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Conserved domains on  [gi|39654746]
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Chain A, Protein-tyrosine phosphatase yopH

Protein Classification

COG5599 family protein( domain architecture ID 11475662)

COG5599 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
24-306 1.96e-134

Protein tyrosine phosphatase [Signal transduction mechanisms];


:

Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 382.52  E-value: 1.96e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  24 VSPYGPEA----RAELSSRLTTLRNTLAPATNDPRYLQACGGEKLNRFRDIQCRRQTAVRAD---LNANYIQV-GNTRTI 95
Cdd:COG5599   1 VSPKNPIAikseEEKINSRLSTLTNELAPSHNDPQYLQNINGSPLNRFRDIQPYKETALRANlgyLNANYIQViGNHRYI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  96 ACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRFGMPDYFRQSGTYGSITVESKMTQQVGLGDGIMADMYTLTIR 175
Cdd:COG5599  81 ATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKPKVKMPVYFRQDGEYGKYEVSSELTESIQLRDGIEARTYVLTIK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 176 EAGQKTISVPVVHVGNWPDQTAVSSEVTKALASLVDQTAETKrnmyeskgssavaDDSKLRPVIHCRAGVGRTAQLIGAM 255
Cdd:COG5599 161 GTGQKKIEIPVLHVKNWPDHGAISAEALKNLADLIDKKEKIK-------------DPDKLLPVVHCRAGVGRTGTLIACL 227

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 39654746 256 CMNDSRNSQ----LSVEDMVSQMRVQRNGIMVQKDEQLDVLIKLAEGQGRPLLNS 306
Cdd:COG5599 228 ALSKSINALvqitLSVEEIVIDMRTSRNGGMVQTSEQLDVLVKLAEQQIRPLLRS 282
 
Name Accession Description Interval E-value
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
24-306 1.96e-134

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 382.52  E-value: 1.96e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  24 VSPYGPEA----RAELSSRLTTLRNTLAPATNDPRYLQACGGEKLNRFRDIQCRRQTAVRAD---LNANYIQV-GNTRTI 95
Cdd:COG5599   1 VSPKNPIAikseEEKINSRLSTLTNELAPSHNDPQYLQNINGSPLNRFRDIQPYKETALRANlgyLNANYIQViGNHRYI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  96 ACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRFGMPDYFRQSGTYGSITVESKMTQQVGLGDGIMADMYTLTIR 175
Cdd:COG5599  81 ATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKPKVKMPVYFRQDGEYGKYEVSSELTESIQLRDGIEARTYVLTIK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 176 EAGQKTISVPVVHVGNWPDQTAVSSEVTKALASLVDQTAETKrnmyeskgssavaDDSKLRPVIHCRAGVGRTAQLIGAM 255
Cdd:COG5599 161 GTGQKKIEIPVLHVKNWPDHGAISAEALKNLADLIDKKEKIK-------------DPDKLLPVVHCRAGVGRTGTLIACL 227

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 39654746 256 CMNDSRNSQ----LSVEDMVSQMRVQRNGIMVQKDEQLDVLIKLAEGQGRPLLNS 306
Cdd:COG5599 228 ALSKSINALvqitLSVEEIVIDMRTSRNGGMVQTSEQLDVLVKLAEQQIRPLLRS 282
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 65-294 9.43e-124

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: 353.24  E-value: 9.43e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  65 NRFRDIQCRRQTAVRADLNANYIQVGN-TRTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIanQRFGMPDYFRQS 143
Cdd:cd14559   1 NRFTNIQTRVSTPVGKNLNANRVQIGNkNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDI--QRKGLPPYFRQS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 144 GTYGSITVESKMTQQVGLGDGIMADMYTLTIREaGQKTISVPVVHVGNWPDQTAVSSEVTKALASLVDQTAETKRNMYES 223
Cdd:cd14559  79 GTYGSVTVKSKKTGKDELVDGLKADMYNLKITD-GNKTITIPVVHVTNWPDHTAISSEGLKELADLVNKSAEEKRNFYKS 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39654746 224 KGSSAVADDSKLRPVIHCRAGVGRTAQLIGAMCMNDSRNsQLSVEDMVSQMRVQRNGIMVQKDEQLDVLIK 294
Cdd:cd14559 158 KGSSAINDKNKLLPVIHCRAGVGRTGQLAAAMELNKSPN-NLSVEDIVSDMRTSRNGKMVQKDEQLDTLKE 227
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
63-296 1.67e-42

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 147.04  E-value: 1.67e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746     63 KLNRFRDIQCRRQTAVRAD---------LNANYIQV--GNTRTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEiaN 131
Cdd:smart00194  29 DKNRYKDVLPYDHTRVKLKpppgegsdyINASYIDGpnGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVE--K 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746    132 QRFGMPDYF----RQSGTYGSITVESKMTQQVGlgdgiMADMYTLTIREAGQ-KTISVPVVHVGNWPDQTAVSS-EVTKA 205
Cdd:smart00194 107 GREKCAQYWpdeeGEPLTYGDITVTLKSVEKVD-----DYTIRTLEVTNTGCsETRTVTHYHYTNWPDHGVPESpESILD 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746    206 LASLVDQTAETKRNmyeskgssavaddsklRPVIHCRAGVGRTAQLIGAMCMNDS--RNSQLSVEDMVSQMRVQRNGiMV 283
Cdd:smart00194 182 LIRAVRKSQSTSTG----------------PIVVHCSAGVGRTGTFIAIDILLQQleAGKEVDIFEIVKELRSQRPG-MV 244

                          250
                   ....*....|...
gi 39654746    284 QKDEQLDVLIKLA 296
Cdd:smart00194 245 QTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
65-289 1.44e-26

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 104.25  E-value: 1.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746    65 NRFRDIQCRRQTAVRAD--------LNANYIQ-VGNTRT-IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRF 134
Cdd:pfam00102   5 NRYKDVLPYDHTRVKLTgdpgpsdyINASYIDgYKKPKKyIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGREKC 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746   135 GM--PDYFRQSGTYGSITVEskMTQQVGLGDGIMadMYTLTIREAGQKTI-SVPVVHVGNWPDQTAVSSevTKALASLVD 211
Cdd:pfam00102  85 AQywPEEEGESLEYGDFTVT--LKKEKEDEKDYT--VRTLEVSNGGSEETrTVKHFHYTGWPDHGVPES--PNSLLDLLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746   212 QTaetkRNMYESKGSSAVaddsklrpVIHCRAGVGRTAQLIGAMCMNDS--RNSQLSVEDMVSQMRVQRNGiMVQKDEQL 289
Cdd:pfam00102 159 KV----RKSSLDGRSGPI--------VVHCSAGIGRTGTFIAIDIALQQleAEGEVDIFQIVKELRSQRPG-MVQTLEQY 225
PRK15375 PRK15375
type III secretion system effector GTPase-activating protein SptP;
90-299 4.93e-23

type III secretion system effector GTPase-activating protein SptP;


Pssm-ID: 185273 [Multi-domain]  Cd Length: 535  Bit Score: 98.72  E-value: 4.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746   90 GNTRTIACQYPLQS--QLESHFRMLAENRTPVLAVLASSSEIANQRfgMPDYFRQSGTYGSITVESKMTQQVGLGDGIma 167
Cdd:PRK15375 332 GKPVALAGSYPKNTpdALEAHMKMLLEKECSCLVVLTSEDQMQAKQ--LPPYFRGSYTFGEVHTNSQKVSSASQGEAI-- 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  168 DMYTLTIrEAGQKTISVPVVHVGNWPDQTAVSSevTKALASLVDQTAETKRNmyeskGSSAVADDSKLRPVIHCRAGVGR 247
Cdd:PRK15375 408 DQYNMQL-SCGEKRYTIPVLHVKNWPDHQPLPS--TDQLEYLADRVKNSNQN-----GAPGRSSSDKHLPMIHCLGGVGR 479

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 39654746  248 TAQLIGAMCMNDSRNSQLsvEDMVSQMRVQRNGIMVQKDEQLdVLIKLAEGQ 299
Cdd:PRK15375 480 TGTMAAALVLKDNPHSNL--EQVRADFRNSRNNRMLEDASQF-VQLKAMQAQ 528
 
Name Accession Description Interval E-value
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
24-306 1.96e-134

