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Conserved domains on  [gi|352645611|emb|CCD64995|]
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Tyrosine-protein phosphatase domain-containing protein [Caenorhabditis elegans]

Protein Classification

protein tyrosine phosphatase family protein( domain architecture ID 12193126)

cys-based protein tyrosine phosphatase (PTP) family protein, such as tyrosine-protein phosphatase that catalyzes the dephosphorylation of phosphotyrosine groups in phosphoproteins

CATH:  3.90.190.10
EC:  3.1.3.-
Gene Ontology:  GO:0004721|GO:0006470
PubMed:  27514797|17057753

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
155-408 1.86e-60

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 197.50  E-value: 1.86e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611   155 IRAEYIEACAATKVNIDKDCQLWKKNLQMNQADNYPILDSTIVK---NPAQPDSYVNMSSVIVPHCRYPILMAQMPKRGF 231
Cdd:smart00194   2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKlkpPPGEGSDYINASYIDGPNGPKAYIATQGPLPST 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611   232 EEEFWRAAFNESVVIMYVLMgTEDEKN-----DFFPTTMGAYVYYGAMFVNIRKVEKMDEeRTRYTIEVLPNGFSNSVMM 306
Cdd:smart00194  82 VEDFWRMVWEQKVTVIVMLT-ELVEKGrekcaQYWPDEEGEPLTYGDITVTLKSVEKVDD-YTIRTLEVTNTGCSETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611   307 NVYVHTGWEASGVPvryaNTTRSVVDVMNFVKTSSGTEK--MLVVSKNGCGRAGFFLSLGAAFCCLNDNSEPRIGEIVKA 384
Cdd:smart00194 160 THYHYTNWPDHGVP----ESPESILDLIRAVRKSQSTSTgpIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                          250       260
                   ....*....|....*....|....
gi 352645611   385 IRSQRPNAVDSIKQYASIYLCFVY 408
Cdd:smart00194 236 LRSQRPGMVQTEEQYIFLYRAILE 259
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
155-408 1.86e-60

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 197.50  E-value: 1.86e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611   155 IRAEYIEACAATKVNIDKDCQLWKKNLQMNQADNYPILDSTIVK---NPAQPDSYVNMSSVIVPHCRYPILMAQMPKRGF 231
Cdd:smart00194   2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKlkpPPGEGSDYINASYIDGPNGPKAYIATQGPLPST 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611   232 EEEFWRAAFNESVVIMYVLMgTEDEKN-----DFFPTTMGAYVYYGAMFVNIRKVEKMDEeRTRYTIEVLPNGFSNSVMM 306
Cdd:smart00194  82 VEDFWRMVWEQKVTVIVMLT-ELVEKGrekcaQYWPDEEGEPLTYGDITVTLKSVEKVDD-YTIRTLEVTNTGCSETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611   307 NVYVHTGWEASGVPvryaNTTRSVVDVMNFVKTSSGTEK--MLVVSKNGCGRAGFFLSLGAAFCCLNDNSEPRIGEIVKA 384
Cdd:smart00194 160 THYHYTNWPDHGVP----ESPESILDLIRAVRKSQSTSTgpIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                          250       260
                   ....*....|....*....|....
gi 352645611   385 IRSQRPNAVDSIKQYASIYLCFVY 408
Cdd:smart00194 236 LRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
180-408 4.25e-50

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 169.73  E-value: 4.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611  180 NLQMNQADNYPILDSTIVKNPAQPDS--YVNMSSVIVPHCRYPILMAQMPKRGFEEEFWRAAFNESVVImYVLMGTEDEK 257
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGPsdYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTI-IVMLTELEEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611  258 N-----DFFPTTMGAYVYYGAMFVNIRKvEKMDEERTRYTIEVLPNGFSNSV-MMNVYVHTGWEASGVPvryaNTTRSVV 331
Cdd:pfam00102  80 GrekcaQYWPEEEGESLEYGDFTVTLKK-EKEDEKDYTVRTLEVSNGGSEETrTVKHFHYTGWPDHGVP----ESPNSLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611  332 DVMNFVKTSSGTEK---MLVVSKNGCGRAGFFLSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSIKQYASIYLCFVY 408
Cdd:pfam00102 155 DLLRKVRKSSLDGRsgpIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 206-403 7.94e-43

