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Conserved domains on  [gi|1133451038|ref|XP_019860969|]
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PREDICTED: receptor-type tyrosine-protein phosphatase F-like [Amphimedon queenslandica]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
882-1136 2.90e-121

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 374.69  E-value: 2.90e-121
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   882 KFSEEYEKVSAVGLDH-SKDASLLPENRAKNRYTNILAYDHSRVKLESIDDEPgSDYINANYIPGYRMRRAYIATQGPLP 960
Cdd:smart00194    1 GLEEEFEKLDRLKPDDeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   961 STFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWP--GAQPEVYGEINVDMLSETEKSDWIVRKFKITKEKRS--RTI 1036
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPdeEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSetRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  1037 THYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQH 1116
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                           250       260
                    ....*....|....*....|
gi 1133451038  1117 RNHMIQTEPQYVFIHKAMVD 1136
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 83-174 1.33e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.08  E-value: 1.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   83 PTSPSDVSYINISSTSIEVSWNPPTDFNGPNEGYVITYIRLESDT-ESMSTNRLTGTSFVIENLEKYEQYSVTVVAFTDK 161
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|...
gi 1133451038  162 GPGASSDVLSVLT 174
Cdd:cd00063     81 GESPPSESVTVTT 93
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
40-342 5.79e-14

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 76.58  E-value: 5.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   40 TSDTSYNISGLDVYTDYNVSVAAYTSAGTGPFDSVIRRT-DSTVPTSPSDVSYINISSTSIEVSWNPPTDFNGpnEGYVI 118
Cdd:COG3401    189 STTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESDA--TGYRV 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  119 tYIRLESDTESMSTNRLTGTSFVIENLEKYEQYSVTVVAFTDKG-PGASSDVLSVLTDEDLPGPPSNVS-TMSTNTSISI 196
Cdd:COG3401    267 -YRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTPPAAPSGLTaTAVGSSSITL 345

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  197 TWSPPLDPNglLLSYSINVTLNSTYaqylSFDVMTMSVSQNifSYTLFDLLPFAGYDISLQASTSVGLGTP------AIE 270
Cdd:COG3401    346 SWTASSDAD--VTGYNVYRSTSGGG----TYTKIAETVTTT--SYTDTGLTPGTTYYYKVTAVDAAGNESApseevsATT 417

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133451038  271 TETTLQAAPAAPVANPMASPVSSTAVNVSWLPPNLSNWNGLITNYTIEYRTNDEYIRPSIEVTATLSSFANS 342
Cdd:COG3401    418 ASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANL 489
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 495-587 1.60e-13

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.52  E-value: 1.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  495 PSAPDPVIVKRRNDTAIQVNWTRPAEPNGIILGYLIYYIGTKNNTGTEysninvliiINVTDPNTLSYLITNLLADTQYF 574
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKE---------VEVTPGSETSYTLTGLKPGTEYE 71

                           90
                   ....*....|...
gi 1133451038  575 INVTAYTSAGLGA 587
Cdd:cd00063     72 FRVRAVNGGGESP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 397-487 6.09e-10

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 57.12  E-value: 6.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  397 GPPLDVSVIVDSPSTARISWSPPmyIDRNGIIVNYTVRIITTVRGTIRETNISNVSGNYYDASDLPQFASFNVTVAAATS 476
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPP--EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|.
gi 1133451038  477 VGLGPYSPSVS 487
Cdd:cd00063     80 GGESPPSESVT 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 2-69 3.20e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


:

Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 54.93  E-value: 3.20e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133451038     2 SLRITWTELLEDDQNGVIIGYNISYFSLPAVGQPINNFTSDTSYNISGLDVYTDYNVSVAAYTSAGTG 69
Cdd:smart00060   16 SVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
UP_III_II super family cl06408
Uroplakin IIIb, IIIa and II; Uroplakins (UPs) are a family of proteins that associate with ...
 690-753 9.14e-03

Uroplakin IIIb, IIIa and II; Uroplakins (UPs) are a family of proteins that associate with each other to form plaques on the apical surface of the urothelium, the pseudo-stratified epithelium lining the urinary tract from renal pelvis to the bladder outlet. UPs are classified into 3 types: UPIa and UPIb, UPII, and UPIIIa and IIIb. UPIs are tetraspanins that have four transmembrane domains separating one large and one small extracellular domain while UPII and UPIIIs are single-pass transmembrane proteins. UPIa and UPIb form specific heterodimers with UPII and UPIII, respectively, which allows them to exit the endoplasmatic rediculum. UPII/UPIa and UPIIIs/UPIb form heterotetramers; six of these tetramers form the 16nm particle, seen in the hexagonal array of the asymmetric unit membrane, which is believed to form a urinary tract barrier. Uroplakins are also believed to play a role during urinary tract morphogenesis.


The actual alignment was detected with superfamily member cd09966:

Pssm-ID: 471435  Cd Length: 181  Bit Score: 38.56  E-value: 9.14e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1133451038  690 RKRQAGGETVAETIGTNNSCGPNDivCNGPLKPGTQYQFKYRVYNsdDDDSYVESQYSGPIRTD 753
Cdd:cd09966     85 RNRRDIVSAYVLRVGNTTTCLSGY--CNTPLPGPGPYRVKYLVMN--GSGPSAQTEWSTPIRLN 144
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
882-1136 2.90e-121

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 374.69  E-value: 2.90e-121
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   882 KFSEEYEKVSAVGLDH-SKDASLLPENRAKNRYTNILAYDHSRVKLESIDDEPgSDYINANYIPGYRMRRAYIATQGPLP 960
Cdd:smart00194    1 GLEEEFEKLDRLKPDDeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   961 STFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWP--GAQPEVYGEINVDMLSETEKSDWIVRKFKITKEKRS--RTI 1036
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPdeEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSetRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  1037 THYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQH 1116
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                           250       260
                    ....*....|....*....|
gi 1133451038  1117 RNHMIQTEPQYVFIHKAMVD 1136
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 912-1132 8.09e-117

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: 361.29  E-value: 8.09e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  912 RYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTK 991
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  992 CHRYWP-GAQPEVYGEINVDMLSETEKSDWIVRKFKITKEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSA 1070
Cdd:cd14548     81 CDHYWPfDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQE 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133451038 1071 FGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHK 1132
Cdd:cd14548    161 KGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
907-1136 5.57e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 343.46  E-value: 5.57e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  907 NRAKNRYTNILAYDHSRVKLEsiDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVE 986
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  987 RGRTKCHRYWPGA--QPEVYGEINVDMLSETE-KSDWIVRKFKITK--EKRSRTITHYQFVSWPDHGVPDEAGPALDFVR 1061
Cdd:pfam00102   79 KGREKCAQYWPEEegESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1133451038 1062 EVHEVASSAF-GPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVD 1136
Cdd:pfam00102  159 KVRKSSLDGRsGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PHA02738 PHA02738
hypothetical protein; Provisional
 884-1134 7.34e-49

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 176.65  E-value: 7.34e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  884 SEEYEKVSAVGLDHSKDASLlpENRAKNRYTNILAYDHSRVKLESidDEPGSDYINANYIPGYRMRRAYIATQGPLPSTF 963
Cdd:PHA02738    28 TREHQKVISEKVDGTFNAEK--KNRKLNRYLDAVCFDHSRVILPA--ERNRGDYINANYVDGFEYKKKFICGQAPTRQTC 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  964 DDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWpgaqpevygeinvdmlSETEKSDWIVRKFKITKEKRSR--------- 1034
Cdd:PHA02738   104 YDFYRMLWMEHVQIIVMLCKKKENGREKCFPYW----------------SDVEQGSIRFGKFKITTTQVEThphyvkstl 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1035 ----------TITHYQFVSWPDHGVPDEAGPALDFVREVH----EVASSAFG---------PVIVHCSAGVGRTGTFIAL 1091
Cdd:PHA02738   168 lltdgtsatqTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRqcqkELAQESLQighnrlqppPIVVHCNAGLGRTPCYCVV 247

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1133451038 1092 GTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAM 1134
Cdd:PHA02738   248 DISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
872-1134 1.94e-42

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 156.79  E-value: 1.94e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  872 VEDMLNDagfKFSEEYEKVSAVGLDHSKDASLlpENRAKNRYTNILAYDHSRVklesiddEPGSDYINANYIPGYRMRRa 951
Cdd:COG5599     12 EEEKINS---RLSTLTNELAPSHNDPQYLQNI--NGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIGNHR- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  952 YIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVE--RGRTKCHRYWPgAQPEvYGEINVDmlSETEKSDWI-----VRK 1024
Cdd:COG5599     79 YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFR-QDGE-YGKYEVS--SELTESIQLrdgieART 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1025 FKITKE---KRSRTITHYQFVSWPDH-GVPDEAGPAL-DFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIK 1099
Cdd:COG5599    155 YVLTIKgtgQKKIEIPVLHVKNWPDHgAISAEALKNLaDLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSIN 234

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1133451038 1100 DHD--WVDLFGLASEMRQHRN-HMIQTEPQYVFIHKAM 1134
Cdd:COG5599    235 ALVqiTLSVEEIVIDMRTSRNgGMVQTSEQLDVLVKLA 272
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 83-174 1.33e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.08  E-value: 1.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   83 PTSPSDVSYINISSTSIEVSWNPPTDFNGPNEGYVITYIRLESDT-ESMSTNRLTGTSFVIENLEKYEQYSVTVVAFTDK 161
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|...
gi 1133451038  162 GPGASSDVLSVLT 174
Cdd:cd00063     81 GESPPSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
40-342 5.79e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 76.58  E-value: 5.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   40 TSDTSYNISGLDVYTDYNVSVAAYTSAGTGPFDSVIRRT-DSTVPTSPSDVSYINISSTSIEVSWNPPTDFNGpnEGYVI 118
Cdd:COG3401    189 STTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESDA--TGYRV 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  119 tYIRLESDTESMSTNRLTGTSFVIENLEKYEQYSVTVVAFTDKG-PGASSDVLSVLTDEDLPGPPSNVS-TMSTNTSISI 196
Cdd:COG3401    267 -YRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTPPAAPSGLTaTAVGSSSITL 345

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  197 TWSPPLDPNglLLSYSINVTLNSTYaqylSFDVMTMSVSQNifSYTLFDLLPFAGYDISLQASTSVGLGTP------AIE 270
Cdd:COG3401    346 SWTASSDAD--VTGYNVYRSTSGGG----TYTKIAETVTTT--SYTDTGLTPGTTYYYKVTAVDAAGNESApseevsATT 417

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133451038  271 TETTLQAAPAAPVANPMASPVSSTAVNVSWLPPNLSNWNGLITNYTIEYRTNDEYIRPSIEVTATLSSFANS 342
Cdd:COG3401    418 ASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANL 489
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 495-587 1.60e-13

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.52  E-value: 1.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  495 PSAPDPVIVKRRNDTAIQVNWTRPAEPNGIILGYLIYYIGTKNNTGTEysninvliiINVTDPNTLSYLITNLLADTQYF 574
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKE---------VEVTPGSETSYTLTGLKPGTEYE 71

                           90
                   ....*....|...
gi 1133451038  575 INVTAYTSAGLGA 587
Cdd:cd00063     72 FRVRAVNGGGESP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 83-164 1.74e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 64.17  E-value: 1.74e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038    83 PTSPSDVSYINISSTSIEVSWNPPTDfnGPNEGYVITYI---RLESDTESMSTNRLTGTSFVIENLEKYEQYSVTVVAFT 159
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPD--DGITGYIVGYRveyREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 1133451038   160 DKGPG 164
Cdd:smart00060   79 GAGEG 83
fn3 pfam00041
Fibronectin type III domain;
496-586 2.03e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 2.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  496 SAPDPVIVKRRNDTAIQVNWTRPAEPNGIILGYLIYYIGTknNTGTEYSNINVliiinvtDPNTLSYLITNLLADTQYFI 575
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPK--NSGEPWNEITV-------PGTTTSVTLTGLKPGTEYEV 71