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 382.52  E-value: 1.96e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  24 VSPYGPEA----RAELSSRLTTLRNTLAPATNDPRYLQACGGEKLNRFRDIQCRRQTAVRAD---LNANYIQV-GNTRTI 95
Cdd:COG5599   1 VSPKNPIAikseEEKINSRLSTLTNELAPSHNDPQYLQNINGSPLNRFRDIQPYKETALRANlgyLNANYIQViGNHRYI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  96 ACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRFGMPDYFRQSGTYGSITVESKMTQQVGLGDGIMADMYTLTIR 175
Cdd:COG5599  81 ATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKPKVKMPVYFRQDGEYGKYEVSSELTESIQLRDGIEARTYVLTIK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 176 EAGQKTISVPVVHVGNWPDQTAVSSEVTKALASLVDQTAETKrnmyeskgssavaDDSKLRPVIHCRAGVGRTAQLIGAM 255
Cdd:COG5599 161 GTGQKKIEIPVLHVKNWPDHGAISAEALKNLADLIDKKEKIK-------------DPDKLLPVVHCRAGVGRTGTLIACL 227

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 39654746 256 CMNDSRNSQ----LSVEDMVSQMRVQRNGIMVQKDEQLDVLIKLAEGQGRPLLNS 306
Cdd:COG5599 228 ALSKSINALvqitLSVEEIVIDMRTSRNGGMVQTSEQLDVLVKLAEQQIRPLLRS 282
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 65-294 9.43e-124

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: 353.24  E-value: 9.43e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  65 NRFRDIQCRRQTAVRADLNANYIQVGN-TRTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIanQRFGMPDYFRQS 143
Cdd:cd14559   1 NRFTNIQTRVSTPVGKNLNANRVQIGNkNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDI--QRKGLPPYFRQS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 144 GTYGSITVESKMTQQVGLGDGIMADMYTLTIREaGQKTISVPVVHVGNWPDQTAVSSEVTKALASLVDQTAETKRNMYES 223
Cdd:cd14559  79 GTYGSVTVKSKKTGKDELVDGLKADMYNLKITD-GNKTITIPVVHVTNWPDHTAISSEGLKELADLVNKSAEEKRNFYKS 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39654746 224 KGSSAVADDSKLRPVIHCRAGVGRTAQLIGAMCMNDSRNsQLSVEDMVSQMRVQRNGIMVQKDEQLDVLIK 294
Cdd:cd14559 158 KGSSAINDKNKLLPVIHCRAGVGRTGQLAAAMELNKSPN-NLSVEDIVSDMRTSRNGKMVQKDEQLDTLKE 227
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
63-296 1.67e-42

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 147.04  E-value: 1.67e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746     63 KLNRFRDIQCRRQTAVRAD---------LNANYIQV--GNTRTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEiaN 131
Cdd:smart00194  29 DKNRYKDVLPYDHTRVKLKpppgegsdyINASYIDGpnGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVE--K 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746    132 QRFGMPDYF----RQSGTYGSITVESKMTQQVGlgdgiMADMYTLTIREAGQ-KTISVPVVHVGNWPDQTAVSS-EVTKA 205
Cdd:smart00194 107 GREKCAQYWpdeeGEPLTYGDITVTLKSVEKVD-----DYTIRTLEVTNTGCsETRTVTHYHYTNWPDHGVPESpESILD 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746    206 LASLVDQTAETKRNmyeskgssavaddsklRPVIHCRAGVGRTAQLIGAMCMNDS--RNSQLSVEDMVSQMRVQRNGiMV 283
Cdd:smart00194 182 LIRAVRKSQSTSTG----------------PIVVHCSAGVGRTGTFIAIDILLQQleAGKEVDIFEIVKELRSQRPG-MV 244

                          250
                   ....*....|...
gi 39654746    284 QKDEQLDVLIKLA 296
Cdd:smart00194 245 QTEEQYIFLYRAI 257
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 82-294 1.91e-32

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: 118.93  E-value: 1.91e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQV--GNTRTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEiaNQRFGMPDYFRQSG----TYGSITVESKM 155
Cdd:cd00047   2 INASYIDGyrGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVE--KGREKCERYWPEEGgkplEYGDITVTLVS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 156 TQQVGlgdgiMADMYTLTIREAG-QKTISVPVVHVGNWPDQTAVSSevTKALASLVDQTAETKRNmyeskgssavaddSK 234
Cdd:cd00047  80 EEELS-----DYTIRTLELSPKGcSESREVTHLHYTGWPDHGVPSS--PEDLLALVRRVRKEARK-------------PN 139

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39654746 235 LRPVIHCRAGVGRTAQLIGAMCMNDS--RNSQLSVEDMVSQMRVQRNGiMVQKDEQLDVLIK 294
Cdd:cd00047 140 GPIVVHCSAGVGRTGTFIAIDILLERleAEGEVDVFEIVKALRKQRPG-MVQTLEQYEFIYE 200
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
65-289 1.44e-26

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 104.25  E-value: 1.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746    65 NRFRDIQCRRQTAVRAD--------LNANYIQ-VGNTRT-IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRF 134
Cdd:pfam00102   5 NRYKDVLPYDHTRVKLTgdpgpsdyINASYIDgYKKPKKyIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGREKC 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746   135 GM--PDYFRQSGTYGSITVEskMTQQVGLGDGIMadMYTLTIREAGQKTI-SVPVVHVGNWPDQTAVSSevTKALASLVD 211
Cdd:pfam00102  85 AQywPEEEGESLEYGDFTVT--LKKEKEDEKDYT--VRTLEVSNGGSEETrTVKHFHYTGWPDHGVPES--PNSLLDLLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746   212 QTaetkRNMYESKGSSAVaddsklrpVIHCRAGVGRTAQLIGAMCMNDS--RNSQLSVEDMVSQMRVQRNGiMVQKDEQL 289
Cdd:pfam00102 159 KV----RKSSLDGRSGPI--------VVHCSAGIGRTGTFIAIDIALQQleAEGEVDIFQIVKELRSQRPG-MVQTLEQY 225
PRK15375 PRK15375
type III secretion system effector GTPase-activating protein SptP;
90-299 4.93e-23

type III secretion system effector GTPase-activating protein SptP;


Pssm-ID: 185273 [Multi-domain]  Cd Length: 535  Bit Score: 98.72  E-value: 4.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746   90 GNTRTIACQYPLQS--QLESHFRMLAENRTPVLAVLASSSEIANQRfgMPDYFRQSGTYGSITVESKMTQQVGLGDGIma 167
Cdd:PRK15375 332 GKPVALAGSYPKNTpdALEAHMKMLLEKECSCLVVLTSEDQMQAKQ--LPPYFRGSYTFGEVHTNSQKVSSASQGEAI-- 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  168 DMYTLTIrEAGQKTISVPVVHVGNWPDQTAVSSevTKALASLVDQTAETKRNmyeskGSSAVADDSKLRPVIHCRAGVGR 247
Cdd:PRK15375 408 DQYNMQL-SCGEKRYTIPVLHVKNWPDHQPLPS--TDQLEYLADRVKNSNQN-----GAPGRSSSDKHLPMIHCLGGVGR 479

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 39654746  248 TAQLIGAMCMNDSRNSQLsvEDMVSQMRVQRNGIMVQKDEQLdVLIKLAEGQ 299
Cdd:PRK15375 480 TGTMAAALVLKDNPHSNL--EQVRADFRNSRNNRMLEDASQF-VQLKAMQAQ 528
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
183-294 4.60e-18

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 77.78  E-value: 4.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746    183 SVPVVHVGNWPDQTAVSSEVtkalaSLVDQTAETKRNMYESKGSSAVaddsklrpVIHCRAGVGRTAQLIGA---MCMND 259
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPD-----SILELLRAVKKNLNQSESSGPV--------VVHCSAGVGRTGTFVAIdilLQQLE 67

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 39654746    260 SRNSQLSVEDMVSQMRVQRNGiMVQKDEQLDVLIK 294
Cdd:smart00404  68 AEAGEVDIFDTVKELRSQRPG-MVQTEEQYLFLYR 101
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 183-294 4.60e-18

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: 77.78  E-value: 4.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746    183 SVPVVHVGNWPDQTAVSSEVtkalaSLVDQTAETKRNMYESKGSSAVaddsklrpVIHCRAGVGRTAQLIGA---MCMND 259
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPD-----SILELLRAVKKNLNQSESSGPV--------VVHCSAGVGRTGTFVAIdilLQQLE 67

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 39654746    260 SRNSQLSVEDMVSQMRVQRNGiMVQKDEQLDVLIK 294
Cdd:smart00012  68 AEAGEVDIFDTVKELRSQRPG-MVQTEEQYLFLYR 101
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 236-294 6.65e-15

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: 69.69  E-value: 6.65e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 39654746 236 RPVIHCRAGVGRTAQLIGAMCMNDSRNsqlSVEDMVSQMRVQRNGIMVQKDEQLDVLIK 294
Cdd:cd14494  58 PVLVHCKAGVGRTGTLVACYLVLLGGM---SAEEAVRIVRLIRPGGIPQTIEQLDFLIK 113
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 82-288 8.38e-14

