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Conserved domains on  [gi|2462566584|ref|XP_054177569|]
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receptor-type tyrosine-protein phosphatase H isoform X14 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 870-989 2.35e-78

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.


The actual alignment was detected with superfamily member cd14619:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 233  Bit Score: 255.58  E-value: 2.35e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 870 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 949
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462566584 950 KCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQ 989
Cdd:cd14619    81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQ 120
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 408-486 1.54e-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: 58.66  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 408 PNPVRNLHMETQTNSSIALCWEVPDGPYPQDYTYWVEYTGDGGGT----ETRNTTNTSVTAERLEPGTLYTFSVWAEKNG 483
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ...
gi 2462566584 484 ARG 486
Cdd:cd00063    81 GES 83
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
285-709 3.72e-10

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: 63.87  E-value: 3.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 285 TVDGLGPGSLYTCSVWVEKDGVNSSVEIVTSATAPNPVRNLTVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGGRAG 364
Cdd:COG3401     7 TSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 365 TRSTAHTNITVDRLE----PGCLYVFSVWVGKNGINSSRETRNATTAPNPVRNLHMETQTNSSIALCWEVPDGPYPQDYT 440
Cdd:COG3401    87 APPTATGLTTLTGSGsvggATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 441 YWVEYTGDGGGTETRNTTNTSVT------AERLEPGTLYTFSVWAEKNGARGSRQN----VSISTVPNAVTSLSKQDWTN 510
Cdd:COG3401   167 GVVVSPDTSATAAVATTSLTVTSttlvdgGGDIEPGTTYYYRVAATDTGGESAPSNevsvTTPTTPPSAPTGLTATADTP 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 511 STIALRWTAPQGPGQSSY------SYWVSWVREGmtdpRTQSTSGTDitlKELEAGSLYHLTVWAE--RNEVRGYNSTLT 582
Cdd:COG3401   247 GSVTLSWDPVTESDATGYrvyrsnSGDGPFTKVA----TVTTTSYTD---TGLTNGTTYYYRVTAVdaAGNESAPSNVVS 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 583 AAT---APNEVTDLQNETQTKNSVMLWWKAPGDPHSQLY-VYwvqwaskghprRGQDPQANWVNQTSRTNETWYKVEALE 658
Cdd:COG3401   320 VTTdltPPAAPSGLTATAVGSSSITLSWTASSDADVTGYnVY-----------RSTSGGGTYTKIAETVTTTSYTDTGLT 388

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462566584 659 PGTLYNFTVWAERNDVASSTQSLCASTYPDTVTITSCVSTSAGYGVNLIWS 709
Cdd:COG3401   389 PGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVA 439
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 231-314 8.96e-09

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: 53.65  E-value: 8.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 231 NPVRNLRVEAQTTSSISLSWEVPDGTDPQNSTYCVQCTGDGGRT----ETRNTTDTRVTVDGLGPGSLYTCSVWVEKDGV 306
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                          90
                  ....*....|..
gi 2462566584 307 NS----SVEIVT 314
Cdd:cd00063    82 ESppseSVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 141-228 1.71e-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: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 141 PNPVRNLRVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGG----RAGTRSTAHTNITVDGLEPGCLYAFSMW-VGKN 215
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRaVNGG 80

                          90
                  ....*....|...
gi 2462566584 216 GINSSRETRNATT 228
Cdd:cd00063    81 GESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 52-139 1.72e-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: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584  52 PNPGRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTT----ETRNTTATNVTVDGLGPGSLYTCSVWVEKDG 127
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|..
gi 2462566584 128 VNSSVGTVTTAT 139
Cdd:cd00063    81 GESPPSESVTVT 92
 
Name Accession Description Interval E-value
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 870-989 2.35e-78

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: 255.58  E-value: 2.35e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 870 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 949
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462566584 950 KCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQ 989
Cdd:cd14619    81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQ 120
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
841-987 2.16e-59

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 204.04  E-value: 2.16e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584  841 GFADEYQQL-SLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPgSDYINASFMPGLWSPQEFIATQGPLP 919
Cdd:smart00194   1 GLEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566584  920 QTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLD-SQPCTHGHLRVTLVGEEVMENWTVRELLL 987
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKVDDYTIRTLEV 148
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
866-987 8.40e-54

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 187.45  E-value: 8.40e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 866 NNAKNRYRNVLPYDWSRVPLKPihEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME 945
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTG--DPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462566584 946 AGRVKCEHYWPLDS-QPCTHGHLRVTLVGEE-VMENWTVRELLL 987
Cdd:pfam00102  79 KGREKCAQYWPEEEgESLEYGDFTVTLKKEKeDEKDYTVRTLEV 122
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 865-987 2.90e-21

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 95.45  E-value: 2.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 865 ENNAKNRYRNVLPYDWSRVPLKPihEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCM 944
Cdd:PHA02742   51 KNMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462566584 945 EAGRVKCEHYW-PLDSQPCTHGHLRVTLVGEEVMENWTVRELLL 987
Cdd:PHA02742  129 EDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCL 172
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
865-960 1.76e-12

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 68.96  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 865 ENNAKNRYRNVLPYDWSRVplkpiheEPGSDYINASFMPGLwSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCM 944
Cdd:COG5599    41 NGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                          90
                  ....*....|....*...
gi 2462566584 945 EAG--RVKCEHYWPLDSQ 960
Cdd:COG5599   113 EISkpKVKMPVYFRQDGE 130
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 408-486 1.54e-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: 58.66  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 408 PNPVRNLHMETQTNSSIALCWEVPDGPYPQDYTYWVEYTGDGGGT----ETRNTTNTSVTAERLEPGTLYTFSVWAEKNG 483
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ...
gi 2462566584 484 ARG 486
Cdd:cd00063    81 GES 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
285-709 3.72e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 63.87  E-value: 3.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 285 TVDGLGPGSLYTCSVWVEKDGVNSSVEIVTSATAPNPVRNLTVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGGRAG 364
Cdd:COG3401     7 TSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 365 TRSTAHTNITVDRLE----PGCLYVFSVWVGKNGINSSRETRNATTAPNPVRNLHMETQTNSSIALCWEVPDGPYPQDYT 440
Cdd:COG3401    87 APPTATGLTTLTGSGsvggATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 441 YWVEYTGDGGGTETRNTTNTSVT------AERLEPGTLYTFSVWAEKNGARGSRQN----VSISTVPNAVTSLSKQDWTN 510
Cdd:COG3401   167 GVVVSPDTSATAAVATTSLTVTSttlvdgGGDIEPGTTYYYRVAATDTGGESAPSNevsvTTPTTPPSAPTGLTATADTP 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 511 STIALRWTAPQGPGQSSY------SYWVSWVREGmtdpRTQSTSGTDitlKELEAGSLYHLTVWAE--RNEVRGYNSTLT 582
Cdd:COG3401   247 GSVTLSWDPVTESDATGYrvyrsnSGDGPFTKVA----TVTTTSYTD---TGLTNGTTYYYRVTAVdaAGNESAPSNVVS 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 583 AAT---APNEVTDLQNETQTKNSVMLWWKAPGDPHSQLY-VYwvqwaskghprRGQDPQANWVNQTSRTNETWYKVEALE 658
Cdd:COG3401   320 VTTdltPPAAPSGLTATAVGSSSITLSWTASSDADVTGYnVY-----------RSTSGGGTYTKIAETVTTTSYTDTGLT 388