                           90
                   ....*....|.
gi 1133451038  576 NVTAYTSAGLG 586
Cdd:pfam00041   72 RVQAVNGGGEG 82
fn3 pfam00041
Fibronectin type III domain;
85-167 2.20e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 2.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   85 SPSDVSYINISSTSIEVSWNPPTDFNGPNEGYVITYIrlESDTESMSTNRLTG---TSFVIENLEKYEQYSVTVVAFTDK 161
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYR--PKNSGEPWNEITVPgttTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 1133451038  162 GPGASS 167
Cdd:pfam00041   80 GEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 495-586 3.35e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 63.40  E-value: 3.35e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   495 PSAPDPVIVKRRNDTAIQVNWTRPAEPNGIilGYLIYYIGTKNNTGTEYSNINVliiinvtDPNTLSYLITNLLADTQYF 574
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVGYRVEYREEGSEWKEVNV-------TPSSTSYTLTGLKPGTEYE 71

                            90
                    ....*....|..
gi 1133451038   575 INVTAYTSAGLG 586
Cdd:smart00060   72 FRVRAVNGAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 397-487 6.09e-10

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 57.12  E-value: 6.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  397 GPPLDVSVIVDSPSTARISWSPPmyIDRNGIIVNYTVRIITTVRGTIRETNISNVSGNYYDASDLPQFASFNVTVAAATS 476
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPP--EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|.
gi 1133451038  477 VGLGPYSPSVS 487
Cdd:cd00063     80 GGESPPSESVT 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 2-69 3.20e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 54.93  E-value: 3.20e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133451038     2 SLRITWTELLEDDQNGVIIGYNISYFSLPAVGQPINNFTSDTSYNISGLDVYTDYNVSVAAYTSAGTG 69
Cdd:smart00060   16 SVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 179-274 1.73e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 52.88  E-value: 1.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  179 PGPPSNVS-TMSTNTSISITWSPPLDPNGLLLSYSInvtlnsTYAQYLSFDVMTMSVSQ-NIFSYTLFDLLPFAGYDISL 256
Cdd:cd00063      1 PSPPTNLRvTDVTSTSVTLSWTPPEDDGGPITGYVV------EYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRV 74

                           90
                   ....*....|....*...
gi 1133451038  257 QASTSVGLGTPAIETETT 274
Cdd:cd00063     75 RAVNGGGESPPSESVTVT 92
fn3 pfam00041
Fibronectin type III domain;
180-267 8.01e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.88  E-value: 8.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  180 GPPSNVS-TMSTNTSISITWSPPLDPNGLLLSYSInvtlnsTYAQYLSFDVM-TMSVSQNIFSYTLFDLLPFAGYDISLQ 257
Cdd:pfam00041    1 SAPSNLTvTDVTSTSLTVSWTPPPDGNGPITGYEV------EYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQ 74

                           90
                   ....*....|
gi 1133451038  258 ASTSVGLGTP 267
Cdd:pfam00041   75 AVNGGGEGPP 84
fn3 pfam00041
Fibronectin type III domain;
2-71 9.37e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.88  E-value: 9.37e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133451038    2 SLRITWTELleDDQNGVIIGYNISYFSL--PAVGQPINNFTSDTSYNISGLDVYTDYNVSVAAYTSAGTGPF 71
Cdd:pfam00041   15 SLTVSWTPP--PDGNGPITGYEVEYRPKnsGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 179-265 1.66e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 49.92  E-value: 1.66e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   179 PGPPSNVS-TMSTNTSISITWSPPLDPNGllLSYSINVTLNStyaQYLSFDVMTMSVSQNIFSYTLFDLLPFAGYDISLQ 257
Cdd:smart00060    1 PSPPSNLRvTDVTSTSVTLSWEPPPDDGI--TGYIVGYRVEY---REEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVR 75


                    ....*...
gi 1133451038   258 ASTSVGLG 265
Cdd:smart00060   76 AVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
397-483 5.39e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.57  E-value: 5.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  397 GPPLDVSVIVDSPSTARISWSPPMyiDRNGIIVNYTVRIITTVRGTI-RETNISNVSgNYYDASDLPQFASFNVTVAAAT 475
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPP--DGNGPITGYEVEYRPKNSGEPwNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVN 77


                   ....*...
gi 1133451038  476 SVGLGPYS 483
Cdd:pfam00041   78 GGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 2-71 2.48e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 2.48e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133451038    2 SLRITWTELLEDdqNGVIIGYNISYFSLPA--VGQPINNFTSDTSYNISGLDVYTDYNVSVAAYTSAGTGPF 71
Cdd:cd00063     16 SVTLSWTPPEDD--GGPITGYVVEYREKGSgdWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPP 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 397-480 2.38e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 43.76  E-value: 2.38e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   397 GPPLDVSVIVDSPSTARISWSPPMYIDRNGIIVNYTVRIITTVRGTIRETNisNVSGNYYDASDLPQFASFNVTVAAATS 476
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNV--TPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 1133451038   477 VGLG 480
Cdd:smart00060   80 AGEG 83
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
41-205 3.44e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 48.40  E-value: 3.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   41 SDTSYNISGLDvytdYNVSVAAYTSAGTGPFDSVIRRTDSTVPTSPSDVSYINISSTSIEVSWNPPTDfngpnegyVITY 120
Cdd:COG4733    500 EDGTYTITAVQ----HAPEKYAAIDAGAFDDVPPQWPPVNVTTSESLSVVAQGTAVTTLTVSWDAPAG--------AVAY 567

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  121 -IRLESDTES-MSTNRLTGTSFVIENLekYE-QYSVTVVAFTDKG---PGASSDVLSVLTDEDLPGPPSNVSTMSTNTSI 194
Cdd:COG4733    568 eVEWRRDDGNwVSVPRTSGTSFEVPGI--YAgDYEVRVRAINALGvssAWAASSETTVTGKTAPPPAPTGLTATGGLGGI 645

                          170
                   ....*....|.
gi 1133451038  195 SITWSPPLDPN 205
Cdd:COG4733    646 TLSWSFPVDAD 656
UP_III_II cd09966
Uroplakin IIIb, IIIa and II; Uroplakins (UPs) are a family of proteins that associate with ...
 690-753 9.14e-03

Uroplakin IIIb, IIIa and II; Uroplakins (UPs) are a family of proteins that associate with each other to form plaques on the apical surface of the urothelium, the pseudo-stratified epithelium lining the urinary tract from renal pelvis to the bladder outlet. UPs are classified into 3 types: UPIa and UPIb, UPII, and UPIIIa and IIIb. UPIs are tetraspanins that have four transmembrane domains separating one large and one small extracellular domain while UPII and UPIIIs are single-pass transmembrane proteins. UPIa and UPIb form specific heterodimers with UPII and UPIII, respectively, which allows them to exit the endoplasmatic rediculum. UPII/UPIa and UPIIIs/UPIb form heterotetramers; six of these tetramers form the 16nm particle, seen in the hexagonal array of the asymmetric unit membrane, which is believed to form a urinary tract barrier. Uroplakins are also believed to play a role during urinary tract morphogenesis.


Pssm-ID: 197375  Cd Length: 181  Bit Score: 38.56  E-value: 9.14e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1133451038  690 RKRQAGGETVAETIGTNNSCGPNDivCNGPLKPGTQYQFKYRVYNsdDDDSYVESQYSGPIRTD 753
Cdd:cd09966     85 RNRRDIVSAYVLRVGNTTTCLSGY--CNTPLPGPGPYRVKYLVMN--GSGPSAQTEWSTPIRLN 144
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
882-1136 2.90e-121

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 374.69  E-value: 2.90e-121
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   882 KFSEEYEKVSAVGLDH-SKDASLLPENRAKNRYTNILAYDHSRVKLESIDDEPgSDYINANYIPGYRMRRAYIATQGPLP 960
Cdd:smart00194    1 GLEEEFEKLDRLKPDDeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   961 STFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWP--GAQPEVYGEINVDMLSETEKSDWIVRKFKITKEKRS--RTI 1036
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPdeEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSetRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  1037 THYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQH 1116
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                           250       260
                    ....*....|....*....|
gi 1133451038  1117 RNHMIQTEPQYVFIHKAMVD 1136
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 912-1132 8.09e-117

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: 361.29  E-value: 8.09e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  912 RYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTK 991
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  992 CHRYWP-GAQPEVYGEINVDMLSETEKSDWIVRKFKITKEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSA 1070
Cdd:cd14548     81 CDHYWPfDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQE 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133451038 1071 FGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHK 1132
Cdd:cd14548    161 KGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
907-1136 5.57e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 343.46  E-value: 5.57e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  907 NRAKNRYTNILAYDHSRVKLEsiDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVE 986
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  987 RGRTKCHRYWPGA--QPEVYGEINVDMLSETE-KSDWIVRKFKITK--EKRSRTITHYQFVSWPDHGVPDEAGPALDFVR 1061
Cdd:pfam00102   79 KGREKCAQYWPEEegESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1133451038 1062 EVHEVASSAF-GPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVD 1136
Cdd:pfam00102  159 KVRKSSLDGRsGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 896-1132 8.90e-107

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: 335.71  E-value: 8.90e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  896 DHSKDASLLPENRAKNRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNS 975
Cdd:cd14614      1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  976 HVIVMLTQLVERGRTKCHRYWP-GAQPEVYGEINVDMLSETEKSDWIVRKFKITKEKRSRTITHYQFVSWPDHGVP--DE 1052
Cdd:cd14614     81 QIIVMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPtaNA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1053 AGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHK 1132
Cdd:cd14614    161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 907-1137 1.46e-104

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: 329.36  E-value: 1.46e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  907 NRAKNRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVE 986
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  987 RGRTKCHRYWPGAQPEVYGEINVDMLSETEKSDWIVRKFKITKEKRS--RTITHYQFVSWPDHGVPDEAGPALDFVREVH 1064
Cdd:cd14553     83 RSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSekREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1133451038 1065 EVASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVDA 1137
Cdd:cd14553    163 ACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEA 235
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 937-1132 1.28e-96

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: 306.13  E-value: 1.28e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWP--GAQPEVYGEINVDMLSE 1014
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPeeGGKPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1015 TEKSDWIVRKFKITK--EKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALG 1092
Cdd:cd00047     81 EELSDYTIRTLELSPkgCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1133451038 1093 TLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHK 1132
Cdd:cd00047    161 ILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 867-1137 7.15e-95

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: 304.65  E-value: 7.15e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  867 DFPSYVEDMLNDAGFKFSEEYEKVSAvGLDHSKDASLLPENRAKNRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGY 946
Cdd:cd14626      2 DLADNIERLKANDGLKFSQEYESIDP-GQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  947 RMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGAQPEVYGEINVDMLSETEKSDWIVRKFK 1026
Cdd:cd14626     81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1027 ITKEKRS--RTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWV 1104
Cdd:cd14626    161 LYKNGSSekREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTV 240

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1133451038 1105 DLFGLASEMRQHRNHMIQTEPQYVFIHKAMVDA 1137
Cdd:cd14626    241 DIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEA 273
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 911-1132 4.18e-94