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: 68.99  E-value: 8.38e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQ--VGNTRTIACQYPLQSQLESHFRMLAENRTPVlaVLASSSEIANQRFGMPDYFRQSG----TYGSITVESKM 155
Cdd:cd14542   2 INANFIKgvSGSKAYIATQGPLPNTVLDFWRMIWEYNVQV--IVMACREFEMGKKKCERYWPEEGeeqlQFGPFKISLEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 156 TQQVGlgDGIMadMYTLTIReAGQKTISVPVVHVGNWPDQTAVSSevtkalaslVDQTAETKRNMYESKGSSAVaddskl 235
Cdd:cd14542  80 EKRVG--PDFL--IRTLKVT-FQKESRTVYQFHYTAWPDHGVPSS---------VDPILDLVRLVRDYQGSEDV------ 139

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39654746 236 rPV-IHCRAGVGRTaqliGAMCMND---------SRNSQLSVEDMVSQMRVQRNGiMVQKDEQ 288
Cdd:cd14542 140 -PIcVHCSAGCGRT----GTICAIDyvwnllktgKIPEEFSLFDLVREMRKQRPA-MVQTKEQ 196
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 83-292 9.27e-14

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: 68.81  E-value: 9.27e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  83 NANYIQVGNT---RTIACQYPLQSQLEsHF-RMLAENRTPVLAVLASSSEianQRFGMPDYFRQSGT----YGSITVESK 154
Cdd:cd18533   3 NASYITLPGTsskRYIATQGPLPATIG-DFwKMIWQNNVGVIVMLTPLVE---NGREKCDQYWPSGEyegeYGDLTVELV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 155 MTQQVGLGDGIMAdmyTLTIREAGQKTISVPVVHVGNWPDQTAVSSevTKALASLVDQtaetkrnmyeskgSSAVADDSK 234
Cdd:cd18533  79 SEEENDDGGFIVR---EFELSKEDGKVKKVYHIQYKSWPDFGVPDS--PEDLLTLIKL-------------KRELNDSAS 140

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39654746 235 LRP--VIHCRAGVGRTAQLIgAM-----CMNDSRNSQLSVEDM-------VSQMRVQRNGiMVQKDEQLDVL 292
Cdd:cd18533 141 LDPpiIVHCSAGVGRTGTFI-ALdslldELKRGLSDSQDLEDSedpvyeiVNQLRKQRMS-MVQTLRQYIFL 210
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 82-288 1.03e-13

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: 68.55  E-value: 1.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYI--QVGNT--RTIACQYPLQSQLESHFRMLAENRTPVLAVLA---SSSEIANQRFgMPDYFRQSGT-YGSITVES 153
Cdd:cd14538   2 INASHIriPVGGDtyHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTqdvEGGKVKCHRY-WPDSLNKPLIcGGRLEVSL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 154 KMTQQVglgDGIMADMYTLTIREAGqKTISVPVVHVGNWPDQTAVSSEVtkalaSLVDQTaetkRNMYESKGSSAVadds 233
Cdd:cd14538  81 EKYQSL---QDFVIRRISLRDKETG-EVHHITHLNFTTWPDHGTPQSAD-----PLLRFI----RYMRRIHNSGPI---- 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 39654746 234 klrpVIHCRAGVGRTAQLI---GAMCMNDsRNSQLSVEDMVSQMRVQRNGiMVQKDEQ 288
Cdd:cd14538 144 ----VVHCSAGIGRTGVLItidVALGLIE-RDLPFDIQDIVKDLREQRQG-MIQTKDQ 195
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 65-288 3.15e-13

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: 67.81  E-value: 3.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  65 NRFRDIQCRRQTAV---RAD-------LNANYIQvG----NTRTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEiA 130
Cdd:cd14547   1 NRYKTILPNEHSRVclpSVDddplssyINANYIR-GydgeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-A 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 131 NQRfgMPDYF--RQSGTYGSITVeskMTQQVGLGDGimadmYT---LTIREAGQKtISVPVVHVGNWPDQTavSSEVTKA 205
Cdd:cd14547  79 KEK--CAQYWpeEENETYGDFEV---TVQSVKETDG-----YTvrkLTLKYGGEK-RYLKHYWYTSWPDHK--TPEAAQP 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 206 LASLVdQTAETKRNMYESKGSsavaddsklrPVIHCRAGVGRT----AQLIGamCMNDSRNSQLSVEDMVSQMRVQRNGi 281
Cdd:cd14547 146 LLSLV-QEVEEARQTEPHRGP----------IVVHCSAGIGRTgcfiATSIG--CQQLREEGVVDVLGIVCQLRLDRGG- 211


                ....*..
gi 39654746 282 MVQKDEQ 288
Cdd:cd14547 212 MVQTAEQ 218
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 82-288 3.22e-12

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: 64.29  E-value: 3.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQvGNTRT---IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRFGMpdYFRQSGT--YGSITVESKMT 156
Cdd:cd14549   2 INANYVD-GYNKArayIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQ--YWPKEGTetYGNIQVTLLST 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 157 QqvglgdgIMADmYTL---TIREAGQKTI----SVPVV---HVGNWPDQtAVSSEVTKALaSLVDQtaetkrnmyeskgs 226
Cdd:cd14549  79 E-------VLAT-YTVrtfSLKNLKLKKVkgrsSERVVyqyHYTQWPDH-GVPDYTLPVL-SFVRK-------------- 134

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39654746 227 SAVADDSKLRP-VIHCRAGVGRTAQ--LIGAMCMNDSRNSQLSVEDMVSQMRVQRNgIMVQKDEQ 288
Cdd:cd14549 135 SSAANPPGAGPiVVHCSAGVGRTGTyiVIDSMLQQIQDKGTVNVFGFLKHIRTQRN-YLVQTEEQ 198
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 82-288 2.47e-11

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: 62.21  E-value: 2.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQ-VGNTRT-IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEiaNQRFGMPDYF---RQSGTYGSITVESKmt 156
Cdd:cd14619  28 INANYMPgYWSSQEfIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCME--AGRVKCEHYWpldYTPCTYGHLRVTVV-- 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 157 qqvglGDGIMADMytlTIRE------AGQKTISVPVVHVGNWPDQTAVSSEVT-KALASLVDQTAETKRnmyeSKGSsav 229
Cdd:cd14619 104 -----SEEVMENW---TVREfllkqvEEQKTLSVRHFHFTAWPDHGVPSSTDTlLAFRRLLRQWLDQTM----SGGP--- 168

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39654746 230 addsklrPVIHCRAGVGRTAQLIG--AMCMNDSRNSQLSVEDMVSQMRVQRNgIMVQKDEQ 288
Cdd:cd14619 169 -------TVVHCSAGVGRTGTLIAldVLLQQLQSEGLLGPFSFVQKMRENRP-LMVQTESQ 221
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 47-288 2.51e-11

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: 62.77  E-value: 2.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  47 APATNDPRYLQACGGEKlNRFRDIQCRRQTAVR---------AD-LNANYI---QVGNTrTIACQYPLQSQLESHFRMLA 113
Cdd:cd14543  16 PPAGTFLCSLAPANQEK-NRYGDVLCLDQSRVKlpkrngderTDyINANFMdgyKQKNA-YIATQGPLPKTYSDFWRMVW 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 114 ENRTPVLAVLASSSEIANQRFGM--PDYFRQSGTYGSITVESKMTQqvglgdgIMADmYTLTIREA--GQKTISVPVVHV 189
Cdd:cd14543  94 EQKVLVIVMTTRVVERGRVKCGQywPLEEGSSLRYGDLTVTNLSVE-------NKEH-YKKTTLEIhnTETDESRQVTHF 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 190 G--NWPDQTAVSSEvtkalASLVDQTAETKRnmYESKGSSAVADDSKLRP-----VIHCRAGVGRTaqliGAMCMNDSRN 262
Cdd:cd14543 166 QftSWPDFGVPSSA-----AALLDFLGEVRQ--QQALAVKAMGDRWKGHPpgppiVVHCSAGIGRT----GTFCTLDICL 234

                       250       260       270
                ....*....|....*....|....*....|..
gi 39654746 263 SQLS------VEDMVSQMRVQRnGIMVQKDEQ 288
Cdd:cd14543 235 SQLEdvgtlnVMQTVRRMRTQR-AFSIQTPDQ 265
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 63-288 6.46e-11

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: 61.38  E-value: 6.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  63 KLNRFRDIQCRRQTAVRAD-----LNANYIQ--VGNTR--TIACQYPLQSQLESHFRMLAENRTPVLAVLASSSE---IA 130
Cdd:cd14597   5 KKNRYKNILPYDTTRVPLGdeggyINASFIKmpVGDEEfvYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEggkIK 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 131 NQRFgMPDYFRQSGTYGS---ITVEsKMTQQVGLGDGIMaDMYTLTIREAGQktisvpVVHVG--NWPDQ-TAVSSEVTK 204
Cdd:cd14597  85 CQRY-WPEILGKTTMVDNrlqLTLV-RMQQLKNFVIRVL-ELEDIQTREVRH------ITHLNftAWPDHdTPSQPEQLL 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 205 ALASLVdqtaetkRNMYESKgssavaddsklrPVI-HCRAGVGRTAQLIgamCMND-----SRNSQLSVEDMVSQMRVQR 278
Cdd:cd14597 156 TFISYM-------RHIHKSG------------PIItHCSAGIGRSGTLI---CIDVvlgliSKDLDFDISDIVRTMRLQR 213