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: 149.74  E-value: 7.94e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 206 YVNMSSVIVPHCRYPILMAQMPKRGFEEEFWRAAFNESVVIMyVLMGTEDEKND-----FFPTTMGAYVYYGAMFVNIRK 280
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVI-VMLTNLVEKGRekcerYWPEEGGKPLEYGDITVTLVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 281 VEKMdEERTRYTIEVLPNGFSNSVMMNVYVHTGWEASGVPVRYANTTRSVVDVMNFVKTSSGteKMLVVSKNGCGRAGFF 360
Cdd:cd00047   80 EEEL-SDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNG--PIVVHCSAGVGRTGTF 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 352645611 361 LSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSIKQYASIY 403
Cdd:cd00047  157 IAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 179-411 2.47e-08

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 55.39  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 179 KNLQMNQADNYPILDSTIVKNPAQP--DSYVNMSSVIVPHCRYPILMAQMPKRGFEEEFWRAAFNESV-VIMYVLMGTED 255
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRVILKIEDggDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVrVIVMITKIMED 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 256 EKNDFFPTTMG---AYVYYGAMFVNIRKVEKMdeertRY----TIEVLPNGFSNSVMMNVYVHTGWEASGVP-------- 320
Cdd:PHA02742 131 GKEACYPYWMPherGKATHGEFKIKTKKIKSF-----RNyavtNLCLTDTNTGASLDIKHFAYEDWPHGGLPrdpnkfld 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 321 ----VRYANTTrsvVDVMNFVKTSSGTEKMLVVSKNGCGRAGFFLSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSI 396
Cdd:PHA02742 206 fvlaVREADLK---ADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLP 282

                        250
                 ....*....|....*
gi 352645611 397 KQYASIYLCFVYYIK 411
Cdd:PHA02742 283 QQYIFCYFIVLIFAK 297
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
155-408 1.86e-60

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 197.50  E-value: 1.86e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611   155 IRAEYIEACAATKVNIDKDCQLWKKNLQMNQADNYPILDSTIVK---NPAQPDSYVNMSSVIVPHCRYPILMAQMPKRGF 231
Cdd:smart00194   2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKlkpPPGEGSDYINASYIDGPNGPKAYIATQGPLPST 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611   232 EEEFWRAAFNESVVIMYVLMgTEDEKN-----DFFPTTMGAYVYYGAMFVNIRKVEKMDEeRTRYTIEVLPNGFSNSVMM 306
Cdd:smart00194  82 VEDFWRMVWEQKVTVIVMLT-ELVEKGrekcaQYWPDEEGEPLTYGDITVTLKSVEKVDD-YTIRTLEVTNTGCSETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611   307 NVYVHTGWEASGVPvryaNTTRSVVDVMNFVKTSSGTEK--MLVVSKNGCGRAGFFLSLGAAFCCLNDNSEPRIGEIVKA 384
Cdd:smart00194 160 THYHYTNWPDHGVP----ESPESILDLIRAVRKSQSTSTgpIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                          250       260
                   ....*....|....*....|....
gi 352645611   385 IRSQRPNAVDSIKQYASIYLCFVY 408
Cdd:smart00194 236 LRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
180-408 4.25e-50

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 169.73  E-value: 4.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611  180 NLQMNQADNYPILDSTIVKNPAQPDS--YVNMSSVIVPHCRYPILMAQMPKRGFEEEFWRAAFNESVVImYVLMGTEDEK 257
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGPsdYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTI-IVMLTELEEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611  258 N-----DFFPTTMGAYVYYGAMFVNIRKvEKMDEERTRYTIEVLPNGFSNSV-MMNVYVHTGWEASGVPvryaNTTRSVV 331
Cdd:pfam00102  80 GrekcaQYWPEEEGESLEYGDFTVTLKK-EKEDEKDYTVRTLEVSNGGSEETrTVKHFHYTGWPDHGVP----ESPNSLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611  332 DVMNFVKTSSGTEK---MLVVSKNGCGRAGFFLSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSIKQYASIYLCFVY 408
Cdd:pfam00102 155 DLLRKVRKSSLDGRsgpIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 206-403 7.94e-43

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: 149.74  E-value: 7.94e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 206 YVNMSSVIVPHCRYPILMAQMPKRGFEEEFWRAAFNESVVIMyVLMGTEDEKND-----FFPTTMGAYVYYGAMFVNIRK 280
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVI-VMLTNLVEKGRekcerYWPEEGGKPLEYGDITVTLVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 281 VEKMdEERTRYTIEVLPNGFSNSVMMNVYVHTGWEASGVPVRYANTTRSVVDVMNFVKTSSGteKMLVVSKNGCGRAGFF 360
Cdd:cd00047   80 EEEL-SDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNG--PIVVHCSAGVGRTGTF 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 352645611 361 LSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSIKQYASIY 403
Cdd:cd00047  157 IAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
305-405 7.87e-13