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462566584 659 PGTLYNFTVWAERNDVASSTQSLCASTYPDTVTITSCVSTSAGYGVNLIWS 709
Cdd:COG3401   389 PGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVA 439
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 408-480 1.15e-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: 55.70  E-value: 1.15e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462566584  408 PNPVRNLHMETQTNSSIALCWEVPDGPYPQDYT--YWVEYTGDGGGTETRNTTN--TSVTAERLEPGTLYTFSVWAE 480
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIvgYRVEYREEGSEWKEVNVTPssTSYTLTGLKPGTEYEFRVRAV 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 587-670 2.14e-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: 2.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584  587 PNEVTDLQNETQTKNSVMLWWKAPGDPHSQLYV--YWVQWASKGHprrgqdpqaNWVNQTSRTNETWYKVEALEPGTLYN 664
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIvgYRVEYREEGS---------EWKEVNVTPSSTSYTLTGLKPGTEYE 71


                   ....*.
gi 2462566584  665 FTVWAE 670
Cdd:smart00060  72 FRVRAV 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 319-406 5.45e-09

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: 54.04  E-value: 5.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 319 PNPVRNLTVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGG----RAGTRSTAHTNITVDRLEPGCLYVFSVW-VGKN 393
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRaVNGG 80

                          90
                  ....*....|...
gi 2462566584 394 GINSSRETRNATT 406
Cdd:cd00063    81 GESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 231-314 8.96e-09

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: 53.65  E-value: 8.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 231 NPVRNLRVEAQTTSSISLSWEVPDGTDPQNSTYCVQCTGDGGRT----ETRNTTDTRVTVDGLGPGSLYTCSVWVEKDGV 306
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                          90
                  ....*....|..
gi 2462566584 307 NS----SVEIVT 314
Cdd:cd00063    82 ESppseSVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 141-228 1.71e-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: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 141 PNPVRNLRVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGG----RAGTRSTAHTNITVDGLEPGCLYAFSMW-VGKN 215
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRaVNGG 80

                          90
                  ....*....|...
gi 2462566584 216 GINSSRETRNATT 228
Cdd:cd00063    81 GESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 52-139 1.72e-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: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584  52 PNPGRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTT----ETRNTTATNVTVDGLGPGSLYTCSVWVEKDG 127
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|..
gi 2462566584 128 VNSSVGTVTTAT 139
Cdd:cd00063    81 GESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 232-308 1.08e-06

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: 47.22  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584  232 PVRNLRVEAQTTSSISLSWEVP--DGTDPQNSTYCVQCTGDGGRTETRNTT--DTRVTVDGLGPGSLYTCSVWVEKDGVN 307
Cdd:smart00060   3 PPSNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKEVNVTpsSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                   .
gi 2462566584  308 S 308
Cdd:smart00060  83 G 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 141-212 1.47e-06

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: 46.84  E-value: 1.47e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462566584  141 PNPVRNLRVEAQTNSSIALTWEVPdgPDPQNSTYGVEYTGDGGRAG------TRSTAHTNITVDGLEPGCLYAFSMWV 212
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPP--PDDGITGYIVGYRVEYREEGsewkevNVTPSSTSYTLTGLKPGTEYEFRVRA 76
fn3 pfam00041
Fibronectin type III domain;
589-667 4.36e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.87  E-value: 4.36e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566584 589 EVTDLQNETQTKNSVMLWWKAPGDPHSQLYVYWVQWASKGHPRRgqdpqanWVNQTSRTNETWYKVEALEPGTLYNFTV 667
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEP-------WNEITVPGTTTSVTLTGLKPGTEYEVRV 73
fn3 pfam00041
Fibronectin type III domain;
232-299 7.61e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.10  E-value: 7.61e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462566584 232 PVRNLRVEAQTTSSISLSWEVPDGTDPQNSTYCVQC----TGDGGRTETRNTTDTRVTVDGLGPGSLYTCSV 299
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYrpknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV 73
fn3 pfam00041
Fibronectin type III domain;
410-486 1.57e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.33  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 410 PVRNLHMETQTNSSIALCWEVPDGPYPQDYTYWVEYTGDGGGTETRNTTN----TSVTAERLEPGTLYTFSVWAEKNGAR 485
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVpgttTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                  .
gi 2462566584 486 G 486
Cdd:pfam00041  82 G 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 52-130 2.71e-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: 43.37  E-value: 2.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584   52 PNPGRNLTVETQTTSSISLSWEVP--DGLDSQNSNYWVQCTGDGGTTE--TRNTTATNVTVDGLGPGSLYTCSVWVEKDG 127
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKevNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                   ...
gi 2462566584  128 VNS 130
Cdd:smart00060  81 GEG 83
fn3 pfam00041
Fibronectin type III domain;
50-121 1.24e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 41.63  E-value: 1.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462566584  50 SAPnpgRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTTETRNTTATN----VTVDGLGPGSLYTCSV 121
Cdd:pfam00041   1 SAP---SNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGtttsVTLTGLKPGTEYEVRV 73
fn3 pfam00041
Fibronectin type III domain;
143-223 4.97e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.71  E-value: 4.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 143 PVRNLRVEAQTNSSIALTWEVPDGPDPQNSTYGVEY----TGDGGRAGTRSTAHTNITVDGLEPGCLYAFSMwVGKNGIN 218
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYrpknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV-QAVNGGG 80


                  ....*
gi 2462566584 219 SSRET 223
Cdd:pfam00041  81 EGPPS 85
 
Name Accession Description Interval E-value
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 870-989 2.35e-78

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: 255.58  E-value: 2.35e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 870 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 949
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462566584 950 KCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQ 989
Cdd:cd14619    81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQ 120
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 871-989 1.94e-75

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: 246.88  E-value: 1.94e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 871 RYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVK 950
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462566584 951 CEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQ 989
Cdd:cd14548    81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLER 119
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
841-987 2.16e-59

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 204.04  E-value: 2.16e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584  841 GFADEYQQL-SLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPgSDYINASFMPGLWSPQEFIATQGPLP 919
Cdd:smart00194   1 GLEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566584  920 QTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLD-SQPCTHGHLRVTLVGEEVMENWTVRELLL 987
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKVDDYTIRTLEV 148
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
866-987 8.40e-54

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 187.45  E-value: 8.40e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 866 NNAKNRYRNVLPYDWSRVPLKPihEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME 945
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTG--DPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462566584 946 AGRVKCEHYWPLDS-QPCTHGHLRVTLVGEE-VMENWTVRELLL 987
Cdd:pfam00102  79 KGREKCAQYWPEEEgESLEYGDFTVTLKKEKeDEKDYTVRTLEV 122
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 870-987 9.35e-53

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


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 184.38  E-value: 9.35e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 870 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 949
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462566584 950 KCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLL 987
Cdd:cd14618    81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKL 118
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 866-985 1.36e-48