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: 300.68  E-value: 4.18e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  911 NRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRT 990
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  991 KCHRYWPGAQ-PEVYGEINVDMLSETEKSDWIVRKFKITKEKR---SRTITHYQFVSWPDHGVPDEAGPALDFVREVHEV 1066
Cdd:cd14617     81 KCDHYWPADQdSLYYGDLIVQMLSESVLPEWTIREFKICSEEQldaPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133451038 1067 A--SSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHK 1132
Cdd:cd14617    161 InrTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 885-1132 4.66e-94

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: 302.36  E-value: 4.66e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  885 EEYEKVSAVGLDHSKDASLLPENRAKNRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFD 964
Cdd:cd14543      7 EEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYS 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  965 DFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWP--GAQPEVYGEINVDMLSETEKSDWIVRKFKI--TKEKRSRTITHYQ 1040
Cdd:cd14543     87 DFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPleEGSSLRYGDLTVTNLSVENKEHYKKTTLEIhnTETDESRQVTHFQ 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1041 FVSWPDHGVPDEAGPALDF---VREVHEVASSAFG----------PVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLF 1107
Cdd:cd14543    167 FTSWPDFGVPSSAAALLDFlgeVRQQQALAVKAMGdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVM 246

                          250       260
                   ....*....|....*....|....*
gi 1133451038 1108 GLASEMRQHRNHMIQTEPQYVFIHK 1132
Cdd:cd14543    247 QTVRRMRTQRAFSIQTPDQYYFCYK 271
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 937-1131 1.76e-93

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: 297.73  E-value: 1.76e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGAQPEVYGEINVDMLSETE 1016
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1017 KSDWIVRKFKI--TKEKRS------RTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTF 1088
Cdd:cd14549     81 LATYTVRTFSLknLKLKKVkgrsseRVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1133451038 1089 IALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIH 1131
Cdd:cd14549    161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 883-1137 3.88e-92

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: 296.95  E-value: 3.88e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  883 FSEEYEKVSAVGLDHSKDA--SLLPENRAKNRYTNILAYDHSRVKLESI--DDEPGSDYINANYIPGYRMRRAYIATQGP 958
Cdd:cd17667      1 FSEDFEEVQRCTADMNITAehSNHPDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  959 LPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGAQPEVYGEINVDMLSETEKSDWIVRKFKI--TKEKR---- 1032
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIrnTKVKKgqkg 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1033 -------SRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVD 1105
Cdd:cd17667    161 npkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1133451038 1106 LFGLASEMRQHRNHMIQTEPQYVFIHKAMVDA 1137
Cdd:cd17667    241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEA 272
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 911-1136 2.47e-88

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: 284.79  E-value: 2.47e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  911 NRYTNILAYDHSRVKLeSIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRT 990
Cdd:cd14615      1 NRYNNVLPYDISRVKL-SVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  991 KCHRYWPGAQPEVYGEINVDMLSETEKSDWIVRKFKIT--KEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVAS 1068
Cdd:cd14615     80 KCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKnaQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYMK 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1069 --SAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVD 1136
Cdd:cd14615    160 qnPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 867-1137 2.76e-87

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


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 284.32  E-value: 2.76e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  867 DFPSYVEDMLNDAGFKFSEEYEKVSAvGLDHSKDASLLPENRAKNRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGY 946
Cdd:cd14624      8 ELADHIERLKANDNLKFSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGY 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  947 RMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGAQPEVYGEINVDMLSETEKSDWIVRKFK 1026
Cdd:cd14624     87 RKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVELATYCVRTFA 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1027 ITKEKRS--RTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWV 1104
Cdd:cd14624    167 LYKNGSSekREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTV 246

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1133451038 1105 DLFGLASEMRQHRNHMIQTEPQYVFIHKAMVDA 1137
Cdd:cd14624    247 DIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEA 279
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 865-1137 2.41e-86

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


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 281.60  E-value: 2.41e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  865 LRDFPSYVEDMLNDAGFKFSEEYEKVSAvGLDHSKDASLLPENRAKNRYTNILAYDHSRVKLESIDDEPGSDYINANYIP 944
Cdd:cd14625      6 ISELAEHTERLKANDNLKLSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYID 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  945 GYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGAQPEVYGEINVDMLSETEKSDWIVRK 1024
Cdd:cd14625     85 GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELATFCVRT 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1025 FKITKEKRS--RTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHD 1102
Cdd:cd14625    165 FSLHKNGSSekREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEK 244

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1133451038 1103 WVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVDA 1137
Cdd:cd14625    245 TVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEA 279
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 911-1131 3.29e-85

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: 276.20  E-value: 3.29e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  911 NRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRM-RRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERgR 989
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  990 TKCHRYWPGAQPEVYGEINVDMLSETEKSDWIVRKFKITKEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASS 1069
Cdd:cd14547     80 EKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEARQT 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1133451038 1070 AF--GPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIH 1131
Cdd:cd14547    160 EPhrGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 911-1136 2.47e-84

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: 274.07  E-value: 2.47e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  911 NRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRT 990
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  991 KCHRYWP-GAQPEVYGEINVDMLSETEKSDWIVRKF--KITKEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVA 1067
Cdd:cd14619     81 KCEHYWPlDYTPCTYGHLRVTVVSEEVMENWTVREFllKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133451038 1068 SSAF--GPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVD 1136
Cdd:cd14619    161 DQTMsgGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 911-1135 1.83e-82

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: 268.73  E-value: 1.83e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  911 NRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRT 990
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  991 KCHRYWPG-AQPEVYGEINVDMLSETEKSDWIVRKFKITKE--KRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHE-- 1065
Cdd:cd14618     81 LCDHYWPSeSTPVSYGHITVHLLAQSSEDEWTRREFKLWHEdlRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREhv 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1066 VASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMV 1135
Cdd:cd14618    161 QATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 907-1134 5.12e-82

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 268.18  E-value: 5.12e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  907 NRAKNRYTNILAYDHSRVKLESID-DEPGSDYINANYI-------PGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVI 978
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDpNVPGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  979 VMLTQLVERGRTKCHRYWPG-AQPEVYGEINVDMLSETEKSDWIVRKFKITKEKRS---RTITHYQFVSWPDHGVPDEAG 1054
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPDeGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGdpiREIWHYQYLSWPDHGVPSDPG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1055 PALDFVREVHEVASS--AFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHdwvdlfGLASEM---------RQHRNHMIQT 1123
Cdd:cd14544    161 GVLNFLEDVNQRQESlpHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRK------GLDCDIdiqktiqmvRSQRSGMVQT 234

                          250
                   ....*....|.
gi 1133451038 1124 EPQYVFIHKAM 1134
Cdd:cd14544    235 EAQYKFIYVAV 245
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 904-1133 5.25e-82

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: 267.85  E-value: 5.25e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  904 LPENRAKNRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQ 983
Cdd:cd14554      3 LPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  984 LVERGRTKCHRYWPGAQPEVYGEINVDMLSETEKSDWIVRKFKIT--KEKRSRTITHYQFVSWPDHGVPDEAGPALDFVR 1061
Cdd:cd14554     83 LREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIG 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1133451038 1062 EVHEvASSAF---GPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKA 1133
Cdd:cd14554    163 QVHK-TKEQFgqeGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 906-1138 2.48e-81

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: 265.74  E-value: 2.48e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  906 ENRAKNRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLV 985
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  986 ERGRTKCHRYWPGaQPEVYGEINVDMLSETEKSDWIVRKFKITKEKRS--RTITHYQFVSWPDHGVPDEAGPALDFVREV 1063
Cdd:cd14630     82 EVGRVKCVRYWPD-DTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHeiREIRQFHFTSWPDHGVPCYATGLLGFVRQV 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1133451038 1064 HEVASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVDAC 1138
Cdd:cd14630    161 KFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEAC 235
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 911-1132 2.63e-78

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: 257.14  E-value: 2.63e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  911 NRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRT 990
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  991 KCHRYWP-GAQP-EVYGEINVDMLSETEKSDWIVRKFKITKEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVAS 1068
Cdd:cd14616     81 RCHQYWPeDNKPvTVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRASRA 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1133451038 1069 SAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHK 1132
Cdd:cd14616    161 HDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 867-1138 4.29e-77

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 255.74  E-value: 4.29e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  867 DFPSYVEDMLNDAGFKFSEEYEKVSAvGLDHSKDASLLPENRAKNRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGY 946
Cdd:cd14633      1 DLLQHITQMKCAEGYGFKEEYESFFE-GQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  947 RMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGaQPEVYGEINVDMLSETEKSDWIVRKFK 1026
Cdd:cd14633     80 HRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD-DTEIYKDIKVTLIETELLAEYVIRTFA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1027 ItkEKRS----RTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHD 1102
Cdd:cd14633    159 V--EKRGvheiREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREG 236

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1133451038 1103 WVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVDAC 1138
Cdd:cd14633    237 VVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEAC 272
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 937-1131 6.30e-75

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: 247.16  E-value: 6.30e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYI-PGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWP-GAQPEVYGEINVDMLSE 1014
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPsGEYEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1015 TEKSDW--IVRKFKITKEKR-SRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAF--GPVIVHCSAGVGRTGTFI 1089
Cdd:cd18533     81 EENDDGgfIVREFELSKEDGkVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASldPPIIVHCSAGVGRTGTFI 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1133451038 1090 ALGTLLQHIKDHDWVDLFGLAS---------EMRQHRNHMIQTEPQYVFIH 1131
Cdd:cd18533    161 ALDSLLDELKRGLSDSQDLEDSedpvyeivnQLRKQRMSMVQTLRQYIFLY 211
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 883-1136 8.90e-72

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: 241.47  E-value: 8.90e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  883 FSEEYEKVSAVGLDHSKDASLLPENRAKNRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPST 962
Cdd:cd14621     28 FREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEET 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  963 FDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGAQPEVYGEINVDMLSETEKSDWIVRKF------KITKEKRSRTI 1036
Cdd:cd14621    108 VNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFciqqvgDVTNKKPQRLI 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1037 THYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQH 1116
Cdd:cd14621    188 TQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQ 267

                          250       260
                   ....*....|....*....|
gi 1133451038 1117 RNHMIQTEPQYVFIHKAMVD 1136
Cdd:cd14621    268 RCQMVQTDMQYVFIYQALLE 287
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 905-1134 1.06e-71

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: 240.11  E-value: 1.06e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  905 PENRAKNRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQL 984
Cdd:cd14603     28 KENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACRE 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  985 VERGRTKCHRYWPGAQ-PEVYGEINVDMLSETE-KSDWIVRKFKITKEKRSRTITHYQFVSWPDHGVPDEAGPALDFVRE 1062
Cdd:cd14603    108 IEMGKKKCERYWAQEQePLQTGPFTITLVKEKRlNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIEL 187

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1133451038 1063 VHEVASSAFGPVIVHCSAGVGRTGTFIALG-----TLLQHIKDHdwVDLFGLASEMRQHRNHMIQTEPQYVFIHKAM 1134
Cdd:cd14603    188 ARRLQGSGPEPLCVHCSAGCGRTGVICTVDyvrqlLLTQRIPPD--FSIFDVVLEMRKQRPAAVQTEEQYEFLYHTV 262
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 904-1136 1.07e-71

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: 241.17  E-value: 1.07e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  904 LPENRAKNRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQ 983
Cdd:cd14628     49 LPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTK 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  984 LVERGRTKCHRYWPGAQPEVYGEINVDMLSETEKSDWIVRKFKIT--KEKRSRTITHYQFVSWPDHGVPDEAGPALDFVR 1061
Cdd:cd14628    129 LREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIG 208

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1133451038 1062 EVHEVASS--AFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVD 1136
Cdd:cd14628    209 QVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 913-1136 1.13e-71