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 64.30  E-value: 7.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611   305 MMNVYVHTGWEASGVPVRYANTTRSVVDVMNFVKTSSGTEKMLVVSKNGCGRAGFFLSLGAAFCCLNDNS-EPRIGEIVK 383
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80

                           90       100
                   ....*....|....*....|..
gi 352645611   384 AIRSQRPNAVDSIKQYASIYLC 405
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRA 102
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 305-405 7.87e-13

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: 64.30  E-value: 7.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611   305 MMNVYVHTGWEASGVPVRYANTTRSVVDVMNFVKTSSGTEKMLVVSKNGCGRAGFFLSLGAAFCCLNDNS-EPRIGEIVK 383
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80

                           90       100
                   ....*....|....*....|..
gi 352645611   384 AIRSQRPNAVDSIKQYASIYLC 405
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRA 102
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 206-403 2.68e-09

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


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 57.01  E-value: 2.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 206 YVNMSSV--IVPHCRyPILMAQMPKRGFEEEFWRAAF--NESVVIMYVLMGTEDEKN--DFFPTTMGAYVYYGAMFVNIR 279
Cdd:cd14539    1 YINASLIedLTPYCP-RFIATQAPLPGTAADFWLMVYeqQVSVIVMLVSEQENEKQKvhRYWPTERGQALVYGAITVSLQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 280 KVEKMDE--ERtRYTIEVLPNGFSNSVmmnvyVH---TGWEASGVPVRYANTTRSVVDVMNFVKTSSGTEKMLVV-SKNG 353
Cdd:cd14539   80 SVRTTPThvER-IISIQHKDTRLSRSV-----VHlqfTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVhCSSG 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 352645611 354 CGRAGFFLSLGAAFCCLN-DNSEPRIGEIVKAIRSQRPNAVDSIKQYASIY 403
Cdd:cd14539  154 VGRTGAFCLLYAAVQEIEaGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 206-408 1.07e-08

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: 55.33  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 206 YVNMSSVIVP---HCRYpILMaQMPKRGFEEEFWRAAFNESVVImyVLMGTEDEKND------FFPTTMGaYVYYGAMFV 276
Cdd:cd18533    1 YINASYITLPgtsSKRY-IAT-QGPLPATIGDFWKMIWQNNVGV--IVMLTPLVENGrekcdqYWPSGEY-EGEYGDLTV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 277 NIRKVEKMDEER-TRYTIEVLPNgfsNSVMMNVYvH---TGWEASGVPvryaNTTRSVVDVMNFV----KTSSGTEKMLV 348
Cdd:cd18533   76 ELVSEEENDDGGfIVREFELSKE---DGKVKKVY-HiqyKSWPDFGVP----DSPEDLLTLIKLKrelnDSASLDPPIIV 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 352645611 349 VSKNGCGRAGFFLSLGAAFCCLNDNSEPR---------IGEIVKAIRSQRPNAVDSIKQYasiylCFVY 408
Cdd:cd18533  148 HCSAGVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQY-----IFLY 211
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 179-411 2.47e-08

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 55.39  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 179 KNLQMNQADNYPILDSTIVKNPAQP--DSYVNMSSVIVPHCRYPILMAQMPKRGFEEEFWRAAFNESV-VIMYVLMGTED 255
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRVILKIEDggDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVrVIVMITKIMED 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 256 EKNDFFPTTMG---AYVYYGAMFVNIRKVEKMdeertRY----TIEVLPNGFSNSVMMNVYVHTGWEASGVP-------- 320
Cdd:PHA02742 131 GKEACYPYWMPherGKATHGEFKIKTKKIKSF-----RNyavtNLCLTDTNTGASLDIKHFAYEDWPHGGLPrdpnkfld 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 321 ----VRYANTTrsvVDVMNFVKTSSGTEKMLVVSKNGCGRAGFFLSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSI 396
Cdd:PHA02742 206 fvlaVREADLK---ADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLP 282

                        250
                 ....*....|....*
gi 352645611 397 KQYASIYLCFVYYIK 411
Cdd:PHA02742 283 QQYIFCYFIVLIFAK 297
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 197-403 7.00e-08