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: 173.15  E-value: 1.36e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 866 NNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME 945
Cdd:cd14614    12 NRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462566584 946 AGRVKCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVREL 985
Cdd:cd14614    92 KRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREF 131
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 870-985 1.85e-47

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: 168.94  E-value: 1.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 870 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 949
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462566584 950 KCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVREL 985
Cdd:cd14617    81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREF 116
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 870-987 1.40e-46

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: 166.53  E-value: 1.40e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 870 NRYRNVLPYDWSRVPLKpIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 949
Cdd:cd14615     1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462566584 950 KCEHYWPlDSQPCTHGHLRVTLVGEEVMENWTVRELLL 987
Cdd:cd14615    80 KCEEYWP-SKQKKDYGDITVTMTSEIVLPEWTIRDFTV 116
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 866-987 8.05e-46

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: 164.88  E-value: 8.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 866 NNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME 945
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462566584 946 AGRVKCEHYWPLDSQPcTHGHLRVTLVGEEVMENWTVRELLL 987
Cdd:cd14553    83 RSRVKCDQYWPTRGTE-TYGLIQVTLLDTVELATYTVRTFAL 123
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 841-985 1.27e-42

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: 156.76  E-value: 1.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 841 GFADEYQQLSLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQ 920
Cdd:cd14543     4 GIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPK 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462566584 921 TVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPC-THGHLRVTLVGEEVMENWTVREL 985
Cdd:cd14543    84 TYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSlRYGDLTVTNLSVENKEHYKKTTL 149
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 870-985 2.31e-42

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: 154.29  E-value: 2.31e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 870 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 949
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462566584 950 KCEHYWPLDSQPCT-HGHLRVTLVGEEVMENWTVREL 985
Cdd:cd14616    81 RCHQYWPEDNKPVTvFGDIVITKLMEDVQIDWTIRDL 117
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 826-990 2.92e-39

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: 147.10  E-value: 2.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 826 DFADHVRKNERDSNCGFADEYQQLSlVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGL 905
Cdd:cd14626     2 DLADNIERLKANDGLKFSQEYESID-PGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 906 WSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPcTHGHLRVTLVGEEVMENWTVREL 985
Cdd:cd14626    81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTE-TYGMIQVTLLDTVELATYSVRTF 159


                  ....*
gi 2462566584 986 LLLQS 990
Cdd:cd14626   160 ALYKN 164
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 896-987 7.61e-39

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: 143.19  E-value: 7.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLD-SQPCTHGHLRVTLVGE 974
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEgGKPLEYGDITVTLVSE 80

                          90
                  ....*....|...
gi 2462566584 975 EVMENWTVRELLL 987
Cdd:cd00047    81 EELSDYTIRTLEL 93
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 857-987 6.21e-38

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: 143.04  E-value: 6.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 857 SQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHT 936
Cdd:cd14603    21 STVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKV 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462566584 937 LVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGEE-VMENWTVRELLL 987
Cdd:cd14603   101 ILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKrLNEEVILRTLKV 152
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 822-989 1.71e-37

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: 142.86  E-value: 1.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 822 IPAEDFADHVRKNERDSNCGFADEYQQLSLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASF 901
Cdd:cd14621     8 LPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 902 MPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPldSQPC-THGHLRVTLVGEEVMENW 980
Cdd:cd14621    88 INGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP--DQGCwTYGNIRVSVEDVTVLVDY 165


                  ....*....
gi 2462566584 981 TVRELLLLQ 989
Cdd:cd14621   166 TVRKFCIQQ 174
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 822-990 8.53e-37

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: 140.25  E-value: 8.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 822 IPAEDFADHVRKNERDSNCGFADEYQQLSlVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASF 901
Cdd:cd14624     4 IPILELADHIERLKANDNLKFSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 902 MPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPcTHGHLRVTLVGEEVMENWT 981
Cdd:cd14624    83 IDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTE-TYGLIQVTLLDTVELATYC 161


                  ....*....
gi 2462566584 982 VRELLLLQS 990
Cdd:cd14624   162 VRTFALYKN 170
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 896-987 3.37e-36

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: 135.94  E-value: 3.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPcTHGHLRVTLVGEE 975
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE-TYGNIQVTLLSTE 79

                          90
                  ....*....|..
gi 2462566584 976 VMENWTVRELLL 987
Cdd:cd14549    80 VLATYTVRTFSL 91
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 826-983 1.02e-35

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: 137.10  E-value: 1.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 826 DFADHVRKNERDSNCGFADEYQQLsLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGL 905
Cdd:cd14633     1 DLLQHITQMKCAEGYGFKEEYESF-FEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGY 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462566584 906 WSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQpcTHGHLRVTLVGEEVMENWTVR 983
Cdd:cd14633    80 HRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKDIKVTLIETELLAEYVIR 155
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 822-987 1.69e-35

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: 136.76  E-value: 1.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 822 IPAEDFADHVRKNERDSNCGFADEYQQLSlVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASF 901
Cdd:cd14625     4 IPISELAEHTERLKANDNLKLSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 902 MPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPlDSQPCTHGHLRVTLVGEEVMENWT 981
Cdd:cd14625    83 IDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP-SRGTETYGMIQVTLLDTIELATFC 161


                  ....*.
gi 2462566584 982 VRELLL 987
Cdd:cd14625   162 VRTFSL 167
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 865-983 6.01e-35

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: 133.61  E-value: 6.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 865 ENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCM 944
Cdd:cd14630     2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462566584 945 EAGRVKCEHYWPLDSQpcTHGHLRVTLVGEEVMENWTVR 983
Cdd:cd14630    82 EVGRVKCVRYWPDDTE--VYGDIKVTLIETEPLAEYVIR 118
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 861-984 3.55e-34

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: 131.11  E-value: 3.55e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 861 ASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVML 940
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462566584 941 TNCMEAGRVKCEHYWPLDsQPCTHGHLRVTLVGEEVMENWTVRE 984
Cdd:cd14554    81 TKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEYNMPQYILRE 123
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 869-988 6.95e-34

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: 130.20  E-value: 6.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 869 KNRYRNVLPYDWSRVPLKpIHEEpGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGR 948
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVK-LKQG-DNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462566584 949 VKCEHYWPLDSQP---CTHGHLRVTLVGEEVMENWTVRELLLL 988
Cdd:cd14545    79 IKCAQYWPQGEGNamiFEDTGLKVTLLSEEDKSYYTVRTLELE 121
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 865-987 7.65e-34

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: 132.36  E-value: 7.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 865 ENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCM 944
Cdd:cd14604    56 ENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREF 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462566584 945 EAGRVKCEHYWPL-DSQPCTHGHLRVTLVGEEVMENWTVRELLL 987
Cdd:cd14604   136 EMGRKKCERYWPLyGEEPMTFGPFRISCEAEQARTDYFIRTLLL 179
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 865-987 9.09e-34

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: 129.95  E-value: 9.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 865 ENNAKNRYRNVLPYDWSRVPLKPIHeepgsDYINASFMPGLWSPQEF--IATQGPLPQTVGDFWRLVWEQQSHTLVMLTN 942
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPLGDEG-----GYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462566584 943 CMEAGRVKCEHYWP--LDSQPCTHGHLRVTLVGEEVMENWTVRELLL 987
Cdd:cd14597    77 EVEGGKIKCQRYWPeiLGKTTMVDNRLQLTLVRMQQLKNFVIRVLEL 123
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 872-985 1.43e-33