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: 238.69  E-value: 1.13e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  913 YTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKC 992
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  993 HRYWPGAQPEVYGEINVDMLSETEKSDWIVRKFKITKE-----KRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVA 1067
Cdd:cd14620     81 YQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSVN 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1133451038 1068 SSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVD 1136
Cdd:cd14620    161 PVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 904-1136 2.25e-71

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: 240.02  E-value: 2.25e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  904 LPENRAKNRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQ 983
Cdd:cd14627     50 LPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTK 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  984 LVERGRTKCHRYWPGAQPEVYGEINVDMLSETEKSDWIVRKFKIT--KEKRSRTITHYQFVSWPDHGVPDEAGPALDFVR 1061
Cdd:cd14627    130 LREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIG 209

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1133451038 1062 EVHEVASS--AFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVD 1136
Cdd:cd14627    210 QVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 906-1134 5.29e-71

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: 237.61  E-value: 5.29e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  906 ENRAKNRYTNILAYDHSRVKLESID-DEPGSDYINANYI-PGY-------RMRRAYIATQGPLPSTFDDFWRMTWEQNSH 976
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIImPEFetkcnnsKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  977 VIVMLTQLVERGRTKCHRYWPGAQP-EVYGEINVDMLSETEKSDWIVRKFKITKEKR---SRTITHYQFVSWPDHGVPDE 1052
Cdd:cd14605     81 VIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRVRNVKESAAHDYILRELKLSKVGQgntERTVWQYHFRTWPDHGVPSD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1053 AGPALDFVREVH--EVASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIK----DHDwVDLFGLASEMRQHRNHMIQTEPQ 1126
Cdd:cd14605    161 PGGVLDFLEEVHhkQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIRekgvDCD-IDVPKTIQMVRSQRSGMVQTEAQ 239


                   ....*...
gi 1133451038 1127 YVFIHKAM 1134
Cdd:cd14605    240 YRFIYMAV 247
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 937-1135 7.28e-71

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: 235.64  E-value: 7.28e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGAQPEVYGEINVDMLSETE 1016
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1017 KSDWIVRKFKI--TKEKR--------SRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTG 1086
Cdd:cd17668     81 LAYYTVRNFTLrnTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1133451038 1087 TFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMV 1135
Cdd:cd17668    161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 904-1136 8.27e-71

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: 238.47  E-value: 8.27e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  904 LPENRAKNRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQ 983
Cdd:cd14629     50 LPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTK 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  984 LVERGRTKCHRYWPGAQPEVYGEINVDMLSETEKSDWIVRKFKIT--KEKRSRTITHYQFVSWPDHGVPDEAGPALDFVR 1061
Cdd:cd14629    130 LREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIG 209

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1133451038 1062 EVHEVASS--AFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVD 1136
Cdd:cd14629    210 QVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 897-1134 2.76e-70

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: 236.32  E-value: 2.76e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  897 HSKDASLLPENRAKNRYTNILAYDHSRVKLESIDDE-PGSDYINANYIPGYRM-----RRAYIATQGPLPSTFDDFWRMT 970
Cdd:cd14606      8 HQRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNQLLgpdenAKTYIASQGCLEATVNDFWQMA 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  971 WEQNSHVIVMLTQLVERGRTKCHRYWP--GAQPEvYGEINVDMLSETEKSDWIVRKFKITKEKRS---RTITHYQFVSWP 1045
Cdd:cd14606     88 WQENSRVIVMTTREVEKGRNKCVPYWPevGMQRA-YGPYSVTNCGEHDTTEYKLRTLQVSPLDNGeliREIWHYQYLSWP 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1046 DHGVPDEAGPALDFVREVHEVASS--AFGPVIVHCSAGVGRTGTFIALGTLLQHIK----DHDwVDLFGLASEMRQHRNH 1119
Cdd:cd14606    167 DHGVPSEPGGVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENIStkglDCD-IDIQKTIQMVRAQRSG 245

                          250
                   ....*....|....*
gi 1133451038 1120 MIQTEPQYVFIHKAM 1134
Cdd:cd14606    246 MVQTEAQYKFIYVAI 260
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 936-1137 7.49e-70

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: 232.60  E-value: 7.49e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  936 DYINANY----IPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWP-GAQPEVYGEINVD 1010
Cdd:cd14541      1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPdLGETMQFGNLQIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1011 MLSETEKSDWIVRKFKIT--KEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTF 1088
Cdd:cd14541     81 CVSEEVTPSFAFREFILTntNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1133451038 1089 IALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVDA 1137
Cdd:cd14541    161 ITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 904-1134 4.06e-68

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: 229.34  E-value: 4.06e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  904 LPENRAKNRYTNILAYDHSRVKLESIDDEPG-SDYINANYIPGYRMR-RAYIATQGPLPSTFDDFWRMTWEQNSHVIVML 981
Cdd:cd14612     12 IPGHASKDRYKTILPNPQSRVCLRRAGSQEEeGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVMI 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  982 TQLVERgRTKCHRYWPGAQpEVYGEINVDMLSETEKSDWIVRKFKITKEKRSRTITHYQFVSWPDHGVPDEAGPALDFVR 1061
Cdd:cd14612     92 TKLKEK-KEKCVHYWPEKE-GTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGPLLRLVA 169

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1133451038 1062 EVHEVASSA--FGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAM 1134
Cdd:cd14612    170 EVEESRQTAasPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTL 244
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 937-1138 6.06e-67

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 224.41  E-value: 6.06e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPgAQPEVYGEINVdMLSETE 1016
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-DDTEVYGDIKV-TLVETE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1017 K-SDWIVRKFKITKEKRS--RTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALGT 1093
Cdd:cd14555     79 PlAEYVVRTFALERRGYHeiREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVIDI 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1133451038 1094 LLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVDAC 1138
Cdd:cd14555    159 MLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEAC 203
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 937-1132 7.76e-67

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: 223.94  E-value: 7.76e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGAQ--PEVYGEINVDMLSE 1014
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEegSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1015 TEKSDWIVRKFKIT--KEKRS-RTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIAL 1091
Cdd:cd14557     81 KICPDYIIRKLNINnkKEKGSgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1133451038 1092 GTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHK 1132
Cdd:cd14557    161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 882-1135 1.02e-66

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: 226.27  E-value: 1.02e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  882 KFSEEYEKVSAVGLDHSKdaslLPENRAKNRYTNILAYDHSRVKLESiddepGSDYINANY----IPGYRMRRAYIATQG 957
Cdd:cd14600     19 QFEQLYRKKPGLAITCAK----LPQNMDKNRYKDVLPYDATRVVLQG-----NEDYINASYvnmeIPSANIVNKYIATQG 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  958 PLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGAqPEV--YGEINVDMLSETEKSDWIVRKFKITKEK--RS 1033
Cdd:cd14600     90 PLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDP-PDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQtgEE 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1034 RTITHYQFVSWPDHGVPDEAGPALDFVREVHE--VASSafgPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLAS 1111
Cdd:cd14600    169 RTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSkrVENE---PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVR 245

                          250       260
                   ....*....|....*....|....
gi 1133451038 1112 EMRQHRNHMIQTEPQYVFIHKAMV 1135
Cdd:cd14600    246 KMRDQRAMMVQTSSQYKFVCEAIL 269
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 910-1134 6.16e-66

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: 223.59  E-value: 6.16e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  910 KNRYTNILAYDHSRVKLESID-DEPGSDYINANYIPGY-RMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVER 987
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDqDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  988 GRtKCHRYWPGAQPeVYGEINVDMLSETEKSDWIVRKFKITKEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVA 1067
Cdd:cd14613    108 NE-KCTEYWPEEQV-TYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVEEAR 185

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1068 SSA---FGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAM 1134
Cdd:cd14613    186 QQAepnCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 937-1135 4.87e-65

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: 218.68  E-value: 4.87e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGAQPEVYGEINVDMLSETE 1016
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1017 KSDWIVRKFKIT--KEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVH-EVASSAFGPVIVHCSAGVGRTGTFIALGT 1093
Cdd:cd14552     81 YEDYTLRDFLVTkgKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQkQQQQSGNHPITVHCSAGAGRTGTFCALST 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1133451038 1094 LLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMV 1135
Cdd:cd14552    161 VLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 907-1129 7.21e-65

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: 219.57  E-value: 7.21e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  907 NRakNRYTNILAYDHSRVKLESIDdepgSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVE 986
Cdd:cd14545      2 NR--YRDRDPYDHDRSRVKLKQGD----NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLME 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  987 RGRTKCHRYWPgaQPEVYGEI------NVDMLSETEKSDWIVRKFKIT--KEKRSRTITHYQFVSWPDHGVPDEAGPALD 1058
Cdd:cd14545     76 KGQIKCAQYWP--QGEGNAMIfedtglKVTLLSEEDKSYYTVRTLELEnlKTQETREVLHFHYTTWPDFGVPESPAAFLN 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1133451038 1059 FVREVHE--VASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDW--VDLFGLASEMRQHRNHMIQTEPQYVF 1129
Cdd:cd14545    154 FLQKVREsgSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 910-1136 2.90e-64

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: 217.79  E-value: 2.90e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  910 KNRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGR 989
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  990 TKCHRYW--PGAQPEVYGEINVDMLSETEKSDWIVRKFKITKEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVA 1067
Cdd:cd14602     81 KKCERYWaePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133451038 1068 SSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDH---DWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVD 1136
Cdd:cd14602    161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 937-1137 5.29e-64

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 216.09  E-value: 5.29e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYI--PGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGAQPE---VYGEINVDM 1011
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKpliCGGRLEVSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1012 LSETEKSDWIVRKFKITKEK--RSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSafGPVIVHCSAGVGRTGTFI 1089
Cdd:cd14538     81 EKYQSLQDFVIRRISLRDKEtgEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNS--GPIVVHCSAGIGRTGVLI 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1133451038 1090 ALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVDA 1137
Cdd:cd14538    159 TIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 937-1132 5.88e-64

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: 215.55  E-value: 5.88e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGAQPEVYGEINVDMLSETE 1016
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1017 KSDWIVRKFKITK------EKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIA 1090
Cdd:cd14551     81 LVDYTTRKFCIQKvnrgigEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTFIV 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1133451038 1091 LGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHK 1132
Cdd:cd14551    161 IDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 923-1138 9.36e-64

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: 215.65  E-value: 9.36e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  923 RVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPgAQPE 1002
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1003 VYGEINVDMLSETEKSDWIVRKFkiTKEKRS----RTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHC 1078
Cdd:cd14631     80 VYGDFKVTCVEMEPLAEYVVRTF--TLERRGyneiREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHC 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1079 SAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVDAC 1138
Cdd:cd14631    158 SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEAC 217
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 937-1132 1.59e-63

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: 214.59  E-value: 1.59e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWP--GAQPEVYGEINVDMLSE 1014
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPeeGEEQLQFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1015 TEKS-DWIVRKFKITKEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALG- 1092
Cdd:cd14542     81 KRVGpDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAIDy 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1133451038 1093 --TLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHK 1132
Cdd:cd14542    161 vwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 906-1134 2.75e-63

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: 217.49  E-value: 2.75e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  906 ENRAKNRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLV 985
Cdd:cd14604     56 ENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREF 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  986 ERGRTKCHRYWP--GAQPEVYGEINVDMLSETEKSDWIVRKFKITKEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREV 1063
Cdd:cd14604    136 EMGRKKCERYWPlyGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLM 215

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1133451038 1064 HEVASSAFGPVIVHCSAGVGRTGTFIALG---TLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAM 1134
Cdd:cd14604    216 RKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 910-1131 4.18e-63