                       250
                ....*....|
gi 39654746 279 NGiMVQKDEQ 288
Cdd:cd14597 214 HG-MVQTEDQ 222
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 82-288 1.08e-10

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: 59.99  E-value: 1.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQVGNTRT--IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRfgMPDYFRQSGT--YGSITVESKMTQ 157
Cdd:cd17668   2 INANYVDGYNKPKayIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRK--CDQYWPADGSeeYGNFLVTQKSVQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 158 QVGLGDGIMADMYTLTIREAGQKTIS----VPVVHVGNWPDQTAvsSEVTKALASLVDQTAETKRnmyeskgssavaddS 233
Cdd:cd17668  80 VLAYYTVRNFTLRNTKIKKGSQKGRPsgrvVTQYHYTQWPDMGV--PEYTLPVLTFVRKASYAKR--------------H 143

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39654746 234 KLRPVI-HCRAGVGRTaqliGAMCMNDSRNSQLSVEDMVS------QMRVQRNgIMVQKDEQ 288
Cdd:cd17668 144 AVGPVVvHCSAGVGRT----GTYIVLDSMLQQIQHEGTVNifgflkHIRSQRN-YLVQTEEQ 200
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 52-292 3.15e-10

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: 59.46  E-value: 3.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  52 DPRYLQACGGEKLNRFRDIQ-------CRRQTAVRAD----LNANYIQ--VGNTRT-IACQYPLQSQLESHFRMLAENRT 117
Cdd:cd14612   6 SPEELDIPGHASKDRYKTILpnpqsrvCLRRAGSQEEegsyINANYIRgyDGKEKAyIATQGPMLNTVSDFWEMVWQEEC 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 118 PVLAVLASSSEiANQRFGMpdYF-RQSGTYGSITVESKMTQQvglgdgimADMYT---LTIREAGQktiSVPVVHV--GN 191
Cdd:cd14612  86 PIIVMITKLKE-KKEKCVH--YWpEKEGTYGRFEIRVQDMKE--------CDGYTirdLTIQLEEE---SRSVKHYwfSS 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 192 WPDQTavSSEVTKALASLVDQTAETkRNMYESKGSSavaddsklrpVIHCRAGVGRTAQLIGAM--CMNDSRNSQLSVED 269
Cdd:cd14612 152 WPDHQ--TPESAGPLLRLVAEVEES-RQTAASPGPI----------VVHCSAGIGRTGCFIATSigCQQLKDTGKVDILG 218

                       250       260
                ....*....|....*....|...
gi 39654746 270 MVSQMRVQRNGiMVQKDEQLDVL 292
Cdd:cd14612 219 IVCQLRLDRGG-MIQTSEQYQFL 240
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 82-288 4.32e-10

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: 58.24  E-value: 4.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQVGN----TRTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEiANQRFGMPDYF----RQSGTYGSITVES 153
Cdd:cd17658   2 INASLVETPAseslPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVD-NYSTAKCADYFpaeeNESREFGRISVTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 154 KmtqqvglgdGIMADMYTLTIR--EAGQKTISVPVVHV-----GNWPDQTavssevtkalaslVDQTAETKRNMYesKGS 226
Cdd:cd17658  81 K---------KLKHSQHSITLRvlEVQYIESEEPPLSVlhiqyPEWPDHG-------------VPKDTRSVRELL--KRL 136

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39654746 227 SAVADDskLRP-VIHCRAGVGRTaqliGAMCMNDSR--------NSQLSVEDMVSQMRVQRNGiMVQKDEQ 288
Cdd:cd17658 137 YGIPPS--AGPiVVHCSAGIGRT----GAYCTIHNTirrilegdMSAVDLSKTVRKFRSQRIG-MVQTQDQ 200
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 82-288 4.91e-10

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: 59.11  E-value: 4.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQV--GNTRT-IACQYPLQSQLESHFRMLAENRTPVLaVLASSSEIANQRfgMPDYF-RQSGTYGSITVeskMTQ 157
Cdd:cd14613  57 INANYIRGygGEEKVyIATQGPTVNTVGDFWRMVWQERSPII-VMITNIEEMNEK--CTEYWpEEQVTYEGIEI---TVK 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 158 QVglgdgIMADMYTL---TIREAGQKTIsvpVVHV--GNWPDQTavSSEVTKALASLVDQTAETKRNMYESKGssavadd 232
Cdd:cd14613 131 QV-----IHADDYRLrliTLKSGGEERG---LKHYwyTSWPDQK--TPDNAPPLLQLVQEVEEARQQAEPNCG------- 193

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 39654746 233 sklrPVI-HCRAGVGRTAQLIGA--MCMNDSRNSQLSVEDMVSQMRVQRNGiMVQKDEQ 288
Cdd:cd14613 194 ----PVIvHCSAGIGRTGCFIATsiCCKQLRNEGVVDILRTTCQLRLDRGG-MIQTCEQ 247
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 82-288 5.99e-10

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: 58.89  E-value: 5.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQVGNTRT--IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRFGMPDYFRQSGTYGSITVESKMTQqv 159
Cdd:cd17667  60 INANYVDGYNKAKayIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTK-- 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 160 glgdgIMAdMYTL---TIREA----GQK--------TISVPVVHVGNWPDQTAvsSEVTKALASLVDQtaetkrnmyesk 224
Cdd:cd17667 138 -----IHA-CYTVrrfSIRNTkvkkGQKgnpkgrqnERTVIQYHYTQWPDMGV--PEYALPVLTFVRR------------ 197

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39654746 225 gsSAVADDSKLRPV-IHCRAGVGRTAQ--LIGAMCMNDSRNSQLSVEDMVSQMRVQRNgIMVQKDEQ 288
Cdd:cd17667 198 --SSAARTPEMGPVlVHCSAGVGRTGTyiVIDSMLQQIKDKSTVNVLGFLKHIRTQRN-YLVQTEEQ 261
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 63-288 7.43e-10

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: 58.68  E-value: 7.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  63 KLNRFRDIQCRRQTAVRADL----------NANYIQ--VGNTRTIACQYPLQSQLESHFRMLAENRTPVlaVLASSSEIA 130
Cdd:cd14603  32 KKNRYKDILPYDQTRVILSLlqeeghsdyiNANFIKgvDGSRAYIATQGPLSHTVLDFWRMIWQYGVKV--ILMACREIE 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 131 NQRFGMPDYF---RQSGTYGSITVESkmTQQVGLGDGIMADMYTLTIREAGQKTISVPVVhvgNWPDqtavssevtKALA 207
Cdd:cd14603 110 MGKKKCERYWaqeQEPLQTGPFTITL--VKEKRLNEEVILRTLKVTFQKESRSVSHFQYM---AWPD---------HGIP 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 208 SLVDQTAETKRNMYESKGSSAVaddsklrPV-IHCRAGVGRTaqliGAMCMNDSRNSQL---------SVEDMVSQMRVQ 277
Cdd:cd14603 176 DSPDCMLAMIELARRLQGSGPE-------PLcVHCSAGCGRT----GVICTVDYVRQLLltqrippdfSIFDVVLEMRKQ 244

                       250
                ....*....|.
gi 39654746 278 RNGiMVQKDEQ 288
Cdd:cd14603 245 RPA-AVQTEEQ 254
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 82-288 7.64e-10

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: 57.90  E-value: 7.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQVGNTRT--IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIAnqRFGMPDYF--RQSGTYGSITVesKMTQ 157
Cdd:cd14615  27 INANYMPGYNSKKefIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQG--RTKCEEYWpsKQKKDYGDITV--TMTS 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 158 QVGLGDGIMADmYTLTIREAGQKTiSVPVVHVGNWPDQTavsseVTKALASLVDQTAETKRNMYESKGSSAVaddsklrp 237
Cdd:cd14615 103 EIVLPEWTIRD-FTVKNAQTNESR-TVRHFHFTSWPDHG-----VPETTDLLINFRHLVREYMKQNPPNSPI-------- 167

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 39654746 238 VIHCRAGVGRTAQLIGA---MCMNDSRNSqLSVEDMVSQMRVQRNgIMVQKDEQ 288
Cdd:cd14615 168 LVHCSAGVGRTGTFIAIdrlIYQIENENV-VDVYGIVYDLRMHRP-LMVQTEDQ 219
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 82-288 1.67e-09