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: 129.29  E-value: 1.43e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 872 YRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKC 951
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462566584 952 EHYWPldSQPC-THGHLRVTLVGEEVMENWTVREL 985
Cdd:cd14620    81 YQYWP--DQGCwTYGNIRVAVEDCVVLVDYTIRKF 113
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 861-987 3.90e-33

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: 129.58  E-value: 3.90e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 861 ASASENNAKNRYRNVLPYDWSRVPLkpiheEPGSDYINASFM----PGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHT 936
Cdd:cd14600    35 AKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYVnmeiPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSL 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462566584 937 LVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLL 987
Cdd:cd14600   110 IVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLL 160
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 842-985 8.51e-33

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: 128.61  E-value: 8.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 842 FADEYQQlslVGHSQSQMVASAS-----ENNAKNRYRNVLPYDWSRVPLKPI--HEEPGSDYINASFMPGLWSPQEFIAT 914
Cdd:cd17667     1 FSEDFEE---VQRCTADMNITAEhsnhpDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIAT 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462566584 915 QGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPcTHGHLRVTLVGEEVMENWTVREL 985
Cdd:cd17667    78 QGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE-EYGNIIVTLKSTKIHACYTVRRF 147
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 866-987 1.54e-32

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: 126.81  E-value: 1.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 866 NNAKNRYRNVLPYDWSRVPLKPI-HEEPGSDYINASF-MPGLWSPQE------FIATQGPLPQTVGDFWRLVWEQQSHTL 937
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRdPNVPGSDYINANYiRNENEGPTTdenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462566584 938 VMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLL 987
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQV 130
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 869-985 2.79e-32

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: 125.72  E-value: 2.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 869 KNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGR 948
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462566584 949 VKCEHYWP-LDSQPCTHGHLRVTLVGEEVMENWTVREL 985
Cdd:cd14602    81 KKCERYWAePGEMQLEFGPFSVTCEAEKRKSDYIIRTL 118
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 842-987 2.33e-31

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: 124.37  E-value: 2.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 842 FADEYQQLSlvgHSQSQM---VASASENNAKNRYRNVLPYDWSRVPLkpiHEEpGSDYINASFMPGLWSPQEFIATQGPL 918
Cdd:cd14608     1 WAAIYQDIR---HEASDFpcrVAKLPKNKNRNRYRDVSPFDHSRIKL---HQE-DNDYINASLIKMEEAQRSYILTQGPL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462566584 919 PQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQP---CTHGHLRVTLVGEEVMENWTVRELLL 987
Cdd:cd14608    74 PNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKemiFEDTNLKLTLISEDIKSYYTVRQLEL 145
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 870-989 3.03e-31

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: 122.51  E-value: 3.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 870 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGlWSPQE--FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAg 947
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRG-YDGEEkaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462566584 948 RVKCEHYWPlDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQ 989
Cdd:cd14547    79 KEKCAQYWP-EEENETYGDFEVTVQSVKETDGYTVRKLTLKY 119
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 821-985 6.59e-30

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: 120.61  E-value: 6.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 821 DIPAEDFADHVRKNER----DSNCGFADEYQQL-SLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSD 895
Cdd:cd14628     2 EVPARNLYAYIQKLTQietgENVTGMELEFKRLaSSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDsQPCTHGHLRVTLVGEE 975
Cdd:cd14628    82 YINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEY 160

                         170
                  ....*....|
gi 2462566584 976 VMENWTVREL 985
Cdd:cd14628   161 NMPQYILREF 170
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 821-985 9.74e-30

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: 120.22  E-value: 9.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 821 DIPAEDFADHVRKNER----DSNCGFADEYQQL-SLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSD 895
Cdd:cd14629     3 EVPARNLYAHIQKLTQvppgESVTAMELEFKLLaNSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDsQPCTHGHLRVTLVGEE 975
Cdd:cd14629    83 YINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEY 161

                         170
                  ....*....|
gi 2462566584 976 VMENWTVREL 985
Cdd:cd14629   162 NMPQYILREF 171
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 895-987 1.32e-29

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: 117.05  E-value: 1.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 895 DYINASF----MPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVT 970
Cdd:cd14541     1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                          90
                  ....*....|....*..
gi 2462566584 971 LVGEEVMENWTVRELLL 987
Cdd:cd14541    81 CVSEEVTPSFAFREFIL 97
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 854-991 1.56e-29

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: 118.53  E-value: 1.56e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 854 HSQSQMVASASENNAKNRYRNVLPYDWSRVPLkpihEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQ 933
Cdd:cd14607    12 HDYPHRVAKYPENRNRNRYRDVSPYDHSRVKL----QNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQK 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462566584 934 SHTLVMLTNCMEAGRVKCEHYWPLDSQPC---THGHLRVTLVGEEVMENWTVReLLLLQSL 991
Cdd:cd14607    88 TKAVVMLNRIVEKDSVKCAQYWPTDEEEVlsfKETGFSVKLLSEDVKSYYTVH-LLQLENI 147
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 882-987 4.61e-29

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: 115.89  E-value: 4.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 882 RVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQp 961
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE- 79

                          90       100
                  ....*....|....*....|....*.
gi 2462566584 962 cTHGHLRVTLVGEEVMENWTVRELLL 987
Cdd:cd14631    80 -VYGDFKVTCVEMEPLAEYVVRTFTL 104
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 821-985 5.15e-29

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: 117.91  E-value: 5.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 821 DIPAEDFADHVRKNER----DSNCGFADEYQQLS-LVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSD 895
Cdd:cd14627     3 EVPARNLYSYIQKLAQvevgEHVTGMELEFKRLAnSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDsQPCTHGHLRVTLVGEE 975
Cdd:cd14627    83 YINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEY 161

                         170
                  ....*....|
gi 2462566584 976 VMENWTVREL 985
Cdd:cd14627   162 NMPQYILREF 171
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 865-985 7.16e-29

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: 116.90  E-value: 7.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 865 ENNAKNRYRNVLPYDWSRVPLKPIHEE-PGSDYINASFMPG-LWSPQE----FIATQGPLPQTVGDFWRLVWEQQSHTLV 938
Cdd:cd14606    17 ENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNqLLGPDEnaktYIASQGCLEATVNDFWQMAWQENSRVIV 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462566584 939 MLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVREL 985
Cdd:cd14606    97 MTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTL 143
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 896-985 3.40e-28

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: 112.87  E-value: 3.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQpcTHGHLRVTLVGEE 975
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK--TYGDIEVELKDTE 78

                          90
                  ....*....|
gi 2462566584 976 VMENWTVREL 985
Cdd:cd14558    79 KSPTYTVRVF 88
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 865-989 8.31e-28

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: 113.19  E-value: 8.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 865 ENNAKNRYRNVLPYDWSRVPLkpiHE----EPGSDYINASF-MPGLWS-------PQEFIATQGPLPQTVGDFWRLVWEQ 932
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVL---HDgdpnEPVSDYINANIiMPEFETkcnnskpKKSYIATQGCLQNTVNDFWRMVFQE 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462566584 933 QSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQ 989
Cdd:cd14605    78 NSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSK 134
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 896-987 4.70e-27