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: 53.12  E-value: 7.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 197 VKNPAQPDSYVNMSSVIVPHCRYPILMAQMPKRGFEEEFWRAAF---NESVVIMYVLMGTEDEK-NDFFPTTmgAYVYYG 272
Cdd:cd14623   17 VKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWewkSCSIVMLTELEERGQEKcAQYWPSD--GSVSYG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 273 AMFVNIRKvekmDEERTRYTIE---VLPNGFSNSVMMNVYVHTGWEASGVPvryaNTTRSVVDVMNFVKTS---SGTEKM 346
Cdd:cd14623   95 DITIELKK----EEECESYTVRdllVTNTRENKSRQIRQFHFHGWPEVGIP----SDGKGMINIIAAVQKQqqqSGNHPI 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 352645611 347 LVVSKNGCGRAGFFLSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSIKQYASIY 403
Cdd:cd14623  167 TVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCY 223
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 224-414 1.41e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 53.11  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 224 AQMPKRGFEEEFWRAAF--NESVVIMYVLMGTEDEKNDFFPTTMGAY-VYYGAMFVNIRKV-EKMDEERTRYTIEVLPNG 299
Cdd:PHA02746 118 AQGPKEDTSEDFFKLISehESQVIVSLTDIDDDDEKCFELWTKEEDSeLAFGRFVAKILDIiEELSFTKTRLMITDKISD 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 300 FSNSVMMNVYVHtgWEASGVPVRYANTTRSVVDV----MNFVKTSSGTEKML----VVSKNGCGRAGFFLSLGAAFCCLN 371
Cdd:PHA02746 198 TSREIHHFWFPD--WPDNGIPTGMAEFLELINKVneeqAELIKQADNDPQTLgpivVHCSAGIGRAGTFCAIDNALEQLE 275

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 352645611 372 DNSEPRIGEIVKAIRSQRPNAVDSIKQYASIYLCFVYYIKKKI 414
Cdd:PHA02746 276 KEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAIIEEA 318
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 184-404 1.44e-07

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: 52.23  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 184 NQADNYPILDSTIVKNPAQPDS----YVNMSSVIVPHCRYPILMAQMPKRGFEEEFWRAAFNESV-VIMYVLMGTEDEK- 257
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDpcsdYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVhNIVMVTQCVEKGRv 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 258 --NDFFPTTMGAYvYYGAMFV-----------NIRKVEKMDEERTRYtievlpngfsnSVMMNVYVHTGWEASGVPvrya 324
Cdd:cd14617   81 kcDHYWPADQDSL-YYGDLIVqmlsesvlpewTIREFKICSEEQLDA-----------PRLVRHFHYTVWPDHGVP---- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 325 NTTRSVVD----VMNFVKTSSGTEKMLVVSKNGCGRAGFFLSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSIKQYA 400
Cdd:cd14617  145 ETTQSLIQfvrtVRDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYV 224


                 ....
gi 352645611 401 SIYL 404
Cdd:cd14617  225 YLHQ 228
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 233-403 6.36e-07

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: 50.00  E-value: 6.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 233 EEFWRAAFN---ESVVIMYVLMGTEDEKN-DFFPTTmgAYVYYGAMFVNIRKVEKMDEERTRYTIEVLPNGFSNSVMMNV 308
Cdd:cd14622   29 EDFWRMVWEwkcHTIVMLTELQEREQEKCvQYWPSE--GSVTHGEITIEIKNDTLLETISIRDFLVTYNQEKQTRLVRQF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 309 YVHtGWEASGVPVRyantTRSVVDVMNFVKTS---SGTEKMLVVSKNGCGRAGFFLSLGAAFCCLNDNSEPRIGEIVKAI 385
Cdd:cd14622  107 HFH-GWPEIGIPAE----GKGMIDLIAAVQKQqqqTGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSL 181

                        170
                 ....*....|....*...
gi 352645611 386 RSQRPNAVDSIKQYASIY 403
Cdd:cd14622  182 RLQRPHMVQTLEQYEFCY 199
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 203-403 8.85e-07

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: 49.94  E-value: 8.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 203 PDSYVNMSSVIVPHCRYPILMAQMPKRGFEEEFWRAAFNESVVIMYVLMGTEDEKND----FFPTtMGAYVYyGAMFVNI 278
Cdd:cd14620   22 CSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEkcyqYWPD-QGCWTY-GNIRVAV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 279 RKVEKMDEertrYTIE------VLPNGFSNSVMMNVYVHTGWEASGVPVRYANTTRSVVDVMNFVKTSSGteKMLVVSKN 352
Cdd:cd14620  100 EDCVVLVD----YTIRkfciqpQLPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSVNPVHAG--PIVVHCSA 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 352645611 353 GCGRAGFFLSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSIKQYASIY 403
Cdd:cd14620  174 GVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIY 224
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 233-403 1.45e-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: 48.80  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 233 EEFWRAAF---NESVVIMYVLMGTEDEKNDFFPTTMGAyVYYGAMFVNIRKvekmDEERTRYTIE--VLPNGFSNSVMMN 307
Cdd:cd14552   28 EDFWRMIWewkSCSIVMLTEIKERSQNKCAQYWPEDGS-VSSGDITVELKD----QTDYEDYTLRdfLVTKGKGGSTRTV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 308 VYVH-TGWEASGVPvryaNTTRSVVDVMNFVKTS---SGTEKMLVVSKNGCGRAGFFLSLGAAFCCLNDNSEPRIGEIVK 383
Cdd:cd14552  103 RQFHfHGWPEVGIP----DNGKGMIDLIAAVQKQqqqSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGVLDVFQVVK 178