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: 56.85  E-value: 1.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQ--VGNTRT-IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEiANQRFGMpdYF-RQSGTYGSITVESKMTQ 157
Cdd:cd14611  31 INANYIRgyGGKEKAfIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE-KNEKCVL--YWpEKRGIYGKVEVLVNSVK 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 158 QvglgdgimADMYT---LTIREAGQkTISVPVVHVGNWPDQTAVSSevTKALASLVDQTAETKRNmyeSKGSSAVaddsk 234
Cdd:cd14611 108 E--------CDNYTirnLTLKQGSQ-SRSVKHYWYTSWPDHKTPDS--AQPLLQLMLDVEEDRLA---SPGRGPV----- 168

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 39654746 235 lrpVIHCRAGVGRTAQLIGAM--CMNDSRNSQLSVEDMVSQMRVQRNGiMVQKDEQ 288
Cdd:cd14611 169 ---VVHCSAGIGRTGCFIATTigCQQLKEEGVVDVLSIVCQLRVDRGG-MVQTSEQ 220
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 82-288 3.91e-09

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: 55.82  E-value: 3.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQVGNTRT--IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEiaNQRFGMPDYF---RQSGTYGSITVEskMT 156
Cdd:cd14548  27 INANYIPGYNSPRefIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCME--KGRVKCDHYWpfdQDPVYYGDITVT--ML 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 157 QQVGLGDGIMADmytLTIrEAGQKTISVPVVHVGNWPDQtavssEVTKALASLVD--QTAETKRNmyESKGSsavaddsk 234
Cdd:cd14548 103 SESVLPDWTIRE---FKL-ERGDEVRSVRQFHFTAWPDH-----GVPEAPDSLLRfvRLVRDYIK--QEKGP-------- 163

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 39654746 235 lrPVIHCRAGVGRTAQLIGAMCMNDSRNSQLSVE--DMVSQMRVQRNgIMVQKDEQ 288
Cdd:cd14548 164 --TIVHCSAGVGRTGTFIALDRLLQQIESEDYVDifGIVYDLRKHRP-LMVQTEAQ 216
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 63-292 6.80e-09

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: 56.09  E-value: 6.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  63 KLNRFRDIQCRRQTAVRADL----------NANYIQ--VGNTRTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIA 130
Cdd:cd14604  59 KKNRYKDILPFDHSRVKLTLktssqdsdyiNANFIKgvYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMG 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 131 N---QRFgMPDYFRQSGTYGS--ITVESKMTQQvglgdgimaDMY--TLTIrEAGQKTISVPVVHVGNWPDQtavssEVT 203
Cdd:cd14604 139 RkkcERY-WPLYGEEPMTFGPfrISCEAEQART---------DYFirTLLL-EFQNETRRLYQFHYVNWPDH-----DVP 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 204 KALASLVDQTAETKRnmYESKgssavaDDSKLrpVIHCRAGVGRTaqliGAMCMNDSR---------NSQLSVEDMVSQM 274
Cdd:cd14604 203 SSFDSILDMISLMRK--YQEH------EDVPI--CIHCSAGCGRT----GAICAIDYTwnllkagkiPEEFNVFNLIQEM 268

                       250
                ....*....|....*...
gi 39654746 275 RVQRNGiMVQKDEQLDVL 292
Cdd:cd14604 269 RTQRHS-AVQTKEQYELV 285
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 82-288 2.36e-08

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: 53.21  E-value: 2.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQ--VGNT--RTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSE---IANQRFgMPDYFRQSGTYGSITVESK 154
Cdd:cd14596   2 INASYITmpVGEEelFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVErgkVKCHRY-WPETLQEPMELENYQLRLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 155 MTQQVglgDGIMADMYTLTIREAGQKTiSVPVVHVGNWPDQ-TAVSSevtkalaslvDQTAETKRNMYESKGSSAVadds 233
Cdd:cd14596  81 NYQAL---QYFIIRIIKLVEKETGENR-LIKHLQFTTWPDHgTPQSS----------DQLVKFICYMRKVHNTGPI---- 142

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 234 klrpVIHCRAGVGRTAQLIgamCMND-----SRNSQLSVEDMVSQMRVQRNGiMVQKDEQ 288
Cdd:cd14596 143 ----VVHCSAGIGRAGVLI---CVDVllsliEKDLSFNIKDIVREMRQQRYG-MIQTKDQ 194
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 82-288 4.86e-08

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: 52.97  E-value: 4.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQVGNT--RTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEiaNQRFGMPDYF---RQSGTYGSITVEskMT 156
Cdd:cd14614  43 INANYIPGYNSpqEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE--KRRVKCDHYWpftEEPVAYGDITVE--ML 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 157 QQVGLGDGIMADmYTLTIREAGQKtisvpVVHVG--NWPDQTAVSSEVTKALASLVdQTAETKRNmyESKGSSavaddsk 234
Cdd:cd14614 119 SEEEQPDWAIRE-FRVSYADEVQD-----VMHFNytAWPDHGVPTANAAESILQFV-QMVRQQAV--KSKGPM------- 182

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 39654746 235 lrpVIHCRAGVGRTAQLIGAMC-MNDSRNSQ-LSVEDMVSQMRVQRNGiMVQKDEQ 288
Cdd:cd14614 183 ---IIHCSAGVGRTGTFIALDRlLQHIRDHEfVDILGLVSEMRSYRMS-MVQTEEQ 234
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 82-288 5.85e-08

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: 52.14  E-value: 5.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQ--VGNTRTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRFGM--PDYFRQSGTYGSITVesKMTQ 157
Cdd:cd14557   2 INASYIDgfKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQywPSMEEGSRAFGDVVV--KINE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 158 QVGLGDGIMAdmyTLTIREAGQKTISVPVVHVG--NWPDQTAvsSEVTKALASLvdqtaETKRNMYESKGSSAVaddskl 235
Cdd:cd14557  80 EKICPDYIIR---KLNINNKKEKGSGREVTHIQftSWPDHGV--PEDPHLLLKL-----RRRVNAFNNFFSGPI------ 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 39654746 236 rpVIHCRAGVGRTAQLIGAMCMNDSRNSQ--LSVEDMVSQMRVQRnGIMVQKDEQ 288
Cdd:cd14557 144 --VVHCSAGVGRTGTYIGIDAMLEGLEAEgrVDVYGYVVKLRRQR-CLMVQVEAQ 195
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 82-288 7.24e-08

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: 52.73  E-value: 7.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQVGNTRT--IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEiaNQRFGMPDYF--RQSGTYGSItveskmtq 157
Cdd:cd14626  72 INANYIDGYRKQNayIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE--KSRVKCDQYWpiRGTETYGMI-------- 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 158 QVGLGDGIMADMYTLTI----REAGQKTISVPVVHVGNWPDQtAVSSEVTKALASLVDQTAETKrnmyeskgssavADDS 233
Cdd:cd14626 142 QVTLLDTVELATYSVRTfalyKNGSSEKREVRQFQFMAWPDH-GVPEYPTPILAFLRRVKACNP------------PDAG 208

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 39654746 234 KLrpVIHCRAGVGRTA--QLIGAMCMNDSRNSQLSVEDMVSQMRVQRNgIMVQKDEQ 288
Cdd:cd14626 209 PM--VVHCSAGVGRTGcfIVIDAMLERMKHEKTVDIYGHVTCMRSQRN-YMVQTEDQ 262
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 82-296 7.67e-08

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: 52.14  E-value: 7.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQVGNTRT--IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRfgMPDYF--RQSGTYGSITV----ES 153
Cdd:cd14554  37 INASFIDGYRQRGayIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLREMGREK--CHQYWpaERSARYQYFVVdpmaEY 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 154 KMTQQVgLGDGIMADMYTLTIREAGQktisvpvVHVGNWPDQTAVSSevTKALASLVDQTAETKRNmYESKGSSAVadds 233
Cdd:cd14554 115 NMPQYI-LREFKVTDARDGQSRTVRQ-------FQFTDWPEQGVPKS--GEGFIDFIGQVHKTKEQ-FGQEGPITV---- 179

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39654746 234 klrpviHCRAGVGRTAQLIgAMCMNDSRNSQLSVEDM---VSQMRVQRNGiMVQKDEQLDVLIKLA 296
Cdd:cd14554 180 ------HCSAGVGRTGVFI-TLSIVLERMRYEGVVDVfqtVKLLRTQRPA-MVQTEDQYQFCYRAA 237
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 82-288 2.73e-07