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: 214.01  E-value: 4.18e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  910 KNRYTNILAYDHSRVKLESID-DEPGSDYINANYIPGYR-MRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVER 987
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  988 GRtKCHRYWPgAQPEVYGEINVDMLSETEKSDWIVRKFKITKEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHE-- 1065
Cdd:cd14611     82 NE-KCVLYWP-EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEdr 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1133451038 1066 VASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIH 1131
Cdd:cd14611    160 LASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 906-1135 1.07e-61

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: 210.46  E-value: 1.07e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  906 ENRAKNRYTNILAYDHSRVKLesiDDEPGsdYINANYI--PGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQ 983
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPL---GDEGG--YINASFIkmPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  984 LVERGRTKCHRYWP---GAQPEVYGEINVDMLSETEKSDWIVRKFKI--TKEKRSRTITHYQFVSWPDHGVPDEAGPALD 1058
Cdd:cd14597     77 EVEGGKIKCQRYWPeilGKTTMVDNRLQLTLVRMQQLKNFVIRVLELedIQTREVRHITHLNFTAWPDHDTPSQPEQLLT 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133451038 1059 FVREVHEVASSafGPVIVHCSAGVGRTGTFIALGTLLQHI-KDHDWvDLFGLASEMRQHRNHMIQTEPQYVFIHKAMV 1135
Cdd:cd14597    157 FISYMRHIHKS--GPIITHCSAGIGRSGTLICIDVVLGLIsKDLDF-DISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 937-1138 6.55e-61

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: 207.21  E-value: 6.55e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPgAQPEVYGEINVDMLSETE 1016
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1017 KSDWIVRKFKItkEKRSRTITH----YQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALG 1092
Cdd:cd14632     80 LAEYSVRTFAL--ERRGYSARHevkqFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLD 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1133451038 1093 TLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVDAC 1138
Cdd:cd14632    158 VMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEAC 203
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 887-1142 6.28e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 207.19  E-value: 6.28e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  887 YEKVSAVGLDHSKDASLLPENRAKNRYTNILAYDHSRVKLESIDDepgsDYINANYIPGYRMRRAYIATQGPLPSTFDDF 966
Cdd:cd14608      5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDN----DYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  967 WRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGAQ--PEVYGEIN--VDMLSETEKSDWIVRKFKITK--EKRSRTITHYQ 1040
Cdd:cd14608     81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEekEMIFEDTNlkLTLISEDIKSYYTVRQLELENltTQETREILHFH 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1041 FVSWPDHGVPDEAGPALDFVREVHEVAS--SAFGPVIVHCSAGVGRTGTFIALGT---LLQHIKDHDWVDLFGLASEMRQ 1115
Cdd:cd14608    161 YTTWPDFGVPESPASFLNFLFKVRESGSlsPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRK 240

                          250       260
                   ....*....|....*....|....*..
gi 1133451038 1116 HRNHMIQTEPQYVFIHKAMVDACKSSM 1142
Cdd:cd14608    241 FRMGLIQTADQLRFSYLAVIEGAKFIM 267
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 912-1134 1.80e-59

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: 203.74  E-value: 1.80e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  912 RYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTK 991
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  992 CHRYWPGAQPEVYGEINVDMLSETEKSDWIVRKFKIT--KEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVH-EVAS 1068
Cdd:cd14623     81 CAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTntRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQkQQQQ 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1133451038 1069 SAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAM 1134
Cdd:cd14623    161 SGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 936-1136 2.14e-59

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: 202.93  E-value: 2.14e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  936 DYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGAQPEVYGEINVDMLSET 1015
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1016 EKSDWIVRKFKIT--KEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVH-EVASSAFGPVIVHCSAGVGRTGTFIALG 1092
Cdd:cd14622     81 LLETISIRDFLVTynQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQkQQQQTGNHPIVVHCSAGAGRTGTFIALS 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1133451038 1093 TLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVD 1136
Cdd:cd14622    161 NILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 870-1136 7.96e-59

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


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 204.13  E-value: 7.96e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  870 SYVEDMLNDAGfKFSEEYEKVSAVGLD-HSKDASLLPENRAKNRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRM 948
Cdd:cd14610      7 SYMEDHLKNKN-RLEKEWEALCAYQAEpNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDP 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  949 RR-AYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGAQPEVYGEINVDMLSE-TEKSDWIVRKF- 1025
Cdd:cd14610     86 RNpAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEhIWCEDFLVRSFy 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1026 -KITKEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALGTLLQHI-KDHDW 1103
Cdd:cd14610    166 lKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKE 245

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1133451038 1104 VDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVD 1136
Cdd:cd14610    246 IDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 278
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 936-1135 2.04e-58

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: 200.17  E-value: 2.04e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  936 DYINANYI----PGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPG-AQPEVYGEINVD 1010
Cdd:cd14601      1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpSGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1011 MLSETEKSDWIVRKFKIT--KEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTF 1088
Cdd:cd14601     81 CHSEEGNPAYVFREMTLTnlEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGVL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1133451038 1089 IALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMV 1135
Cdd:cd14601    161 ITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 207
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 870-1136 3.91e-57

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


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 199.11  E-value: 3.91e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  870 SYVEDMLNDAGfKFSEEYEKVSAVGLD-HSKDASLLPENRAKNRYTNILAYDHSRVKLESIDDEPGSDYINANYIPGYRM 948
Cdd:cd14609      5 AYMEDHLRNRD-RLAKEWQALCAYQAEpNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHDP 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  949 RR-AYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGAQPEVYGEINVDMLSE-TEKSDWIVRKF- 1025
Cdd:cd14609     84 RMpAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEhIWCEDFLVRSFy 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1026 -KITKEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALGTLLQHI-KDHDW 1103
Cdd:cd14609    164 lKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKE 243

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1133451038 1104 VDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVD 1136
Cdd:cd14609    244 IDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 905-1134 4.56e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 198.27  E-value: 4.56e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  905 PENRAKNRYTNILAYDHSRVKLESIDDepgsDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQL 984
Cdd:cd14607     22 PENRNRNRYRDVSPYDHSRVKLQNTEN----DYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRI 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  985 VERGRTKCHRYWPGAQPEV--YGE--INVDMLSETEKSDWIVRKFKI--TKEKRSRTITHYQFVSWPDHGVPDEAGPALD 1058
Cdd:cd14607     98 VEKDSVKCAQYWPTDEEEVlsFKEtgFSVKLLSEDVKSYYTVHLLQLenINSGETRTISHFHYTTWPDFGVPESPASFLN 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1059 FVREVHEVASSAF--GPVIVHCSAGVGRTGTFIALGT--LLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAM 1134
Cdd:cd14607    178 FLFKVRESGSLSPehGPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 937-1132 1.65e-56

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: 194.52  E-value: 1.65e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRA-YIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPG--AQPEVYGEINVDMLS 1013
Cdd:cd14539      1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTerGQALVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1014 ETEKSDWIVRKFKITK--EKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHE---VASSAFGPVIVHCSAGVGRTGTF 1088
Cdd:cd14539     81 VRTTPTHVERIISIQHkdTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShylQQRSLQTPIVVHCSSGVGRTGAF 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1133451038 1089 IALGTLLQHIK-DHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHK 1132
Cdd:cd14539    161 CLLYAAVQEIEaGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 937-1135 9.19e-56

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: 193.06  E-value: 9.19e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIP---GYRMRRaYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWP----GAQPEVYGEINV 1009
Cdd:cd14540      1 YINASHITatvGGKQRF-YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPtlggEHDALTFGEYKV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1010 DMLSETEKSDWIVRKFKI--TKEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFG---------PVIVHC 1078
Cdd:cd14540     80 STKFSVSSGCYTTTGLRVkhTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQdvaghnrnpPTLVHC 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1133451038 1079 SAGVGRTGTFIaLGTLLQHIKDHDW-VDLFGLASEMRQHRNHMIQTEPQYVFIHKAMV 1135
Cdd:cd14540    160 SAGVGRTGVVI-LADLMLYCLDHNEeLDIPRVLALLRHQRMLLVQTLAQYKFVYNVLI 216
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 937-1137 2.35e-55

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: 191.11  E-value: 2.35e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIpgyRMR-----RAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGA--QPEVYGEINV 1009
Cdd:cd14596      1 YINASYI---TMPvgeeeLFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlqEPMELENYQL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1010 DMLSETEKSDWIVRKFKITKEK--RSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSafGPVIVHCSAGVGRTGT 1087
Cdd:cd14596     78 RLENYQALQYFIIRIIKLVEKEtgENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT--GPIVVHCSAGIGRAGV 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1088 FIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVDA 1137
Cdd:cd14596    156 LICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 886-1135 1.86e-52

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: 185.97  E-value: 1.86e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  886 EYEKVSAVGLDHSKDASLLPENRAKNRYTNILAYDHSRVKLESIDDEPgSDYINANYIP----GYRMRraYIATQGPLPS 961
Cdd:cd14599     17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENN-TGYINASHIKvtvgGEEWH--YIATQGPLPH 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  962 TFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWP--GAQ--PEVYGEINVDMLSETEKSDWIVRKFKITK--EKRSRT 1035
Cdd:cd14599     94 TCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklGSKhsSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERT 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1036 ITHYQFVSWPDHGVPDEAGPALDFVREVHEV----------ASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVD 1105
Cdd:cd14599    174 VWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVrrhtnsmldsTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVE 253

                          250       260       270
                   ....*....|....*....|....*....|
gi 1133451038 1106 LFGLASEMRQHRNHMIQTEPQYVFIHKAMV 1135
Cdd:cd14599    254 VPVMLRHLREQRMFMIQTIAQYKFVYQVLI 283
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 937-1133 4.84e-52

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: 181.87  E-value: 4.84e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRR-AYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGAQPEVYGEINVDMLSET 1015
Cdd:cd14546      1 YINASTIYDHDPRNpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1016 EKS-DWIVRKF--KITKEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALG 1092
Cdd:cd14546     81 IWCdDYLVRSFylKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILID 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1133451038 1093 TLLQHI-KDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKA 1133
Cdd:cd14546    161 MVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTA 202
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 937-1131 6.73e-52

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


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 181.07  E-value: 6.73e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTkCHRYWPGAQPEVYGEINVDMLSETE 1016
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWPDEGSGTYGPIQVEFVSTTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1017 KSDWIVRKFKITKEKR----SRTITHYQFVSWPDHG-VPDEAGPALDFVREVHE-VASSAFGPVIVHCSAGVGRTGTFIA 1090
Cdd:cd14556     80 DEDVISRIFRLQNTTRpqegYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKwQEQSGEGPIVVHCLNGVGRSGVFCA 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1133451038 1091 LGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIH 1131
Cdd:cd14556    160 ISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PHA02738 PHA02738
hypothetical protein; Provisional
 884-1134 7.34e-49

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 176.65  E-value: 7.34e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  884 SEEYEKVSAVGLDHSKDASLlpENRAKNRYTNILAYDHSRVKLESidDEPGSDYINANYIPGYRMRRAYIATQGPLPSTF 963
Cdd:PHA02738    28 TREHQKVISEKVDGTFNAEK--KNRKLNRYLDAVCFDHSRVILPA--ERNRGDYINANYVDGFEYKKKFICGQAPTRQTC 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  964 DDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWpgaqpevygeinvdmlSETEKSDWIVRKFKITKEKRSR--------- 1034
Cdd:PHA02738   104 YDFYRMLWMEHVQIIVMLCKKKENGREKCFPYW----------------SDVEQGSIRFGKFKITTTQVEThphyvkstl 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1035 ----------TITHYQFVSWPDHGVPDEAGPALDFVREVH----EVASSAFG---------PVIVHCSAGVGRTGTFIAL 1091
Cdd:PHA02738   168 lltdgtsatqTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRqcqkELAQESLQighnrlqppPIVVHCNAGLGRTPCYCVV 247