                        170       180
                 ....*....|....*....|
gi 352645611 384 AIRSQRPNAVDSIKQYASIY 403
Cdd:cd14552  179 SLRLQRPHMVQTLEQYEFCY 198
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 222-403 3.97e-06

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: 48.11  E-value: 3.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 222 LMAQMPKRGFEEEFWRAAF--NESVVIMYV-LMGTEDEKND-FFPTTMGAYvyYGAMFVNIRKVEKMdeerTRYTIEVL- 296
Cdd:cd17667   75 IATQGPLKSTFEDFWRMIWeqNTGIIVMITnLVEKGRRKCDqYWPTENSEE--YGNIIVTLKSTKIH----ACYTVRRFs 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 297 -------------PNGFSNSVMMNVYVHTGWEASGVPvRYAnttrsvVDVMNFVKTSSGTEK-----MLVVSKNGCGRAG 358
Cdd:cd17667  149 irntkvkkgqkgnPKGRQNERTVIQYHYTQWPDMGVP-EYA------LPVLTFVRRSSAARTpemgpVLVHCSAGVGRTG 221

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 352645611 359 FFLSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSIKQYASIY 403
Cdd:cd17667  222 TYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 266
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 222-407 2.93e-05

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: 44.97  E-value: 2.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 222 LMAQMPKRGFEEEFWRAAFNESVVIMyVLMGTEDEK-----NDFFPTTMGAyvYYGAMFVNIRKVEKMdeerTRYTIE-- 294
Cdd:cd17668   17 IAAQGPLKSTAEDFWRMIWEHNVEVI-VMITNLVEKgrrkcDQYWPADGSE--EYGNFLVTQKSVQVL----AYYTVRnf 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 295 VLPN---------GFSNSVMMNVYVHTGWEASGVPvryanttRSVVDVMNFVKTSSGTEK-----MLVVSKNGCGRAGFF 360
Cdd:cd17668   90 TLRNtkikkgsqkGRPSGRVVTQYHYTQWPDMGVP-------EYTLPVLTFVRKASYAKRhavgpVVVHCSAGVGRTGTY 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 352645611 361 LSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSIKQYASIYLCFV 407
Cdd:cd17668  163 IVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PHA02738 PHA02738
hypothetical protein; Provisional
 178-410 4.42e-05

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 45.30  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 178 KKNLQMNQADNYPILDSTIVKNPAQPD--SYVNMSSVIVPHCRYPILMAQMPKRGFEEEFWRAAFNESVVIMYVL-MGTE 254
Cdd:PHA02738  47 KKNRKLNRYLDAVCFDHSRVILPAERNrgDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLcKKKE 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 255 DEKNDFFP---TTMGAYVYYGAMFVNIRKVEKMdEERTRYTIEvLPNGFSNSVMMNVYVHTGWEASGVPvryanttRSVV 331
Cdd:PHA02738 127 NGREKCFPywsDVEQGSIRFGKFKITTTQVETH-PHYVKSTLL-LTDGTSATQTVTHFNFTAWPDHDVP-------KNTS 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 332 DVMNFVKTSSGTEKML-----------------VVSKN-GCGRAGFFLSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAV 393
Cdd:PHA02738 198 EFLNFVLEVRQCQKELaqeslqighnrlqpppiVVHCNaGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSL 277

                        250
                 ....*....|....*..
gi 352645611 394 DSIKQYASIYLCFVYYI 410
Cdd:PHA02738 278 FIPFQYFFCYRAVKRYV 294
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 206-405 4.53e-05