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: 110.03  E-value: 4.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFM-PGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGE 974
Cdd:cd18533     1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                          90
                  ....*....|....*
gi 2462566584 975 EV--MENWTVRELLL 987
Cdd:cd18533    81 EEndDGGFIVREFEL 95
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 829-987 2.73e-26

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: 109.76  E-value: 2.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 829 DHVRKNERdsncgFADEYQQL-SLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINAS-FMPGLW 906
Cdd:cd14610    11 DHLKNKNR-----LEKEWEALcAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASpIMDHDP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 907 SPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHlRVTLVGEEV-MENWTVREL 985
Cdd:cd14610    86 RNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIY-EVNLVSEHIwCEDFLVRSF 164


                  ..
gi 2462566584 986 LL 987
Cdd:cd14610   165 YL 166
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 896-987 2.82e-26

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: 107.31  E-value: 2.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQpcTHGHLRVTLVGEE 975
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTE--VYGDIKVTLVETE 78

                          90
                  ....*....|..
gi 2462566584 976 VMENWTVRELLL 987
Cdd:cd14555    79 PLAEYVVRTFAL 90
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 871-987 3.66e-26

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: 107.82  E-value: 3.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 871 RYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVK 950
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462566584 951 CEHYWPLDSQpCTHGHLRVTLVGEEVMENWTVRELLL 987
Cdd:cd14623    81 CAQYWPSDGS-VSYGDITIELKKEEECESYTVRDLLV 116
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 829-987 1.01e-25

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: 108.20  E-value: 1.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 829 DHVRKNERdsncgFADEYQQLSLVGHSQSQMVASASENN-AKNRYRNVLPYDWSRVPLKPIHEEPGSDYINAS------- 900
Cdd:cd14609     9 DHLRNRDR-----LAKEWQALCAYQAEPNTCSTAQGEANvKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpiiehdp 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 901 FMPGlwspqeFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHlRVTLVGEEV-MEN 979
Cdd:cd14609    84 RMPA------YIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIY-EVNLVSEHIwCED 156


                  ....*...
gi 2462566584 980 WTVRELLL 987
Cdd:cd14609   157 FLVRSFYL 164
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 896-987 1.44e-25

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: 105.43  E-value: 1.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQpCTHGHLRVTLVGEE 975
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGS-VSSGDITVELKDQT 79

                          90
                  ....*....|..
gi 2462566584 976 VMENWTVRELLL 987
Cdd:cd14552    80 DYEDYTLRDFLV 91
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 896-989 1.45e-25

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: 105.53  E-value: 1.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFM--PGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWP--LDSQPCTHGHLRVTL 971
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdsLNKPLICGGRLEVSL 80

                          90
                  ....*....|....*...
gi 2462566584 972 VGEEVMENWTVRELLLLQ 989
Cdd:cd14538    81 EKYQSLQDFVIRRISLRD 98
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 896-987 2.16e-25

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: 104.75  E-value: 2.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQpcTHGHLRVTLVGEE 975
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSD--TYGDIKITLLKTE 78

                          90
                  ....*....|..
gi 2462566584 976 VMENWTVRELLL 987
Cdd:cd14632    79 TLAEYSVRTFAL 90
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 895-987 5.46e-25

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: 103.55  E-value: 5.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 895 DYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQpCTHGHLRVTLVGE 974
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGS-VTHGEITIEIKND 79

                          90
                  ....*....|...
gi 2462566584 975 EVMENWTVRELLL 987
Cdd:cd14622    80 TLLETISIRDFLV 92
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 896-990 8.76e-25

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: 102.98  E-value: 8.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWP-LDSQPCTHGHLRVTLVGE 974
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsMEEGSRAFGDVVVKINEE 80

                          90
                  ....*....|....*.
gi 2462566584 975 EVMENWTVRELLLLQS 990
Cdd:cd14557    81 KICPDYIIRKLNINNK 96
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 896-989 1.61e-24

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: 102.30  E-value: 1.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPlDSQPCTHGHLRVTLVGEE 975
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGCWTYGNLRVRVEDTV 79

                          90
                  ....*....|....
gi 2462566584 976 VMENWTVRELLLLQ 989
Cdd:cd14551    80 VLVDYTTRKFCIQK 93
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 868-985 2.14e-24

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: 103.38  E-value: 2.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 868 AKNRYRNVLPYDWSRVPLK-PIHEEPGSDYINASFMPGL-WSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME 945
Cdd:cd14612    17 SKDRYKTILPNPQSRVCLRrAGSQEEEGSYINANYIRGYdGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462566584 946 aGRVKCEHYWPldSQPCTHGHLRVTLVGEEVMENWTVREL 985
Cdd:cd14612    97 -KKEKCVHYWP--EKEGTYGRFEIRVQDMKECDGYTIRDL 133
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 845-970 3.49e-23

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: 100.84  E-value: 3.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 845 EYQQLSLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPgSDYINASFMPGLWSPQE--FIATQGPLPQTV 922
Cdd:cd14599    17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENN-TGYINASHIKVTVGGEEwhYIATQGPLPHTC 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462566584 923 GDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWP-LDSQ--PCTHGHLRVT 970
Cdd:cd14599    96 HDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPkLGSKhsSATYGKFKVT 146
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 896-987 6.00e-23

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: 97.78  E-value: 6.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGrvKCEHYWPLDSQPCTHGHLRVTLVGEE 975
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECETFKVTLSGED 78

                          90
                  ....*....|....*..
gi 2462566584 976 VM-----ENWTVRELLL 987
Cdd:cd14550    79 HSclsneIRLIVRDFIL 95
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 896-987 7.77e-23

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: 97.49  E-value: 7.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPC-THGHLRVTLVGE 974
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlQFGPFKISLEKE 80

                          90
                  ....*....|....
gi 2462566584 975 EVM-ENWTVRELLL 987
Cdd:cd14542    81 KRVgPDFLIRTLKV 94
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 896-987 1.60e-22

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: 96.59  E-value: 1.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPcTHGHLRVTLVGEE 975
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE-EYGNFLVTQKSVQ 79

                          90
                  ....*....|..
gi 2462566584 976 VMENWTVRELLL 987
Cdd:cd17668    80 VLAYYTVRNFTL 91
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 869-987 9.14e-22

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: 96.08  E-value: 9.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 869 KNRYRNVLPYDWSRVPLK-PIHEEPGSDYINASFMPGLWSPQE-FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEA 946
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTsPDQDDPLSSYINANYIRGYGGEEKvYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462566584 947 GRvKCEHYWPLDSqpCTHGHLRVTLVGEEVMENWTVRELLL 987
Cdd:cd14613   108 NE-KCTEYWPEEQ--VTYEGIEITVKQVIHADDYRLRLITL 145
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 896-989 1.84e-21

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: 93.66  E-value: 1.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASF--MPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLD-SQPCTHGHLRVTLV 972
Cdd:cd14596     1 YINASYitMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLE 80