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1133451038 1092 GTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAM 1134
Cdd:PHA02738   248 DISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 937-1131 1.15e-47

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: 169.11  E-value: 1.15e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWpGAQPEVYGEINVDmLSETE 1016
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYW-GDEKKTYGDIEVE-LKDTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1017 KS-DWIVRKFKITKEKR--SRTITHYQFVSWPDHGVPDEAGPALDFVREVHE------VASSAFGPVIVHCSAGVGRTGT 1087
Cdd:cd14558     79 KSpTYTVRVFEITHLKRkdSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQklpyknSKHGRSVPIVVHCSDGSSRTGI 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1133451038 1088 FIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIH 1131
Cdd:cd14558    159 FCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 937-1131 1.23e-46

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 166.10  E-value: 1.23e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYI--PGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRT-KCHRYWPGA--QPEVYGEINVDM 1011
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1012 LSETEKSDWIVRKF----KITKEKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEVASSAfGPVIVHCSAGVGRTGT 1087
Cdd:cd17658     81 KKLKHSQHSITLRVlevqYIESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSA-GPIVVHCSAGIGRTGA 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1133451038 1088 FIALGTLLQHIKDHDW--VDLFGLASEMRQHRNHMIQTEPQYVFIH 1131
Cdd:cd17658    160 YCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 874-1134 4.99e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 165.97  E-value: 4.99e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  874 DMLNDAGF-KF-SEEYEKVSAVGLDHSKDASLLPENRAKNRYTNILAYDHSRV-------------------KLESIDDE 932
Cdd:PHA02746    16 DKTNHAKFcEFvLLEHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVvinaheslkmfdvgdsdgkKIEVTSED 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  933 PGSDYINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQlVERGRTKCHRYW--PGAQPEVYGEINVD 1010
Cdd:PHA02746    96 NAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELAFGRFVAK 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1011 MLSETEKSDWIVRKFKITKE--KRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHE----------VASSAFGPVIVHC 1078
Cdd:PHA02746   175 ILDIIEELSFTKTRLMITDKisDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQTLGPIVVHC 254

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1133451038 1079 SAGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAM 1134
Cdd:PHA02746   255 SAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 886-1131 8.49e-43

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 159.01  E-value: 8.49e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  886 EYEKVSAVGLDHSKDASLLPENRAKNRYTNILAYDHSRVKLESiDDEPGSDYINANYIPGYRMRRAYIATQGPLPSTFDD 965
Cdd:PHA02747    30 EHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCAD 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  966 FWRMTWEQNSHVIVMLTQL-VERGRTKCHRYW-PGAQPEVYGE-INVDMLSETEKSDWIVRKFKITKE--KRSRTITHYQ 1040
Cdd:PHA02747   109 FWKAVWQEHCSIIVMLTPTkGTNGEEKCYQYWcLNEDGNIDMEdFRIETLKTSVRAKYILTLIEITDKilKDSRKISHFQ 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1041 FVSWPDHGVPDEAGPALDFVR---EVHEVASSAFG-------PVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGLA 1110
Cdd:PHA02747   189 CSEWFEDETPSDHPDFIKFIKiidINRKKSGKLFNpkdallcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTA 268

                          250       260
                   ....*....|....*....|.
gi 1133451038 1111 SEMRQHRNHMIQTEPQYVFIH 1131
Cdd:PHA02747   269 EKIREQRHAGIMNFDDYLFIQ 289
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
872-1134 1.94e-42

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 156.79  E-value: 1.94e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  872 VEDMLNDagfKFSEEYEKVSAVGLDHSKDASLlpENRAKNRYTNILAYDHSRVklesiddEPGSDYINANYIPGYRMRRa 951
Cdd:COG5599     12 EEEKINS---RLSTLTNELAPSHNDPQYLQNI--NGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIGNHR- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  952 YIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVE--RGRTKCHRYWPgAQPEvYGEINVDmlSETEKSDWI-----VRK 1024
Cdd:COG5599     79 YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFR-QDGE-YGKYEVS--SELTESIQLrdgieART 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1025 FKITKE---KRSRTITHYQFVSWPDH-GVPDEAGPAL-DFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIK 1099
Cdd:COG5599    155 YVLTIKgtgQKKIEIPVLHVKNWPDHgAISAEALKNLaDLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSIN 234

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1133451038 1100 DHD--WVDLFGLASEMRQHRN-HMIQTEPQYVFIHKAM 1134
Cdd:COG5599    235 ALVqiTLSVEEIVIDMRTSRNgGMVQTSEQLDVLVKLA 272
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 885-1138 3.72e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 156.70  E-value: 3.72e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  885 EEYEKVSAVGLDHSKDASLLPENRAKNRYTNILAYDHSRVKLESIDDepGSDYINANYIPGYRMRRAYIATQGPLPSTFD 964
Cdd:PHA02742    30 EEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEETAL 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  965 DFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWPGAQ--PEVYGEINVDMLSETEKSDWIVRKFKITKEKR--SRTITHYQ 1040
Cdd:PHA02742   108 DFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHErgKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTgaSLDIKHFA 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1041 FVSWPDHGVPDEAGPALDFVREVHEVASSA-----------FGPVIVHCSAGVGRTGTFIALGTLLQHIKDHDWVDLFGL 1109
Cdd:PHA02742   188 YEDWPHGGLPRDPNKFLDFVLAVREADLKAdvdikgenivkEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSI 267

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1133451038 1110 ASEMRQHRNHMIQTEPQYVFIH-------KAMVDAC 1138
Cdd:PHA02742   268 VRDLRKQRHNCLSLPQQYIFCYfivlifaKLMADKC 303
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 937-1135 2.30e-39

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: 145.89  E-value: 2.30e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGY--RMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKCHRYWP--GAQPEV--YGEINVD 1010
Cdd:cd14598      1 YINASHIKVTvgGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlGSRHNTvtYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1011 MLSETEKSDWIVRKFKITK--EKRSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEV---------ASSAFGPVIVHCS 1079
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKHllTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVrrhtnstidPKSPNPPVLVHCS 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1133451038 1080 AGVGRTGTFIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMV 1135
Cdd:cd14598    161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLI 216
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1035-1136 1.10e-37

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 136.72  E-value: 1.10e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  1035 TITHYQFVSWPDHGVPDEAGPALDFVREVHEV--ASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKD-HDWVDLFGLAS 1111
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1133451038  1112 EMRQHRNHMIQTEPQYVFIHKAMVD 1136
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1035-1136 1.10e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 136.72  E-value: 1.10e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  1035 TITHYQFVSWPDHGVPDEAGPALDFVREVHEV--ASSAFGPVIVHCSAGVGRTGTFIALGTLLQHIKD-HDWVDLFGLAS 1111
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1133451038  1112 EMRQHRNHMIQTEPQYVFIHKAMVD 1136
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 937-1132 1.94e-36

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 136.68  E-value: 1.94e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKChrYWPGAQPEVYGE-INVDMLSET 1015
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPLECEtFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1016 EKSDW-----IVRKFKI--TKEKRSRTITHYQFVSWPDHGVPDEAgpALDFVREVHEVASSAFGPVIVHCSAGVGRTGTF 1088
Cdd:cd14550     79 HSCLSneirlIVRDFILesTQDDYVLEVRQFQCPSWPNPCSPIHT--VFELINTVQEWAQQRDGPIVVHDRYGGVQAATF 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1133451038 1089 IALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHK 1132
Cdd:cd14550    157 CALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 937-1136 1.20e-33

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


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 128.99  E-value: 1.20e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLveRGRTKCHRYWPGAQPEVYGEINVDMLSETE 1016
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSADI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1017 KSDWIVRKFKITKEKRS----RTITHYQFVSWPDH-GVPDEAGPALDFVREV---HEVASSAFGPVIVHCSAGVGRTGTF 1088
Cdd:cd14634     79 DEDIISRIFRICNMARPqdgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLekwQEQYDGREGRTVVHCLNGGGRSGTF 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1133451038 1089 IALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVD 1136
Cdd:cd14634    159 CAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 937-1129 8.03e-31

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 120.78  E-value: 8.03e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRT-KCHRYWPGAQPEVYGEINVDMLSET 1015
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1016 EKSDWIVRKFKITKEKRSR----TITHYQFVSW-PDHGVPDEAGPALDFVREVHE-VASSAFGPVIVHCSAGVGRTGTFI 1089
Cdd:cd14637     81 ADEDIVTRLFRVQNITRLQeghlMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKwQRESGEGRTVVHCLNGGGRSGTYC 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1133451038 1090 ALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVF 1129
Cdd:cd14637    161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRF 200
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 937-1131 3.08e-29

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 116.28  E-value: 3.08e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQL-VERGrtkCHRYWPGAQPEVYGEINVDMLSET 1015
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1016 EKSDWIVRKFKITKEKRSR----TITHYQFVSWPDH-GVPDEAGPALDFVREV---HEVASSAFGPVIVHCSAGVGRTGT 1087
Cdd:cd14636     78 MDCDVISRIFRICNLTRPQegylMVQQFQYLGWASHrEVPGSKRSFLKLILQVekwQEECDEGEGRTIIHCLNGGGRSGM 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1133451038 1088 FIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIH 1131
Cdd:cd14636    158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 937-1135 4.96e-29

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 115.48  E-value: 4.96e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRTKChRYWPGA-QPEVYGEINVDMLSE- 1014
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKdEPINCETFKVTLIAEe 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1015 ----TEKSDWIVRKF--KITKEKRSRTITHYQFVSWPDhgvPDEA-GPALDFVREVHEVASSAFGPVIVHCSAGVGRTGT 1087
Cdd:cd17669     80 hkclSNEEKLIIQDFilEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAANRDGPMIVHDEHGGVTAGT 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1133451038 1088 FIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMV 1135
Cdd:cd17669    157 FCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 937-1135 5.83e-29

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 115.55  E-value: 5.83e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQlvERGRTKCHR-YWPGAQPEVYGE------INV 1009
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEFvYWPSREESMNCEaftvtlISK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1010 DMLSETEKSDWIVRKF--KITKEKRSRTITHYQFVSWPDHGVPDEAgpALDFVREVHEVASSAFGPVIVHCSAGVGRTGT 1087
Cdd:cd17670     79 DRLCLSNEEQIIIHDFilEATQDDYVLEVRHFQCPKWPNPDAPISS--TFELINVIKEEALTRDGPTIVHDEFGAVSAGT 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1133451038 1088 FIALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMV 1135
Cdd:cd17670    157 LCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 937-1136 4.75e-27