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: 44.29  E-value: 4.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 206 YVNMSSVIVPHC--RYPILMAQMPKRGFEEEFWRAAF-NESVVIMYVLMGTEDEK---NDFFP-TTMGAYVYYGAMFVNI 278
Cdd:cd14538    1 YINASHIRIPVGgdTYHYIACQGPLPNTTGDFWQMVWeQKSEVIAMVTQDVEGGKvkcHRYWPdSLNKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 279 RKVEKMDEERTRY-TIEVLPNGFSNSVM-MNvyvHTGWEASGVPVryanTTRSVVDVMNFVKTSSGTEKMLVVSKNGCGR 356
Cdd:cd14538   81 EKYQSLQDFVIRRiSLRDKETGEVHHIThLN---FTTWPDHGTPQ----SADPLLRFIRYMRRIHNSGPIVVHCSAGIGR 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 352645611 357 AGFFLSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSIKQYASIYLC 405
Cdd:cd14538  154 TGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKA 202
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 204-404 5.03e-05

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: 44.27  E-value: 5.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 204 DSYVNMSSVIVPHCRYPILMAQMPKRGFEEEFWRAAFNESV---VIMYVLMGTEDEKND-FFPTTMgAYVYYGAMFVNIR 279
Cdd:cd14548   24 SDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNShtiVMLTQCMEKGRVKCDhYWPFDQ-DPVYYGDITVTML 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 280 KVEKMDEeRTRYTIEVLPNGFSNSVMMNVYvhTGWEASGVPvryaNTTRSVVDVMNFVKTSSGTEK--MLVVSKNGCGRA 357
Cdd:cd14548  103 SESVLPD-WTIREFKLERGDEVRSVRQFHF--TAWPDHGVP----EAPDSLLRFVRLVRDYIKQEKgpTIVHCSAGVGRT 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 352645611 358 GFFLSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSIKQYasIYL 404
Cdd:cd14548  176 GTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQY--IFL 220
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 206-404 5.96e-05

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: 44.44  E-value: 5.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 206 YVNMSSVIVPHCRYPILMAQMPKRGFEEEFWRAAF--NESVVIMYV-LMGTEDEK-NDFFPTTMGAYVYYgamFVnirkV 281
Cdd:cd14554   36 YINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWehNSTIIVMLTkLREMGREKcHQYWPAERSARYQY---FV----V 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 282 EKMDE-ERTRYTI---EVLPNGFSNSVMMNVYVHTGWEASGVPvryaNTTRSVVDVMNFV---KTSSGTEKMLVVS-KNG 353
Cdd:cd14554  109 DPMAEyNMPQYILrefKVTDARDGQSRTVRQFQFTDWPEQGVP----KSGEGFIDFIGQVhktKEQFGQEGPITVHcSAG 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 352645611 354 CGRAGFFLSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSIKQYASIYL 404
Cdd:cd14554  185 VGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 234-403 8.36e-05

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: 43.57  E-value: 8.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 234 EFWRA--AFNESVVIMYVL---MGTEDEKNdFFPTTMGAYVYYGAMFVNIRKVEKMDEErtrYTIEVLPNGFSN-SVMMN 307
Cdd:cd14542   29 DFWRMiwEYNVQVIVMACRefeMGKKKCER-YWPEEGEEQLQFGPFKISLEKEKRVGPD---FLIRTLKVTFQKeSRTVY 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 308 VYVHTGWEASGVPvryaNTTRSVVDVMNFVKT--SSGTEKMLVVSKNGCGRAGFFLSLGAAFCCLNDNSEPR---IGEIV 382
Cdd:cd14542  105 QFHYTAWPDHGVP----SSVDPILDLVRLVRDyqGSEDVPICVHCSAGCGRTGTICAIDYVWNLLKTGKIPEefsLFDLV 180

                        170       180
                 ....*....|....*....|.
gi 352645611 383 KAIRSQRPNAVDSIKQYASIY 403
Cdd:cd14542  181 REMRKQRPAMVQTKEQYELVY 201
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 206-403 2.30e-04

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: 42.21  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 206 YVNMSSVIVPHCRYPILMAQMPKRGFEEEFWRAAFNESVVIMYVLMGTEDEK----NDFFPTTmGAYvYYGAMFVNIRKV 281
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKekkcSQYWPDQ-GCW-TYGNLRVRVEDT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 282 EKMDEERTRYTI--EVLPNGFSNSVMMNVYVH-TGWEASGVPVRYANTTRSVVDVMNFVKTSSGTekMLVVSKNGCGRAG 358
Cdd:cd14551   79 VVLVDYTTRKFCiqKVNRGIGEKRVRLVTQFHfTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGP--IVVHCSAGVGRTG 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 352645611 359 FFLSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSIKQYASIY 403
Cdd:cd14551  157 TFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 206-411 3.60e-04