                          90
                  ....*....|....*..
gi 2462566584 973 GEEVMENWTVRELLLLQ 989
Cdd:cd14596    81 NYQALQYFIIRIIKLVE 97
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 895-987 2.06e-21

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: 93.47  E-value: 2.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 895 DYINASFM----PGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVT 970
Cdd:cd14601     1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                          90
                  ....*....|....*..
gi 2462566584 971 LVGEEVMENWTVRELLL 987
Cdd:cd14601    81 CHSEEGNPAYVFREMTL 97
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 865-987 2.90e-21

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 95.45  E-value: 2.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 865 ENNAKNRYRNVLPYDWSRVPLKPihEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCM 944
Cdd:PHA02742   51 KNMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462566584 945 EAGRVKCEHYW-PLDSQPCTHGHLRVTLVGEEVMENWTVRELLL 987
Cdd:PHA02742  129 EDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCL 172
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 896-983 3.33e-21

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: 92.83  E-value: 3.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGL--WSPQeFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLD-SQPCTHGHLRVTLV 972
Cdd:cd14539     1 YINASLIEDLtpYCPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQALVYGAITVSLQ 79

                          90
                  ....*....|.
gi 2462566584 973 GEEVMENWTVR 983
Cdd:cd14539    80 SVRTTPTHVER 90
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 869-989 1.91e-20

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: 91.13  E-value: 1.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 869 KNRYRNVLPYDWSRVPLKPIH-EEPGSDYINASFMPGLWSPQE-FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEA 946
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYGGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462566584 947 GRvKCEHYWPldSQPCTHGHLRVTLVGEEVMENWTVRELLLLQ 989
Cdd:cd14611    82 NE-KCVLYWP--EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQ 121
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 824-958 5.41e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 88.91  E-value: 5.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 824 AEDFADhvRKNERDSNCGFADEYQQLSLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPiHEEPGSDYINASFMP 903
Cdd:PHA02747   11 AIDFLK--RRNQLNCFGIIRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWID 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462566584 904 GLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME-AGRVKCEHYWPLD 958
Cdd:PHA02747   88 GFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGtNGEEKCYQYWCLN 143
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 896-987 5.42e-19

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: 86.31  E-value: 5.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLtNCMEAGRVKCEHYWPlDSQPCTHGHLRVTLVGEE 975
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWP-DEGSGTYGPIQVEFVSTT 78

                          90
                  ....*....|..
gi 2462566584 976 VMENWTVRELLL 987
Cdd:cd14556    79 IDEDVISRIFRL 90
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 896-987 8.56e-18

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: 83.27  E-value: 8.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQE--FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPC---THGHLRVT 970
Cdd:cd14540     1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdalTFGEYKVS 80

                          90
                  ....*....|....*..
gi 2462566584 971 LVGEEVMENWTVRELLL 987
Cdd:cd14540    81 TKFSVSSGCYTTTGLRV 97
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 896-987 4.90e-17

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: 80.95  E-value: 4.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGlWSPQE--FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCtHGHLRVTLVG 973
Cdd:cd14546     1 YINASTIYD-HDPRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEV-YHIYEVHLVS 78

                          90
                  ....*....|....*
gi 2462566584 974 EEVM-ENWTVRELLL 987
Cdd:cd14546    79 EHIWcDDYLVRSFYL 93
PHA02738 PHA02738
hypothetical protein; Provisional
 866-955 1.04e-16

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 82.28  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 866 NNAKNRYRNVLPYDWSRVPLkPIHEEPGsDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME 945
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVIL-PAERNRG-DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                          90
                  ....*....|
gi 2462566584 946 AGRVKCEHYW 955
Cdd:PHA02738  127 NGREKCFPYW 136
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 896-970 5.54e-16

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: 77.50  E-value: 5.54e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566584 896 YINASFM--PGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGR-VKCEHYWPL-DSQPCTHGHLRVT 970
Cdd:cd17658     1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAeENESREFGRISVT 79
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 896-979 1.42e-15

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: 76.60  E-value: 1.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLtNCMEAGRVkCEHYWPlDSQPCTHGHLRVTLVGEE 975
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDAAQL-CMQYWP-EKTSCCYGPIQVEFVSAD 77


                  ....
gi 2462566584 976 VMEN 979
Cdd:cd14634    78 IDED 81
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 896-987 3.37e-15

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: 75.42  E-value: 3.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEhYWPLDSQPCTHGHLRVTLVGEE 975
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPINCETFKVTLIAEE 79

                          90
                  ....*....|....*..
gi 2462566584 976 VM-----ENWTVRELLL 987
Cdd:cd17669    80 HKclsneEKLIIQDFIL 96
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 865-955 3.12e-13

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 71.98  E-value: 3.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 865 ENNAKNRYRNVLPYDWSRVPLKP-------------------IHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDF 925
Cdd:PHA02746   50 ENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDF 129

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462566584 926 WRLVWEQQSHTLVMLTNcMEAGRVKCEHYW 955
Cdd:PHA02746  130 FKLISEHESQVIVSLTD-IDDDDEKCFELW 158
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 896-975 3.16e-13

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: 69.71  E-value: 3.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNcmEAGRVKCEH-YWPLDSQPCTHGHLRVTLVGE 974
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEFvYWPSREESMNCEAFTVTLISK 78


                  .
gi 2462566584 975 E 975
Cdd:cd17670    79 D 79
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
865-960 1.76e-12

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 68.96  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 865 ENNAKNRYRNVLPYDWSRVplkpiheEPGSDYINASFMPGLwSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCM 944
Cdd:COG5599    41 NGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                          90
                  ....*....|....*...
gi 2462566584 945 EAG--RVKCEHYWPLDSQ 960
Cdd:COG5599   113 EISkpKVKMPVYFRQDGE 130
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 896-970 7.64e-12

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: 65.77  E-value: 7.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQE--FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWP-LDSQ--PCTHGHLRVT 970
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrLGSRhnTVTYGRFKIT 80
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 896-983 1.80e-11

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: 64.71  E-value: 1.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRvkCEHYWPlDSQPCTHGHLRVTLVGEE 975
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWP-ENGVHRHGPIQVEFVSAD 77


                  ....*...
gi 2462566584 976 VMENWTVR 983
Cdd:cd14635    78 LEEDIISR 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 408-486 1.54e-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: 58.66  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 408 PNPVRNLHMETQTNSSIALCWEVPDGPYPQDYTYWVEYTGDGGGT----ETRNTTNTSVTAERLEPGTLYTFSVWAEKNG 483
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ...
gi 2462566584 484 ARG 486
Cdd:cd00063    81 GES 83
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 896-956 1.82e-10