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: 50.53  E-value: 2.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQ--VGNT--RTIACQYPLQSQLESHFRMLAENRTPVLAVLasSSEIANQRFGMPDYFRQSG------TYGSITV 151
Cdd:cd14540   2 INASHITatVGGKqrFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMV--TAEEEGGREKCFRYWPTLGgehdalTFGEYKV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 152 ESKMTQQVGLGDGIMADMYTLTIREagqktiSVPVVHV--GNWPDQtAVSSEVTKALaSLVDQTAETKRNMYeskgsSAV 229
Cdd:cd14540  80 STKFSVSSGCYTTTGLRVKHTLSGQ------SRTVWHLqyTDWPDH-GCPEDVSGFL-DFLEEINSVRRHTN-----QDV 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39654746 230 ADDSKLRP-VIHCRAGVGRTAQLIGA--MCMNDSRNSQLSVEDMVSQMRVQRNgIMVQKDEQ 288
Cdd:cd14540 147 AGHNRNPPtLVHCSAGVGRTGVVILAdlMLYCLDHNEELDIPRVLALLRHQRM-LLVQTLAQ 207
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 82-288 3.12e-07

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: 50.47  E-value: 3.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQvGNTRT---IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIAnqRFGMPDYF--RQSGTYGSItveskmt 156
Cdd:cd14553  34 INANYCD-GYRKQnayIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEERS--RVKCDQYWptRGTETYGLI------- 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 157 qQVGLGDGIMADMY---TLTIREAGQK-TISVPVVHVGNWPDQtAVSSEVTKALASLVDQTAETKRnmyeskgssavadD 232
Cdd:cd14553 104 -QVTLLDTVELATYtvrTFALHKNGSSeKREVRQFQFTAWPDH-GVPEHPTPFLAFLRRVKACNPP-------------D 168

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 39654746 233 SKlrPVI-HCRAGVGRTAQ--LIGAMCMNDSRNSQLSVEDMVSQMRVQRNgIMVQKDEQ 288
Cdd:cd14553 169 AG--PIVvHCSAGVGRTGCfiVIDSMLERIKHEKTVDIYGHVTCLRAQRN-YMVQTEDQ 224
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 82-288 4.54e-07

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: 49.56  E-value: 4.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQVGN------TRTIACQYPLQSQLESHFRMLAENRTPVLAVLasSSEIANQRFGMPDYFRQ---SGTYGSITVE 152
Cdd:cd14601   3 INANYINMEIpsssiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVML--TTQVERGRVKCHQYWPEpsgSSSYGGFQVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 153 SKMTQqvGLGDGIMADMyTLTIREAGQKTISVPVVHVGnWPDQtAVSSEVTKAL--ASLVDQtaetKRnmyeSKGSSAVa 230
Cdd:cd14601  81 CHSEE--GNPAYVFREM-TLTNLEKNESRPLTQIQYIA-WPDH-GVPDDSSDFLdfVCLVRN----KR----AGKDEPV- 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39654746 231 ddsklrpVIHCRAGVGRTAQLI---GAMCMNDSRNSQLSVeDMVSQMRVQRnGIMVQKDEQ 288
Cdd:cd14601 147 -------VVHCSAGIGRTGVLItmeTAMCLIECNQPVYPL-DIVRTMRDQR-AMMIQTPSQ 198
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 79-297 8.51e-07

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: 48.89  E-value: 8.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  79 RADLNANYIQVG-------NTRTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRfgMPDYFRQSG--TYGSI 149
Cdd:cd14623  19 RGEENTDYVNASfidgyrqKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK--CAQYWPSDGsvSYGDI 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 150 TVESKMTQQVglGDGIMADMYTLTIREagQKTISVPVVHVGNWPdQTAVSSEvTKALASLVdqtAETKRNMYESkGSSAV 229
Cdd:cd14623  97 TIELKKEEEC--ESYTVRDLLVTNTRE--NKSRQIRQFHFHGWP-EVGIPSD-GKGMINII---AAVQKQQQQS-GNHPI 166

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 230 AddsklrpvIHCRAGVGRTAQLIGAMCMNDSRNSQ--LSVEDMVSQMRVQRNGiMVQKDEQLDVLIKLAE 297
Cdd:cd14623 167 T--------VHCSAGAGRTGTFCALSTVLERVKAEgiLDVFQTVKSLRLQRPH-MVQTLEQYEFCYKVVQ 227
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 82-288 1.03e-06

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: 48.37  E-value: 1.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYI---QVGNtRTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEiaNQRFGMPDYFRQSG--TYGSITVesKMT 156
Cdd:cd14551   2 INASYIdgyQEKN-KFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKE--RKEKKCSQYWPDQGcwTYGNLRV--RVE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 157 QQVGLGDGIMAdmyTLTIREAGQKTISVPV-----VHVGNWPDQTAVSSEVtkalaslvdqtaetkrNMYESKGSSAVAD 231
Cdd:cd14551  77 DTVVLVDYTTR---KFCIQKVNRGIGEKRVrlvtqFHFTSWPDFGVPFTPI----------------GMLKFLKKVKSAN 137

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 232 DSKLRP-VIHCRAGVGRTAQLIGAMCMNDSRNSQLSVE--DMVSQMRVQRNgIMVQKDEQ 288
Cdd:cd14551 138 PPRAGPiVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDvfGFVSRIRQQRS-QMVQTDMQ 196
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 65-288 2.72e-06

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: 48.07  E-value: 2.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  65 NRFRDI----QCRRQTAVRADLNANYIQVGNTRT---------IACQYPLQSQLESHFRMLAENRTPVLAVLAssseiAN 131
Cdd:cd14599  42 NRIREVvpyeENRVELVPTKENNTGYINASHIKVtvggeewhyIATQGPLPHTCHDFWQMVWEQGVNVIAMVT-----AE 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 132 QRFGMPDYFR---------QSGTYGSITVESKMTQqvglgDGIMADMYTLTIRE--AGQKTiSVPVVHVGNWPDQTavSS 200
Cdd:cd14599 117 EEGGRSKSHRywpklgskhSSATYGKFKVTTKFRT-----DSGCYATTGLKVKHllSGQER-TVWHLQYTDWPDHG--CP 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 201 EVTKALASLVDQTAETKRNmyeskgSSAVADDSKLRP---VIHCRAGVGRTAQLIGAMCMND--SRNSQLSVEDMVSQMR 275
Cdd:cd14599 189 EEVQGFLSYLEEIQSVRRH------TNSMLDSTKNCNppiVVHCSAGVGRTGVVILTELMIGclEHNEKVEVPVMLRHLR 262

                       250
                ....*....|...
gi 39654746 276 VQRNgIMVQKDEQ 288
Cdd:cd14599 263 EQRM-FMIQTIAQ 274
PHA02738 PHA02738
hypothetical protein; Provisional
 63-278 3.02e-06

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 48.00  E-value: 3.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746   63 KLNRFRDIQCRRQTAV-------RAD-LNANYIQvGNTRT---IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEiaN 131
Cdd:PHA02738  51 KLNRYLDAVCFDHSRVilpaernRGDyINANYVD-GFEYKkkfICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE--N 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  132 QRFGMPDYF----RQSGTYGSITVESkmTQQVGLGDGIMAdmyTLTIREAGQKTISVPVVHVGNWPDQtavssEVTKALA 207
Cdd:PHA02738 128 GREKCFPYWsdveQGSIRFGKFKITT--TQVETHPHYVKS---TLLLTDGTSATQTVTHFNFTAWPDH-----DVPKNTS 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  208 SLVDQTAETKRNMYESKGSSAVADDSKLRP---VIHCRAGVGRTaqliGAMCMNDS------RNSQLSVEDMVSQMRVQR 278
Cdd:PHA02738 198 EFLNFVLEVRQCQKELAQESLQIGHNRLQPppiVVHCNAGLGRT----PCYCVVDIsisrfdACATVSIPSIVSSIRNQR 273
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 95-297 3.19e-06

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: 46.92  E-value: 3.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  95 IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRfgMPDYFRQSG--TYGSITVESKMTQqvgLGDGIMADMYTL 172
Cdd:cd14622  18 IATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEK--CVQYWPSEGsvTHGEITIEIKNDT---LLETISIRDFLV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 173 TIREaGQKTISVPVVHVGNWPdQTAVSSEVTkalaSLVDQTAETKRNMYESkGSSAVaddsklrpVIHCRAGVGRTAQLI 252
Cdd:cd14622  93 TYNQ-EKQTRLVRQFHFHGWP-EIGIPAEGK----GMIDLIAAVQKQQQQT-GNHPI--------VVHCSAGAGRTGTFI 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 39654746 253 GAMCMNDSRNSQ--LSVEDMVSQMRVQRNGiMVQKDEQLDVLIKLAE 297
Cdd:cd14622 158 ALSNILERVKAEglLDVFQTVKSLRLQRPH-MVQTLEQYEFCYRVVQ 203
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 82-288 3.19e-06