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 110.16  E-value: 4.75e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  937 YINANYIPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQlVERGRTkCHRYWPGAQPEVYGEINVDMLSETE 1016
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQL-CPQYWPENGVHRHGPIQVEFVSADL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1017 KSDWIVRKFKITKEKRS----RTITHYQFVSWPDH-GVPDEAGPALDFVREV---HEVASSAFGPVIVHCSAGVGRTGTF 1088
Cdd:cd14635     79 EEDIISRIFRIYNAARPqdgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGGGRSGTF 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1133451038 1089 IALGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHKAMVD 1136
Cdd:cd14635    159 CAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 83-174 1.33e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.08  E-value: 1.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   83 PTSPSDVSYINISSTSIEVSWNPPTDFNGPNEGYVITYIRLESDT-ESMSTNRLTGTSFVIENLEKYEQYSVTVVAFTDK 161
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|...
gi 1133451038  162 GPGASSDVLSVLT 174
Cdd:cd00063     81 GESPPSESVTVTT 93
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 867-1132 2.39e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 84.25  E-value: 2.39e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  867 DFPSYVE--DMLNdagfKFSEEYEKVSAVGLDHSKDASLLPENRAK--NRYTNILAYDHSRVKLESidDEpgsDYINANY 942
Cdd:PHA02740    13 DFINFINkpDLLS----CIIKEYRAIVPEHEDEANKACAQAENKAKdeNLALHITRLLHRRIKLFN--DE---KVLDARF 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  943 IPGYRMRRAYIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERgrtKCH-RYWPGAQPEV--YGEINVDMLSETEKSD 1019
Cdd:PHA02740    84 VDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCFnQFWSLKEGCVitSDKFQIETLEIIIKPH 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1020 WIVRKFKITKEK-RSRTITHYQFVSWPDHGVPDEAGPALDFVREVHEV--------ASSAFGPVIVHCSAGVGRTGTFIA 1090
Cdd:PHA02740   161 FNLTLLSLTDKFgQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLcadlekhkADGKIAPIIIDCIDGISSSAVFCV 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1133451038 1091 LGTLLQHIKDHDWVDLFGLASEMRQHRNHMIQTEPQYVFIHK 1132
Cdd:PHA02740   241 FDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYH 282
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 911-1128 1.68e-16

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 80.14  E-value: 1.68e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  911 NRYTNIlaydHSRVKLEsidDEPGsdyINANYIPGYRMRRAyIATQGPLPSTFDDFWRMTWEQNSHVIVMLTQLVERGRT 990
Cdd:cd14559      1 NRFTNI----QTRVSTP---VGKN---LNANRVQIGNKNVA-IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  991 KCHRYWpgAQPEVYGEINVDmlSETEKSDWIVRKF-------KITKEKRSRTITHYQFVSWPDHG-VPDEAGPAL----- 1057
Cdd:cd14559     70 GLPPYF--RQSGTYGSVTVK--SKKTGKDELVDGLkadmynlKITDGNKTITIPVVHVTNWPDHTaISSEGLKELadlvn 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1058 -------DFVREVHEVASSAFG---PVIvHCSAGVGRTGTFIAlgtLLQHIKDHDWVDLFGLASEMRQHRN-HMIQTEPQ 1126
Cdd:cd14559    146 ksaeekrNFYKSKGSSAINDKNkllPVI-HCRAGVGRTGQLAA---AMELNKSPNNLSVEDIVSDMRTSRNgKMVQKDEQ 221


                   ..
gi 1133451038 1127 YV 1128
Cdd:cd14559    222 LD 223
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
40-342 5.79e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 76.58  E-value: 5.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   40 TSDTSYNISGLDVYTDYNVSVAAYTSAGTGPFDSVIRRT-DSTVPTSPSDVSYINISSTSIEVSWNPPTDFNGpnEGYVI 118
Cdd:COG3401    189 STTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESDA--TGYRV 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  119 tYIRLESDTESMSTNRLTGTSFVIENLEKYEQYSVTVVAFTDKG-PGASSDVLSVLTDEDLPGPPSNVS-TMSTNTSISI 196
Cdd:COG3401    267 -YRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTPPAAPSGLTaTAVGSSSITL 345

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  197 TWSPPLDPNglLLSYSINVTLNSTYaqylSFDVMTMSVSQNifSYTLFDLLPFAGYDISLQASTSVGLGTP------AIE 270
Cdd:COG3401    346 SWTASSDAD--VTGYNVYRSTSGGG----TYTKIAETVTTT--SYTDTGLTPGTTYYYKVTAVDAAGNESApseevsATT 417

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133451038  271 TETTLQAAPAAPVANPMASPVSSTAVNVSWLPPNLSNWNGLITNYTIEYRTNDEYIRPSIEVTATLSSFANS 342
Cdd:COG3401    418 ASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANL 489
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 495-587 1.60e-13

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.52  E-value: 1.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  495 PSAPDPVIVKRRNDTAIQVNWTRPAEPNGIILGYLIYYIGTKNNTGTEysninvliiINVTDPNTLSYLITNLLADTQYF 574
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKE---------VEVTPGSETSYTLTGLKPGTEYE 71

                           90
                   ....*....|...
gi 1133451038  575 INVTAYTSAGLGA 587
Cdd:cd00063     72 FRVRAVNGGGESP 84
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
183-628 1.02e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 72.34  E-value: 1.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  183 SNVSTMSTNTSISITWSPPLDPNGLLLSYSINVTLNSTYAQYLSFDVMTMSVSQNIFSYTLFDLLPFAGYDISLQASTSV 262
Cdd:COG3401     30 GGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNT 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  263 GLGTPAIETETTLQAAPAAPVANPMASPVSSTAVNVSWLPPNLSNWNGlitnytieyrTNDEYIRPSIEVTATLSSFANS 342
Cdd:COG3401    110 GLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASG----------TTASSVAGAGVVVSPDTSATAA 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  343 DDPRAATTPLQLESIIIPSLHEFVNYSFIITLSNSIGQISSLPVHIVTLESTPSGPPLDVSVIVDSPSTARISWSPPMYI 422
Cdd:COG3401    180 VATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTES 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  423 DrngiIVNYTVRIITTVRGTIREtnISNVSGNYYDASDLPQFASFNVTVAAATSVGL-GPYSPSVSNMTFEGVPSAPDPV 501
Cdd:COG3401    260 D----ATGYRVYRSNSGDGPFTK--VATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTDLTPPAAPSGL 333

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  502 IVKRRNDTAIQVNWTRPAEPNgiILGYLIYYigtKNNTGTEYSNINvliiinvTDPNTLSYLITNLLADTQYFINVTAYT 581
Cdd:COG3401    334 TATAVGSSSITLSWTASSDAD--VTGYNVYR---STSGGGTYTKIA-------ETVTTTSYTDTGLTPGTTYYYKVTAVD 401

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1133451038  582 SAGLGAVGDGDSILLPTGRPPTVPPNVTIGTPPTGGTSDPTTATTIR 628
Cdd:COG3401    402 AAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAA 448
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 83-164 1.74e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 64.17  E-value: 1.74e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038    83 PTSPSDVSYINISSTSIEVSWNPPTDfnGPNEGYVITYI---RLESDTESMSTNRLTGTSFVIENLEKYEQYSVTVVAFT 159
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPD--DGITGYIVGYRveyREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 1133451038   160 DKGPG 164
Cdd:smart00060   79 GAGEG 83
fn3 pfam00041
Fibronectin type III domain;
496-586 2.03e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 2.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  496 SAPDPVIVKRRNDTAIQVNWTRPAEPNGIILGYLIYYIGTknNTGTEYSNINVliiinvtDPNTLSYLITNLLADTQYFI 575
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPK--NSGEPWNEITV-------PGTTTSVTLTGLKPGTEYEV 71

                           90
                   ....*....|.
gi 1133451038  576 NVTAYTSAGLG 586
Cdd:pfam00041   72 RVQAVNGGGEG 82
fn3 pfam00041
Fibronectin type III domain;
85-167 2.20e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 2.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   85 SPSDVSYINISSTSIEVSWNPPTDFNGPNEGYVITYIrlESDTESMSTNRLTG---TSFVIENLEKYEQYSVTVVAFTDK 161
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYR--PKNSGEPWNEITVPgttTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 1133451038  162 GPGASS 167
Cdd:pfam00041   80 GEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 495-586 3.35e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 63.40  E-value: 3.35e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   495 PSAPDPVIVKRRNDTAIQVNWTRPAEPNGIilGYLIYYIGTKNNTGTEYSNINVliiinvtDPNTLSYLITNLLADTQYF 574
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVGYRVEYREEGSEWKEVNV-------TPSSTSYTLTGLKPGTEYE 71

                            90
                    ....*....|..
gi 1133451038   575 INVTAYTSAGLG 586
Cdd:smart00060   72 FRVRAVNGAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 397-487 6.09e-10

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 57.12  E-value: 6.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  397 GPPLDVSVIVDSPSTARISWSPPmyIDRNGIIVNYTVRIITTVRGTIRETNISNVSGNYYDASDLPQFASFNVTVAAATS 476
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPP--EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|.
gi 1133451038  477 VGLGPYSPSVS 487
Cdd:cd00063     80 GGESPPSESVT 90
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1057-1132 1.24e-09

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: 56.97  E-value: 1.24e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1133451038 1057 LDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIALGTLLqhikdHDWVDLFGLASEMRQHRNHMI-QTEPQYVFIHK 1132
Cdd:cd14494     42 VDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVL-----LGGMSAEEAVRIVRLIRPGGIpQTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1009-1132 2.73e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 56.90  E-value: 2.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1009 VDMLSETEKSDWIVRKFKITkekrsrtithYQFVSWPDHGVPDEAgPALDFVREVHEvASSAFGPVIVHCSAGVGRTGTF 1088
Cdd:COG2453     30 VSLTEEEELLLGLLEEAGLE----------YLHLPIPDFGAPDDE-QLQEAVDFIDE-ALREGKKVLVHCRGGIGRTGTV 97

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1133451038 1089 IALgTLLQHikdhdwvdlfGLASE-----MRQHRNHMIQTEPQYVFIHK 1132
Cdd:COG2453     98 AAA-YLVLL----------GLSAEealarVRAARPGAVETPAQRAFLER 135
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 2-69 3.20e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 54.93  E-value: 3.20e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133451038     2 SLRITWTELLEDDQNGVIIGYNISYFSLPAVGQPINNFTSDTSYNISGLDVYTDYNVSVAAYTSAGTG 69
Cdd:smart00060   16 SVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 179-274 1.73e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 52.88  E-value: 1.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  179 PGPPSNVS-TMSTNTSISITWSPPLDPNGLLLSYSInvtlnsTYAQYLSFDVMTMSVSQ-NIFSYTLFDLLPFAGYDISL 256
Cdd:cd00063      1 PSPPTNLRvTDVTSTSVTLSWTPPEDDGGPITGYVV------EYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRV 74

                           90
                   ....*....|....*...
gi 1133451038  257 QASTSVGLGTPAIETETT 274
Cdd:cd00063     75 RAVNGGGESPPSESVTVT 92
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1036-1131 2.91e-08

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 55.43  E-value: 2.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1036 ITHYQFvSWPDHGVPDEAGpALDFVRevheVASSAF---GPVIVHCSAGVGRTGTFIALGTL-LQHIKDHDWVDLFglas 1111
Cdd:cd14506     77 IYFYNF-GWKDYGVPSLTT-ILDIVK----VMAFALqegGKVAVHCHAGLGRTGVLIACYLVyALRMSADQAIRLV---- 146

                           90       100
                   ....*....|....*....|
gi 1133451038 1112 emRQHRNHMIQTEPQYVFIH 1131
Cdd:cd14506    147 --RSKRPNSIQTRGQVLCVR 164
fn3 pfam00041
Fibronectin type III domain;
180-267 8.01e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.88  E-value: 8.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  180 GPPSNVS-TMSTNTSISITWSPPLDPNGLLLSYSInvtlnsTYAQYLSFDVM-TMSVSQNIFSYTLFDLLPFAGYDISLQ 257
Cdd:pfam00041    1 SAPSNLTvTDVTSTSLTVSWTPPPDGNGPITGYEV------EYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQ 74

                           90
                   ....*....|
gi 1133451038  258 ASTSVGLGTP 267
Cdd:pfam00041   75 AVNGGGEGPP 84
fn3 pfam00041
Fibronectin type III domain;
2-71 9.37e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.88  E-value: 9.37e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133451038    2 SLRITWTELleDDQNGVIIGYNISYFSL--PAVGQPINNFTSDTSYNISGLDVYTDYNVSVAAYTSAGTGPF 71
Cdd:pfam00041   15 SLTVSWTPP--PDGNGPITGYEVEYRPKnsGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 179-265 1.66e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 49.92  E-value: 1.66e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   179 PGPPSNVS-TMSTNTSISITWSPPLDPNGllLSYSINVTLNStyaQYLSFDVMTMSVSQNIFSYTLFDLLPFAGYDISLQ 257
Cdd:smart00060    1 PSPPSNLRvTDVTSTSVTLSWEPPPDDGI--TGYIVGYRVEY---REEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVR 75