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: 41.88  E-value: 3.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 206 YVNMS--SVIVPHCRYPILMAQMPKRGFEEEFWRAAFNESVVIMYVLMGTED---EKNDFFPTTMGA---YVYYGAMFVN 277
Cdd:cd14598    1 YINAShiKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEggrEKSFRYWPRLGSrhnTVTYGRFKIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 278 IR-KVEKMDEERTRYTIEVLPNGFSNSVMMNVYvhTGWEASGVP------VRYANTTRSVVDVMNFVKTSSGTEK-MLVV 349
Cdd:cd14598   81 TRfRTDSGCYATTGLKIKHLLTGQERTVWHLQY--TDWPEHGCPedlkgfLSYLEEIQSVRRHTNSTIDPKSPNPpVLVH 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 352645611 350 SKNGCGRAGFFLSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSIKQYASIYLCFVYYIK 411
Cdd:cd14598  159 CSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 234-411 4.92e-04

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


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 41.54  E-value: 4.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 234 EFWRAAFNE-SVVIMYVLMGTEDEKND---FFPTTMgAYVYYGAMFV-NIRKVEKMDEERTRYTIEVLPNGFSNSVMMNV 308
Cdd:cd14605   69 DFWRMVFQEnSRVIVMTTKEVERGKSKcvkYWPDEY-ALKEYGVMRVrNVKESAAHDYILRELKLSKVGQGNTERTVWQY 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 309 YVHTgWEASGVPVRYANTTRSVVDVMNFVKTSSGTEKMLVVSKNGCGRAGFFLSLGAAFCCLND---NSEPRIGEIVKAI 385
Cdd:cd14605  148 HFRT-WPDHGVPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREkgvDCDIDVPKTIQMV 226

                        170       180
                 ....*....|....*....|....*.
gi 352645611 386 RSQRPNAVDSIKQYASIYLCFVYYIK 411
Cdd:cd14605  227 RSQRSGMVQTEAQYRFIYMAVQHYIE 252
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 196-403 6.19e-04

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


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 41.05  E-value: 6.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 196 IVKNPAQPDS-YVNMSSVIVPHCRYPILMAQMPKRGFEEEFWRAAFnESVVIMYVLMGTEDEK-----NDFFPTTMGAYV 269
Cdd:cd14616   16 LIADAGVPGSdYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVW-ETRAKTIVMLTQCFEKgrircHQYWPEDNKPVT 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 270 YYGAMFVNiRKVEKMDEERTRYTIEVLPNGfsNSVMMNVYVHTGWEASGVPvryaNTTRSVVDVMNFVKTSSGTEK--ML 347
Cdd:cd14616   95 VFGDIVIT-KLMEDVQIDWTIRDLKIERHG--DYMMVRQCNFTSWPEHGVP----ESSAPLIHFVKLVRASRAHDNtpMI 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 352645611 348 VVSKNGCGRAGFFLSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSIKQYASIY 403
Cdd:cd14616  168 VHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 206-403 8.81e-04

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


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 40.42  E-value: 8.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 206 YVNMSSVIVPHCRYPILMAQMPKRGFEEEFWRAAFNE---SVVIMYVLMGTEDEK-NDFFPTTMGAyvyYGAMFVNIRKV 281
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEhcsSIVMITKLVEVGRVKcSKYWPDDSDT---YGDIKITLLKT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 282 EKMDEERTRyTIEVLPNGFSNSVMMNVYVHTGWEASGVPvrYANTtrSVVDVMNFVKTSSGTEKMLVV--SKNGCGRAGF 359
Cdd:cd14632   78 ETLAEYSVR-TFALERRGYSARHEVKQFHFTSWPEHGVP--YHAT--GLLAFIRRVKASTPPDAGPVVvhCSAGAGRTGC 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 352645611 360 FLSLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSIKQYASIY 403
Cdd:cd14632  153 YIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIH 196
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 206-403 1.70e-03

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 39.68  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 206 YVNMSSVIVPHCRYPILMAQMPKRGFEEEFWRAAFNESVVIMYVLMGTEDEKNDFfpttmgAYVY-------YGAMFVNI 278
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQ------CAQYwgdekktYGDIEVEL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 279 RKVEKMdEERTRYTIEVLPNGFSNSVMMNVYVHTGWEASGVPvryaNTTRSVVDVMNFVK-----TSSGTEK---MLVVS 350
Cdd:cd14558   75 KDTEKS-PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELP----EKPKDLVDMIKSIKqklpyKNSKHGRsvpIVVHC 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 351 KNGCGRAGfflslgaAFCCL-N--DNSEPR----IGEIVKAIRSQRPNAVDSIKQYASIY 403
Cdd:cd14558  150 SDGSSRTG-------IFCALwNllESAETEkvvdVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 206-403 1.96e-03