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: 61.58  E-value: 1.82e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNC-MEAGrvkCEHYWP 956
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWP 59
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
285-709 3.72e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 63.87  E-value: 3.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 285 TVDGLGPGSLYTCSVWVEKDGVNSSVEIVTSATAPNPVRNLTVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGGRAG 364
Cdd:COG3401     7 TSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 365 TRSTAHTNITVDRLE----PGCLYVFSVWVGKNGINSSRETRNATTAPNPVRNLHMETQTNSSIALCWEVPDGPYPQDYT 440
Cdd:COG3401    87 APPTATGLTTLTGSGsvggATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 441 YWVEYTGDGGGTETRNTTNTSVT------AERLEPGTLYTFSVWAEKNGARGSRQN----VSISTVPNAVTSLSKQDWTN 510
Cdd:COG3401   167 GVVVSPDTSATAAVATTSLTVTSttlvdgGGDIEPGTTYYYRVAATDTGGESAPSNevsvTTPTTPPSAPTGLTATADTP 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 511 STIALRWTAPQGPGQSSY------SYWVSWVREGmtdpRTQSTSGTDitlKELEAGSLYHLTVWAE--RNEVRGYNSTLT 582
Cdd:COG3401   247 GSVTLSWDPVTESDATGYrvyrsnSGDGPFTKVA----TVTTTSYTD---TGLTNGTTYYYRVTAVdaAGNESAPSNVVS 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 583 AAT---APNEVTDLQNETQTKNSVMLWWKAPGDPHSQLY-VYwvqwaskghprRGQDPQANWVNQTSRTNETWYKVEALE 658
Cdd:COG3401   320 VTTdltPPAAPSGLTATAVGSSSITLSWTASSDADVTGYnVY-----------RSTSGGGTYTKIAETVTTTSYTDTGLT 388

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462566584 659 PGTLYNFTVWAERNDVASSTQSLCASTYPDTVTITSCVSTSAGYGVNLIWS 709
Cdd:COG3401   389 PGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVA 439
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
268-701 5.62e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 63.10  E-value: 5.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 268 TGDGGRTETRNTTDTRVTVDGLGPGSLYTCSVWVEKDGVNS----SVEIVTSATAPNPVRNLTVEAQTNSSIALTWEVPD 343
Cdd:COG3401    84 VAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTattaTAVAGGAATAGTYALGAGLYGVDGANASGTTASSV 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 344 GPDPQNSTYGVEYTGDGGRAGTRSTAHT-NITVDRLEPGCLYVFSVWVGKNGINSSRETR----NATTAPNPVRNLHMET 418
Cdd:COG3401   164 AGAGVVVSPDTSATAAVATTSLTVTSTTlVDGGGDIEPGTTYYYRVAATDTGGESAPSNEvsvtTPTTPPSAPTGLTATA 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 419 QTNSSIALCWEVPDGPYPQdyTYWVEYTGDGGGTETR--NTTNTSVTAERLEPGTLYTFSVWAEKNGARGSRQNVSIS-- 494
Cdd:COG3401   244 DTPGSVTLSWDPVTESDAT--GYRVYRSNSGDGPFTKvaTVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSvt 321

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 495 ---TVPNAVTSLSKQDWTNSTIALRWTAPQGPGQSSYSYWVSWVREGMTDPRTQSTSGTDITLKELEAGSLYHLTVWAER 571
Cdd:COG3401   322 tdlTPPAAPSGLTATAVGSSSITLSWTASSDADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVD 401

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 572 ---------NEVRGYNSTLTAATAPNEVTDLqNETQTKNSVMLWWKAPGDPHSQLYVYWVQWASKGHPRRGQDPQANWVN 642
Cdd:COG3401   402 aagnesapsEEVSATTASAASGESLTASVDA-VPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTAT 480

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566584 643 QTSRTNETWYKVEALEPGTLYNFTVWAERNDVASSTQSlCASTYPDTVTITSCVSTSAG 701
Cdd:COG3401   481 TTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAA-AVGGAPDGTPNVTGASPVTV 538
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 408-480 1.15e-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: 55.70  E-value: 1.15e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462566584  408 PNPVRNLHMETQTNSSIALCWEVPDGPYPQDYT--YWVEYTGDGGGTETRNTTN--TSVTAERLEPGTLYTFSVWAE 480
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIvgYRVEYREEGSEWKEVNVTPssTSYTLTGLKPGTEYEFRVRAV 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 587-670 2.14e-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: 2.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584  587 PNEVTDLQNETQTKNSVMLWWKAPGDPHSQLYV--YWVQWASKGHprrgqdpqaNWVNQTSRTNETWYKVEALEPGTLYN 664
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIvgYRVEYREEGS---------EWKEVNVTPSSTSYTLTGLKPGTEYE 71


                   ....*.
gi 2462566584  665 FTVWAE 670
Cdd:smart00060  72 FRVRAV 77
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 896-983 4.66e-09

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: 57.61  E-value: 4.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 896 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV-KCEHYWPlDSQPCTHGHLRVTLVGE 974
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP-EPGLQQYGPMEVEFVSG 79


                  ....*....
gi 2462566584 975 EVMENWTVR 983
Cdd:cd14637    80 SADEDIVTR 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 319-406 5.45e-09

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: 54.04  E-value: 5.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 319 PNPVRNLTVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGG----RAGTRSTAHTNITVDRLEPGCLYVFSVW-VGKN 393
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRaVNGG 80

                          90
                  ....*....|...
gi 2462566584 394 GINSSRETRNATT 406
Cdd:cd00063    81 GESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 231-314 8.96e-09

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: 53.65  E-value: 8.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 231 NPVRNLRVEAQTTSSISLSWEVPDGTDPQNSTYCVQCTGDGGRT----ETRNTTDTRVTVDGLGPGSLYTCSVWVEKDGV 306
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                          90
                  ....*....|..
gi 2462566584 307 NS----SVEIVT 314
Cdd:cd00063    82 ESppseSVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 587-676 1.30e-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: 53.27  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 587 PNEVTDLQNETQTKNSVMLWWKAPGDPHSQLYVYWVQWASKGHPRrgqdpqanWVN-QTSRTNETWYKVEALEPGTLYNF 665
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGD--------WKEvEVTPGSETSYTLTGLKPGTEYEF 72

                          90
                  ....*....|.
gi 2462566584 666 TVWAERNDVAS 676
Cdd:cd00063    73 RVRAVNGGGES 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 141-228 1.71e-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: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 141 PNPVRNLRVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGG----RAGTRSTAHTNITVDGLEPGCLYAFSMW-VGKN 215
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRaVNGG 80

                          90
                  ....*....|...
gi 2462566584 216 GINSSRETRNATT 228
Cdd:cd00063    81 GESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 52-139 1.72e-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: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584  52 PNPGRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTT----ETRNTTATNVTVDGLGPGSLYTCSVWVEKDG 127
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|..
gi 2462566584 128 VNSSVGTVTTAT 139
Cdd:cd00063    81 GESPPSESVTVT 92
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
58-534 2.70e-08

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 57.70  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584  58 LTVETQTTSSISLSWEVPDGLDSQNSNYWV-QCTGDGGTTETRNTTATNVTVDGLGPGSLYTCSVWVEKDGVNSSVGTVT 136
Cdd:COG3401    55 LLVAAGLSSGGGLGTGGRAGTTSGVAAVAVaAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGG 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 137 TATAPNPVRNLRVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGGRAGTRSTAHT-NITVDGLEPGCLYAFSMWVGKN 215
Cdd:COG3401   135 AATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTlVDGGGDIEPGTTYYYRVAATDT 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 216 GINSSRETR----NATTAHNPVRNLRVEAQTTSSISLSWEvpDGTDPQNSTYCV--QCTGDGGRTETRNTTDTRVTVDGL 289
Cdd:COG3401   215 GGESAPSNEvsvtTPTTPPSAPTGLTATADTPGSVTLSWD--PVTESDATGYRVyrSNSGDGPFTKVATVTTTSYTDTGL 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 290 GPGSLYTCSVWVEKDGVNSS-----VEIVTSATAPNPVRNLTVEAQTNSSIALTWEVPDGPDPqnSTYGVEYTGDGGRAG 364
Cdd:COG3401   293 TNGTTYYYRVTAVDAAGNESapsnvVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDADV--TGYNVYRSTSGGGTY 370