                    ....*...
gi 1133451038   258 ASTSVGLG 265
Cdd:smart00060   76 AVNGAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2-242 2.10e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 55.39  E-value: 2.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038    2 SLRITWTELLEDDqngvIIGYNISYFSLPAVGQPINNFTSDTSYNISGLDVYTDYNVSVAAYTSAGT--GPFDSVIRRTD 79
Cdd:COG3401    248 SVTLSWDPVTESD----ATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNesAPSNVVSVTTD 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   80 STVPTSPSDVSYINISSTSIEVSWNPPTDFNgpnegyVITYIRLESDTESMSTNRL----TGTSFVIENLEKYEQYSVTV 155
Cdd:COG3401    324 LTPPAAPSGLTATAVGSSSITLSWTASSDAD------VTGYNVYRSTSGGGTYTKIaetvTTTSYTDTGLTPGTTYYYKV 397

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  156 VAFTDKGP-GASSDVLSVLTDEDLPGPPSN--VSTMSTNTSISITWSPPLDPNGLLLSYSINVTLNSTYAQYLSFDVMTM 232
Cdd:COG3401    398 TAVDAAGNeSAPSEEVSATTASAASGESLTasVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTV 477

                          250
                   ....*....|
gi 1133451038  233 SVSQNIFSYT 242
Cdd:COG3401    478 TATTTDTTTA 487
fn3 pfam00041
Fibronectin type III domain;
397-483 5.39e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.57  E-value: 5.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  397 GPPLDVSVIVDSPSTARISWSPPMyiDRNGIIVNYTVRIITTVRGTI-RETNISNVSgNYYDASDLPQFASFNVTVAAAT 475
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPP--DGNGPITGYEVEYRPKNSGEPwNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVN 77


                   ....*...
gi 1133451038  476 SVGLGPYS 483
Cdd:pfam00041   78 GGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 2-71 2.48e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 2.48e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133451038    2 SLRITWTELLEDdqNGVIIGYNISYFSLPA--VGQPINNFTSDTSYNISGLDVYTDYNVSVAAYTSAGTGPF 71
Cdd:cd00063     16 SVTLSWTPPEDD--GGPITGYVVEYREKGSgdWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPP 85
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1026-1132 5.23e-06

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 47.64  E-value: 5.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1026 KITKEKRSRTItHYQFvswPDHGVPDEAGPALDFVREVHEvASSAFGPVIVHCSAGVGRTGTfIALGTLLQHIKDHDWVD 1105
Cdd:cd14505     66 EQYQQAGITWH-HLPI---PDGGVPSDIAQWQELLEELLS-ALENGKKVLIHCKGGLGRTGL-IAACLLLELGDTLDPEQ 139

                           90       100
                   ....*....|....*....|....*..
gi 1133451038 1106 LFglaSEMRQHRNHMIQTEPQYVFIHK 1132
Cdd:cd14505    140 AI---AAVRALRPGAIQTPKQENFLHQ 163
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 397-480 2.38e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 43.76  E-value: 2.38e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   397 GPPLDVSVIVDSPSTARISWSPPMYIDRNGIIVNYTVRIITTVRGTIRETNisNVSGNYYDASDLPQFASFNVTVAAATS 476
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNV--TPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 1133451038   477 VGLG 480
Cdd:smart00060   80 AGEG 83
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
41-205 3.44e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 48.40  E-value: 3.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   41 SDTSYNISGLDvytdYNVSVAAYTSAGTGPFDSVIRRTDSTVPTSPSDVSYINISSTSIEVSWNPPTDfngpnegyVITY 120
Cdd:COG4733    500 EDGTYTITAVQ----HAPEKYAAIDAGAFDDVPPQWPPVNVTTSESLSVVAQGTAVTTLTVSWDAPAG--------AVAY 567

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  121 -IRLESDTES-MSTNRLTGTSFVIENLekYE-QYSVTVVAFTDKG---PGASSDVLSVLTDEDLPGPPSNVSTMSTNTSI 194
Cdd:COG4733    568 eVEWRRDDGNwVSVPRTSGTSFEVPGI--YAgDYEVRVRAINALGvssAWAASSETTVTGKTAPPPAPTGLTATGGLGGI 645

                          170
                   ....*....|.
gi 1133451038  195 SITWSPPLDPN 205
Cdd:COG4733    646 TLSWSFPVDAD 656
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 1036-1091 5.13e-05

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: 45.14  E-value: 5.13e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1133451038 1036 ITHY--QFvswPDHGVPDEagpalDFVREVHEVASSAFGPVIVHCSAGVGRTGTFIAL 1091
Cdd:cd14499     80 IRHYdlYF---PDGSTPSD-----DIVKKFLDICENEKGAIAVHCKAGLGRTGTLIAC 129
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1049-1090 2.21e-04

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 42.65  E-value: 2.21e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1133451038 1049 VPDEAGPALD----FVREVHEVasSAFG-PVIVHCSAGVGRTGTFIA 1090
Cdd:cd14504     57 IEDYTPPTLEqideFLDIVEEA--NAKNeAVLVHCLAGKGRTGTMLA 101
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 1038-1089 3.20e-04

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


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 42.74  E-value: 3.20e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1133451038 1038 HYQFVSWP--DHGVPdEAGPALDFVREVHE-VASSAFGPVIVHCSAGVGRTGTFI 1089
Cdd:cd14510     73 HNRVERVPidDHNVP-TLDEMLSFTAEVREwMAADPKNVVAIHCKGGKGRTGTMV 126
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 289-390 3.56e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.94  E-value: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  289 SPVSSTAVNVSWLPPnlSNWNGLITNYTIEYRTNDEyiRPSIEVTatlssfansddpraaTTPLQLESIIIPSLHEFVNY 368
Cdd:cd00063     10 TDVTSTSVTLSWTPP--EDDGGPITGYVVEYREKGS--GDWKEVE---------------VTPGSETSYTLTGLKPGTEY 70

                           90       100
                   ....*....|....*....|...
gi 1133451038  369 SFIITLSNSIGQ-ISSLPVHIVT 390
Cdd:cd00063     71 EFRVRAVNGGGEsPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 289-380 5.86e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 39.91  E-value: 5.86e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038   289 SPVSSTAVNVSWLPPNLSNWNGLITNYTIEYRTNDEyirPSIEVTATLSSfansddpraattplqlESIIIPSLHEFVNY 368
Cdd:smart00060   10 TDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGS---EWKEVNVTPSS----------------TSYTLTGLKPGTEY 70

                            90
                    ....*....|..
gi 1133451038   369 SFIITLSNSIGQ 380
Cdd:smart00060   71 EFRVRAVNGAGE 82
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
993-1091 1.88e-03

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


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 41.48  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  993 HRYWPGAQPevygeINVDMLSETEKSDWI-VRKFKITKEKRSRTITHY--QFVSwpdhgvpDEAGPAldFVREVHEVASS 1069
Cdd:COG2365     66 DRLPPGVRY-----VHLPVLPDDAEALLEeLRDGDLTPGDAEEFMLELyrAFVD-------PDAADA--YRAAFRALADA 131

                           90       100
                   ....*....|....*....|..
gi 1133451038 1070 AFGPVIVHCSAGVGRTGTFIAL 1091
Cdd:COG2365    132 ENGPVLFHCTAGKDRTGVAAAL 153
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 1045-1095 1.90e-03

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 40.37  E-value: 1.90e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1133451038 1045 PDHGVPDEAgpALD-FVREVHEVASSAfgPVIVHCSAGVGRTGTFIALGTLL 1095
Cdd:pfam14566  109 TDEKAPLEE--DFDaLISIVKDAPEDT--ALVFNCQMGRGRTTTAMVIADLV 156
fn3 pfam00041
Fibronectin type III domain;
289-380 2.55e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 38.16  E-value: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038  289 SPVSSTAVNVSWLPPnlSNWNGLITNYTIEYRTNDEyirpsievtatlssfanSDDPRAATTPLQLESIIIPSLHEFVNY 368
Cdd:pfam00041    9 TDVTSTSLTVSWTPP--PDGNGPITGYEVEYRPKNS-----------------GEPWNEITVPGTTTSVTLTGLKPGTEY 69

                           90
                   ....*....|..
gi 1133451038  369 SFIITLSNSIGQ 380
Cdd:pfam00041   70 EVRVQAVNGGGE 81
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
1027-1090 3.79e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 38.80  E-value: 3.79e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1133451038  1027 ITKEKRSRTITHYQFVSWP--DHgvpDEAGPALDF---VREVHEVASSAfGPVIVHCSAGVGRTGTFIA 1090
Cdd:smart00195   33 VTNEVPNYNGSDFTYLGVPidDN---TETKISPYFpeaVEFIEDAESKG-GKVLVHCQAGVSRSATLII 97
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 1007-1091 6.30e-03

Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 families.


Pssm-ID: 463853 [Multi-domain]  Cd Length: 243  Bit Score: 39.92  E-value: 6.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133451038 1007 INVDMLSETEKSDWIVRKFKITKEKRSRTIT-HYQfvswpdhGVPDEAGPAldfVREVHEVASSAFGPVIVHCSAGVGRT 1085
Cdd:pfam13350   74 VHLPVADSEASSPELLARRALDPDDGEEFMAeLYR-------DMVTSARAA---YRALFEALADNDGPVLFHCTAGKDRT 143


                   ....*.
gi 1133451038 1086 GTFIAL 1091
Cdd:pfam13350  144 GVAAAL 149
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 1069-1091 7.83e-03

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 38.51  E-value: 7.83e-03
                           10        20
                   ....*....|....*....|...
gi 1133451038 1069 SAFGPVIVHCSAGVGRTGTFIAL 1091
Cdd:cd14529     87 LAPGPVLIHCKHGKDRTGLVSAL 109
UP_III_II cd09966
Uroplakin IIIb, IIIa and II; Uroplakins (UPs) are a family of proteins that associate with ...
 690-753 9.14e-03

Uroplakin IIIb, IIIa and II; Uroplakins (UPs) are a family of proteins that associate with each other to form plaques on the apical surface of the urothelium, the pseudo-stratified epithelium lining the urinary tract from renal pelvis to the bladder outlet. UPs are classified into 3 types: UPIa and UPIb, UPII, and UPIIIa and IIIb. UPIs are tetraspanins that have four transmembrane domains separating one large and one small extracellular domain while UPII and UPIIIs are single-pass transmembrane proteins. UPIa and UPIb form specific heterodimers with UPII and UPIII, respectively, which allows them to exit the endoplasmatic rediculum. UPII/UPIa and UPIIIs/UPIb form heterotetramers; six of these tetramers form the 16nm particle, seen in the hexagonal array of the asymmetric unit membrane, which is believed to form a urinary tract barrier. Uroplakins are also believed to play a role during urinary tract morphogenesis.


Pssm-ID: 197375  Cd Length: 181  Bit Score: 38.56  E-value: 9.14e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1133451038  690 RKRQAGGETVAETIGTNNSCGPNDivCNGPLKPGTQYQFKYRVYNsdDDDSYVESQYSGPIRTD 753
Cdd:cd09966     85 RNRRDIVSAYVLRVGNTTTCLSGY--CNTPLPGPGPYRVKYLVMN--GSGPSAQTEWSTPIRLN 144
 
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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