   123 AVETPAQRAFLER 135
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 431-519 6.64e-09

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 54.96  E-value: 6.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 431 PDHKTPDSAQPLLQLMldvEEDRLASEGRGPVVVHCSAGIGRTGCFIAtsigCQQLKEEGVVDALSIVCQLRVDRGGMVQ 510
Cdd:cd14505    81 PDGGVPSDIAQWQELL---EELLSALENGKKVLIHCKGGLGRTGLIAA----CLLLELGDTLDPEQAIAAVRALRPGAIQ 153


                  ....*....
gi 1284806101 511 TSEQYEFVH 519
Cdd:cd14505   154 TPKQENFLH 162
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 446-518 1.64e-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: 50.74  E-value: 1.64e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1284806101 446 MLDVEEDRLASEGrgPVVVHCSAGIGRTGCFIAtsigCqQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFV 518
Cdd:cd14504    71 FLDIVEEANAKNE--AVLVHCLAGKGRTGTMLA----C-YLVKTGKISAVDAINEIRRIRPGSIETSEQEKFV 136
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 403-506 8.52e-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: 48.73  E-value: 8.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 403 CDNYTIRNLVLKQGSHTQHVKHYWYT-SWPDHKTPdsaqPLLQLM--LDVEEDRLASEGRGPVVVHCSAGIGRTGcFIAT 479
Cdd:cd14497    40 PDHYMIFNLSEEEYDDDSKFEGRVLHyGFPDHHPP----PLGLLLeiVDDIDSWLSEDPNNVAVVHCKAGKGRTG-TVIC 114

                          90       100
                  ....*....|....*....|....*..
gi 1284806101 480 SIGCQQLKEEGVVDALSIVCQLRVDRG 506
Cdd:cd14497   115 AYLLYYGQYSTADEALEYFAKKRFKEG 141
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 429-519 2.23e-05

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 45.42  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 429 SWPDHKTPDsaqplLQLMLD-VEEDRLASEGRGPVVVHCSAGIGRTGCFIAtsigCQQLKEEGVV--DALSIVcqlRVDR 505
Cdd:cd14506    83 GWKDYGVPS-----LTTILDiVKVMAFALQEGGKVAVHCHAGLGRTGVLIA----CYLVYALRMSadQAIRLV---RSKR 150

                          90
                  ....*....|....
gi 1284806101 506 GGMVQTSEQYEFVH 519
Cdd:cd14506   151 PNSIQTRGQVLCVR 164
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
437-474 4.98e-04

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


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 41.87  E-value: 4.98e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1284806101 437 DSAQPLLQLMLDVeedrLASEGRGPVVVHCSAGIGRTG 474
Cdd:COG2365   115 PDAADAYRAAFRA----LADAENGPVLFHCTAGKDRTG 148
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 459-478 8.05e-04

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


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 40.51  E-value: 8.05e-04
                          10        20
                  ....*....|....*....|
gi 1284806101 459 RGPVVVHCSAGIGRTGCFIA 478
Cdd:cd14499   109 KGAIAVHCKAGLGRTGTLIA 128
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 415-495 2.02e-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: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 415 QGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDrlasegrGPVVVHCSAGIGRTGCFIA-TSIGCQQLKEEGVVD 493
Cdd:cd14529    52 AAAKIDGVKYVNLPLSATRPTESDVQSFLLIMDLKLAP-------GPVLIHCKHGKDRTGLVSAlYRIVYGGSKEEANED 124


                  ..
gi 1284806101 494 AL 495
Cdd:cd14529   125 YR 126
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 431-520 2.76e-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: 38.88  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284806101 431 PDHKTPDsaqplLQLMLDV---EEDRLASEGRGPVVVHCSAGIGRTGCFIAT----SIGCQQLKEegvvdALSIVCQLRV 503
Cdd:cd14510    82 DDHNVPT-----LDEMLSFtaeVREWMAADPKNVVAIHCKGGKGRTGTMVCAwliySGQFESAKE-----ALEYFGERRT 151

                          90       100
                  ....*....|....*....|..
gi 1284806101 504 DRGGM-----VQTSEQYEFVHH 520
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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