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 365 T---RSTAHTNITVDRLEPGCLYVFSV-WVGKNGINSSRETRNATTAPNPVRNLH--------METQTNSSIALCWEVPD 432
Cdd:COG3401   371 TkiaETVTTTSYTDTGLTPGTTYYYKVtAVDAAGNESAPSEEVSATTASAASGESltasvdavPLTDVAGATAAASAASN 450

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 433 GPYPQDYTYWVEYTGDGGGTETRNTTNTSVTAERLEPGTLYTFSVWAEKNGARGSRQNVSISTVPNAVTSLSKQDWTNST 512
Cdd:COG3401   451 PGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNV 530

                         490       500
                  ....*....|....*....|..
gi 2462566584 513 IALRWTAPQGPGQSSYSYWVSW 534
Cdd:COG3401   531 TGASPVTVGASTGDVLITDLVS 552
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 319-390 3.92e-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: 48.76  E-value: 3.92e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462566584  319 PNPVRNLTVEAQTNSSIALTWEVPdgPDPQNSTYGVEYTGDGGRAG------TRSTAHTNITVDRLEPGCLYVFSVWV 390
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPP--PDDGITGYIVGYRVEYREEGsewkevNVTPSSTSYTLTGLKPGTEYEFRVRA 76
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 497-585 6.37e-07

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: 48.26  E-value: 6.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 497 PNAVTSLSKQDWTNSTIALRWTAPQGPGQSSYSYWVSWVREGMTDPR---TQSTSGTDITLKELEAGSLYHLTVWAERNE 573
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKeveVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|..
gi 2462566584 574 VRGYNSTLTAAT 585
Cdd:cd00063    81 GESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 232-308 1.08e-06

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: 47.22  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584  232 PVRNLRVEAQTTSSISLSWEVP--DGTDPQNSTYCVQCTGDGGRTETRNTT--DTRVTVDGLGPGSLYTCSVWVEKDGVN 307
Cdd:smart00060   3 PPSNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKEVNVTpsSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                   .
gi 2462566584  308 S 308
Cdd:smart00060  83 G 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 141-212 1.47e-06

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: 46.84  E-value: 1.47e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462566584  141 PNPVRNLRVEAQTNSSIALTWEVPdgPDPQNSTYGVEYTGDGGRAG------TRSTAHTNITVDGLEPGCLYAFSMWV 212
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPP--PDDGITGYIVGYRVEYREEGsewkevNVTPSSTSYTLTGLKPGTEYEFRVRA 76
fn3 pfam00041
Fibronectin type III domain;
589-667 4.36e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.87  E-value: 4.36e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566584 589 EVTDLQNETQTKNSVMLWWKAPGDPHSQLYVYWVQWASKGHPRRgqdpqanWVNQTSRTNETWYKVEALEPGTLYNFTV 667
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEP-------WNEITVPGTTTSVTLTGLKPGTEYEVRV 73
fn3 pfam00041
Fibronectin type III domain;
232-299 7.61e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.10  E-value: 7.61e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462566584 232 PVRNLRVEAQTTSSISLSWEVPDGTDPQNSTYCVQC----TGDGGRTETRNTTDTRVTVDGLGPGSLYTCSV 299
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYrpknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV 73
fn3 pfam00041
Fibronectin type III domain;
410-486 1.57e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.33  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 410 PVRNLHMETQTNSSIALCWEVPDGPYPQDYTYWVEYTGDGGGTETRNTTN----TSVTAERLEPGTLYTFSVWAEKNGAR 485
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVpgttTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                  .
gi 2462566584 486 G 486
Cdd:pfam00041  82 G 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 52-130 2.71e-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: 43.37  E-value: 2.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584   52 PNPGRNLTVETQTTSSISLSWEVP--DGLDSQNSNYWVQCTGDGGTTE--TRNTTATNVTVDGLGPGSLYTCSVWVEKDG 127
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKevNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                   ...
gi 2462566584  128 VNS 130
Cdd:smart00060  81 GEG 83
fn3 pfam00041
Fibronectin type III domain;
321-401 1.18e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 41.63  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 321 PVRNLTVEAQTNSSIALTWEVPDGPDPQNSTYGVEY----TGDGGRAGTRSTAHTNITVDRLEPGCLYVFSVwVGKNGIN 396
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYrpknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV-QAVNGGG 80


                  ....*
gi 2462566584 397 SSRET 401
Cdd:pfam00041  81 EGPPS 85
fn3 pfam00041
Fibronectin type III domain;
50-121 1.24e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 41.63  E-value: 1.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462566584  50 SAPnpgRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTTETRNTTATN----VTVDGLGPGSLYTCSV 121
Cdd:pfam00041   1 SAP---SNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGtttsVTLTGLKPGTEYEVRV 73
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
51-375 1.48e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 45.76  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584  51 APNPGRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTTETRNTTATNVTVDGLGPGSLYTCSVWVEKDGVNS 130
Cdd:COG3401   232 PPSAPTGLTATADTPGSVTLSWDPVTESDATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNE 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 131 S-----VGTVTTATAPNPVRNLRVEAQTNSSIALTWEVPDGPDPqnSTYGVEYTGDGGRAGT---RSTAHTNITVDGLEP 202
Cdd:COG3401   312 SapsnvVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDADV--TGYNVYRSTSGGGTYTkiaETVTTTSYTDTGLTP 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 203 GCLYAFS-MWVGKNGINSSR---------ETRNATTAHNPVRNLRVEAQTTSSISLSWEVPDGTDPQNstycvqcTGDGG 272
Cdd:COG3401   390 GTTYYYKvTAVDAAGNESAPseevsattaSAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAV-------LADGG 462

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 273 RTETRNTTDTRVTVDGLGPGSLYTCSVWVEKDGVNSSVEIVTSATAPNPVRNLTVEAQTNSSIALTWEVPDGPDPQNSTY 352
Cdd:COG3401   463 DTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGAST 542

                         330       340
                  ....*....|....*....|...
gi 2462566584 353 GVEYTGDGGRAGTRSTAHTNITV 375
Cdd:COG3401   543 GDVLITDLVSLTTSASSSVSGAG 565
fn3 pfam00041
Fibronectin type III domain;
143-223 4.97e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.71  E-value: 4.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566584 143 PVRNLRVEAQTNSSIALTWEVPDGPDPQNSTYGVEY----TGDGGRAGTRSTAHTNITVDGLEPGCLYAFSMwVGKNGIN 218
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYrpknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV-QAVNGGG 80


                  ....*
gi 2462566584 219 SSRET 223
Cdd:pfam00041  81 EGPPS 85
 
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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