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: 46.88  E-value: 3.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQVGNTRT--IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRFGMpdYFRQSG--TYGSITVEskmtq 157
Cdd:cd14552   2 INASFIDGYRQKDayIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQ--YWPEDGsvSSGDITVE----- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 158 qvgLGDGIMADMYT----LTIREAGQKTISVPVVHVGNWPdQTAVSSEVTkalaSLVDQTAETKRNMYESkGSSAVAdds 233
Cdd:cd14552  75 ---LKDQTDYEDYTlrdfLVTKGKGGSTRTVRQFHFHGWP-EVGIPDNGK----GMIDLIAAVQKQQQQS-GNHPIT--- 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 39654746 234 klrpvIHCRAGVGRTAQLIGAMCMNDSRNSQ--LSVEDMVSQMRVQRNGiMVQKDEQ 288
Cdd:cd14552 143 -----VHCSAGAGRTGTFCALSTVLERVKAEgvLDVFQVVKSLRLQRPH-MVQTLEQ 193
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 65-288 4.29e-06

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: 47.14  E-value: 4.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  65 NRFRDI----QCRRQTA-VRAD-----LNANYIQ--VGNTRTIACQYPLQSQLESHFRMLAENRtpVLAVLASSSEIANQ 132
Cdd:cd14602   2 NRYKDIlpydHSRVELSlITSDedsdyINANFIKgvYGPRAYIATQGPLSTTLLDFWRMIWEYS--VLIIVMACMEFEMG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 133 RFGMPDYFRQSGT----YG--SITVESKMTQqvglGDgimadmYTLTIREA--GQKTISVPVVHVGNWPDQTAVSSevtk 204
Cdd:cd14602  80 KKKCERYWAEPGEmqleFGpfSVTCEAEKRK----SD------YIIRTLKVkfNSETRTIYQFHYKNWPDHDVPSS---- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 205 alaslVDQTAETKRNMyeskgSSAVADDSKlrPV-IHCRAGVGRTaqliGAMCMNDSRNSQL---------SVEDMVSQM 274
Cdd:cd14602 146 -----IDPILELIWDV-----RCYQEDDSV--PIcIHCSAGCGRT----GVICAIDYTWMLLkdgiipenfSVFSLIQEM 209

                       250
                ....*....|....
gi 39654746 275 RVQRNGImVQKDEQ 288
Cdd:cd14602 210 RTQRPSL-VQTKEQ 222
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 82-252 5.88e-06

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: 46.47  E-value: 5.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQvGNTRT---IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEiaNQRFGMPDYFRQSG---TYGSITVESkM 155
Cdd:cd14618  28 INANFIP-GYTSPqefIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGME--NGRVLCDHYWPSEStpvSYGHITVHL-L 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 156 TQQvglgdgiMADMYTLTI----REAGQKTISVPVVHVGNWPDQTAvsSEVTKALASLVDQTAEtkrNMYESKGSSAVad 231
Cdd:cd14618 104 AQS-------SEDEWTRREfklwHEDLRKERRVKHLHYTAWPDHGI--PESTSSLMAFRELVRE---HVQATKGKGPT-- 169

                       170       180
                ....*....|....*....|.
gi 39654746 232 dsklrpVIHCRAGVGRTAQLI 252
Cdd:cd14618 170 ------LVHCSAGVGRSGTFI 184
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 64-290 8.52e-06

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: 46.23  E-value: 8.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  64 LNRFRDIQCRRQTAVRADL--------NANYIQV--GNTRTIACQYPLQSQLESHFRMLAENRTPvlAVLASSSEIANQR 133
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVKLkqgdndyiNASLVEVeeAKRSYILTQGPLPNTSGHFWQMVWEQNSK--AVIMLNKLMEKGQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 134 FGMPDYFRQSGTYGSITVESKMtqQVGLGDGIMADMYTLTIRE----AGQKTISVPVVHVGNWPDQTavsseVTKALASL 209
Cdd:cd14545  79 IKCAQYWPQGEGNAMIFEDTGL--KVTLLSEEDKSYYTVRTLElenlKTQETREVLHFHYTTWPDFG-----VPESPAAF 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 210 VDQTAETKRnmyeskgsSAVADDSKLRPVIHCRAGVGRTaqliGAMCMNDS-------RN-SQLSVEDMVSQMRVQRNGi 281
Cdd:cd14545 152 LNFLQKVRE--------SGSLSSDVGPPVVHCSAGIGRS----GTFCLVDTclvliekGNpSSVDVKKVLLEMRKYRMG- 218


                ....*....
gi 39654746 282 MVQKDEQLD 290
Cdd:cd14545 219 LIQTPDQLR 227
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 82-288 3.41e-05

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: 44.16  E-value: 3.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQ--VGNTRTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRfgMPDYFRQSG--TYGSItveskmtq 157
Cdd:cd14620  26 INASYIDgyKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEK--CYQYWPDQGcwTYGNI-------- 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 158 QVGLGDGIMADMYTL---TIREAGQKTISVP----VVHVGNWPDQTAVSSEVtkalaslvdqtaetkrNMYESKGSSAVA 230
Cdd:cd14620  96 RVAVEDCVVLVDYTIrkfCIQPQLPDGCKAPrlvtQLHFTSWPDFGVPFTPI----------------GMLKFLKKVKSV 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39654746 231 DDSKLRP-VIHCRAGVGRTAQLIGAMCMNDSRNSQ--LSVEDMVSQMRVQRNGiMVQKDEQ 288
Cdd:cd14620 160 NPVHAGPiVVHCSAGVGRTGTFIVIDAMIDMMHAEqkVDVFEFVSRIRNQRPQ-MVQTDMQ 219
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 238-288 3.45e-05

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: 43.86  E-value: 3.45e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 39654746 238 VIHCRAGVGRTAQLI---GAMCMNDSrNSQLSVEDMVSQMRVQRnGIMVQKDEQ 288
Cdd:cd14541 147 VVHCSAGIGRTGVLItmeTAMCLIEA-NEPVYPLDIVRTMRDQR-AMLIQTPSQ 198
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 237-288 3.71e-05

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: 44.46  E-value: 3.71e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 39654746 237 PVI-HCRAGVGRTAQLIG---AMCMNDsRNSQLSVEDMVSQMRVQRnGIMVQKDEQ 288
Cdd:cd14600 207 PVLvHCSAGIGRTGVLVTmetAMCLTE-RNQPVYPLDIVRKMRDQR-AMMVQTSSQ 260
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 82-295 5.50e-05

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: 43.43  E-value: 5.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQ--VGNTR--TIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRfgmpdYFR---------QSGTYGS 148
Cdd:cd14598   2 INASHIKvtVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREK-----SFRywprlgsrhNTVTYGR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 149 ItvesKMTQQVGLGDGIMADMyTLTIRE--AGQKTiSVPVVHVGNWPDQTAvsSEVTKALASLVDQTAETKRNMyeskGS 226
Cdd:cd14598  77 F----KITTRFRTDSGCYATT-GLKIKHllTGQER-TVWHLQYTDWPEHGC--PEDLKGFLSYLEEIQSVRRHT----NS 144

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39654746 227 SAVADDSKLRPVIHCRAGVGRTAQLIGAMCMND--SRNSQLSVEDMVSQMRVQRNgIMVQKDEQLDVLIKL 295
Cdd:cd14598 145 TIDPKSPNPPVLVHCSAGVGRTGVVILSEIMIAclEHNEMLDIPRVLDMLRQQRM-MMVQTLSQYTFVYKV 214
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 95-296 5.79e-05

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: 43.95  E-value: 5.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  95 IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRFGMPDYFRQSGTYGSITVESkmTQQVGLGDGIMADMYTLTI 174
Cdd:cd14629  99 IATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDP--MAEYNMPQYILREFKVTDA 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 175 REAGQKTISVpvVHVGNWPDQTAvsSEVTKALASLVDQTAETKRNMyeskgssavADDSKLrpVIHCRAGVGRTAQLIgA 254
Cdd:cd14629 177 RDGQSRTIRQ--FQFTDWPEQGV--PKTGEGFIDFIGQVHKTKEQF---------GQDGPI--TVHCSAGVGRTGVFI-T 240

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 39654746 255 MCMNDSRNSQLSVEDM---VSQMRVQRNGiMVQKDEQLDVLIKLA 296
Cdd:cd14629 241 LSIVLERMRYEGVVDMfqtVKTLRTQRPA-MVQTEDQYQLCYRAA 284
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 65-288 7.33e-05