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: 39.37  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 206 YVNMSSVIVP-HCRYPILMA-QMPKRGFEEEFWRAAFNES--VVIM---YVLMGTEDEKNDFFPTTMGAYVYYGAMFVNI 278
Cdd:cd17658    1 YINASLVETPaSESLPKFIAtQGPLPHTFEDFWEMVIQQRcpVIIMltrLVDNYSTAKCADYFPAEENESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 279 RKVEKMDEERTRYTIEVLPNGFSNSVMMNVYV-HTGWEASGVPvryaNTTRSVVDVMNFVKTSSGTEKMLVV-SKNGCGR 356
Cdd:cd17658   81 KKLKHSQHSITLRVLEVQYIESEEPPLSVLHIqYPEWPDHGVP----KDTRSVRELLKRLYGIPPSAGPIVVhCSAGIGR 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 352645611 357 AGfflslgaAFCCLN---------DNSEPRIGEIVKAIRSQRPNAVDSIKQYASIY 403
Cdd:cd17658  157 TG-------AYCTIHntirrilegDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 234-403 2.87e-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: 39.23  E-value: 2.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 234 EFWRAAFNE-SVVIMYVLMGTEDEKNDFFPTTMGAYVYYGAMFVNIRKVEKMDEERTRyTIEVLPNGFSNSVMMNVYVHT 312
Cdd:cd14631   43 DFWRMIWQEqSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCVEMEPLAEYVVR-TFTLERRGYNEIREVKQFHFT 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 313 GWEASGVPvrYANTtrSVVDVMNFVKTSS--GTEKMLVVSKNGCGRAGFFLSLGAAFCCLNDNSEPRIGEIVKAIRSQRP 390
Cdd:cd14631  122 GWPDHGVP--YHAT--GLLSFIRRVKLSNppSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRI 197

                        170
                 ....*....|...
gi 352645611 391 NAVDSIKQYASIY 403
Cdd:cd14631  198 NMVQTEEQYIFIH 210
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 206-403 3.34e-03

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


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 38.85  E-value: 3.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 206 YVNMSSVIVPHCRYPILMAQMPKRGFEEEFWRAAFNE---SVVIMYVLMGTEDEKN-DFFPTTMGAYvyyGAMFVNIRKV 281
Cdd:cd14630   33 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQEnsaSVVMVTNLVEVGRVKCvRYWPDDTEVY---GDIKVTLIET 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 282 EKMDEERTRyTIEVLPNGFSNSVMMNVYVHTGWEASGVPVrYANTTRSVVDVMNFVKTSSGTeKMLVVSKNGCGRAGFFL 361
Cdd:cd14630  110 EPLAEYVIR-TFTVQKKGYHEIREIRQFHFTSWPDHGVPC-YATGLLGFVRQVKFLNPPDAG-PIVVHCSAGAGRTGCFI 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 352645611 362 SLGAAFCCLNDNSEPRIGEIVKAIRSQRPNAVDSIKQYASIY 403
Cdd:cd14630  187 AIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVH 228
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 173-406 3.72e-03

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: 38.88  E-value: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 173 DCQLWKKNLQMNQADNYPILDSTIVKNPA----QPDSYVNMSSVIVPHCRYPILMAQMPKRGFEEEFWRAAFNESVVImy 248
Cdd:cd14543   22 LCSLAPANQEKNRYGDVLCLDQSRVKLPKrngdERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLV-- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 249 VLMGTEDEKN------DFFPTTMGAYVYYGAMFV-NIRKVEKMDEERTRYTIEVLPNGFSNSVMMnvYVHTGWEASGVP- 320
Cdd:cd14543  100 IVMTTRVVERgrvkcgQYWPLEEGSSLRYGDLTVtNLSVENKEHYKKTTLEIHNTETDESRQVTH--FQFTSWPDFGVPs 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352645611 321 -------VRYANTTRSVVDVMNFVKTSSGTEK---MLVVSKNGCGRAGFFLSLGaaFCC--LNDNSEPRIGEIVKAIRSQ 388
Cdd:cd14543  178 saaalldFLGEVRQQQALAVKAMGDRWKGHPPgppIVVHCSAGIGRTGTFCTLD--ICLsqLEDVGTLNVMQTVRRMRTQ 255

                        250
                 ....*....|....*...
gi 352645611 389 RPNAVDSIKQYasiYLCF 406
Cdd:cd14543  256 RAFSIQTPDQY---YFCY 270
 
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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