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: 43.33  E-value: 7.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  65 NRFRDI----------QCRRQTAVRAD-LNANYIQ---VGNT----RTIACQYPLQSQLESHFRMLAENRTPVlaVLASS 126
Cdd:cd14606  22 NRYKNIlpfdhsrvilQGRDSNIPGSDyINANYVKnqlLGPDenakTYIASQGCLEATVNDFWQMAWQENSRV--IVMTT 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 127 SEIANQRFGMPDYFRQSGT---YGSITVESkmtqqVGLGDGIMADMYTL--TIREAGQKTISVPVVHVGNWPDQtAVSSE 201
Cdd:cd14606 100 REVEKGRNKCVPYWPEVGMqraYGPYSVTN-----CGEHDTTEYKLRTLqvSPLDNGELIREIWHYQYLSWPDH-GVPSE 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 202 VTKALaSLVDQTAEtkrnMYESKGSSAVAddsklrpVIHCRAGVGRTAQLIGAMCMNDS-----RNSQLSVEDMVSQMRV 276
Cdd:cd14606 174 PGGVL-SFLDQINQ----RQESLPHAGPI-------IVHCSAGIGRTGTIIVIDMLMENistkgLDCDIDIQKTIQMVRA 241

                       250
                ....*....|..
gi 39654746 277 QRNGiMVQKDEQ 288
Cdd:cd14606 242 QRSG-MVQTEAQ 252
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 95-287 7.52e-05

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: 43.57  E-value: 7.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  95 IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRFGMPDYFRQSGTYGSITVESkmTQQVGLGDGIMADMYTLTI 174
Cdd:cd14627  99 IATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDP--MAEYNMPQYILREFKVTDA 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 175 REAGQKTISVpvVHVGNWPDQTAVSSevTKALASLVDQTAETKRNMYESKGSSavaddsklrpvIHCRAGVGRTAQLIG- 253
Cdd:cd14627 177 RDGQSRTVRQ--FQFTDWPEQGVPKS--GEGFIDFIGQVHKTKEQFGQDGPIS-----------VHCSAGVGRTGVFITl 241

                       170       180       190
                ....*....|....*....|....*....|....*
gi 39654746 254 AMCMNDSR-NSQLSVEDMVSQMRVQRNGIMVQKDE 287
Cdd:cd14627 242 SIVLERMRyEGVVDIFQTVKMLRTQRPAMVQTEDE 276
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 82-288 1.23e-04

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: 42.60  E-value: 1.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQVGNTRT--IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEiaNQRFGMPDYF---RQSGTYGSITVESkmt 156
Cdd:cd14617  28 INASYIPGNNFRReyIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVE--KGRVKCDHYWpadQDSLYYGDLIVQM--- 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 157 qqvgLGDGIMADMytlTIRE---AGQKTISVPVV----HVGNWPDQTAvsSEVTKALASLVdQTAETKRNMYESKGSSav 229
Cdd:cd14617 103 ----LSESVLPEW---TIREfkiCSEEQLDAPRLvrhfHYTVWPDHGV--PETTQSLIQFV-RTVRDYINRTPGSGPT-- 170

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39654746 230 addsklrpVIHCRAGVGRTAQLIG--AMCMNDSRNSQLSVEDMVSQMRVQRNgIMVQKDEQ 288
Cdd:cd14617 171 --------VVHCSAGVGRTGTFIAldRILQQLDSKDSVDIYGAVHDLRLHRV-HMVQTECQ 222
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
168-297 1.35e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 41.11  E-value: 1.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 168 DMYTLTIREAGQKTISVPvvhvgnWPDQTAVSSEvtkALASLVDQTAEtkrnmyeskgssAVADDSKLrpVIHCRAGVGR 247
Cdd:COG2453  37 ELLLGLLEEAGLEYLHLP------IPDFGAPDDE---QLQEAVDFIDE------------ALREGKKV--LVHCRGGIGR 93

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 39654746 248 TAQLIGAMCMNDSrnsqLSVEDMVSQMRVQRNGImVQKDEQLDVLIKLAE 297
Cdd:COG2453  94 TGTVAAAYLVLLG----LSAEEALARVRAARPGA-VETPAQRAFLERFAK 138
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 95-288 3.33e-04

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: 41.64  E-value: 3.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  95 IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRFGMPDYFRQSGTYGSITVESkmTQQVGLGDGIMADMYTLTI 174
Cdd:cd14628  98 IATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDP--MAEYNMPQYILREFKVTDA 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 175 REAGQKTISVpvVHVGNWPDQTAVSSevTKALASLVDQTAETKRNMYESKGSSavaddsklrpvIHCRAGVGRTAQLIG- 253
Cdd:cd14628 176 RDGQSRTVRQ--FQFTDWPEQGVPKS--GEGFIDFIGQVHKTKEQFGQDGPIS-----------VHCSAGVGRTGVFITl 240

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 39654746 254 AMCMNDSR-NSQLSVEDMVSQMRVQRNGiMVQKDEQ 288
Cdd:cd14628 241 SIVLERMRyEGVVDIFQTVKMLRTQRPA-MVQTEDQ 275
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
239-282 3.95e-04

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 39.96  E-value: 3.95e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 39654746    239 IHCRAGVGRTAQLIGAMCMnDSRNsqLSVEDMVSQMRVQRNGIM 282
Cdd:smart00195  83 VHCQAGVSRSATLIIAYLM-KTRN--MSLNDAYDFVKDRRPIIS 123
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 82-288 4.71e-04

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: 41.16  E-value: 4.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQ--VGNTRTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEiaNQRFGMPDYFRQSG--TYGSITVESKMTQ 157
Cdd:cd14621  83 INASFINgyQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKE--RKECKCAQYWPDQGcwTYGNIRVSVEDVT 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 158 qvglgdgIMADmYTL---TIREAGQKTISVPV-----VHVGNWPDQTAVSSEVtkalaSLVDQTAETKRNMYESKGSSav 229
Cdd:cd14621 161 -------VLVD-YTVrkfCIQQVGDVTNKKPQrlitqFHFTSWPDFGVPFTPI-----GMLKFLKKVKNCNPQYAGAI-- 225

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39654746 230 addsklrpVIHCRAGVGRTAQLIGAMCMNDSRNSQLSVE--DMVSQMRVQRNGiMVQKDEQ 288
Cdd:cd14621 226 --------VVHCSAGVGRTGTFIVIDAMLDMMHAERKVDvyGFVSRIRAQRCQ-MVQTDMQ 277
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 239-282 1.15e-03

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


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 38.40  E-value: 1.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 39654746   239 IHCRAGVGRTAQLIGAMCMnDSRNsqLSVEDMVSQMRVQRNGIM 282
Cdd:pfam00782  74 VHCQAGISRSATLIIAYLM-KTRN--LSLNEAYSFVKERRPGIS 114
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 239-257 3.75e-03

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


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 37.43  E-value: 3.75e-03
                        10
                ....*....|....*....
gi 39654746 239 IHCRAGVGRTAQLIGAMCM 257
Cdd:cd14499 114 VHCKAGLGRTGTLIACYLM 132
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 82-297 7.40e-03

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: 37.04  E-value: 7.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQVGNTRT---IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRfgMPDYFRQSG--TYGSITVeSKMT 156
Cdd:cd14546   2 INASTIYDHDPRNpayIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQ--CARYWPEEGseVYHIYEV-HLVS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 157 QQVGLGDGIMADMYTLTIREagQKTISVPVVHVGNWPDQTAVSSevTKALAslvdqtaETKRNMYES-KG-SSAVaddsk 234
Cdd:cd14546  79 EHIWCDDYLVRSFYLKNLQT--SETRTVTQFHFLSWPDEGIPAS--AKPLL-------EFRRKVNKSyRGrSCPI----- 142

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39654746 235 lrpVIHCRAGVGRTAQ--LIGAMCMNDSRNS-QLSVEDMVSQMRVQRNGiMVQKDEQLD-VLIKLAE 297
Cdd:cd14546 143 ---VVHCSDGAGRTGTyiLIDMVLNRMAKGAkEIDIAATLEHLRDQRPG-MVKTKDQFEfVLTAVAE 205
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 82-288 7.52e-03

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: 36.92  E-value: 7.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746  82 LNANYIQvGNTRT---IACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIAnqRFGMPDYF-RQSGTYGSITVESKMTQ 157
Cdd:cd14631  16 INANYID-GYQRPshyIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVG--RVKCYKYWpDDTEVYGDFKVTCVEME 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39654746 158 QvgLGDGIMAdmyTLTIREAGQKTI-SVPVVHVGNWPDQtAVSSEVTKALASLvdqtaeTKRNMYESKGSSAVaddsklr 236
Cdd:cd14631  93 P--LAEYVVR---TFTLERRGYNEIrEVKQFHFTGWPDH-GVPYHATGLLSFI------RRVKLSNPPSAGPI------- 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 39654746 237 pVIHCRAGVGRTAQLIGAMCMND--SRNSQLSVEDMVSQMRVQRNGiMVQKDEQ 288
Cdd:cd14631 154 -VVHCSAGAGRTGCYIVIDIMLDmaEREGVVDIYNCVKALRSRRIN-MVQTEEQ 205
 
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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